WO2022084303A2 - Use of polypeptides having dnase activity - Google Patents

Use of polypeptides having dnase activity Download PDF

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Publication number
WO2022084303A2
WO2022084303A2 PCT/EP2021/078926 EP2021078926W WO2022084303A2 WO 2022084303 A2 WO2022084303 A2 WO 2022084303A2 EP 2021078926 W EP2021078926 W EP 2021078926W WO 2022084303 A2 WO2022084303 A2 WO 2022084303A2
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WIPO (PCT)
Prior art keywords
seq
polypeptide
perfume
dnase
dnase activity
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PCT/EP2021/078926
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French (fr)
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WO2022084303A3 (en
Inventor
Ting Yang
Lilian Eva Tang BALTSEN
Klaus GORI
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Novozymes A/S
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Priority to EP21815367.4A priority Critical patent/EP4232539A2/en
Publication of WO2022084303A2 publication Critical patent/WO2022084303A2/en
Publication of WO2022084303A3 publication Critical patent/WO2022084303A3/en

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/21—Endodeoxyribonucleases producing 5'-phosphomonoesters (3.1.21)
    • C12Y301/21001—Deoxyribonuclease I (3.1.21.1)
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/50—Perfumes
    • C11D2111/12—

Definitions

  • the present invention relates to compositions such as cleaning compositions comprising an enzyme having DNase activity and at least one perfume compound.
  • the invention further relates to use of the detergent compositions in cleaning processes and/or for deep cleaning of organic stains, to methods of using said compositions for removal or reduction of components of organic matter, and to methods for increasing binding of a perfume to a textile, for boosting the effect of perfumes in detergent compositions, for increasing perfume retention on a textile and for producing perfume-containing compositions with a reduced amount of perfume.
  • perfumes may be chemical compounds or e.g. natural oils such as essential oils and other natural compounds.
  • the perfumes often have a double function of providing a desired scent and masking undesirable odors, which may stem from the detergent itself or from the fabric.
  • perfume in laundry detergents has faced several challenges. For example, may perfume components are released very quickly, thus the “freshness” effect of perfume often does not last very long.
  • perfume allergy there is a trend to use detergents containing less or no perfume.
  • perfume is expensive and can represent a significant factor in the overall cost of e.g. laundry detergents.
  • Enzymes have been used in cleaning compositions for decades. Usually a cocktail of various enzymes is added to cleaning compositions, wherein each enzyme targets a specific substrate, e.g. amylases are active towards starch stains, proteases on protein stains and so forth. The effectiveness of these commercial enzymes provides cleaning compositions which remove much of the soiling.
  • components of organic matters such as biofilm and extracellular polymeric substances (EPS) constitute a challenging type of staining due to the complex nature of such organic matter, and commercially available cleaning compositions are generally not able to effectively remove or reduce EPS and/or biofilm related stains.
  • EPS extracellular polymeric substances
  • Textile surfaces and hard surfaces such as dishes or the inner space of a laundry or dishwashing machine enduring a number of wash/cleaning cycles, become soiled with many different types of soiling which may be composed of proteins, grease, starch etc.
  • Some types of stain may be associated with organic matter such as biofilm, EPS, etc. , which may be composed of different molecules such as polysaccharides, extracellular DNA (eDNA), and proteins.
  • Some organic matter comprises an extracellular polymeric matrix, which may be sticky or gluing, which when present on textiles attracts soils and may cause redeposition or backstaining of soil, resulting in a greying of the textile.
  • organic matters such as biofilms often cause malodor issues as various malodor molecules can be adhered by the polysaccharides, extracellular DNA (eDNA) and proteins in the complex extracellular matrix and be slowly released to cause a noticeable malodor.
  • WO 2014/08701 1 WO 2015/155350 and WO 2017/060475.
  • WO 201 1/163325 describes various perfume raw materials, perfume delivery systems and consumer products comprising such perfume raw materials and/or such perfume delivery systems.
  • the present invention is based on the surprising discovery that the use of a DNase in a detergent composition results in an enhanced effect of perfume compounds in the composition that allows for the amount of perfume to be reduced while still maintaining a freshness and cleanliness effect of the perfume on a textile washed with the detergent composition.
  • the present invention relates to detergent compositions comprising an enzyme having DNase activity and at least one perfume compound, as well as to use of a polypeptide having DNase activity in detergent compositions comprising a perfume, e.g. for increasing binding of a perfume to a textile during a laundry process, for increasing perfume retention on a textile after wash, and/or for enhancing the effect of a perfume in a detergent composition.
  • the invention further relates to a method for increasing binding of a perfume to a textile during a laundry process, and/or for increasing perfume retention on a textile, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity.
  • the invention further relates to a method for enhancing the effect of a perfume in a laundry detergent composition, and/or for preparing a detergent composition with a reduced perfume content while maintaining perfume effect after wash, the method comprising preparing a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity.
  • the invention further relates to a method for cleaning an item, wherein the item is preferably a textile, comprising the steps of: a) contacting the item with a detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, and optionally b) rinsing the item.
  • SEQ ID NO: 1 DNase polypeptide obtained from Aspergillus oryzae
  • SEQ ID NO: 6 mature DNase polypeptide obtained from Metabacillus indicus (previously known as Bacillus cibi)
  • SEQ ID NO 7 mature polypeptide obtained from Bacillus sp-62451
  • SEQ ID NO 8 mature polypeptide obtained from Bacillus horikoshii
  • SEQ ID NO 10 mature polypeptide obtained from Bacillus sp-62520
  • SEQ ID NO 12 mature polypeptide obtained from Bacillus horikoshii
  • SEQ ID NO 14 mature polypeptide obtained from Bacillus sp-16840
  • SEQ ID NO 15 mature polypeptide obtained from Bacillus sp-62668
  • SEQ ID NO 19 mature polypeptide obtained from Bacillus sp-18318
  • SEQ ID NO 20 mature polypeptide obtained from Bacillus idriensis
  • SEQ ID NO 23 mature polypeptide obtained from Bacillus vietnamensis
  • SEQ ID NO 24 mature polypeptide obtained from Bacillus hwajinpoensis
  • SEQ ID NO 25 mature polypeptide obtained from Paenibacillus mucilaginosus
  • SEQ ID NO 26 mature polypeptide obtained from Bacillus indicus
  • SEQ ID NO 27 mature polypeptide obtained from Bacillus marisflavi
  • SEQ ID NO 28 mature polypeptide obtained from Bacillus luciferensis
  • SEQ ID NO 30 mature polypeptide obtained from Bacillus sp. SA2-6
  • SEQ ID NO 33 mature polypeptide obtained from Pyrenochaetopsis sp.
  • SEQ ID NO 34 mature polypeptide obtained from Vibrissea flavovirens
  • SEQ ID NO 35 mature polypeptide obtained from Setosphaeria rostrate
  • SEQ ID NO 36 mature polypeptide obtained from Endophragmiella valdina
  • SEQ ID NO 37 mature polypeptide obtained from Corynespora cassiicola
  • SEQ ID NO 38 mature polypeptide obtained from Paraphoma sp. XZ1965
  • SEQ ID NO 39 mature polypeptide obtained from Monilinia fructicola
  • SEQ ID NO 40 mature polypeptide obtained from Curvularia lunata
  • SEQ ID NO 41 mature polypeptide obtained from Penicillium reticulisporum
  • SEQ ID NO 42 mature polypeptide obtained from Penicillium quercetorum
  • SEQ ID NO 43 mature polypeptide obtained from Setophaeosphaeria sp.
  • SEQ ID NO 44 mature polypeptide obtained from Alternaria sp. XZ2545
  • SEQ ID NO 45 mature polypeptide obtained from Alternaria sp.
  • SEQ ID NO 48 mature polypeptide obtained from Trichoderma reesei
  • SEQ ID NO 50 mature polypeptide obtained from Scytalidium thermophilum obtained from Scytalidium thermophilum
  • SEQ ID NO 53 mature polypeptide obtained from Acremonium sp. XZ2007
  • SEQ ID NO 54 mature polypeptide obtained from Acremonium dichromosporum
  • SEQ ID NO 55 mature polypeptide obtained from Sarocladium sp. XZ2014
  • SEQ ID NO 56 mature polypeptide obtained from Metarhizium sp. HNA15-2
  • SEQ ID NO 58 mature polypeptide obtained from Isaria tenuipes
  • SEQ ID NO 60 mature polypeptide obtained from Metarhizium lepidiotae
  • DNase deoxyribonuclease
  • the term “DNase” means a polypeptide or an enzyme with DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA.
  • DNase activity is determined according to the procedure described in Assay 1 or Assay 2 herein.
  • Biofilm A “biofilm” is organic matter produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS).
  • EPS extracellular polymeric substance
  • Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides. Biofilms may form on living or non-living surfaces.
  • the microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium.
  • Bacteria living in a biofilm usually have significantly different properties from planktonic bacteria of the same species, as the dense and protected environment of the film allows them to cooperate and interact in various ways.
  • One benefit of this environment for the microorganisms is increased resistance to detergents and antibiotics, as the dense extracellular matrix and the outer layer of cells protect the interior of the community.
  • biofilm living bacteria do not lose their ability to live as planktonic cells if the biofilm matrix is compromised.
  • biofilm- or EPS-producing bacteria can e.g. be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis and Stenotrophomonas sp.
  • Clade means a group of polypeptides clustered together on the basis of homologous features traced to a common ancestor. Polypeptide clades can be visualized as phylogenetic trees and a clade is a group of polypeptides that consists of a common ancestor and all its lineal descendants.
  • Deep cleaning refers to disruption or removal of a biofilm or components of a biofilm such as polysaccharides, proteins, DNA, soil or other components present in the biofilm.
  • Detergent component means a detergent adjunct ingredient that is different from the DNase polypeptide of this invention.
  • cleaning component means a detergent adjunct ingredient that is different from the DNase polypeptide of this invention. The precise nature of these additional cleaning or adjunct components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used.
  • Suitable detergent components include, but are not limited to the components described below, such as surfactants, builders and co-builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes (other than the enzymes of the invention), enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti- redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • surfactants such as surfactants, builders and co-builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes (other than the enzymes of the invention), enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric
  • Detergent compositions will typically contain at least one surfactant along with additional components such as at least one builder and/or at least one bleach component.
  • Detergent composition The term “detergent composition” or “cleaning composition” refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles.
  • the detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning.
  • the term encompasses any materials/compounds selected for the particular type of detergent composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions such as liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment.
  • detergent compositions such as liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment.
  • the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, mannanases, nucleases or any mixture thereof), and/or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferases, hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • additional enzymes such as proteases,
  • Detergent enzyme refers to enzymes that are not encompassed by the term “DNase” as defined herein.
  • the term “detergent enzyme” includes enzymes traditionally used in detergent compositions, including but not limited to proteases, amylases, lipases, mannanases, pectate lyases and cellulases. Other detergent enzymes may e.g. include carbohydrases, pectinases, arabinases, galactanases, xylanases, oxidases or peroxidases.
  • expression includes any step involved in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion.
  • fragment means a polypeptide having one or more amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide or domain , where the fragment has DNase activity.
  • host cell means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention.
  • host cell encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.
  • isolated means a polypeptide, nucleic acid, cell, or other specified material or component that is separated from at least one other component with which it is naturally associated, including but not limited to, for example, other proteins, nucleic acids, cells, etc.
  • An isolated polypeptide, nucleic acid, cell or other material is thus in a form that does not occur in nature.
  • Laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention.
  • the laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand .
  • a “laundry process” is intended to include any steps related to laundry, whether by hand or by machine, including but not limited to pre-treatment of fabrics, washing steps using a solution containing a laundry detergent composition, and rinsing steps e.g. using a fabric softener.
  • malodor means an odor which is not desired on clean items.
  • malodor is compounds with an unpleasant smell, which may be produced by microorganisms.
  • unpleasant smells which can be sweat or body odor adhered to an item which has been in contact with human or animal.
  • malodor can be the odor from spices which stick to items, for example curry or other spices which smell strongly.
  • Mature polypeptide means a polypeptide in its mature form following N-terminal processing (e.g., removal of signal peptide). It is known in the art that a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C- terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.
  • Mature polypeptides of the invention may therefore have slight differences at the N- and/or C-terminal due to such differentiated expression by the host cell, while still having the same enzyme activity.
  • a mature polypeptide having one or more amino acids absent from the N- and/or C-terminal may be considered to be a “fragment” of the full-length polypeptide.
  • a mature polypeptide having one or more additional amino acids at the N- and/or C-terminal due to differentiated expression may be considered to be an “extended” polypeptide.
  • Perfume effect in the context of the present invention is related to the human perception of perfume on washed clothes.
  • the perfume effect of a polypeptide of the invention having DNase activity can be analyzed e.g. by means of a sensory evaluation such as that described in Example 1 .
  • the perfume effect can alternatively be measured by GC-MS analysis and expressed quantitatively as a “fragrance intensity” e.g. as described in Examples 2 and 3.
  • An increased perfume effect can thus be expressed as an increased fragrance intensity, such that washing an item with a DNase polypeptide according to the invention results in an increase in fragrance intensity compared to washing the item under the same conditions but without the DNase polypeptide.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
  • sequence identity is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled “longest identity” is used as the percent identity and is calculated as follows:
  • Textile means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles), and is intended to include the term “fabric” as well.
  • the textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and towelling.
  • the textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g.
  • the textile or fabric may also be non -cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non -cellulose based fibers.
  • non -cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non -cellulose based fibers.
  • blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g.
  • Fabric may be conventional washable laundry, for example stained household laundry.
  • fabric or garment it is intended to include the broader term textiles as well.
  • variant means a polypeptide having DNase activity comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more positions.
  • a substitution means replacement of the amino acid occupying a position with a different amino acid;
  • a deletion means removal of the amino acid occupying a position; and
  • an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
  • wash cycle is defined herein as a washing operation wherein textiles are immersed in a wash liquor, mechanical action of some kind is applied to the textile in order to release stains and to facilitate flow of wash liquor in and out of the textile, and finally the superfluous wash liquor is removed. After one or more wash cycles, the textile is generally rinsed and dried.
  • wash liquor is intended to mean the solution or mixture of water and detergents, in particular a detergent composition of the invention, used for laundering textiles, or for hard surface cleaning or dishwashing.
  • the term is also intended to include e.g. rinse solutions comprising a fabric softener comprising a DNase polypeptide used for rinsing textiles.
  • the nomenclature [E/Q] or [EQ] means that the amino acid at this position may be a glutamic acid (Glu, E) or a glutamine (Gin, Q).
  • the nomenclature [V/G/A/l] or [VGAI] means that the amino acid at this position may be a valine (Vai, V), glycine (Gly, G), alanine (Ala, A) or isoleucine (lie, I), and so forth for other combinations as described herein.
  • the amino acid X is defined such that it may be any of the 20 natural amino acids.
  • substitutions are typically indicated with the original amino acid, the position number, and the replacement amino acid.
  • A226V indicates that the original alanine residue in position 226 has been replaced by a valine residue.
  • G184* indicates that the original glycine residue in position 184 has been deleted.
  • Insertions are indicated by listing the original amino acid, the position number, the original amino acid and the inserted amino acid. For example, S97SD indicates that an aspartic acid residue has been inserted after the serine residue in position 97.
  • the inventors have surprisingly found that enzymes having DNase activity act synergistically with volatile perfume compounds, resulting in an enhanced binding of perfume compounds to textiles washed with a detergent composition comprise a DNase and one or more perfume compounds. As a result of the increased retention of perfume compounds by the textiles, an enhanced perfume effect is obtained, allowing the amount of perfume in such detergent compositions to be reduced while still maintaining the desired perfume effect.
  • Volatile perfume compounds are often added to detergent compositions, e.g. laundry detergents or fabric softeners, to mask malodors and to provide a fresh and clean scent in the washed items, e.g. textiles. These malodors may come from various sources.
  • One example is buildup of organic matter such as sebum, body soils, cell debris, biofilm, EPS etc. It has previously been shown that polypeptides having DNase activity can be used for preventing or removing biofilm on items such as textiles or fabric; see e.g. WO 2015/155350, WO 2017/060475 and Morales-Garcia et al, J Surfact Deterg (2020) DOI 10.1002/jsde.12398.
  • Polypeptides having DNase activity have also been shown to be able to reduce malodor in washed textiles.
  • perfumes and the associated fresh and clean scent are often desired by consumers in detergent compositions such as laundry detergents, there are as noted above disadvantages to the use of perfumes, including the high cost of perfume compounds as well as the risk of allergy.
  • the present invention addresses these challenges by providing detergent compositions comprising polypeptides with DNase activity that have been found to have synergistic effects with perfume compounds, and which can thereby reduce the need for perfume addition to detergent compositions, in particular laundry detergent compositions.
  • one embodiment of the invention relates to a detergent composition
  • a detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, where the amount of perfume is reduced compared to a comparable detergent composition without a DNase.
  • Such compositions will have a perfume effect corresponding to that of a comparable detergent composition without the DNase and with a greater amount of perfume.
  • This may allow the amount of perfume to be reduced to e.g. no more than 90%, such as no more than 80% or even lower, e.g. no more than 70% or no more than 60%, relative to the comparable composition without a DNase, with substantially the same perfume effect.
  • This may be assessed e.g. using a sensory evaluation such as that described in Example 1 or quantitatively by GC-MS analysis e.g. as described in Example 2.
  • the invention thus provides a detergent composition comprising a DNase and at least one perfume compound, wherein the composition has an increased perfume effect relative to a comparable detergent composition without a DNase.
  • the detergent composition is a laundry detergent composition, wherein the composition provides an increased perfume retention on a textile.
  • the invention thus provides a laundry detergent composition comprising a DNase and at least one perfume compound, wherein the composition has increased perfume retention on a textile after wash relative to a comparable detergent composition without a DNase.
  • the detergent composition is a fabric softener composition, wherein the composition provides an increased perfume retention on a textile.
  • the invention thus provides a fabric softener composition comprising a DNase and at least one perfume compound, wherein the composition has increased perfume retention on a textile after rinse relative to a comparable fabric softener composition without a DNase.
  • the detergent composition may be for cleaning of hard surfaces, for example for dishwashing, or for cleaning hard surfaces such as those found in kitchens and bathrooms.
  • the DNase in the detergent compositions, uses and methods of the present invention is a nuclease polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA.
  • the terms “DNase” and “polypeptide with/having DNase activity” may be used interchangeably herein.
  • X 1 , 2, 3, 4, 5, 6, 7, 8 or 9 e.g. Deoxyribonuclease I, Deoxyribonuclease IV, Type I site-specific deoxyribonuclease, Type II site-specific deoxyribonuclease, Type III site-specific deoxyribonucle
  • Y 1 , 2, 4 or 5, e.g. Deoxyribonuclease II, Aspergillus deoxyribonuclease K(1 ), Crossover junction endo- deoxyribonuclease, or Deoxyribonuclease X.
  • the DNase activity is obtained from a microorganism, and the DNase is a microbial enzyme.
  • the DNase is more preferably of fungal or bacterial origin.
  • the polypeptide having DNase activity may for example be a fungal DNase obtained from Aspergillus, for example from Aspergillus oryzae.
  • Suitable bacterial DNases may, for example, be obtained from species of Bacillus and related genera (cf. Patel and Gupta, Int. J. Syst. Evol. Microbiol. 2020; 70:406-438, who proposed six new Bacillaceae genera from species formerly classified as belonging to the genus Bacillus), e.g. from Bacillus, Cytobacillus, Metabacillus, Alkalihalobacillus, Rossellomorea or Mesobacillus.
  • DNases examples include Bacillus licheniformis, Bacillus subtilis, Bacillus horikoshii, Cytobacillus horneckiae, Metabacillus indicus, Alkalihalobacillus algicola, Rossellomorea vietnamensis, Alkalihalobacillus hwajinpoensis, Metabacillus indicus, Mesobacillus campisalis, Bacillus idriensis, Bacillus algicola, Bacillus marisflavi and Bacillus luciferensis.
  • Preferred bacterial DNases include those obtained from Metabacillus indicus (previously known as Bacillus cibi) and variants thereof.
  • the DNase may also be obtained from any of the following: Pyrenochaetopsis sp., Vibrissea flavovirens, Setosphaeria rostrate, Endophragmiella valdina, Corynespora cassiicola, Paraphoma sp., Mon i Unia fructicola, Curvularia lunata, Penicillium reticulisporum, Penicillium quercetorum, Setophaeosphaeria sp., Alternaria, Alternaria sp., Trichoderma reesei, Chaetomium thermophilum, Scytalidium thermophilum, Metapochonia suchlasporia, Daldinia fissa, Acremonium sp., Acremonium dichromosporum, Sarocladium sp., Metarhizium sp.
  • HNA 15-2 Isaria tenuipes Scytalidium circinatum, Metarhizium lepidiotae, Thermobispora bispora, Sporormia fimetaria, Pycnidiophora cf. dispera, Clavicipitaceae sp., Westerdykella sp., Humicolopsis cephalosporioides, Neosartorya massa, Roussoella intermedia, Pleosporales, Phaeosphaeria or Didymosphaeria futilis.
  • the polypeptides having DNase activity are polypeptides comprising the PFAM domain DUF1524 ((pfam.xfam.org/), “The Pfam protein families database: towards a more sustainable future”, R.D. Finn, et.al. Nucleic Acids Research (2016) Database Issue 44:D279-D285”).
  • the DUF1524 domain contains a conserved HXXP sequence (where H is the amino acid histidine, P is the amino acid proline, and X is any amino acid motif) commonly found in nucleases (M.A. Machnicka, et al.
  • DUF stands for domain of unknown function, and polypeptide families comprising, e.g., DUF have been collected in the Pfam database, which provides sequence alignments and hidden Markov models that define the collected protein domains.
  • the polypeptides having DNase activity in the composition of the invention comprise the DUF1524 domain.
  • DNases comprising the DUF1524 domain see WO 2017/060475, which is hereby incorporated by reference.
  • the DNase is a NUC1 or NUC1_A DNase.
  • a NUC1 DNase is a DNase comprising a domain termed NUC1 , and polypeptides with this domain are in addition to having DNase activity characterized by comprising certain motifs.
  • a NUC1 sub-domain had been identified, termed the NUC1_A domain, which also is characterized by comprising certain motifs.
  • the NUC1 and NUC1_A DNases are described in WO 2017/060475 and WO 2018/184873, which are hereby incorporated by reference.
  • the preparation of the polypeptide having DNase activity as described herein can e.g. be performed as described in WO 2017/059802 (incorporated herein by reference), in particular in the sections Nucleic Acid Construct, Expression Vectors, Host Cells, Methods of Production and Fermentation Broth Formulations. See also WO 2015/155350, WO 2017/060475, WO 2017/060505, WO 2017/064269 and WO 2018/177936, the contents of which are incorporated herein by reference.
  • the polypeptide having DNase activity is a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 , or a fragment thereof having DNase activity.
  • a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C-terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.
  • the N-terminal amino acid portion e.g. the 15 or 17 N-terminal amino acid residues
  • the mature polypeptide is a fragment of SEQ ID NO: 1 comprising 206 amino acid residues, corresponding to amino acids 16 to 221 of SEQ ID NO: 1 (shown as SEQ ID NO: 2).
  • the mature polypeptide is a fragment of SEQ ID NO: 1 comprising 204 amino acid residues, corresponding to amino acids 18 to 221 of SEQ ID NO: 1 (shown as SEQ ID NO: 3).
  • the polypeptide having DNase activity may thus be a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the mature polypeptide of SEQ ID NO: 2 or SEQ ID NO: 3.
  • a polypeptide having DNase activity and at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 , or a fragment thereof having DNase activity, e.g. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 2 or SEQ ID NO: 3, may be a variant having one or more alterations, e.g. substitutions, compared to SEQ ID NO: 1 .
  • Polypeptide variants may be engineered using protein engineering methods known in the art to produce a polypeptide having one or more improved properties compared to the parent polypeptide, for example improved detergent stability and/or wash performance, e.g. an improved deep cleaning effect.
  • a variant of the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 may, for example, include any of the alterations disclosed in WO 2017/064269 (incorporated herein by reference).
  • the polypeptide may thus be a variant of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 having DNase activity and comprising a substitution at one or more positions corresponding to positions 4, 17, 19, 36, 38, 39, 40, 41 , 45, 51 , 53, 54, 55, 57, 64, 66, 67, 68, 69, 70, 71 , 72, 74, 75, 77, 82, 83, 84, 85, 86, 88, 91 , 99, 101 , 105, 106, 115, 1 16, 135, 136, 138, 139, 140, 141 , 151 , 152, 153, 154, 162, 163, 164, 166, 168, 169, 173,
  • a DNase variant of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 may e.g. comprise one or more substitutions selected from the group consisting of N4E, L17E, T19A, T19G, T19I, K36P, Q38P, S39V, S39R, A40P, A40H, L41 T, L41 H, V45H, L51 G, K53T, K53P, G54P, A55P, N57H, E64A, E64Q, E64R, E64T, E64I, E64S, T66H, K67A, K67T, N68V, N68P, N68I, N68H, S69A, S69D, S69E, S69K, S69L, S69W, S69Y, S69Q, N70T, N70H, N70G, R71 T, D72E, S74H, S74G, G75I, N77T, K82P, K82I, D
  • the polypeptide having DNase activity belongs to the GYS-clade and comprises one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5).
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 6, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity may be a variant having one or more alterations, e.g. substitutions, compared to SEQ ID NO: 6.
  • a variant of the polypeptide of SEQ ID NO: 6 may, for example, include any of the alterations disclosed in WO 2018/01 1277 (incorporated herein by reference).
  • the polypeptide thus may be a variant of SEQ ID NO: 6 having DNase activity and comprising a substitution at one or more positions corresponding to positions 1 , 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 16, 17, 19, 21 , 22, 24, 25, 27, 28, 29, 30, 32, 38, 39, 40, 42, 49, 51 , 52, 55, 56, 57, 58, 59, 61 , 63, 65, 68, 76, 77, 78, 79, 80, 82, 83, 92, 93, 94, 99, 101 , 102, 104, 105, 107, 109, 1 12, 116, 125, 126, 127, 130, 132, 135, 138, 139, 143, 144, 145, 147, 149, 152, 156, 157, 159, 160,
  • a DNase variant of SEQ ID NO: 6 may e.g. comprise one or more substitutions selected from the group consisting of T1 I, T1 L, T1 V, T1 F, T1 Y, T1 M, T1 E, G4N, T5F, T5C, P6V, P6G, S7D, S7T, K8V, S9K, S9Q, S9V, S9L, S9F, S9P, S9R, A10D, A10M, A10I, A10Q, A10T, A10V, A10L, A10K, Q12S, Q12V, Q12E, S13D, S13Y, S13T, S13Q, S13F, S13R, S13V, S13N, S13H, S13M, S13W, S13K, S13L, S13E, Q14M, Q14R, N16S, A17C, A17V, A17E, A17T, A17S, T19K
  • the polypeptide having DNase activity may be a DNase variant which compared to the DNase of SEQ ID NO: 6 comprises two or more substitutions selected from the group consisting of: T1 1, T1 L, T1 V, S13Y, T22P, S25P, S27L, S39P, S42G, S42A, S42T, S57W, S57Y, S57F, S59V, S59I, S59L, V76L, V76I, Q109R, S1 16D, S116E, T127V, T127I, T127L, S144P, A147H, S167L, S167I, S167V, G175D and G175E, wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 6 of at least 80%, e.g. at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99%. DNase variants comprising such
  • the polypeptide having DNase activity may be a DNase variant which compared to a DNase of SEQ ID NO: 6 comprises at least one substitution selected from the group consisting of: G4K, S7G, K8R, S9I, N16G, S27K, S27R, D32F, D32I, D32L, D32R, D32V, L33H ,L33R, L33K, L33V, L33Y, S39C, G41 P, S42H, D45E, Q48D, N61 E, T65M, T65W, S66R ,S66M, S66W, S66Y, S66V, F78L, P91 L, S101 N, S106L, S106R, S106H, Q109E, A1 12E, T127P, S130A, S130Y, T138D, Q140V, Q140G, A147P, C148A, W154Y, T157V, Y159A, Y159R, G
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 7, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 8, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 9, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 10, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 11 , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 2, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 13, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 14, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 135, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 6, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 7, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 8, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 9, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 21 , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 22, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 23, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 24, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 25, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 26, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 27, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 28, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 29, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 30, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity belongs to the NAWK clade and comprises one or both of the motifs [V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32).
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 33, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 34, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 35, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 36, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 37, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 38, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 39, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 40, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 41 , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 42, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 43, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 44, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 45, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity belongs to the KNAW clade and comprises one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47).
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 48, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 49, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 50, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 51 , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 52, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 53, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 54, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 55, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 56, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 57, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 58, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 59, or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 60, or a fragment thereof having DNase activity.
  • the DNase used in the present invention may be any of those that are disclosed in WO 2018/177203, WO 2018/177936 or WO 2018/177938, the contents of which are incorporated herein by reference.
  • the DNase may be the mature polypeptide obtained from Morchella costata disclosed as SEQ ID NO: 12 in WO 2018/177203 (SEQ ID NO: 61 herein), or a variant thereof; or a mature polypeptide obtained from Rhizoctonia solani disclosed in WO 2018/177938, such as the polypeptide of SEQ ID NO: 33, 36, 39, 42, 45, 48 or 51 therein, or a variant thereof, for example SEQ ID NO: 45 disclosed in WO 2018/177938 (SEQ ID NO: 62 herein), or a variant thereof.
  • the polypeptide having DNase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 61 , or a fragment thereof having DNase activity.
  • the polypeptide having DNase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 62, or a fragment thereof having DNase activity.
  • the DNase can be included in the detergent composition of the invention at a level of from 0.01 to 1000 ppm, from 1 to 1000 ppm, from 10 to 1000 ppm, from 50 to 1000 ppm, from 100 to 1000 ppm, from 150 to 1000 ppm, from 200 to 1000 ppm, from 250 to 1000 ppm, from 250 to 750 ppm, or from 250 to 500 ppm based on active protein.
  • the DNase can be included in a wash liquor solution at a level of from 0.00001 to 100 ppm, from 0.00005 to 50 ppm, from 0.0001 to 50 ppm, from 0.0002 to 20 ppm, from 0.001 to 10 ppm, from 0.002 to 10 ppm, from 0.01 to 10 ppm, from 0.02 to 10 ppm, from 0.1 to 10 ppm, from 0.2 to 10 ppm, or from 0.5 to 5 ppm based on active protein.
  • Perfumes from 0.00001 to 100 ppm, from 0.00005 to 50 ppm, from 0.0001 to 50 ppm, from 0.0002 to 20 ppm, from 0.001 to 10 ppm, from 0.002 to 10 ppm, from 0.01 to 10 ppm, from 0.02 to 10 ppm, from 0.1 to 10 ppm, from 0.2 to 10 ppm, or from 0.5 to 5 ppm based on active protein.
  • perfume compound refers to a volatile fragrance compound that is suitable for use in a perfume.
  • a “perfume compound” may also be referred to by similar terms such as a “perfume component” or a “fragrance compound”.
  • fragrance includes perfume raw materials and compositions, scents and oils, e.g. essential oils.
  • perfume i.e., perfume
  • compounds such as aldehydes, ketones and esters.
  • plant and animal oils and exudates comprising complex mixtures of various chemical components are known for use as fragrances.
  • a perfume is a blend of volatile compounds with different volatilities which can bind to receptors in the nose and therefore has a smell or odor, usually a pleasant one. These compounds are also known as odorants or fragrances. Most perfumes possess molar weights of up to approximately 200 g/mol, in some cases up to about 300 g/mol. Larger molecules are not volatile enough to be perceived by the human nose.
  • the volatility of a compound describes how readily it vaporizes by way of evaporation or boiling. Perfume compounds vaporize, depending on their volatility, by evaporation at room temperature and atmospheric pressure. Volatility is often described using vapor pressure or boiling point, with a high vapor pressure or low boiling point indicating a high volatility. Although the volatility of a compound is related to its molecular weight, other factors such as structure and polarity also play a role, as does interaction between fragrance compounds.
  • top notes The most volatile fragrance compounds are referred to as top notes or head notes, whereas increasingly less volatile compounds are referred to as heart notes or middle notes, and the least volatile as base notes or back notes.
  • the top notes are responsible for the first impression of a detergent, and the heart notes represent the characteristic smell.
  • the base notes ensure the more substantial, long-lasting effect of the perfume.
  • top, heart (middle) and base notes may be grouped based in different criteria.
  • One such grouping is that of Poucher (Poucher, W. A. (1993).
  • Fragrance manufacturers and sellers provide information about their fragrance compounds such as molecular weight, vapor pressure and boiling point, and may also indicate whether individual fragrance compounds are top notes, middle notes or base notes. Such information is e.g. provided at iff.com/portfolio/products/fragrance-ingredients/online- compendium and at shop.perfumersapprentice.com.
  • top, heart and base notes may also be defined based on retention time (in minutes) in GC-MS performed using the parameters as defined in Example 2 herein.
  • top notes are defined as fragrance compounds that have a retention time in GC-MS of less than 8.76 min
  • heart notes are defined as fragrance compounds that have a retention time in GC-MS in the range of from 8.76 to 16.51 min
  • base notes are defined as fragrance compounds that have a retention time in GC-MS of more than 16.51 min.
  • the presence of a polypeptide having DNase activity in a detergent composition results in an increase in binding and/or retention of top note and/or heart note perfume compounds compared to base note compounds, and thus an increased relative perfume effect for these notes.
  • a detergent composition e.g. a laundry detergent composition or a fabric softener
  • the heart note compounds are increased relative to the base note compounds.
  • the top note and heart note compounds are increased relative to the base note compounds.
  • at least the top note compounds are increased relative to the base note compounds.
  • the presence of a polypeptide having DNase activity in a detergent composition results in an increase in binding and/or retention of top note and/or heart note perfume compounds compared to base note compounds when measured on a polyester material.
  • any given fragrance compound as being a top, heart or base note is not important. Rather, as it will be apparent from the explanation above, it is a question of how a DNase polypeptide in a detergent composition effects the overall binding and/or retention of the different groups of fragrance compounds, where such compounds are broadly classified into the three categories of top, heart and base notes.
  • the odor detection threshold of the fragrance compounds is also important for the perfume functions.
  • the odor detection threshold value is defined as the minimal concentration of a substance that can be detected by a human nose. Thus, compounds with a lower detection odor threshold are more easily detected by humans.
  • the threshold is subjective and may vary, it mainly depends on three factors, the vapor pressure, water solubility and the water/organic solvent (octanol) partition coefficient, which together account for 77% of variance in threshold values (Rodriguez et aL, 2011 , Flavour and Fragrance Journal 26: 421 -428).
  • malodors are also volatile compounds that can bind to receptors in the nose.
  • malodors are perceived as unpleasant.
  • a perfume can interfere with the perception of malodors by competing with the receptors in the nose, thereby masking the malodors.
  • fragrances do not interact with malodors, and malodors are not physically removed or chemically eliminated. Rather, perfume compositions are carefully designed to mask the anticipated malodors.
  • the duration of the “freshness” or “cleanliness” effect provided by a perfume in a detergent composition is influenced by how fragrances and malodors are retained on the washed fabric.
  • Laundry malodors can come from various sources, including human body odor as well as malodors from the environment such as kitchen odors, cigarettes, food stains, etc.
  • Another important source of malodors is from microbes present in the textile, which can metabolize the substances transferred from the human body (sweat, dead cells, sebum, etc.) and generate malodors during drying, storage or wearing (Bockmuehl et aL, 2019, Microbial Cell 6: 299-306).
  • Fiber type also plays an important role in retaining and release of odor compounds, e.g. malodor compounds may be more effectively removed from cotton than from polyester. This is partly related to the polarity (hydrophilicity) of the odor compounds and that of the textile fibers, with cotton containing mainly highly polar cellulosic fibers, while fibers of polyester and wool are relatively non-polar compared to cotton fibers.
  • polarity hydrophilicity
  • the order of compound polarity of perfume compounds from high to low is as follows: Amide > Acid > Alcohol > Ketone ⁇ Aldehyde > Ester > Alkane.
  • “invisible dirt” present on the textile also affects odor retention.
  • Used textiles often contain human secretion (e.g. sebum, keratin) and microbial soil (e.g. biofilm, DNA, carbohydrates), which may not be visible but which contribute to binding of odor compounds on the textile.
  • human secretion e.g. sebum, keratin
  • microbial soil e.g. biofilm, DNA, carbohydrates
  • Perfume compounds used in laundry detergents may be chemical compounds from any of several different classes or essential oils or other natural compounds.
  • the perfumes that may be used in the context of the present invention are not subject to any restrictions.
  • synthetic or natural odorant substance compounds of the types esters, ethers, aldehydes (fragrance aldehydes, odorant aldehydes), ketones (fragrance ketones, odorant ketones), alcohols, hydrocarbons, acids, carbonic acid esters, aromatic hydrocarbons, aliphatic hydrocarbons, saturated and/or unsaturated hydrocarbons and mixtures of these may be used as perfume compounds.
  • perfume compounds e.g. synthetic products of the ester, ether, aldehyde, ketone, alcohol, and hydrocarbon types
  • mixtures of different perfume compounds which together generate an attractive scent note.
  • Such mixtures can also contain natural perfume mixtures such as those accessible from plant sources, e.g. pine, citrus, jasmine, patchouli, rose or ylang-ylang oil.
  • Suitable perfumes of the ester type include e.g. benzyl acetate, phenoxy ethyl isobutyrate, p-tert-butyl cyclohexyl acetate, linalyl acetate, dimethyl benzyl carbinyl acetate (DMBCA), phenyl ethyl acetate, ethyl methyl phenyl glycinate, allyl cyclohexyl propionate, styrallyl propionate, benzyl salicylate, cyclohexyl salicylate, floramate, melusate and jasmacyclate.
  • DMBCA dimethyl benzyl carbinyl acetate
  • phenyl ethyl acetate ethyl methyl phenyl glycinate
  • allyl cyclohexyl propionate styrallyl propionate
  • benzyl salicylate
  • Odorant substance compounds of the hydrocarbon type include e.g. terpenes such as limonene and pinene.
  • Suitable perfumes of the ether type include e.g. benzyl ethyl ether and ambroxan.
  • Suitable perfume alcohols include e.g. 10-undecen-1 -ol, 2,6-dimethyl heptan-2-ol, 2- methyl butanol, 2-methyl pentanol, 2-phenoxy ethanol, 2-phenyl propanol, 2-tert-butyl cyclohexanol, 3,5,5-trimethyl cyclohexanol, 3-hexanol, 3-methyl-5-phenyl pentanol, 3-octanol, 1 - octen-3-ol, 3-phenyl propanol, 4-heptenol, 4-isopropyl cyclohexanol, 4-tert-butyl cyclohexanol, 6,8-dimethyl-2-nonanol, 6-nonen-1 -ol, 9-decen-1 -ol, alpha-methyl benzyl alcohol, alphaterpineol, amyl salicylate, benzyl alcohol, benz
  • Suitable perfume ketones can include all ketones that can lend a desired scent or a sensation of freshness. Mixtures of different ketones can also be used.
  • the ketone can be selected from the group consisting of buccoxime, iso-jasmone, methyl-beta-naphthyl ketone, Moschus indanone, Tonalid/Moschus plus, alpha-damascone, beta-damascone, delta- damascone, isodamascone, damascenone, damarose, methyl dihydro jasmonate, menthone, carvone, campher, fenchone, alpha-ionene, beta-ionone, dihydro-beta-ionone, gamma-methyl ionone, fleuramone, dihydro jasmone, cis-jasmone, iso-E-Super, methyl cedrenyl ketone or methyl cedrylone, aceto
  • ketones may e.g. be selected from alpha-damascone, delta-damascone, isodamascone, carvone, gamma-methyl ionone, iso-E-super, 2,4,4,7-tetramethyl-oct-6-en-3-one, benzyl acetone, beta-damascone, damascenone, methyl dihydro jasmonate, methyl cedrylone, hedione and mixtures thereof.
  • Suitable perfume aldehydes can be any aldehydes that produce a desired scent or a sensation of freshness. They may be individual aldehydes or mixtures of aldehydes. Exemplary suitable aldehydes are melonal, triplal, ligustral, adoxal, anis aldehyde, cymal, ethyl vanillin, florhydral, helional, heliotropine, hydroxy citronellal, koavone, laurin aldehyde, lyral, methyl nonyl acetaldehyde, para-tert-bucinal, phenyl acetaldehyde, undecylene aldehyde, vanillin, 2,6,10- trimethyl-9-andecenal, 3-dodecen-1 -al, alpha-n-amyl cinnamaldehyde, 4-methoxy benzaldehyde, benzaldehyde, 3-
  • Preferred aldehydes may e.g. be selected from cis/trans-3,7-dimethyl-2,6-octadien-1 -al, heliotropin, 2,4,6-trimethyl-3- cyclohexene-1 -carboxaldehyde, 2,6-nonadienal, alpha-n-amyl cinnamaldehyde, alpha-n-hexyl cinnamaldehyde, para-tert-bucinal, lyral, cymal, methyl nonyl acetaldehyde, trans-2-nonenal, lilial, trans-2-nonenal and mixtures thereof.
  • Perfume compounds may also be natural odorant mixtures such as those accessible from plant sources, e.g. pine, citrus, jasmine, patchouli, rose or ylang-ylang oil. Also suitable are muscat, sage oil, chamomile oil, clove oil, mint oil, cinnamon leaf oil, lime blossom oil, juniper berry oil, vetiver oil, olibanum (frankincense) oil, galbanum oil and labdanlum oil as well as orange blossom oil, neroli oil, orange peel oil and sandalwood oil.
  • the perfume compounds may also be essential oils, e.g.
  • angelica root oil anise oil, arnica blossom oil, basal oil, bay oil, champaca blossom oil, silver fir oil, silver fir cone oil, elemi oil, eucalyptus oil, fennel oil, spruce needle oil, geranium oil, gingergrass oil, guaiac wood oil, gurjun balsam oil, helichrysum oil, ho leaf oil, ginger oil, iris oil, cajeput oil, calmus oil, camphor oil, canaga oil, cardamom oil, cassia oil, copaiva balsam oil, coriander oil, spearmint oil, caraway oil, cumen oil, lavender oil, lemongrass oil, lime oil, mandarin oil, lemon balm oil, musk seed oil, myrrh oil, niaouli oil, origanum oil, palmarosa oil, peru balsam oil, petit grain oil, pepper oil, peppermint oil, pimento oil, rosemary oil, celery oil, spike oil, stemanis
  • fragrance ingredients may be obtained from The International Fragrance Association (IFRA), which publishes a list of all fragrance ingredients used in consumer goods (ifrafragrance.org/initiatives/transparency/ifra-transparency-list).
  • IFRA International Fragrance Association
  • a plurality of perfume compounds may be included in a detergent composition of the invention.
  • the compositions of the invention may therefore e.g. contain three or more, such as four or more, five or more, six or more or seven or more different perfume components.
  • compositions of the invention will typically contain one or more perfume components in a total amount (by weight) of from 0.0001 % to 2.5%, such as 0.001 -2%, e.g. 0.01 -1.5%, for example 0.1 -1 % percent, based on the total amount of perfume components and the total weight of the composition.
  • detergent compositions there are no limitations on the type of detergent composition in which perfumes may be incorporated. They may, for example, be included in detergent compositions that are in the form of liquids, gels, powders, granulates, tablets, pods, pouches and soap bars.
  • Perfume components may be incorporated into detergent compositions in physical forms and using methods known in the art, e.g. adding the perfume components as liquids, solid particles and/or microcapsules.
  • Cleaning components e.g. adding the perfume components as liquids, solid particles and/or microcapsules.
  • cleaning components may include, for textile care, the consideration of the type of textile to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product.
  • components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.
  • the cleaning composition may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof.
  • the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants.
  • the surfactant is typically present at a level of from about 1 % to 70% by weight, such as about 1 wt% to about 40 wt%, or about 3 wt% to about 20 wt%, or about 3 wt% to about 10 wt%.
  • the one or more surfactants are chosen based on the desired cleaning application, and may include any conventional surfactants known in the art.
  • the detergent When included therein the detergent will usually contain from about 1% to about 70% by weight of an anionic surfactant, such as from about 5 wt % to about 50 wt %, including from about 5 wt % to about 20 wt %, or from about 15 wt % to about 20 wt %, or from about 20 wt % to about 25 wt % or at least 30 wt%, at least 40 wt% or at least 50 wt% of an anionic surfactant.
  • an anionic surfactant such as from about 5 wt % to about 50 wt %, including from about 5 wt % to about 20 wt %, or from about 15 wt % to about 20 wt %, or from about 20 wt % to about 25 wt % or at least 30 wt%, at least 40 wt% or at least 50 wt% of an anionic surfactant.
  • anionic surfactants include sulfates and sulfonates, in particular, alkylbenzenesulfonates, such as linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sul
  • SDS
  • the detergent When included therein the detergent will usually contain from about 1% to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • a cationic surfactant for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.
  • ADMEAQ alkyldimethylethanolamine quat
  • CAB cetyltrimethylammonium bromide
  • DMDMAC dimethyldistearylammonium chloride
  • AQA alkoxylated quaternary ammonium
  • the detergent When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5 wt% to about 30 wt %, in particular from about 1 wt % to about 20 wt %, from about 3 wt % to about 10 wt %, such as from about 3% wt to about 5 wt %, from about 8 wt % to about 12 wt %, or from about 10 wt % to about 12 wt %.
  • a nonionic surfactant for example from about 0.5 wt% to about 30 wt %, in particular from about 1 wt % to about 20 wt %, from about 3 wt % to about 10 wt %, such as from about 3% wt to about 5 wt %, from about 8 wt % to about 12 wt %, or from about 10 wt % to about 12 wt
  • Nonlimiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a semipolar surfactant.
  • semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N- (tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, , and combinations thereof.
  • AO amine oxides
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant.
  • zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.
  • more than one surfactant is present in the cleaning composition, for example at least one anionic and at least one non-ionic surfactant.
  • the amount of all surfactant present i.e. the amount of anionic, non-ionic, zwitterionic and cationic surfactant present is preferably from about 1 wt% to 80 wt% by weight, such as about 1 wt% to 70 wt%, such as about 1 wt% to 50 wt% such as about 1 wt% to about 40 wt%, or about 5 wt% to about 40 wt%, or about 10 wt% to about 60 wt%.
  • the ratio between the surfactants present depends on the specific composition but the weight ratios may be when an anionic and non-ionic surfactant is included in the composition a weight ratio of the anionic to nonionic surfactant from; 30:1 to 10:1 , 20:1 to 1 :10, 25: 1 to 1 :2, 20:1 to 1 :5.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a polypeptide having DNase activity, wherein the cleaning component is at least one surfactant, preferably anionic and/or nonionic, preferably wherein the composition comprises from 1 to 70 wt%, preferably from 5 to 40 wt % surfactant, wherein the surfactant preferably is selected from alkylbenzenesulfonates e.g. LAS, alkyl sulfates (AS) and mixtures thereof, preferably the cleaning composition comprises at least 20 wt % alkylbenzenesulfonate surfactant.
  • the cleaning component is at least one surfactant, preferably anionic and/or nonionic, preferably wherein the composition comprises from 1 to 70 wt%, preferably from 5 to 40 wt % surfactant, wherein the surfactant preferably is selected from alkylbenzenesulfonates e.g. LAS, alkyl sulfates (AS) and
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a polypeptide having DNase activity, wherein the cleaning composition comprises at least one anionic surfactant and wherein the cleaning composition additionally comprises a nonionic surfactant, and preferably wherein the weight ratio of the anionic to nonionic surfactant is from 25: 1 to 1 :2 or from 1 .5:1 to 1 :10.
  • the cleaning composition may contain about 0-65% by weight, such as about 5% to about 50%, such as about 0.5% to about 20% of a detergent builder or co-builder, or a mixture thereof.
  • the level of builder is typically 40-65%, particularly 50-65%.
  • the builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized.
  • Nonlimiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1 -ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1 -ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl)inulin (CMI), and combinations thereof.
  • zeolites such as 2-aminoethan-1 -ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1 -ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl
  • the detergent composition may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder.
  • the detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder.
  • co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA).
  • PAA/PMA poly(acrylic acid)
  • Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid.
  • NTA 2,2’,2”-nitrilotriacetic acid
  • EDTA ethylenediaminetetraacetic acid
  • DTPA diethylenetriaminepentaacetic acid
  • IDS iminodisuccinic acid
  • EDDS ethylenediamine-N,N’-disuccinic acid
  • MGDA methylglycinediacetic acid
  • GLDA glutamic acid-N,N-diacetic acid
  • HEDP ethylenediaminetetra(methylenephosphonic acid)
  • DTMPA or DTPMPA N-(2-hydroxyethyl)iminodiacetic acid
  • ASMA aspartic acid-N-monoacetic acid
  • ASDA aspartic acid-N,N-diacetic acid
  • ASDA aspartic acid-N- monopropionic acid
  • ASMA aspartic acid-N-monoacetic acid
  • ASDA aspartic acid-N,N-diacetic acid
  • ASDA aspart
  • the cleaning composition may contain 0-30% by weight, such as about 1% to about 20%, such as about 0.01% to about 10% of a bleaching system.
  • a bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.
  • Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide— urea (1/1).
  • Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.
  • Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-a-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, e-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid
  • Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3, 5, 5-trimethylhexanoyl)oxy]benzene-1 -sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1 -sulfonate (LOBS), sodium 4- (decanoyloxy)benzene-l -sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4- (nonanoyloxy)benzene-l -sulfonate (NOBS), and/or those disclosed in WO98/17767.
  • TAED tetraacetylethylenediamine
  • ISONOBS sodium 4-[(3, 5, 5-trimethylhexanoyl)oxy]benzene-1 -sulfonate
  • ATC acetyl triethyl citrate
  • ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly.
  • acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators.
  • ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.
  • the bleaching system may also include a bleach catalyst or booster.
  • bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1 ,4,7-trimethyl-1 ,4,7-triazacyclononane (Me3-TACN) or 1 ,2,4,7-tetramethyl- 1 ,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1 ,2- diylazanylylidene-KN-methanylylidene)triphenol
  • an organic bleach catalyst or bleach booster may be used having one of the following formulae:
  • each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 1 1 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.
  • Suitable bleaching systems are described e.g. in W02007/087258, W02007/087244, W02007/087259, EP1867708 (Vitamin K) and W02007/087242.
  • Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
  • Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:
  • benzatriazoles including benzotriazole or bis-benzotriazole and substituted derivatives thereof.
  • Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or completely substituted.
  • Suitable substituents include linear or branch-chain Ci-C20- alkyl groups (e.g., C1 -C20- alkyl groups) and hydroxyl, thio, phenyl or halogen such as fluorine, chlorine, bromine and iodine.
  • metal salts and complexes chosen from the group consisting of zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cerium salts and/or complexes, the metals being in one of the oxidation states II, III, IV, V or VI.
  • suitable metal salts and/or metal complexes may be chosen from the group consisting of Mn(ll) sulphate, Mn(ll) citrate, Mn(ll) stearate, Mn(ll) acetylacetonate, K A TiF6 (e.g., K2TiF6), K A ZrF6 (e.g., K2ZrF6), CoS04, Co(NOs)2 and Ce(NOs)3, zinc salts, for example zinc sulphate, hydrozincite or zinc acetate;
  • K A TiF6 e.g., K2TiF6
  • K A ZrF6 e.g., K2ZrF6
  • CoS04 Co(NOs)2 and Ce(NOs)3
  • zinc salts for example zinc sulphate, hydrozincite or zinc acetate
  • silicates including sodium or potassium silicate, sodium disilicate, sodium metasilicate, crystalline phyllosilicate and mixtures thereof.
  • composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.
  • the cleaning composition may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope.
  • a hydrotrope Any hydrotrope known in the art for use in detergents may be utilized.
  • Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.
  • the cleaning composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized.
  • the polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties.
  • Some polymers may have more than one of the above-mentioned properties and/or more than one of the below- mentioned motifs.
  • Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone- vinylimidazole (PVPVI
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aquaion, and Sokalan® HP 165, Sokalan® HP 50 (Dispersing agent), Sokalan® HP 53 (Dispersing agent), Sokalan® HP 59 (Dispersing agent), Sokalan® HP 56 (dye transfer inhibitor), Sokalan® HP 66 K (dye transfer inhibitor) from BASF.
  • Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate.
  • exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.
  • the cleaning compositions of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light.
  • fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum.
  • Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments.
  • Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.
  • the detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent.
  • the composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and W02007/087243.
  • the cleaning compositions of the present invention can also contain dispersants.
  • powdered detergents may comprise dispersants.
  • Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
  • Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
  • the cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents.
  • Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
  • the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01 % to about 5% or even from about 0.1 % to about 3% by weight of the composition.
  • the cleaning compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agents or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 0.5%.
  • Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.
  • diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2- diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s- triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)- s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2-yl)stilbene-2,2'- disulfonate and sodium 5-(2H-naphtho[1 ,2-d][1 ,2,3]triazol-2-yl)-2-[(E)-2-phenyl
  • Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland.
  • Tinopal DMS is the disodium salt of 4,4'-bis-(2- morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate.
  • Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate.
  • fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India.
  • fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7- alkylaminocoumarins.
  • Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%.
  • the cleaning compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics.
  • the soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
  • Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure.
  • the core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference).
  • random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference).
  • Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1 -C6 mono-carboxylic acid, Cl-C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof.
  • Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da.
  • the molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1 : 1 to 1 :5, or from 1 : 1 .2 to 1 :2.
  • the average number of graft sites per ethylene oxide units can be less than 1 , or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, or from 0.2 to 0.4.
  • a suitable polyethylene glycol polymer is Sokalan HP22.
  • Suitable soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1867808 or WO 2003/040279 (both are hereby incorporated by reference).
  • Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof.
  • Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cation ically modified cellulose, zwitterionically modified cellulose, and mixtures thereof.
  • Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.
  • the cleaning compositions of the present invention may also include one or more anti- redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines.
  • CMC carboxymethylcellulose
  • PVA polyvinyl alcohol
  • PVP polyvinylpyrrolidone
  • PEG polyethyleneglycol
  • homopolymers of acrylic acid copolymers of acrylic acid and maleic acid
  • the cellulose based polymers described under soil release polymers above may also function as antiredeposition agents.
  • the cleaning compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents.
  • the rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition.
  • the rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.
  • Suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.
  • the cleaning composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized.
  • the polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties.
  • Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs.
  • Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (P
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aquaion, and Sokalan® HP 165, Sokalan® HP 50 (Dispersing agent), Sokalan® HP 53 (Dispersing agent), Sokalan® HP 59 (Dispersing agent), Sokalan® HP 56 (dye transfer inhibitor), Sokalan® HP 66 K (dye transfer inhibitor) from BASF.
  • Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate.
  • exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor. Additional enzymes
  • the cleaning composition may comprise, in addition to the at least one polypeptide having DNase activity and optionally at least one DNase, one or more additional enzymes such as one or more lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • the properties of the selected enzymes should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzymes should be present in effective amounts.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes A/S).
  • Suitable cellulases include complete cellulases or mono-component endoglucanases of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the cellulase may for example be a mono-component or a mixture of mono-component endo-1 ,4-beta- glucanase often just termed endoglucanases.
  • Suitable cellulases include a fungal cellulase from Humicola insolens (US 4,435,307) or from Trichoderma, e.g. T. reesei or T. viride. Examples of cellulases are described in EP 0 495 257. Other suitable cellulases are from Thielavia e.g.
  • Thielavia terrestris as described in WO 96/29397 or Fusarium oxysporum as described in WO 91/17244 or from Bacillus as described in, WO 02/099091 and JP 2000210081 .
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307
  • Commercially available cellulases include Carezyme®, Celluzyme®, Celluclean®, Celluclast® and Endolase®; Renozyme®; Whitezyme® (Novozymes A/S) Puradax®, Puradax HA, and Puradax EG (available from Genencor).
  • Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants.
  • the protease may be an alkaline protease, such as a serine protease or a metalloprotease.
  • a serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as a subtilisin.
  • a metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M35 families.
  • subtilases refers to a sub-group of serine proteases according to Siezen et aL, Protein Eng. 4 (1991 ) 719-737 and Siezen et aL, Protein Sci. 6 (1997) 501 -523.
  • Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus
  • detergent proteases have generally been obtained from bacteria and in particular from Bacillus.
  • Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii.
  • Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93/18140).
  • Other useful proteases are e.g. those described in WO 01/16285 and WO 02/16547.
  • trypsin-like proteases examples include the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
  • metalloproteases include the neutral metalloproteases described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015/158723 and WO 2016/075078.
  • proteases examples include the protease variants described in WO 89/06279 WO 92/19729, WO 96/34946, WO 98/201 15, WO 98/20116, WO 99/1 1768, WO 01/44452, WO 03/006602, WO 2004/003186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2014/207227, WO 2016/087617 and WO 2016/174234.
  • Preferred protease variants may, for example, comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101 A, V102I, V102Y, V102N, S104A, G116V, G1 16R, H1 18D, H1 18N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161 A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189
  • Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Bacillus lentus protease (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016/001449.
  • protease of interest is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 91/02792, and variants thereof which are described for example in WO 92/21760, WO 95/23221 , EP 1921 147, EP 1921148 and WO 2016/096711.
  • the protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004/067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 1 11 , 171 , 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO 2004/067737.
  • TY145 variants of interest are described in e.g. WO 2015/014790, WO 2015/014803, WO 2015/014804, WO 2016/097350, WO 2016/097352, WO 2016/097357 and WO 2016/097354.
  • proteases examples include:
  • variants of SEQ ID NO: 1 of WO 2016/001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D and L262E, for example a variant with the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261 W and L262E, or with the substitutions S9E, N43R, N76D, N185E, S188E, Q191 N, A194P, Q206L, Y209W, S259D and L262E, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, PrimaseTM, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In and Progress® Excel (Novozymes A/S), those sold under the tradename MaxataseTM, MaxacaiTM, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2TM, FN3TM, FN4 ex TM, Excellase®, ExcellenzTM P
  • Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H
  • strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grisea (WO10/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (WO1 1/084412), Geobacillus stearothermophilus lipase (W011/084417), lipase from Bacillus subtilis (WO1 1/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (WO12/137147).
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , WO94/25578, WO95/14783, WO95/30744, WO95/35381 , WO95/22615,
  • Preferred commercial lipase products include LipolaseTM, LipexTM; LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades). Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/1 11 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10/100028).
  • Suitable amylases may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 211 , 243, 264, 304, 305, 391 , 408, and 444.
  • amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
  • Other amylases which are suitable are hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof.
  • Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N190, M197, 1201 , A209 and Q264.
  • Most preferred variants of the hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36- 483 of SEQ ID NO: 4 are those having the substitutions:
  • amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269.
  • Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
  • Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7.
  • Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181 , 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184.
  • Most preferred amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
  • amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712.
  • Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 211 and 264.
  • amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof.
  • Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475.
  • More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 1, T165I, K178L, T182G, M201 L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183.
  • Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
  • variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.
  • amylases having SEQ ID NO: 1 of WO13184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181 , E187, N192, M199, I203, S241 , R458, T459, D460, G476 and G477.
  • More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241 QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181 .
  • Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.
  • amylases having SEQ ID NO: 1 of WO10104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21 , D97, V128 K177, R179, S180, 1181 , G182, M200, L204, E242, G477 and G478.
  • SEQ ID NO: 1 More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21 D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of 1181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.
  • suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12.
  • Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R1 18, N174; R181 , G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471 , N484.
  • Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
  • amylase variants such as those described in WO2011/098531 , WO2013/001078 and WO2013/001087.
  • amylases are DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM/EffectenzTM, Powerase, Preferenz® S1000, Preferenz® S100, Preferenz® S1 10 and Preferenz® S210 (from Genencor International Inc./DuPont).
  • a peroxidase may be an enzyme comprised by the enzyme classification EC 1 .11 .1 .7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.
  • Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
  • a peroxidase may also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1 .11 .1 .10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase may be a chloroperoxidase.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-con tai ni ng haloperoxidase.
  • the vanadate-containing haloperoxidase is combined with a source of chloride ion.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • the haloperoxidase may be derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C.
  • Oxidases include any laccase enzyme comprised by the enzyme classification EC 1 .10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1 ), an o-aminophenol oxidase (EC 1 .10.3.4), or a bilirubin oxidase (EC 1 .3.3.5).
  • Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N.
  • thermophilum Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
  • Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
  • a laccase derived from Coprinopsis or Myceliophthora is preferred; in particular a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
  • the detergent additive as well as the detergent composition may also comprise one or more microorganisms, such as one or more fungi, yeast, or bacteria.
  • the one or more microorganisms are dehydrated (for example by lyophilization) bacteria or yeast, such as a strain of Lactobacillus.
  • the microorganisms are one or more microbial spores (as opposed to vegetative cells), such as bacterial spores; or fungal spores, conidia, hypha.
  • the one or more spores are Bacillus endospores; even more preferably the one or more spores are endospores of Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus megaterium.
  • the microorganisms may be included in the detergent composition or additive in the same way as enzymes (see above).
  • the cleaning composition of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for pretreatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.
  • the present invention provides a detergent additive comprising one or more enzymes as described herein.
  • the cleaning composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.
  • Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch.
  • Preferred films are polymeric materials preferably polymers which are formed into a film or sheet.
  • Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC).
  • the level of polymer in the film for example PVA is at least about 60%.
  • Preferred average molecular weight will typically be about 20,000 to about 150,000.
  • Films can also be of blended compositions comprising hydrolytically degradable and water-soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water- soluble film.
  • the compartment for liquid components can be different in composition than compartments containing solids: US2009/0011970 A1 .
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
  • a liquid or gel detergent which is not unit dosed may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water.
  • Other types of liquids including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel.
  • An aqueous liquid or gel detergent may contain from 0-30% organic solvent.
  • a liquid or gel detergent may also be non-aqueous.
  • Non-dusting granulates may be produced e.g. as disclosed in US 4,106,991 and 4,661 ,452 and may optionally be coated by methods known in the art.
  • waxy coating materials are polyethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, di- and triglycerides of fatty acids.
  • film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
  • Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods.
  • Protected enzymes may be prepared according to the method disclosed in EP 238,216.
  • compositions of the invention may be formulated as a granule, for example as a cogranule that combines one or more enzymes. Each enzyme will then be present in more granules, securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes.
  • Methods for producing multi-enzyme co-granulates for the detergent industry are disclosed in the IP.com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013/188331 , which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than 10 wt% zeolite (anhydrous basis); and (c) less than 10 wt% phosphate salt (anhydrous basis), wherein said enzyme co-granule comprises from 10 to 98 wt% moisture sink component and the composition additionally comprises from 20 to 80 wt% detergent moisture sink component.
  • WO 2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a fabric surface comprising the steps of (i) contacting said surface with the detergent composition in aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • a multi-enzyme co-granule may comprise an enzyme of the invention and one or more enzymes selected from the group consisting of proteases, lipases, cellulases, xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases, hemicellulases, proteases, cellulases, cellobiose dehydrogenases, xylanases, phospho lipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase, amylases, nucleases, hexosaminidases and mixtures thereof.
  • An embodiment of the invention relates to an enzyme granule/particle comprising the enzyme of the invention.
  • the granule is composed of a core, and optionally one or more coatings (outer layers) surrounding the core.
  • the granule/particle size, measured as equivalent spherical diameter (volume based average particle size), of the granule is 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250-1200 pm.
  • the core may include additional materials such as fillers, fibre materials (cellulose or synthetic fibres), stabilizing agents, solubilising agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances.
  • additional materials such as fillers, fibre materials (cellulose or synthetic fibres), stabilizing agents, solubilising agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances.
  • the core may include binders, such as synthetic polymer, wax, fat, or carbohydrate.
  • the core may comprise a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend.
  • the core may consist of an inert particle with the enzyme absorbed into it, or applied onto the surface, e.g., by fluid bed coating.
  • the core may have a diameter of 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250- 1200 pm.
  • the core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheron ization, size reduction methods, drum granulation, and/or high shear granulation.
  • granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheron ization, size reduction methods, drum granulation, and/or high shear granulation.
  • the core of the enzyme granule/particle may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule.
  • the optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93/07263 and WO 97/23606.
  • the coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, 1 % or 5%.
  • the amount may be at most 100%, 70%, 50%, 40% or 30%.
  • the coating is preferably at least 0.1 pm thick, particularly at least 0.5 pm, at least 1 pm or at least 5 pm.
  • the thickness of the coating is below 100 pm.
  • the thickness of the coating is below 60 pm.
  • the total thickness of the coating is below 40 pm.
  • the coating should encapsulate the core unit by forming a substantially continuous layer.
  • a substantially continuous layer is to be understood as a coating having few or no holes, so that the core unit it is encapsulating/enclosing has few or none uncoated areas.
  • the layer or coating should be homogeneous in thickness.
  • the coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc.
  • fillers e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc.
  • a salt coating may comprise at least 60% by weight w/w of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight w/w.
  • the salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles is less than 50 pm, such as less than 10 pm or less than 5 pm.
  • the salt coating may comprise a single salt or a mixture of two or more salts.
  • the salt may be water soluble, in particular having a solubility at least 0.1 grams in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water.
  • the salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate.
  • simple organic acids e.g., 6 or less carbon atoms
  • Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminium.
  • anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate.
  • alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used.
  • the salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt e.g., anhydrate).
  • the salt coating may be as described in WO 00/01793 or WO 2006/034710.
  • the salt may be in anhydrous form, or it may be a hydrated salt, i.e. a crystalline salt hydrate with bound water of crystallization, such as described in WO 99/32595.
  • Specific examples include anhydrous sodium sulfate (Na 2 SO 4 ), anhydrous magnesium sulfate (MgSO 4 ), magnesium sulfate heptahydrate (MgSO 4 7H 2 O), zinc sulfate heptahydrate (ZnSO 4 7H 2 O), sodium phosphate dibasic heptahydrate (Na 2 HPO 4 7H 2 O), magnesium nitrate hexahydrate (Mg(NO 3 ) 2 (6H 2 O)), sodium citrate dihydrate and magnesium acetate tetrahydrate.
  • the salt is applied as a solution of the salt, e.g., using a fluid bed.
  • the present invention provides a granule comprising:
  • the granule preferably is a co-granulate comprising one or more additional enzymes, preferably wherein at least one additional enzyme is selected from proteases, amylases and cellulases.
  • the present invention provides a granule comprising:
  • the granule preferably is a co-granulate comprising one or more additional enzymes, preferably wherein at least one additional enzyme is selected from proteases, amylases and cellulases.
  • Fabric softener compositions are well-known in the art. Such compositions include at least one fabric softener component, typically selected from the group consisting of cationic softener components, silicone softener components, paraffins, waxes, dispersible polyolefins and mixtures thereof.
  • Preferred softener components include cationic surfactants, more preferably cationic surfactants of the quaternary ammonium type, for example in the form of a quaternary ammonium ester.
  • the present invention is directed to methods for using the compositions comprising a DNase as defined herein and at least one perfume compound, in particular for cleaning of laundry/textiles/fabrics, including household laundry and industrial laundry, and for hard surface cleaning, including automatic dishwashing (ADW), car washing and industrial surface cleaning.
  • a DNase as defined herein
  • at least one perfume compound in particular for cleaning of laundry/textiles/fabrics, including household laundry and industrial laundry, and for hard surface cleaning, including automatic dishwashing (ADW), car washing and industrial surface cleaning.
  • the detergent composition of the present invention may be formulated, for example, for use as a hand or machine laundry detergent composition, including as a laundry additive composition suitable for pre-treatment of stained fabrics or a rinse added to a fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing.
  • a detergent additive comprising a DNase and at least one perfume compound.
  • the invention relates to use of a DNase in a detergent composition for increasing binding of a perfume to a textile during a laundry process, wherein the detergent composition comprises at least one perfume compound.
  • the invention relates to use of a DNase in a detergent composition for increasing perfume retention on a textile after wash, wherein the detergent composition comprises at least one perfume compound. In one embodiment, the invention relates to use of a DNase for enhancing the effect of a perfume in a laundry detergent composition, wherein the detergent composition comprises at least one perfume compound.
  • the invention provides a method for increasing binding of a perfume to a textile during a laundry process, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a DNase.
  • the invention provides a method for increasing perfume retention on a textile after wash, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a DNase.
  • the invention provides a method for enhancing the effect of a perfume in a laundry detergent composition, the method comprising preparing a detergent composition comprising at least one perfume compound and a DNase.
  • the invention provides a method for preparing a detergent composition with reduced perfume content but with maintained perfume effect after wash relative to a comparable composition without DNase, the method comprising mixing at least one perfume compound, a polypeptide having DNase activity and at least one detergent component.
  • the invention provides a method for cleaning an item, wherein the item is preferably a textile, comprising the steps of: a) contacting the item with a wash liquor comprising a detergent composition as defined herein comprising an enzyme having DNase activity and at least one perfume compound, and optionally b) rinsing the item.
  • the pH of the liquid wash liquor solution is typically in the range of from about 5.5 to about 12, such as from about 7 to about 1 1 , such as from about 7 to about 10, e.g. from about 7 to about 9.
  • the wash liquor may have a temperature in the range of 5 e C to 95 e C, such as in the range of 10 e C to 80 e C, in the range of 10 e C to 70 e C, in the range of 10 e C to 60 e C, in the range of 10 e C to 50 e C, in the range of 15 e C to 40 e C or in the range of 20 e C to 30 e C.
  • DNase activity may be determined on DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which is prepared according to the manual from the supplier. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is tempered to 48°C in water bath, and 20 ml of agar is poured into petri dishes and allowed to solidify by incubation overnight at room temperature. On solidified agar plates, 5 pl of enzyme solutions are added and DNase activity is observed as colorless zones around the spotted enzyme solutions.
  • DNase Test Agar with Methyl Green BD, Franklin Lakes, NJ, USA
  • DNase activity may be determined using the DNaseAlertTM Kit (11 -02-01 -04, IDT Intergrated DNA Technologies) according to the supplier’s manual. Briefly, 95 pl DNase sample is mixed with 5 pl substrate in a microtiter plate, and fluorescence is immediately measured using a Clariostar microtiter reader from BMG Labtech (536 nm excitation, 556 nm emission).
  • Example 1 Sensory evaluation of perfume retention after wash in a liquid detergent with DNase
  • Step 1 Preparation of test items
  • test items were 100% polyester T-shirts weighing 130 g/m 2 .
  • the T-shirts were preaged before being handed out to be used for exercise by test persons.
  • the above ingredients were mixed into a homogenous material by mixing melted lanolin and sebum (melted by heating at 50°C) with the mixed dry ingredients, followed by addition of glycerol and tryptone soy broth and stirring the mixture with a magnetic stirrer at 50°C for about two hours. The mixture was then cooled to room temperature and stored at 5°C.
  • the Wascator was programmed to wash for 12 hours without a final rinse. 75 g of new detergent IEC* A was then added, and a one-hour wash program with two rinses was performed, after which the T-shirts were tumble dried.
  • the T-shirts were then handed out for use by members of either a soccer team or a running team. They were worn for at least one hour of intensive training during two separate training sessions, drying the T-shirts in between. They were then returned to the laboratory and incubated in a safety cupboard for safety reasons for three days, after which they were moved to a climate chamber for a 24h incubation at 30°C and 95% relative humidity, followed by collecting all the T-shirts in a box with a lid and letting them incubate at 30°C for another 24h. All T-shirts were sorted by smell. Those without smell were discarded, while those with intense smell could be used as test material.
  • cutouts from each were made using a 6x8 cm oval template. Cutout swatches from the left and right armpits of each T-shirt were cut into 4 pieces, resulting in a total of 8 pieces from each T-shirt. These were divided among 4 nylon stockings that were used as washing bags, such that pieces from the left and right armpit and from the front and back side of the armpit were divided into different stockings. Cutouts from 4 T- shirts were divided in this manner among 4 nylon stockings, i.e. each stocking contained a total of 8 pieces from 4 different T -shirts. The nylon stockings were sealed with a knot or a rubber band before wash and were discarded after wash.
  • the rest of the T-shirts were cut into two pieces each, with one half T-shirt being washed with DNase and the other half without DNase.
  • the nylon stockings containing the armpit samples were washed together with the half T-shirts as well as ballast consisting of 1 kg of discarded household garments (each cut in two and divided equally between the two washing machines) and 1 .5 kg of clean ballast items in the form of 5 cotton T-shirts, 1 towel and 4-6 tea towels.
  • washing was performed in a standard US top loader washing machine with the armpit samples, half T-shirts and ballast as described above, using the following wash program:
  • the main wash cycle water volume was approx. 67 liters of water with a hardness of water 6 e dH (2:1 :1 .5 Ca:Mg:NaHCO3).
  • the detergent was Arm & Hammer Oxiclean (Church & Dwight, USA), added directly to the machine in a dose of 54.8 g/wash.
  • the DNase of SEQ ID NO: 1 was added to the wash water at a concentration of 2 ppm.
  • a single T-shirt was washed in the same manner as the 2 nd wash with detergent alone, but without ballast. All items were line dried overnight after wash.
  • Swatches were transferred from the dried stockings to 60L Nalophan bags sealed at the bottom and filled with filtered air (swatches from one stocking per bag). Background samples from the 1 st wash were cut out with a similar weight as the test samples and added to 2 bags. The bags are then stored at 30°C for 2 hours, after which they are ready for the sensory evaluation.
  • the sensory evaluation was performed using a PureSniff III device from Olfasense GmbH, Germany.
  • the device has three chambers for simultaneous evaluation.
  • the first chamber contained the background sample, while the other two chambers contained the test samples washed with or without DNase in a blinded order.
  • test panel member senses (smells) first the background sample and then the two test samples.
  • the test is rated as a simple preference test in which the test person chooses the sample that he/she prefers.
  • test is repeated with the remaining 6 test samples from each wash, each time evaluating a sample washed without DNase and a sample washed with DNase in blinded order.
  • Table 1 show that overall, there was a clear preference among the panelists for the T-shirt samples that were washed using a DNase.
  • Example 2 Perfume retention on textile after wash in liquid detergent with a DNase
  • T-shirt samples which were evaluated by the panelists as described in Example 1 were further used for GC-MS analysis.
  • Headspace SPME-GC-MS analysis of fragrances from the commercial detergent on polyester T-shirts was performed using an Agilent 7890 gas chromatograph coupled to an Agilent 5977 mass spectrometry GC-MS system.
  • MS Information Acquisition Mode: Scan. Solvent Delay (minutes): 1. Scan Parameters: Start Time: 1 . Low Mass: 35. High Mass: 350. Threshold: 100. A/D Samples: 4. MSZones: MS Source: 230 e C. MS Quad: 150 e C
  • Polyester T-shirts were prepared in the same manner as described above in Example 1 .
  • they were washed with a commercial powder detergent, Gut & Gunstig (McBride, Germany), in Ell front loader machines (Miele Novotronic, Model W 1935 WTL) using tap water from Bagsvaerd, Denmark with a water hardness of about 20°dH.
  • the wash program was Cotton, Short (1 h 49 min, 1600 rpm) with a wash temperature of 30°C.
  • DNase 2 ppm of the DNase (SEQ ID NO: 1 ) was added directly to the washing machine. After wash, all items were line dried overnight, and then stored refrigerated before analysis.
  • T-shirt armpit samples and remaining half T-shirts (weight 530g) prepared as described in Example 1 were washed together with 1400g of ballast consisting of 6 used half polyester T- shirts, 5 dirty half cotton pillowcases, 3 frotte wash cloths (20x20 cm), 3 half shirts (polyester), and 2 dirty half cotton T-shirts.
  • Example 1 Three washes were performed as described in Example 1 , i.e. a blank wash with a clean T-shirt and detergent to provide a clean background sample, and washes with and without DNase.
  • the sensory evaluation was performed as in Example 1 .
  • the results of the sensory evaluation are provided in Table 3 below.
  • T-shirt samples that had been subjected to a sensory evaluated by test persons as described in Example 3 were further used for GC-MS analysis, which was performed as described in Example 2.
  • the results are provided in Table 4 below.
  • the GC-MS data in Tables 2 and 4 shows that that the fragrance intensity on polyester T-shirts was increased for a variety of different perfume compounds, and that this was the case using different detergents and different washing conditions, when the samples were washed according to the invention with a composition contained a DNase.
  • Example 5 Perfume retention on textile after rinse in fabric softeners containing a DNase
  • Step 1 Preparation of test items
  • Step 1 Preparation of test items
  • Prewash of textiles was done primarily to remove starch, carboxymethyl cellulose (CMC) and other additives from the textiles.
  • Protease Savinase® 16L, Novozymes A/S, Denmark
  • amylase Stainzyme® 12L, Novozymes A/S
  • cellulase Celluclean® ST, Novozymes A/S
  • the textiles were washed three times in 86.1 g/wash detergent W-ECE-2 (wfk Testgewebe GmbH, Germany) using water with 15°dH water hardness (3.00 mL of 0.713 mol/L CaCh, 1.50 mL of 0.357 mol/L MgCh and 0.3371 g of NaHCOs in 1 L deionized water) and containing the following enzymes:
  • the prewashed T-shirts were then cut into small round swatches with a diameter of 2 cm.
  • 47 pl of 1% (w/v) deoxyribonucleic acid (DNA) solution was added at the center of the swatch.
  • the DNA solution was made by dissolving 100 mg deoxyribonucleic acid sodium salt from salmon testes (Sigma Aldrich) in 10 ml MilliQ water in a 25 ml beaker with constant stirring for 1 h at room temperature.
  • the swatches containing the DNA solution were then dried overnight (16 h) at room temperature in a fume hood with constant air flow.
  • Model detergent A2 was used in the main wash of this experiment.
  • a wash solution of liquid model detergent A2 was prepared by weighing out the detergent and dissolving in water with a hardness of 15°dH, with the model detergent A2 dosed at 3.33 g/L.
  • Model detergent A2 contains the following ingredients:
  • Rinse solutions of the above three softeners were prepared by weighing out softeners and dissolving in water with 15°dH hardness. Dosing of the softeners was calculated according to the suggested dosage for each at standard conditions for a 4-5 kg wash load, which was 25 ml, 27 ml and 27 ml for Lenor Weichspuler Aprilfrisch, Dun-let Dream of Freshness and Bamseline Dugfrisk, respectively.
  • the dried swatches from Step 1 were washed in a Mini Launder-O-Meter (MiniLOM) wash.
  • the miniLOM assay is a small-scale version of the Launder-OMeter® (LOM).
  • LOM Launder-OMeter®
  • a miniLOM basically consists of closed test tubes being rotated in a heating cabinet for a given time and at a given temperature. Each test tube represents one small washing machine. It is mainly used in testing of detergents and enzymes at European wash conditions.
  • the glass tubes were then mounted in a Mini-Launder-O-Meter (a Stuart Tube Rotator SB3) and rotated at 30°C for 60 minutes at 30 rpm.
  • a Mini-Launder-O-Meter a Stuart Tube Rotator SB3
  • the rotator was placed at room temperature, and the wash liquor was carefully poured out of each tube. 30 ml of hard water (15° dH water) was then added to each tube. The swatches were then rinsed in the miniLOM at room temperature for 30 min at 30 rpm.
  • the rinse liquor was carefully poured out. 30 ml of rinse solution (softener dissolved in 15° dH water) was then added to each tube. Three replicates (one replicate/tube) were used for each rinse condition (softener/DNase combination). 1 .0 ppm DNase was added to the tubes, and tubes without DNase were included as controls. The swatches were then rinsed in the tubes in the miniLOM at room temperature for 30 min at 30 rpm.
  • each swatch was centrifuged in a falcon tube containing a filter (HOZELOCK K3 kaldness filters, Aquacadabra, eBay) at 4000g for 5 min to remove excess water. This plastic filter separated the excess water from the swatch after centrifuging.
  • a filter HOZELOCK K3 kaldness filters, Aquacadabra, eBay
  • the above fragrances can be grouped into different perfume notes, i.e. top, heart or base notes based on their volatility as explained above in the description. It was found that the intensity of the heart note fragrances on polyester T-shirts was increased most in two of the three softeners, compared to the top notes and base notes, when the samples were rinsed according to the invention with a softener composition contained a DNase (Tables 8 and 9). As shown in Table, 9 however, this softener also resulted in a substantial increase in the top notes that was close to the increase observed for the heart notes. The third softener (Table 10) showed the largest increase in intensities in the top notes, compared to the heart notes and base notes, when the samples were rinsed in the softener containing a DNase.
  • Freshness softener with or without DNase (SEQ ID NO: 1 )

Abstract

The invention relates to detergent compositions comprising an enzyme having DNase activity and at least one perfume compound, as well as to use of a DNase in detergent compositions comprising a perfume for improving the effect of the perfume.

Description

USE OF POLYPEPTIDES HAVING DNASE ACTIVITY
Reference to a Sequence Listing
This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference.
BACKGROUND OF THE INVENTION
Field of the invention
The present invention relates to compositions such as cleaning compositions comprising an enzyme having DNase activity and at least one perfume compound. The invention further relates to use of the detergent compositions in cleaning processes and/or for deep cleaning of organic stains, to methods of using said compositions for removal or reduction of components of organic matter, and to methods for increasing binding of a perfume to a textile, for boosting the effect of perfumes in detergent compositions, for increasing perfume retention on a textile and for producing perfume-containing compositions with a reduced amount of perfume.
Description of the Related Art
Cleaning compositions comprising one or more perfumes are well-known. Perfumes may be chemical compounds or e.g. natural oils such as essential oils and other natural compounds. The perfumes often have a double function of providing a desired scent and masking undesirable odors, which may stem from the detergent itself or from the fabric.
However, the use of perfume in laundry detergents has faced several challenges. For example, may perfume components are released very quickly, thus the “freshness” effect of perfume often does not last very long. In addition, with the increasing awareness of perfume allergy, there is a trend to use detergents containing less or no perfume. Furthermore, perfume is expensive and can represent a significant factor in the overall cost of e.g. laundry detergents.
Enzymes have been used in cleaning compositions for decades. Usually a cocktail of various enzymes is added to cleaning compositions, wherein each enzyme targets a specific substrate, e.g. amylases are active towards starch stains, proteases on protein stains and so forth. The effectiveness of these commercial enzymes provides cleaning compositions which remove much of the soiling. However, components of organic matters such as biofilm and extracellular polymeric substances (EPS) constitute a challenging type of staining due to the complex nature of such organic matter, and commercially available cleaning compositions are generally not able to effectively remove or reduce EPS and/or biofilm related stains. Textile surfaces and hard surfaces, such as dishes or the inner space of a laundry or dishwashing machine enduring a number of wash/cleaning cycles, become soiled with many different types of soiling which may be composed of proteins, grease, starch etc. Some types of stain may be associated with organic matter such as biofilm, EPS, etc. , which may be composed of different molecules such as polysaccharides, extracellular DNA (eDNA), and proteins. Some organic matter comprises an extracellular polymeric matrix, which may be sticky or gluing, which when present on textiles attracts soils and may cause redeposition or backstaining of soil, resulting in a greying of the textile. Additionally, organic matters such as biofilms often cause malodor issues as various malodor molecules can be adhered by the polysaccharides, extracellular DNA (eDNA) and proteins in the complex extracellular matrix and be slowly released to cause a noticeable malodor.
Cleaning compositions and detergents comprising enzymes having DNase activity have been described e.g. in WO 2014/08701 1 , WO 2015/155350 and WO 2017/060475. WO 201 1/163325 describes various perfume raw materials, perfume delivery systems and consumer products comprising such perfume raw materials and/or such perfume delivery systems.
The present invention is based on the surprising discovery that the use of a DNase in a detergent composition results in an enhanced effect of perfume compounds in the composition that allows for the amount of perfume to be reduced while still maintaining a freshness and cleanliness effect of the perfume on a textile washed with the detergent composition.
Summary of the Invention
The present invention relates to detergent compositions comprising an enzyme having DNase activity and at least one perfume compound, as well as to use of a polypeptide having DNase activity in detergent compositions comprising a perfume, e.g. for increasing binding of a perfume to a textile during a laundry process, for increasing perfume retention on a textile after wash, and/or for enhancing the effect of a perfume in a detergent composition.
The invention further relates to a method for increasing binding of a perfume to a textile during a laundry process, and/or for increasing perfume retention on a textile, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity.
The invention further relates to a method for enhancing the effect of a perfume in a laundry detergent composition, and/or for preparing a detergent composition with a reduced perfume content while maintaining perfume effect after wash, the method comprising preparing a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity.
The invention further relates to a method for cleaning an item, wherein the item is preferably a textile, comprising the steps of: a) contacting the item with a detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, and optionally b) rinsing the item. Overview of sequences
SEQ ID NO: 1 DNase polypeptide obtained from Aspergillus oryzae
SEQ ID NO: 2 mature DNase polypeptide obtained from Aspergillus oryzae
SEQ ID NO: 3 mature DNase polypeptide obtained from Aspergillus oryzae
SEQ ID NO: 4 motif [D/M/L][S/T]GYSR[D/N]
SEQ ID NO: 5 motif ASXNRSKG
SEQ ID NO: 6 mature DNase polypeptide obtained from Metabacillus indicus (previously known as Bacillus cibi)
SEQ ID NO 7 mature polypeptide obtained from Bacillus sp-62451
SEQ ID NO 8 mature polypeptide obtained from Bacillus horikoshii
SEQ ID NO 9 mature polypeptide obtained from Bacillus sp-62520
SEQ ID NO 10 mature polypeptide obtained from Bacillus sp-62520
SEQ ID NO 11 mature polypeptide obtained from Bacillus horikoshii
SEQ ID NO 12 mature polypeptide obtained from Bacillus horikoshii
SEQ ID NO 13 mature polypeptide obtained from Bacillus sp-16840
SEQ ID NO 14 mature polypeptide obtained from Bacillus sp-16840
SEQ ID NO 15 mature polypeptide obtained from Bacillus sp-62668
SEQ ID NO 16 mature polypeptide obtained from Bacillus sp-13395
SEQ ID NO 17 mature polypeptide obtained from Bacillus horneckia
SEQ ID NO 18 mature polypeptide obtained from Bacillus sp-11238
SEQ ID NO 19 mature polypeptide obtained from Bacillus sp-18318
SEQ ID NO 20 mature polypeptide obtained from Bacillus idriensis
SEQ ID NO 21 mature polypeptide obtained from Bacillus algicola
SEQ ID NO 22 mature polypeptide obtained from Xanthan alkaline community J
SEQ ID NO 23 mature polypeptide obtained from Bacillus vietnamensis
SEQ ID NO 24 mature polypeptide obtained from Bacillus hwajinpoensis
SEQ ID NO 25 mature polypeptide obtained from Paenibacillus mucilaginosus
SEQ ID NO 26 mature polypeptide obtained from Bacillus indicus
SEQ ID NO 27 mature polypeptide obtained from Bacillus marisflavi
SEQ ID NO 28 mature polypeptide obtained from Bacillus luciferensis
SEQ ID NO 29 mature polypeptide obtained from Bacillus marisflavi
SEQ ID NO 30 mature polypeptide obtained from Bacillus sp. SA2-6
SEQ ID NO 31 motif [V/I]PL[S/A]NAWK
SEQ ID NO 32 motif NPQL
SEQ ID NO 33 mature polypeptide obtained from Pyrenochaetopsis sp.
SEQ ID NO 34 mature polypeptide obtained from Vibrissea flavovirens
SEQ ID NO 35 mature polypeptide obtained from Setosphaeria rostrate SEQ ID NO 36 mature polypeptide obtained from Endophragmiella valdina
SEQ ID NO 37 mature polypeptide obtained from Corynespora cassiicola
SEQ ID NO 38 mature polypeptide obtained from Paraphoma sp. XZ1965
SEQ ID NO 39 mature polypeptide obtained from Monilinia fructicola
SEQ ID NO 40 mature polypeptide obtained from Curvularia lunata
SEQ ID NO 41 mature polypeptide obtained from Penicillium reticulisporum
SEQ ID NO 42 mature polypeptide obtained from Penicillium quercetorum
SEQ ID NO 43 mature polypeptide obtained from Setophaeosphaeria sp.
SEQ ID NO 44 mature polypeptide obtained from Alternaria sp. XZ2545
SEQ ID NO 45 mature polypeptide obtained from Alternaria sp.
SEQ ID NO 46 motif P[Q/E]L[W/Y]
SEQ ID NO 47 motif [K/H/E]NAW
SEQ ID NO 48 mature polypeptide obtained from Trichoderma reesei
SEQ ID NO 49 mature polypeptide obtained from Chaetomium thermophilum
SEQ ID NO 50 mature polypeptide obtained from Scytalidium thermophilum
SEQ ID NO 51 mature polypeptide obtained from Metapochonia suchlasporia
SEQ ID NO 52 mature polypeptide obtained from Daldinia fissa
SEQ ID NO 53 mature polypeptide obtained from Acremonium sp. XZ2007
SEQ ID NO 54 mature polypeptide obtained from Acremonium dichromosporum
SEQ ID NO 55 mature polypeptide obtained from Sarocladium sp. XZ2014
SEQ ID NO 56 mature polypeptide obtained from Metarhizium sp. HNA15-2
SEQ ID NO 57 mature polypeptide obtained from Acremonium sp. XZ2414
SEQ ID NO 58 mature polypeptide obtained from Isaria tenuipes
SEQ ID NO 59 mature polypeptide obtained from Scytalidium circinatum
SEQ ID NO 60 mature polypeptide obtained from Metarhizium lepidiotae
SEQ ID NO 61 mature polypeptide obtained from Morchella costata
SEQ ID NO 62 mature polypeptide obtained from Rhizoctonia solani
Definitions
As used herein, the singular forms "a", "an", and "the" are intended to include the plural forms as well, unless the context clearly indicates otherwise.
If not indicated otherwise, all references to percentages in relation to the disclosed compositions relate to wt.% relative to the total weight of the respective composition.
DNase (deoxyribonuclease): The term “DNase” means a polypeptide or an enzyme with DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. For purposes of the present invention, DNase activity is determined according to the procedure described in Assay 1 or Assay 2 herein. Biofilm: A “biofilm” is organic matter produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS). Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides. Biofilms may form on living or non-living surfaces. The microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium. Bacteria living in a biofilm usually have significantly different properties from planktonic bacteria of the same species, as the dense and protected environment of the film allows them to cooperate and interact in various ways. One benefit of this environment for the microorganisms is increased resistance to detergents and antibiotics, as the dense extracellular matrix and the outer layer of cells protect the interior of the community. The biofilm living bacteria do not lose their ability to live as planktonic cells if the biofilm matrix is compromised. On laundry, biofilm- or EPS-producing bacteria can e.g. be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis and Stenotrophomonas sp.
Clade: The term “clade” means a group of polypeptides clustered together on the basis of homologous features traced to a common ancestor. Polypeptide clades can be visualized as phylogenetic trees and a clade is a group of polypeptides that consists of a common ancestor and all its lineal descendants.
Deep cleaning: The term “deep cleaning” refers to disruption or removal of a biofilm or components of a biofilm such as polysaccharides, proteins, DNA, soil or other components present in the biofilm.
Detergent component: The term “detergent component” (or “cleaning component”) means a detergent adjunct ingredient that is different from the DNase polypeptide of this invention. The precise nature of these additional cleaning or adjunct components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used. Suitable detergent components include, but are not limited to the components described below, such as surfactants, builders and co-builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes (other than the enzymes of the invention), enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti- redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments. Detergent compositions will typically contain at least one surfactant along with additional components such as at least one builder and/or at least one bleach component. Detergent composition: The term “detergent composition” or “cleaning composition” refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles. The detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning. The term encompasses any materials/compounds selected for the particular type of detergent composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions such as liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment. In addition to containing the enzyme of the invention, the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, mannanases, nucleases or any mixture thereof), and/or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferases, hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers. In one preferred embodiment, the detergent composition is a laundry detergent composition. In another preferred embodiment, the detergent composition is a fabric softener.
Detergent enzyme: The term “detergent enzyme” as used herein refers to enzymes that are not encompassed by the term “DNase” as defined herein. The term “detergent enzyme” includes enzymes traditionally used in detergent compositions, including but not limited to proteases, amylases, lipases, mannanases, pectate lyases and cellulases. Other detergent enzymes may e.g. include carbohydrases, pectinases, arabinases, galactanases, xylanases, oxidases or peroxidases.
Expression: The term “expression” includes any step involved in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion.
Fragment: The term “fragment” means a polypeptide having one or more amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide or domain , where the fragment has DNase activity.
Host cell: The term "host cell" means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term “host cell” encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.
Isolated: The term “isolated” means a polypeptide, nucleic acid, cell, or other specified material or component that is separated from at least one other component with which it is naturally associated, including but not limited to, for example, other proteins, nucleic acids, cells, etc. An isolated polypeptide, nucleic acid, cell or other material is thus in a form that does not occur in nature.
Laundering: The term “laundering” relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention. The laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand . A “laundry process” is intended to include any steps related to laundry, whether by hand or by machine, including but not limited to pre-treatment of fabrics, washing steps using a solution containing a laundry detergent composition, and rinsing steps e.g. using a fabric softener.
Malodor: The term ’’malodor” means an odor which is not desired on clean items. One example of malodor is compounds with an unpleasant smell, which may be produced by microorganisms. Another example is unpleasant smells which can be sweat or body odor adhered to an item which has been in contact with human or animal. Another example of malodor can be the odor from spices which stick to items, for example curry or other spices which smell strongly.
Mature polypeptide: The term “mature polypeptide” means a polypeptide in its mature form following N-terminal processing (e.g., removal of signal peptide). It is known in the art that a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C- terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide. Mature polypeptides of the invention may therefore have slight differences at the N- and/or C-terminal due to such differentiated expression by the host cell, while still having the same enzyme activity. A mature polypeptide having one or more amino acids absent from the N- and/or C-terminal may be considered to be a “fragment” of the full-length polypeptide. Similarly, a mature polypeptide having one or more additional amino acids at the N- and/or C-terminal due to differentiated expression may be considered to be an “extended” polypeptide.
Perfume effect: The term “perfume effect” in the context of the present invention is related to the human perception of perfume on washed clothes. The perfume effect of a polypeptide of the invention having DNase activity can be analyzed e.g. by means of a sensory evaluation such as that described in Example 1 . The perfume effect can alternatively be measured by GC-MS analysis and expressed quantitatively as a “fragrance intensity” e.g. as described in Examples 2 and 3. An increased perfume effect can thus be expressed as an increased fragrance intensity, such that washing an item with a DNase polypeptide according to the invention results in an increase in fragrance intensity compared to washing the item under the same conditions but without the DNase polypeptide.
Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”. For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:
(Identical Residues x 100)/(Length of Alignment - Total Number of Gaps in Alignment)
Textile: The term “textile” means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles), and is intended to include the term “fabric” as well. The textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and towelling. The textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose/rayon, cellulose acetate fibers (tricell), lyocell or blends thereof. The textile or fabric may also be non -cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non -cellulose based fibers. Examples of blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing fiber (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fiber, lyocell). Fabric may be conventional washable laundry, for example stained household laundry. When the term fabric or garment is used it is intended to include the broader term textiles as well.
Variant: The term “variant” means a polypeptide having DNase activity comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
Wash cycle: The term “wash cycle” is defined herein as a washing operation wherein textiles are immersed in a wash liquor, mechanical action of some kind is applied to the textile in order to release stains and to facilitate flow of wash liquor in and out of the textile, and finally the superfluous wash liquor is removed. After one or more wash cycles, the textile is generally rinsed and dried.
Wash liquor: The term “wash liquor” is intended to mean the solution or mixture of water and detergents, in particular a detergent composition of the invention, used for laundering textiles, or for hard surface cleaning or dishwashing. The term is also intended to include e.g. rinse solutions comprising a fabric softener comprising a DNase polypeptide used for rinsing textiles.
Nomenclature
For purposes of the present invention, the nomenclature [E/Q] or [EQ] means that the amino acid at this position may be a glutamic acid (Glu, E) or a glutamine (Gin, Q). Likewise, the nomenclature [V/G/A/l] or [VGAI] means that the amino acid at this position may be a valine (Vai, V), glycine (Gly, G), alanine (Ala, A) or isoleucine (lie, I), and so forth for other combinations as described herein. Unless otherwise limited further, the amino acid X is defined such that it may be any of the 20 natural amino acids.
Substitutions are typically indicated with the original amino acid, the position number, and the replacement amino acid. For example, A226V indicates that the original alanine residue in position 226 has been replaced by a valine residue.
Deletions are indicated with an asterisk (*). For example, G184* indicates that the original glycine residue in position 184 has been deleted.
Insertions are indicated by listing the original amino acid, the position number, the original amino acid and the inserted amino acid. For example, S97SD indicates that an aspartic acid residue has been inserted after the serine residue in position 97.
Detailed Description of the Invention
The inventors have surprisingly found that enzymes having DNase activity act synergistically with volatile perfume compounds, resulting in an enhanced binding of perfume compounds to textiles washed with a detergent composition comprise a DNase and one or more perfume compounds. As a result of the increased retention of perfume compounds by the textiles, an enhanced perfume effect is obtained, allowing the amount of perfume in such detergent compositions to be reduced while still maintaining the desired perfume effect.
Volatile perfume compounds are often added to detergent compositions, e.g. laundry detergents or fabric softeners, to mask malodors and to provide a fresh and clean scent in the washed items, e.g. textiles. These malodors may come from various sources. One example is buildup of organic matter such as sebum, body soils, cell debris, biofilm, EPS etc. It has previously been shown that polypeptides having DNase activity can be used for preventing or removing biofilm on items such as textiles or fabric; see e.g. WO 2015/155350, WO 2017/060475 and Morales-Garcia et al, J Surfact Deterg (2020) DOI 10.1002/jsde.12398. Polypeptides having DNase activity have also been shown to be able to reduce malodor in washed textiles. However, there is no suggestion in the art that there might actually be a synergistic effect between polypeptides having DNase activity and perfume compounds present in detergent compositions. While perfumes and the associated fresh and clean scent are often desired by consumers in detergent compositions such as laundry detergents, there are as noted above disadvantages to the use of perfumes, including the high cost of perfume compounds as well as the risk of allergy.
The present invention addresses these challenges by providing detergent compositions comprising polypeptides with DNase activity that have been found to have synergistic effects with perfume compounds, and which can thereby reduce the need for perfume addition to detergent compositions, in particular laundry detergent compositions.
Thus, one embodiment of the invention relates to a detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, where the amount of perfume is reduced compared to a comparable detergent composition without a DNase. It will be understood that such compositions will have a perfume effect corresponding to that of a comparable detergent composition without the DNase and with a greater amount of perfume. This may allow the amount of perfume to be reduced to e.g. no more than 90%, such as no more than 80% or even lower, e.g. no more than 70% or no more than 60%, relative to the comparable composition without a DNase, with substantially the same perfume effect. This may be assessed e.g. using a sensory evaluation such as that described in Example 1 or quantitatively by GC-MS analysis e.g. as described in Example 2.
The invention thus provides a detergent composition comprising a DNase and at least one perfume compound, wherein the composition has an increased perfume effect relative to a comparable detergent composition without a DNase.
In a preferred embodiment, the detergent composition is a laundry detergent composition, wherein the composition provides an increased perfume retention on a textile.
In this embodiment, the invention thus provides a laundry detergent composition comprising a DNase and at least one perfume compound, wherein the composition has increased perfume retention on a textile after wash relative to a comparable detergent composition without a DNase.
In another preferred embodiment, the detergent composition is a fabric softener composition, wherein the composition provides an increased perfume retention on a textile.
In this embodiment, the invention thus provides a fabric softener composition comprising a DNase and at least one perfume compound, wherein the composition has increased perfume retention on a textile after rinse relative to a comparable fabric softener composition without a DNase. In another embodiment, the detergent composition may be for cleaning of hard surfaces, for example for dishwashing, or for cleaning hard surfaces such as those found in kitchens and bathrooms.
Enzyme having DNase activity (DNase)
The DNase in the detergent compositions, uses and methods of the present invention is a nuclease polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA. The terms “DNase” and “polypeptide with/having DNase activity” may be used interchangeably herein.
Preferably, the DNase is selected from any of the enzyme classes E.C. 3.1.21 .X, where X = 1 , 2, 3, 4, 5, 6, 7, 8 or 9, e.g. Deoxyribonuclease I, Deoxyribonuclease IV, Type I site-specific deoxyribonuclease, Type II site-specific deoxyribonuclease, Type III site-specific deoxyribonuclease, CC-preferring endo-deoxyribonuclease, Deoxyribonuclease V, T(4) deoxyribonuclease II, T(4) deoxyribonuclease IV or E.C. 3.1.22.Y where Y = 1 , 2, 4 or 5, e.g. Deoxyribonuclease II, Aspergillus deoxyribonuclease K(1 ), Crossover junction endo- deoxyribonuclease, or Deoxyribonuclease X.
Preferably, the DNase activity is obtained from a microorganism, and the DNase is a microbial enzyme. The DNase is more preferably of fungal or bacterial origin.
The polypeptide having DNase activity may for example be a fungal DNase obtained from Aspergillus, for example from Aspergillus oryzae.
Suitable bacterial DNases may, for example, be obtained from species of Bacillus and related genera (cf. Patel and Gupta, Int. J. Syst. Evol. Microbiol. 2020; 70:406-438, who proposed six new Bacillaceae genera from species formerly classified as belonging to the genus Bacillus), e.g. from Bacillus, Cytobacillus, Metabacillus, Alkalihalobacillus, Rossellomorea or Mesobacillus. Examples of species from which DNases may be obtained include Bacillus licheniformis, Bacillus subtilis, Bacillus horikoshii, Cytobacillus horneckiae, Metabacillus indicus, Alkalihalobacillus algicola, Rossellomorea vietnamensis, Alkalihalobacillus hwajinpoensis, Metabacillus indicus, Mesobacillus campisalis, Bacillus idriensis, Bacillus algicola, Bacillus marisflavi and Bacillus luciferensis. Preferred bacterial DNases include those obtained from Metabacillus indicus (previously known as Bacillus cibi) and variants thereof.
The DNase may also be obtained from any of the following: Pyrenochaetopsis sp., Vibrissea flavovirens, Setosphaeria rostrate, Endophragmiella valdina, Corynespora cassiicola, Paraphoma sp., Mon i Unia fructicola, Curvularia lunata, Penicillium reticulisporum, Penicillium quercetorum, Setophaeosphaeria sp., Alternaria, Alternaria sp., Trichoderma reesei, Chaetomium thermophilum, Scytalidium thermophilum, Metapochonia suchlasporia, Daldinia fissa, Acremonium sp., Acremonium dichromosporum, Sarocladium sp., Metarhizium sp. HNA 15-2, Isaria tenuipes Scytalidium circinatum, Metarhizium lepidiotae, Thermobispora bispora, Sporormia fimetaria, Pycnidiophora cf. dispera, Clavicipitaceae sp., Westerdykella sp., Humicolopsis cephalosporioides, Neosartorya massa, Roussoella intermedia, Pleosporales, Phaeosphaeria or Didymosphaeria futilis.
In some embodiments, the polypeptides having DNase activity are polypeptides comprising the PFAM domain DUF1524 ((pfam.xfam.org/), “The Pfam protein families database: towards a more sustainable future”, R.D. Finn, et.al. Nucleic Acids Research (2016) Database Issue 44:D279-D285”). The DUF1524 domain contains a conserved HXXP sequence (where H is the amino acid histidine, P is the amino acid proline, and X is any amino acid motif) commonly found in nucleases (M.A. Machnicka, et al. Phylogenomics and sequence-structure-function relationships in the GmrSD family of Type IV restriction enzymes, BMC Bioinformatics, 2015, 16, 336). DUF stands for domain of unknown function, and polypeptide families comprising, e.g., DUF have been collected in the Pfam database, which provides sequence alignments and hidden Markov models that define the collected protein domains.
Thus, in some embodiments the polypeptides having DNase activity in the composition of the invention comprise the DUF1524 domain. For further information on DNases comprising the DUF1524 domain, see WO 2017/060475, which is hereby incorporated by reference.
In some embodiments, the DNase is a NUC1 or NUC1_A DNase. A NUC1 DNase is a DNase comprising a domain termed NUC1 , and polypeptides with this domain are in addition to having DNase activity characterized by comprising certain motifs. Similarly, a NUC1 sub-domain had been identified, termed the NUC1_A domain, which also is characterized by comprising certain motifs. The NUC1 and NUC1_A DNases are described in WO 2017/060475 and WO 2018/184873, which are hereby incorporated by reference.
The preparation of the polypeptide having DNase activity as described herein can e.g. be performed as described in WO 2017/059802 (incorporated herein by reference), in particular in the sections Nucleic Acid Construct, Expression Vectors, Host Cells, Methods of Production and Fermentation Broth Formulations. See also WO 2015/155350, WO 2017/060475, WO 2017/060505, WO 2017/064269 and WO 2018/177936, the contents of which are incorporated herein by reference.
In one embodiment, the polypeptide having DNase activity is a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 , or a fragment thereof having DNase activity.
It is known in the art that a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C-terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.
In the context of the polypeptide having SEQ ID NO: 1 , the N-terminal amino acid portion, e.g. the 15 or 17 N-terminal amino acid residues, may be a propeptide sequence. Thus, in one embodiment, the mature polypeptide is a fragment of SEQ ID NO: 1 comprising 206 amino acid residues, corresponding to amino acids 16 to 221 of SEQ ID NO: 1 (shown as SEQ ID NO: 2). In a similar embodiment, the mature polypeptide is a fragment of SEQ ID NO: 1 comprising 204 amino acid residues, corresponding to amino acids 18 to 221 of SEQ ID NO: 1 (shown as SEQ ID NO: 3). The polypeptide having DNase activity may thus be a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the mature polypeptide of SEQ ID NO: 2 or SEQ ID NO: 3.
A polypeptide having DNase activity and at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 , or a fragment thereof having DNase activity, e.g. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 2 or SEQ ID NO: 3, may be a variant having one or more alterations, e.g. substitutions, compared to SEQ ID NO: 1 . Polypeptide variants may be engineered using protein engineering methods known in the art to produce a polypeptide having one or more improved properties compared to the parent polypeptide, for example improved detergent stability and/or wash performance, e.g. an improved deep cleaning effect.
A variant of the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 may, for example, include any of the alterations disclosed in WO 2017/064269 (incorporated herein by reference). In some embodiments, the polypeptide may thus be a variant of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 having DNase activity and comprising a substitution at one or more positions corresponding to positions 4, 17, 19, 36, 38, 39, 40, 41 , 45, 51 , 53, 54, 55, 57, 64, 66, 67, 68, 69, 70, 71 , 72, 74, 75, 77, 82, 83, 84, 85, 86, 88, 91 , 99, 101 , 105, 106, 115, 1 16, 135, 136, 138, 139, 140, 141 , 151 , 152, 153, 154, 162, 163, 164, 166, 168, 169, 173, 182, 183, 184, 185, 186, 189, 212 and 215 of SEQ ID NO: 1 , wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 of at least 80%, e.g. at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99%.
A DNase variant of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3 may e.g. comprise one or more substitutions selected from the group consisting of N4E, L17E, T19A, T19G, T19I, K36P, Q38P, S39V, S39R, A40P, A40H, L41 T, L41 H, V45H, L51 G, K53T, K53P, G54P, A55P, N57H, E64A, E64Q, E64R, E64T, E64I, E64S, T66H, K67A, K67T, N68V, N68P, N68I, N68H, S69A, S69D, S69E, S69K, S69L, S69W, S69Y, S69Q, N70T, N70H, N70G, R71 T, D72E, S74H, S74G, G75I, N77T, K82P, K82I, D83T, D83P, D83I, D83H, D83G, P84H, Q85T, Q85P, Q85H, K86T, K86P, K86H, G88P, G88H, A91 P, W99T, A101W, K105E, K105N, K105T, K105D, S106T, S115T, L116I, Q135L, G136L, V138I, V138L, V138P, V138Q, L139A, N140R, N140L, N140A, G141 L, F151 R, D152Y, D152L, D152I, D152A, P153E, S154R, T162R, W163E, F164R, I166Y, I166R, K168N, F169R, F169E, A173I, A173R, A173T, S182R, N183E, D184I, K185Y, S186I, D189G, D189H, K212G, K212P and K215I, wherein position numbers correspond to the positions of SEQ ID NO 1.
In one aspect, the polypeptide having DNase activity belongs to the GYS-clade and comprises one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5).
In one embodiment of this aspect, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 6, or a fragment thereof having DNase activity. In this embodiment, the polypeptide having DNase activity may be a variant having one or more alterations, e.g. substitutions, compared to SEQ ID NO: 6.
A variant of the polypeptide of SEQ ID NO: 6 may, for example, include any of the alterations disclosed in WO 2018/01 1277 (incorporated herein by reference). In some embodiments, the polypeptide thus may be a variant of SEQ ID NO: 6 having DNase activity and comprising a substitution at one or more positions corresponding to positions 1 , 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 16, 17, 19, 21 , 22, 24, 25, 27, 28, 29, 30, 32, 38, 39, 40, 42, 49, 51 , 52, 55, 56, 57, 58, 59, 61 , 63, 65, 68, 76, 77, 78, 79, 80, 82, 83, 92, 93, 94, 99, 101 , 102, 104, 105, 107, 109, 1 12, 116, 125, 126, 127, 130, 132, 135, 138, 139, 143, 144, 145, 147, 149, 152, 156, 157, 159, 160, 161 , 162, 164, 166, 167, 168, 170, 171 , 172, 173, 174, 175, 176, 177, 178, 179, 181 and 182 of SEQ ID NO: 6, wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 6 of at least 80%, e.g. at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99%.
A DNase variant of SEQ ID NO: 6 may e.g. comprise one or more substitutions selected from the group consisting of T1 I, T1 L, T1 V, T1 F, T1 Y, T1 M, T1 E, G4N, T5F, T5C, P6V, P6G, S7D, S7T, K8V, S9K, S9Q, S9V, S9L, S9F, S9P, S9R, A10D, A10M, A10I, A10Q, A10T, A10V, A10L, A10K, Q12S, Q12V, Q12E, S13D, S13Y, S13T, S13Q, S13F, S13R, S13V, S13N, S13H, S13M, S13W, S13K, S13L, S13E, Q14M, Q14R, N16S, A17C, A17V, A17E, A17T, A17S, T19K, T19N, T19L, T19S, T19I, T19V, K21 Q, K21 E, K21 M, T22P, T22A, T22V, T22D, T22R, T22K, T22M, T22E, T22H, T22L, T22W, T22F, T22C, T22S, T22I, G24Y, S25P, S25T, S27N, S27I, S27M, S27D, S27T, S27V, S27F, S27A, S27C, S27L, S27E, G28L, Y29W, S30K, S30D, S30H, S30T, D32Q, I38V, I38M, S39A, S39P, S39Y, S39H, S39E, S39N, S39M, S39D, Q40V, S42G, S42C, S42D, S42L, S42M, S42F, S42N, S42W, V49R, L511, K52I, K52Q, K52H, A55S, D56I, D56L, D56T, S57W, S57Y, S57F, S57H, S57C, S57P, S57V, S57R, S57T, Y58A, Y58T, S59C, S59T, S59L, S59Q, S59V, S59K, S59R, S59M, S59I, S59H, N61 D, P63A, T65L, T65I, T65V, T65R, T65K, S68V, S68I, S68W, S68K, S68Y, S68H, S68C, S68T, S68L, V76G, V76L, V76C, V76K, V76H, V76E, V76A, V76Y, V76N, V76M, V76R, V76I, V76F, T77N, T77Y, T77W, T77R, F78L, F78I, F78H, F78V, F78Y, F78C, T79G, T79R, N80K, N80S, S82L, S82E, S82K, S82R, S82H, D83C, D83F, D83L, L92T, A93G, E94N, G99S, S101 D, S101A, S102M, S102L, S102V, S102A, S102K, S102T, S102R, T104S, T104P, T104A, T105V, T105I, K107L, K107C, K107R, K107H, K107S, K107M, K107E, K107A, K107Q, K107D, Q109K, Q109R, Q109S, A112S, S116D, S116R, S116Q, S116H, S116V, S116A, S116E, S116K, A125K, S126I, S126E, S126A, S126C, T127C, T127V, T127S, S130E, G132R, D135R, T138Q, W139R, R143E, R143K, S144Q, S144H, S144A, S144L, S144P, S144E, S144K, G145V, G145E, G145D, G145A, A147H, A147R, A147K, A147Q, A147W, A147N, A147S, G149S, K152H, K152R, S156C, S156G, S156K, S156R, S156T, S156A, T157S, Y159H, Y159F, K160R, K160V, W161 L, W161Y, G162Q, G162N, G162D, G162M, G162R, G162A, G162S, G162E, G162L, G162K, G162V, G162H, S164R, S1 64H, S164N, S164T, Q166D, S167M, S167L, S167F, S167W, S167E, S167A, S167Y, S167H, S167C, S167I, S167Q, S167V, S167T, S168V, S168E, S168D, S168L, K170S, K170L, K170F, K170R, T171 D, T171 E, T171 N, T171A, T171S, T171 C, A172G, A172S, L173T, L173A, L173V, Q174L, G175D, G175E, G175N, G175R, G175S, M176H, L177I, N178D, N178E, N178T, N178S, N178A, S179E, S181 R, S181 E, S181 D, S181 I, S181 F, S181 H, S181W, S181 L, S181 M, S181Y, S181Q, S181 V, S181 G, S181 A, Y182M, Y182C, Y182K, Y182G, Y182A, Y182S, Y182V, Y182D, Y182Q, Y182F, Y182L, Y182N, Y182I, Y182E, Y182T and Y182W compared to the polypeptide shown in SEQ ID NO: 6.
In a further embodiments, the polypeptide having DNase activity may be a DNase variant which compared to the DNase of SEQ ID NO: 6 comprises two or more substitutions selected from the group consisting of: T1 1, T1 L, T1 V, S13Y, T22P, S25P, S27L, S39P, S42G, S42A, S42T, S57W, S57Y, S57F, S59V, S59I, S59L, V76L, V76I, Q109R, S1 16D, S116E, T127V, T127I, T127L, S144P, A147H, S167L, S167I, S167V, G175D and G175E, wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 6 of at least 80%, e.g. at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99%. DNase variants comprising such alterations are disclosed in WO 2019/081724 (incorporated herein by reference).
In still further embodiments, the polypeptide having DNase activity may be a DNase variant which compared to a DNase of SEQ ID NO: 6 comprises at least one substitution selected from the group consisting of: G4K, S7G, K8R, S9I, N16G, S27K, S27R, D32F, D32I, D32L, D32R, D32V, L33H ,L33R, L33K, L33V, L33Y, S39C, G41 P, S42H, D45E, Q48D, N61 E, T65M, T65W, S66R ,S66M, S66W, S66Y, S66V, F78L, P91 L, S101 N, S106L, S106R, S106H, Q109E, A1 12E, T127P, S130A, S130Y, T138D, Q140V, Q140G, A147P, C148A, W154Y, T157V, Y159A, Y159R, G162C, Q174N, L177Y, S179L and C180A, wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 6 of at least 80%, e.g. at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99%. DNase variants comprising such alterations are disclosed in WO 2019/081721 (incorporated herein by reference).
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 7, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 8, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 9, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 10, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 11 , or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 2, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 13, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 14, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 135, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 6, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 7, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 8, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 9, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: , or a fragment thereof having DNase activity. In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 21 , or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 22, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 23, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 24, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 25, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 26, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 27, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 28, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 29, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 30, or a fragment thereof having DNase activity.
In one aspect, the polypeptide having DNase activity belongs to the NAWK clade and comprises one or both of the motifs [V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32).
In one embodiment of this aspect, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 33, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 34, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 35, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 36, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 37, or a fragment thereof having DNase activity. In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 38, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 39, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 40, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 41 , or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 42, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 43, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 44, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 45, or a fragment thereof having DNase activity.
In one aspect, the polypeptide having DNase activity belongs to the KNAW clade and comprises one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47).
In one embodiment of this aspect, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 48, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 49, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 50, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 51 , or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 52, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 53, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 54, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 55, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 56, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 57, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 58, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 59, or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 60, or a fragment thereof having DNase activity.
In further aspects, the DNase used in the present invention may be any of those that are disclosed in WO 2018/177203, WO 2018/177936 or WO 2018/177938, the contents of which are incorporated herein by reference. For example, the DNase may be the mature polypeptide obtained from Morchella costata disclosed as SEQ ID NO: 12 in WO 2018/177203 (SEQ ID NO: 61 herein), or a variant thereof; or a mature polypeptide obtained from Rhizoctonia solani disclosed in WO 2018/177938, such as the polypeptide of SEQ ID NO: 33, 36, 39, 42, 45, 48 or 51 therein, or a variant thereof, for example SEQ ID NO: 45 disclosed in WO 2018/177938 (SEQ ID NO: 62 herein), or a variant thereof.
Thus, in another embodiment, the polypeptide having DNase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 61 , or a fragment thereof having DNase activity.
In another embodiment, the polypeptide having DNase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 62, or a fragment thereof having DNase activity.
The DNase can be included in the detergent composition of the invention at a level of from 0.01 to 1000 ppm, from 1 to 1000 ppm, from 10 to 1000 ppm, from 50 to 1000 ppm, from 100 to 1000 ppm, from 150 to 1000 ppm, from 200 to 1000 ppm, from 250 to 1000 ppm, from 250 to 750 ppm, or from 250 to 500 ppm based on active protein.
The DNase can be included in a wash liquor solution at a level of from 0.00001 to 100 ppm, from 0.00005 to 50 ppm, from 0.0001 to 50 ppm, from 0.0002 to 20 ppm, from 0.001 to 10 ppm, from 0.002 to 10 ppm, from 0.01 to 10 ppm, from 0.02 to 10 ppm, from 0.1 to 10 ppm, from 0.2 to 10 ppm, or from 0.5 to 5 ppm based on active protein. Perfumes
The term “perfume compound” refers to a volatile fragrance compound that is suitable for use in a perfume. A “perfume compound” may also be referred to by similar terms such as a “perfume component” or a “fragrance compound”.
The term "perfume" includes perfume raw materials and compositions, scents and oils, e.g. essential oils. A wide variety of chemicals are known for fragrance (i.e., perfume) uses, including compounds such as aldehydes, ketones and esters. Also naturally occurring plant and animal oils and exudates comprising complex mixtures of various chemical components are known for use as fragrances.
A perfume is a blend of volatile compounds with different volatilities which can bind to receptors in the nose and therefore has a smell or odor, usually a pleasant one. These compounds are also known as odorants or fragrances. Most perfumes possess molar weights of up to approximately 200 g/mol, in some cases up to about 300 g/mol. Larger molecules are not volatile enough to be perceived by the human nose.
The volatility of a compound describes how readily it vaporizes by way of evaporation or boiling. Perfume compounds vaporize, depending on their volatility, by evaporation at room temperature and atmospheric pressure. Volatility is often described using vapor pressure or boiling point, with a high vapor pressure or low boiling point indicating a high volatility. Although the volatility of a compound is related to its molecular weight, other factors such as structure and polarity also play a role, as does interaction between fragrance compounds.
The most volatile fragrance compounds are referred to as top notes or head notes, whereas increasingly less volatile compounds are referred to as heart notes or middle notes, and the least volatile as base notes or back notes. The top notes are responsible for the first impression of a detergent, and the heart notes represent the characteristic smell. The base notes ensure the more substantial, long-lasting effect of the perfume.
The top, heart (middle) and base notes may be grouped based in different criteria. One such grouping is that of Poucher (Poucher, W. A. (1993). Poucher's Perfumes, Cosmetics and Soaps, Vol. 2 (Ninth ed.), Chapman & Hall, page 55). Poucher classified fragrance compounds according to an evaporation coefficient, with top notes having a coefficient of from 1 to 14, middle notes having a coefficient of from 15 to 60, and base notes having a coefficient of from 61 to 100.
Fragrance manufacturers and sellers provide information about their fragrance compounds such as molecular weight, vapor pressure and boiling point, and may also indicate whether individual fragrance compounds are top notes, middle notes or base notes. Such information is e.g. provided at iff.com/portfolio/products/fragrance-ingredients/online- compendium and at shop.perfumersapprentice.com.
For purposes of the present invention, top, heart and base notes may also be defined based on retention time (in minutes) in GC-MS performed using the parameters as defined in Example 2 herein. Using this definition, top notes are defined as fragrance compounds that have a retention time in GC-MS of less than 8.76 min, heart notes are defined as fragrance compounds that have a retention time in GC-MS in the range of from 8.76 to 16.51 min, and base notes are defined as fragrance compounds that have a retention time in GC-MS of more than 16.51 min.
In one embodiment of the invention, the presence of a polypeptide having DNase activity in a detergent composition, e.g. a laundry detergent composition or a fabric softener, results in an increase in binding and/or retention of top note and/or heart note perfume compounds compared to base note compounds, and thus an increased relative perfume effect for these notes. In one particular embodiment, at least the heart note compounds are increased relative to the base note compounds. In another particular embodiment, the top note and heart note compounds are increased relative to the base note compounds. In a further particular embodiment, at least the top note compounds are increased relative to the base note compounds.
In an embodiment, the presence of a polypeptide having DNase activity in a detergent composition, e.g. a laundry detergent composition or a fabric softener, results in an increase in binding and/or retention of top note and/or heart note perfume compounds compared to base note compounds when measured on a polyester material.
It should be noted that in the context of the invention, the precise classification of any given fragrance compound as being a top, heart or base note is not important. Rather, as it will be apparent from the explanation above, it is a question of how a DNase polypeptide in a detergent composition effects the overall binding and/or retention of the different groups of fragrance compounds, where such compounds are broadly classified into the three categories of top, heart and base notes.
Besides volatility, the odor detection threshold of the fragrance compounds is also important for the perfume functions. The odor detection threshold value is defined as the minimal concentration of a substance that can be detected by a human nose. Thus, compounds with a lower detection odor threshold are more easily detected by humans. Although the threshold is subjective and may vary, it mainly depends on three factors, the vapor pressure, water solubility and the water/organic solvent (octanol) partition coefficient, which together account for 77% of variance in threshold values (Rodriguez et aL, 2011 , Flavour and Fragrance Journal 26: 421 -428).
Just like fragrances, malodors are also volatile compounds that can bind to receptors in the nose. However, in contrast to fragrances used in perfume, malodors are perceived as unpleasant. A perfume can interfere with the perception of malodors by competing with the receptors in the nose, thereby masking the malodors. In another words, fragrances do not interact with malodors, and malodors are not physically removed or chemically eliminated. Rather, perfume compositions are carefully designed to mask the anticipated malodors.
The duration of the “freshness” or “cleanliness” effect provided by a perfume in a detergent composition is influenced by how fragrances and malodors are retained on the washed fabric. Laundry malodors can come from various sources, including human body odor as well as malodors from the environment such as kitchen odors, cigarettes, food stains, etc. Another important source of malodors is from microbes present in the textile, which can metabolize the substances transferred from the human body (sweat, dead cells, sebum, etc.) and generate malodors during drying, storage or wearing (Bockmuehl et aL, 2019, Microbial Cell 6: 299-306).
Fiber type also plays an important role in retaining and release of odor compounds, e.g. malodor compounds may be more effectively removed from cotton than from polyester. This is partly related to the polarity (hydrophilicity) of the odor compounds and that of the textile fibers, with cotton containing mainly highly polar cellulosic fibers, while fibers of polyester and wool are relatively non-polar compared to cotton fibers. In general, the order of compound polarity of perfume compounds from high to low is as follows: Amide > Acid > Alcohol > Ketone ~ Aldehyde > Ester > Alkane.
When some typical laundry malodor compounds were added to cotton or polyester, they were effectively removed from cotton, while they strongly adhered to the more hydrophobic polyester after wash. The strong association of odorants with the polyester fibers during wash was found to contribute to a more complex odor profile in polyester than in cotton (Munk et aL, 2001 , Journal of Surfactants and Detergents 4: 385-394).
In addition, “invisible dirt” present on the textile also affects odor retention. Used textiles often contain human secretion (e.g. sebum, keratin) and microbial soil (e.g. biofilm, DNA, carbohydrates), which may not be visible but which contribute to binding of odor compounds on the textile.
Perfume compounds used in laundry detergents may be chemical compounds from any of several different classes or essential oils or other natural compounds. The perfumes that may be used in the context of the present invention are not subject to any restrictions. Thus, in particular synthetic or natural odorant substance compounds of the types esters, ethers, aldehydes (fragrance aldehydes, odorant aldehydes), ketones (fragrance ketones, odorant ketones), alcohols, hydrocarbons, acids, carbonic acid esters, aromatic hydrocarbons, aliphatic hydrocarbons, saturated and/or unsaturated hydrocarbons and mixtures of these may be used as perfume compounds.
Individual perfume compounds, e.g. synthetic products of the ester, ether, aldehyde, ketone, alcohol, and hydrocarbon types, can be used as well as mixtures thereof. It is preferred, however, to use mixtures of different perfume compounds, which together generate an attractive scent note. Such mixtures can also contain natural perfume mixtures such as those accessible from plant sources, e.g. pine, citrus, jasmine, patchouli, rose or ylang-ylang oil.
Non-limiting examples of different types of perfumes are provided below.
Suitable perfumes of the ester type include e.g. benzyl acetate, phenoxy ethyl isobutyrate, p-tert-butyl cyclohexyl acetate, linalyl acetate, dimethyl benzyl carbinyl acetate (DMBCA), phenyl ethyl acetate, ethyl methyl phenyl glycinate, allyl cyclohexyl propionate, styrallyl propionate, benzyl salicylate, cyclohexyl salicylate, floramate, melusate and jasmacyclate.
Odorant substance compounds of the hydrocarbon type include e.g. terpenes such as limonene and pinene.
Suitable perfumes of the ether type include e.g. benzyl ethyl ether and ambroxan.
Suitable perfume alcohols include e.g. 10-undecen-1 -ol, 2,6-dimethyl heptan-2-ol, 2- methyl butanol, 2-methyl pentanol, 2-phenoxy ethanol, 2-phenyl propanol, 2-tert-butyl cyclohexanol, 3,5,5-trimethyl cyclohexanol, 3-hexanol, 3-methyl-5-phenyl pentanol, 3-octanol, 1 - octen-3-ol, 3-phenyl propanol, 4-heptenol, 4-isopropyl cyclohexanol, 4-tert-butyl cyclohexanol, 6,8-dimethyl-2-nonanol, 6-nonen-1 -ol, 9-decen-1 -ol, alpha-methyl benzyl alcohol, alphaterpineol, amyl salicylate, benzyl alcohol, benzyl salicylate, beta-terpineol, butyl salicylate, citronellol, cyclohexyl salicylate, decanol, dihydro myrcenol, dimethyl benzyl carbinol, dimethyl heptanol, dimethyl octanol, ethyl salicylate, ethyl vanillin, anethol, eugenol, geraniol, heptanol, hexyl salicylate, isoborneol, isoeugenol, isopulegol, linalool, menthol, myrtenol, n-hexanol, nerol, nonanol, octanol, para-menthan-7-ol, phenyl ethyl alcohol, phenol, phenyl salicylate, tetrahydro geraniol, tetrahydro linalool, thymol, trans-2-cis-6-nonadienol, trans-2-nonen-1 -ol, trans-2- octenol, undecanol, vanillin, and cinnamic alcohol, wherein when multiple perfume alcohols are present, they may be selected independently of one another.
Suitable perfume ketones can include all ketones that can lend a desired scent or a sensation of freshness. Mixtures of different ketones can also be used. For example the ketone can be selected from the group consisting of buccoxime, iso-jasmone, methyl-beta-naphthyl ketone, Moschus indanone, Tonalid/Moschus plus, alpha-damascone, beta-damascone, delta- damascone, isodamascone, damascenone, damarose, methyl dihydro jasmonate, menthone, carvone, campher, fenchone, alpha-ionene, beta-ionone, dihydro-beta-ionone, gamma-methyl ionone, fleuramone, dihydro jasmone, cis-jasmone, iso-E-Super, methyl cedrenyl ketone or methyl cedrylone, acetophenone, methyl acetophenone, para-methoxy acetophenone, benzyl acetone, benzophenone, para-hydroxy-phenyl butanone, celery ketone or livescone, 6-isopropyl decahydro-2-naphtone, dimethyl octenone, frescomenthe, 4-(1 -ethoxyvinyl)-3,3,5,5-tetramethyl cyclohexanone, methyl heptenone, 2-(2-(4-methyl-3-cyclohexen-1 -yl)-propyl) cyclopentanone, 1 - (para-menthen-6(2)-yl)-1 -propanone, 4-(4-hydroxy-3-methoxy phenyl)-2-butanone, 2-acetyl-3,3- dimethyl norbomane, 6,7-dihydro-1 ,1 ,2,3,3-pentamethyl-4(5H)-indanone, 4-damascol, dulcinyl or cassion, gelsone, hexalone, isocyclemone E, methyl cyclocitrone, methyl lavender ketone, orivone, para-tert-butyl cyclohexanone, verdone, delphone, muscone, neobutenone, plicatone, veloutone, 2,4,4,7-tetramethyl-oct-6-en-3-one, tetrameran, hedione and mixtures thereof. Preferred ketones may e.g. be selected from alpha-damascone, delta-damascone, isodamascone, carvone, gamma-methyl ionone, iso-E-super, 2,4,4,7-tetramethyl-oct-6-en-3-one, benzyl acetone, beta-damascone, damascenone, methyl dihydro jasmonate, methyl cedrylone, hedione and mixtures thereof.
Suitable perfume aldehydes can be any aldehydes that produce a desired scent or a sensation of freshness. They may be individual aldehydes or mixtures of aldehydes. Exemplary suitable aldehydes are melonal, triplal, ligustral, adoxal, anis aldehyde, cymal, ethyl vanillin, florhydral, helional, heliotropine, hydroxy citronellal, koavone, laurin aldehyde, lyral, methyl nonyl acetaldehyde, para-tert-bucinal, phenyl acetaldehyde, undecylene aldehyde, vanillin, 2,6,10- trimethyl-9-andecenal, 3-dodecen-1 -al, alpha-n-amyl cinnamaldehyde, 4-methoxy benzaldehyde, benzaldehyde, 3-(4-tert-butylphenyl)-propanal, 2-methyl-3-(para-methoxy phenyl propanal), 2- methyl-4-(2,6,6-trimethyl-2(1 )-cyclohexen-1 -yl)-butanal, 3-phenyl-2-propenal, cis-/trans-3,7- dimethyl-2,6-octadien-1 -al, 3,7-dimethyl-6-octen-1 -al, [(3,7-dimethyl-6-octenyl)-oxy]- acetaldehyde, 4-isopropyl benzyaldehyde, 1 ,2,3,4,5,6,7,8-octahydro-8,8-dimethyl-2- naphthaldehyde, 2,4-dimethyl-3-cyclohexen-1 -carboxyaldehyde, 2-methyl-3-(isopropyl-phenyl)- propanal, decylaldehyde, 2,6-dimethyl-5-heptenal, 4-(tricyclo-[5.2.10-(2,6)]-decylidene-8)- butanal, octahydro-4, 7-methano-1 H-indene carboxaldehyde, 3-ethoxy-4-hydroxy benzaldehyde, para-ethyl-alpha-alpha-dimethyl hydro cinnamaldehyde, alpha-methyl-3,4-(methylene dioxy)- hydro cinnamaldehyde, 3,4-methylene dioxy benzaldehyde, alpha-n-hexyl cinnamaldehyde, m- cymene-7-carboxaldehyde, alpha-methyl phenyl acetaldehyde, 7-hydroxy-3,7-dimethyl octanal, undecenal, 2,4,6-trimethyl-3-cyclohexene-1 -carboxaldehyde, 4-(3)-(4-methyl-3-pentenyl)-3- cyclohexene carboxaldehyde, 1 -dodecanal, 2,4-dimethyl cyclohexene-3-carboxaldehyde, 4-(4- hydroxy-4-methyl pentyl)-3-cyclohexene-1 -carboxaldehyde, 7-methoxy-3,7-dimethyl octan-1 -al, 2-methyl undecanal, 2-methyl decanal, 1 -nonanal, 1 -octanal, 2,6,10-trimethyl-5,9-undecadienal, 2-methyl-3-(4-tert-butyl)-propanal, dihydro cinnamaldehyde, 1 -methyl-4-(4-methyl-3-pentenyl)-3- cyclohexene-1 -carboxaldehyde, 5- or 6-methoxy hexahydro-4, 7-methano indane-1 or 2-carboxy aldehyde, 3,7-dimethyl octan-1 -al, 1 -undecanal, 10-undecen-1 -al, 4-hydroxy-3-methoxy benzaldehyde, 1 -methyl-3-(4-methyl pentyl)-3-cyclohexene carboxy aldehyde, trans-4-decenal,
2.6-nonadienal, para-tolyl-acetaldehyde, 4-methyl phenyl acetaldehyde, 2-methyl-4-(2,6,6- trimethyl-1 -cyclohexen-1 -yl)-2-butenal, ortho-methoxy cinnamaldehyde, 3,5,6-trimethyl-3- cyclohexene carboxaldehyde, 3,7-dimethyl-2-methylene-6-octenal, phenoxy acetaldehyde, 5,9- dimethyl-4,8-decadienal, peony aldehyde (6,1 -dimethyl-3-oxa-5,9-undecadien-1 -al), hexahydro-
4.7-methanoindane-1 -carboxaldehyde, 2-methyloctanal, alpha-methyl-4-(1 -methyl ethylbenzene acetaldehyde, 6,6-dimethyl-2-norpinene-2-propion aldehyde, para-methyl phenoxy acetaldehyde, 2-methyl-3-phenyl-2-propen-1 -al, 3,5,5-trimethyl hexanal, hexahydro-8, 8- dimethyl-2-naphthaldehyde, 3-propyl-bicyclo-[2.2.1 ]-hept-5-ene-2-carbaldehyde, 9-decenal, 3- methyl-5-phenyl-1 -pentanal, 1 -para-menthene-q-carboxaldehyde, citral or mixtures thereof, lilial citral, 1 -decanal, 2, 4-dimethyl-3-cyclohexene-1 -carboxaldehyde. Preferred aldehydes may e.g. be selected from cis/trans-3,7-dimethyl-2,6-octadien-1 -al, heliotropin, 2,4,6-trimethyl-3- cyclohexene-1 -carboxaldehyde, 2,6-nonadienal, alpha-n-amyl cinnamaldehyde, alpha-n-hexyl cinnamaldehyde, para-tert-bucinal, lyral, cymal, methyl nonyl acetaldehyde, trans-2-nonenal, lilial, trans-2-nonenal and mixtures thereof.
Perfume compounds may also be natural odorant mixtures such as those accessible from plant sources, e.g. pine, citrus, jasmine, patchouli, rose or ylang-ylang oil. Also suitable are muscat, sage oil, chamomile oil, clove oil, mint oil, cinnamon leaf oil, lime blossom oil, juniper berry oil, vetiver oil, olibanum (frankincense) oil, galbanum oil and labdanlum oil as well as orange blossom oil, neroli oil, orange peel oil and sandalwood oil. The perfume compounds may also be essential oils, e.g. angelica root oil, anise oil, arnica blossom oil, basal oil, bay oil, champaca blossom oil, silver fir oil, silver fir cone oil, elemi oil, eucalyptus oil, fennel oil, spruce needle oil, geranium oil, gingergrass oil, guaiac wood oil, gurjun balsam oil, helichrysum oil, ho leaf oil, ginger oil, iris oil, cajeput oil, calmus oil, camphor oil, canaga oil, cardamom oil, cassia oil, copaiva balsam oil, coriander oil, spearmint oil, caraway oil, cumen oil, lavender oil, lemongrass oil, lime oil, mandarin oil, lemon balm oil, musk seed oil, myrrh oil, niaouli oil, origanum oil, palmarosa oil, peru balsam oil, petit grain oil, pepper oil, peppermint oil, pimento oil, rosemary oil, celery oil, spike oil, stemanis oil, turpentine oil, thuja oil, thyme oil, verbena oil, vermouth oil, Wintergreen oil, ysop oil, cinnamon oil, citronella oil, lemon oil and cypress oil.
Further information about fragrance ingredients may be obtained from The International Fragrance Association (IFRA), which publishes a list of all fragrance ingredients used in consumer goods (ifrafragrance.org/initiatives/transparency/ifra-transparency-list).
In one embodiment a plurality of perfume compounds, e.g. those listed above or on the list maintained by the IFRA, may be included in a detergent composition of the invention. The compositions of the invention may therefore e.g. contain three or more, such as four or more, five or more, six or more or seven or more different perfume components.
The compositions of the invention will typically contain one or more perfume components in a total amount (by weight) of from 0.0001 % to 2.5%, such as 0.001 -2%, e.g. 0.01 -1.5%, for example 0.1 -1 % percent, based on the total amount of perfume components and the total weight of the composition.
There are no limitations on the type of detergent composition in which perfumes may be incorporated. They may, for example, be included in detergent compositions that are in the form of liquids, gels, powders, granulates, tablets, pods, pouches and soap bars.
Perfume components may be incorporated into detergent compositions in physical forms and using methods known in the art, e.g. adding the perfume components as liquids, solid particles and/or microcapsules. Cleaning components
The choice of cleaning components may include, for textile care, the consideration of the type of textile to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.
Surfactants
The cleaning composition may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant is typically present at a level of from about 1 % to 70% by weight, such as about 1 wt% to about 40 wt%, or about 3 wt% to about 20 wt%, or about 3 wt% to about 10 wt%.
The one or more surfactants are chosen based on the desired cleaning application, and may include any conventional surfactants known in the art.
When included therein the detergent will usually contain from about 1% to about 70% by weight of an anionic surfactant, such as from about 5 wt % to about 50 wt %, including from about 5 wt % to about 20 wt %, or from about 15 wt % to about 20 wt %, or from about 20 wt % to about 25 wt % or at least 30 wt%, at least 40 wt% or at least 50 wt% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, alkylbenzenesulfonates, such as linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.
When included therein the detergent will usually contain from about 1% to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.
When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5 wt% to about 30 wt %, in particular from about 1 wt % to about 20 wt %, from about 3 wt % to about 10 wt %, such as from about 3% wt to about 5 wt %, from about 8 wt % to about 12 wt %, or from about 10 wt % to about 12 wt %. Nonlimiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.
When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N- (tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, , and combinations thereof.
When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.
Typically, more than one surfactant is present in the cleaning composition, for example at least one anionic and at least one non-ionic surfactant. Preferably, the amount of all surfactant present (total amount) i.e. the amount of anionic, non-ionic, zwitterionic and cationic surfactant present is preferably from about 1 wt% to 80 wt% by weight, such as about 1 wt% to 70 wt%, such as about 1 wt% to 50 wt% such as about 1 wt% to about 40 wt%, or about 5 wt% to about 40 wt%, or about 10 wt% to about 60 wt%. The ratio between the surfactants present depends on the specific composition but the weight ratios may be when an anionic and non-ionic surfactant is included in the composition a weight ratio of the anionic to nonionic surfactant from; 30:1 to 10:1 , 20:1 to 1 :10, 25: 1 to 1 :2, 20:1 to 1 :5.
One embodiment relates to a cleaning composition comprising a polypeptide having DNase activity, wherein the cleaning component is at least one surfactant, preferably anionic and/or nonionic, preferably wherein the composition comprises from 1 to 70 wt%, preferably from 5 to 40 wt % surfactant, wherein the surfactant preferably is selected from alkylbenzenesulfonates e.g. LAS, alkyl sulfates (AS) and mixtures thereof, preferably the cleaning composition comprises at least 20 wt % alkylbenzenesulfonate surfactant. One embodiment relates to a cleaning composition comprising a polypeptide having DNase activity, wherein the cleaning composition comprises at least one anionic surfactant and wherein the cleaning composition additionally comprises a nonionic surfactant, and preferably wherein the weight ratio of the anionic to nonionic surfactant is from 25: 1 to 1 :2 or from 1 .5:1 to 1 :10.
Builders and Co-Builders
The cleaning composition may contain about 0-65% by weight, such as about 5% to about 50%, such as about 0.5% to about 20% of a detergent builder or co-builder, or a mixture thereof. In a dish wash detergent, the level of builder is typically 40-65%, particularly 50-65%. The builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized. Nonlimiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1 -ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1 -ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl)inulin (CMI), and combinations thereof.
The detergent composition may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder. The detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2,2’,2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1 -hydroxyethane-1 ,1 -diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis- (methylenephosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N- monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)-aspartic acid (SMAS), N- (2-sulfoethyl)-aspartic acid (SEAS), N-(2-sulfomethyl)-glutamic acid (SMGL), N-(2-sulfoethyl)- glutamic acid (SEGL), N-methyliminodiacetic acid (Ml DA), a-alanine-N,N-diacetic acid (a-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA) , taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2- hydroxyethyl)ethylenediamine-N,N’,N”-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and/or co-builders are described in, e.g., WO 09/102854, US 5977053
Bleaching Systems
The cleaning composition may contain 0-30% by weight, such as about 1% to about 20%, such as about 0.01% to about 10% of a bleaching system. Any bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.
Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide— urea (1/1).
Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.
Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-a-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, e-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of said compounds. It is understood that the peracids mentioned may in some cases be best added as suitable salts, such as alkali metal salts (e.g., Oxone®) or alkaline earth-metal salts.
Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3, 5, 5-trimethylhexanoyl)oxy]benzene-1 -sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1 -sulfonate (LOBS), sodium 4- (decanoyloxy)benzene-l -sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4- (nonanoyloxy)benzene-l -sulfonate (NOBS), and/or those disclosed in WO98/17767. A particular family of bleach activators of interest was disclosed in EP624154 and particularly preferred in that family is acetyl triethyl citrate (ATC). ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators. Finally, ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.
Bleach catalysts and boosters
The bleaching system may also include a bleach catalyst or booster. Some non -limiting examples of bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1 ,4,7-trimethyl-1 ,4,7-triazacyclononane (Me3-TACN) or 1 ,2,4,7-tetramethyl- 1 ,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1 ,2- diylazanylylidene-KN-methanylylidene)triphenolato-K30]manganese(lll). The bleach catalysts may also be other metal compounds; such as iron or cobalt complexes.
In some embodiments, where a source of a peracid is included, an organic bleach catalyst or bleach booster may be used having one of the following formulae:
Figure imgf000034_0001
(iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 1 1 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.
Other exemplary bleaching systems are described e.g. in W02007/087258, W02007/087244, W02007/087259, EP1867708 (Vitamin K) and W02007/087242. Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
Metal care agents
Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:
(a) benzatriazoles, including benzotriazole or bis-benzotriazole and substituted derivatives thereof. Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or completely substituted. Suitable substituents include linear or branch-chain Ci-C20- alkyl groups (e.g., C1 -C20- alkyl groups) and hydroxyl, thio, phenyl or halogen such as fluorine, chlorine, bromine and iodine.
(b) metal salts and complexes chosen from the group consisting of zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cerium salts and/or complexes, the metals being in one of the oxidation states II, III, IV, V or VI. In one aspect, suitable metal salts and/or metal complexes may be chosen from the group consisting of Mn(ll) sulphate, Mn(ll) citrate, Mn(ll) stearate, Mn(ll) acetylacetonate, KATiF6 (e.g., K2TiF6), KAZrF6 (e.g., K2ZrF6), CoS04, Co(NOs)2 and Ce(NOs)3, zinc salts, for example zinc sulphate, hydrozincite or zinc acetate;
(c) silicates, including sodium or potassium silicate, sodium disilicate, sodium metasilicate, crystalline phyllosilicate and mixtures thereof.
Further suitable organic and inorganic redox-active substances that act as silver/copper corrosion inhibitors are disclosed in WO 94/26860 and WO 94/26859. Preferably the composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.
Hydrotropes
The cleaning composition may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.
Polymers
The cleaning composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below- mentioned motifs. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone- vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aquaion, and Sokalan® HP 165, Sokalan® HP 50 (Dispersing agent), Sokalan® HP 53 (Dispersing agent), Sokalan® HP 59 (Dispersing agent), Sokalan® HP 56 (dye transfer inhibitor), Sokalan® HP 66 K (dye transfer inhibitor) from BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.
Fabric hueing agents
The cleaning compositions of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C. I.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in W02005/03274, W02005/03275, W02005/03276 and EP1876226 (hereby incorporated by reference). The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and W02007/087243.
Dispersants
The cleaning compositions of the present invention can also contain dispersants. In particular, powdered detergents may comprise dispersants. Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
Dye Transfer Inhibiting Agents
The cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01 % to about 5% or even from about 0.1 % to about 3% by weight of the composition.
Fluorescent whitening agent
The cleaning compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agents or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2- diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s- triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)- s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2-yl)stilbene-2,2'- disulfonate and sodium 5-(2H-naphtho[1 ,2-d][1 ,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]- benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2- morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7- alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%.
Soil release polymers
The cleaning compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc. Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference). Furthermore, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference). Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1 -C6 mono-carboxylic acid, Cl-C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1 : 1 to 1 :5, or from 1 : 1 .2 to 1 :2. The average number of graft sites per ethylene oxide units can be less than 1 , or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, or from 0.2 to 0.4. A suitable polyethylene glycol polymer is Sokalan HP22. Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1867808 or WO 2003/040279 (both are hereby incorporated by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cation ically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.
Anti-redeposition agents
The cleaning compositions of the present invention may also include one or more anti- redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines. The cellulose based polymers described under soil release polymers above may also function as antiredeposition agents.
Rheology Modifiers
The cleaning compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents. The rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.
Other suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.
Polymers
The cleaning composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aquaion, and Sokalan® HP 165, Sokalan® HP 50 (Dispersing agent), Sokalan® HP 53 (Dispersing agent), Sokalan® HP 59 (Dispersing agent), Sokalan® HP 56 (dye transfer inhibitor), Sokalan® HP 66 K (dye transfer inhibitor) from BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor. Additional enzymes
The cleaning composition may comprise, in addition to the at least one polypeptide having DNase activity and optionally at least one DNase, one or more additional enzymes such as one or more lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase. In general, the properties of the selected enzymes should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzymes should be present in effective amounts.
Mannanases
Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes A/S).
Cellulases
Suitable cellulases include complete cellulases or mono-component endoglucanases of bacterial or fungal origin. Chemically or genetically modified mutants are included. The cellulase may for example be a mono-component or a mixture of mono-component endo-1 ,4-beta- glucanase often just termed endoglucanases. Suitable cellulases include a fungal cellulase from Humicola insolens (US 4,435,307) or from Trichoderma, e.g. T. reesei or T. viride. Examples of cellulases are described in EP 0 495 257. Other suitable cellulases are from Thielavia e.g. Thielavia terrestris as described in WO 96/29397 or Fusarium oxysporum as described in WO 91/17244 or from Bacillus as described in, WO 02/099091 and JP 2000210081 . Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 Commercially available cellulases include Carezyme®, Celluzyme®, Celluclean®, Celluclast® and Endolase®; Renozyme®; Whitezyme® (Novozymes A/S) Puradax®, Puradax HA, and Puradax EG (available from Genencor).
Proteases
Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants. The protease may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as a subtilisin. A metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M35 families.
The term "subtilases" refers to a sub-group of serine proteases according to Siezen et aL, Protein Eng. 4 (1991 ) 719-737 and Siezen et aL, Protein Sci. 6 (1997) 501 -523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
Although proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus, detergent proteases have generally been obtained from bacteria and in particular from Bacillus. Examples of Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii. Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93/18140). Other useful proteases are e.g. those described in WO 01/16285 and WO 02/16547.
Examples of trypsin-like proteases include the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
Examples of metalloproteases include the neutral metalloproteases described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015/158723 and WO 2016/075078.
Examples of useful proteases are the protease variants described in WO 89/06279 WO 92/19729, WO 96/34946, WO 98/201 15, WO 98/20116, WO 99/1 1768, WO 01/44452, WO 03/006602, WO 2004/003186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2014/207227, WO 2016/087617 and WO 2016/174234. Preferred protease variants may, for example, comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101 A, V102I, V102Y, V102N, S104A, G116V, G1 16R, H1 18D, H1 18N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161 A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Q200L, Y203W, S206G, L21 1 Q, L211 D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256D T268A and R269H, wherein position numbers correspond to positions of the Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016/001449. Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449. Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016/001449.
Another protease of interest is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 91/02792, and variants thereof which are described for example in WO 92/21760, WO 95/23221 , EP 1921 147, EP 1921148 and WO 2016/096711.
The protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004/067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 1 11 , 171 , 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO 2004/067737. TY145 variants of interest are described in e.g. WO 2015/014790, WO 2015/014803, WO 2015/014804, WO 2016/097350, WO 2016/097352, WO 2016/097357 and WO 2016/097354.
Examples of preferred proteases include:
(a) variants of SEQ ID NO: 1 of WO 2016/001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D and L262E, for example a variant with the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261 W and L262E, or with the substitutions S9E, N43R, N76D, N185E, S188E, Q191 N, A194P, Q206L, Y209W, S259D and L262E, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(b) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the mutation S99SE, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(c) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the mutation S99AD, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(d) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions Y167A+R170S+A194P, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(e) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S9R+A15T+V68A+N218D+Q245R, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(f) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S9R+A15T+G61 E+V68A+A194P+V205I+Q245R+N261 D, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(g) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S99D+S101 R/E+S103A+V104I+G160S; for example a variant of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S3T+V4I+S99D+S101 E+S103A+V104I+G160S+V205I, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(h) a variant of the polypeptide of SEQ ID NO: 2 of WO 2016/001449 with the substitutions S24G+S53G+S78N+S101 N+G128A/S+Y217Q, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(i) the polypeptide disclosed in GENESEQP under accession number BER84782, corresponding to SEQ ID NO: 302 in WO 2017/210295;
(j) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S99D+S101 E+S103A+V104I+S156D+G160S+L262E, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(k) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions S9R+A15T+G61 E+V68A+N76D+S99G+N218D+Q245R, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
(l) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016/001449 with the substitutions V68A+S106A, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449; and
(m) a variant of the polypeptide of SEQ ID NO: 1 of WO 2004/067737 with the substitutions S27K+N109K+S11 1 E+S171 E+S173P+G174K+S175P+F180Y+G182A+L184F+ Q198E+N199+T297P, wherein position numbers are based on the numbering of SEQ ID NO: 1 of WO 2004/067737.
Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase™, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In and Progress® Excel (Novozymes A/S), those sold under the tradename Maxatase™, Maxacai™, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2™, FN3™, FN4ex™, Excellase®, Excellenz™ P1000, Excellenz™ P1250, Eraser™, Preferenz® P100, Purafect Prime, Preferenz® P1 10, Preferenz® P300, Effectenz P1000™, Purafect®, Effectenz P1050™, Purafect® Ox, Effectenz ™ P2000, Purafast™, Properase®, Opticlean™ and Optimase® (Danisco/DuPont), BLAP (sequence shown in Figure 29 of US 5352604) and variants hereof (Henkel AG), and KAP (Bacillus alkalophilus subtilisin) from Kao.
Upases and Cutinases
Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp. strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grisea (WO10/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (WO1 1/084412), Geobacillus stearothermophilus lipase (W011/084417), lipase from Bacillus subtilis (WO1 1/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (WO12/137147).
Other examples are lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , WO94/25578, WO95/14783, WO95/30744, WO95/35381 , WO95/22615,
W096/00292, W097/04079, W097/07202, WO00/34450, WO00/60063, W001/92502,
W007/87508 and WO09/109500.
Preferred commercial lipase products include Lipolase™, Lipex™; Lipolex™ and Lipoclean™ (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades). Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/1 11 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10/100028).
Amylases
Suitable amylases may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.
Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 211 , 243, 264, 304, 305, 391 , 408, and 444.
Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193. Other amylases which are suitable are hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N190, M197, 1201 , A209 and Q264. Most preferred variants of the hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36- 483 of SEQ ID NO: 4 are those having the substitutions:
M197T;
H156Y+A181 T+N190F+A209V+Q264S; or
G48A+T49I+G107A+H156Y+A181 T+N190F+I201 F+A209V+Q264S.
Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181 , 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712. Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 211 and 264.
Further suitable amylases are amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof. Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 1, T165I, K178L, T182G, M201 L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183. Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
N128C+K178L+T182G+Y305R+G475K;
N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;
S125A+N128C+K178L+T182G+Y305R+G475K; or
S125A+N128C+T131 1+T165I+K178L+T182G+Y305R+G475K wherein the variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.
Further suitable amylases are amylases having SEQ ID NO: 1 of WO13184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181 , E187, N192, M199, I203, S241 , R458, T459, D460, G476 and G477. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241 QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181 . Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
E187P+I203Y+G476K
E187P+I203Y+R458N+T459S+D460T+G476K wherein the variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.
Further suitable amylases are amylases having SEQ ID NO: 1 of WO10104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21 , D97, V128 K177, R179, S180, 1181 , G182, M200, L204, E242, G477 and G478. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21 D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of 1181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
N21 D+D97N+V128I, wherein the variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181. Other suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R1 18, N174; R181 , G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471 , N484. Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
Other examples are amylase variants such as those described in WO2011/098531 , WO2013/001078 and WO2013/001087.
Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes A/S), and Rapidase™, Purastar™/Effectenz™, Powerase, Preferenz® S1000, Preferenz® S100, Preferenz® S1 10 and Preferenz® S210 (from Genencor International Inc./DuPont).
Peroxidases/Oxidases
A peroxidase may be an enzyme comprised by the enzyme classification EC 1 .11 .1 .7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity. Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. A peroxidase may also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1 .11 .1 .10) catalyze formation of hypochlorite from chloride ions. The haloperoxidase may be a chloroperoxidase. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-con tai ni ng haloperoxidase. In a preferred method the vanadate-containing haloperoxidase is combined with a source of chloride ion. Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis. Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens. The haloperoxidase may be derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461 , or Geniculosporium sp. as described in WO 01/79460.
Oxidases include any laccase enzyme comprised by the enzyme classification EC 1 .10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1 ), an o-aminophenol oxidase (EC 1 .10.3.4), or a bilirubin oxidase (EC 1 .3.3.5). Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Pomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. so Ian i, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885). Suitable examples from bacteria include a laccase derivable from a strain of Bacillus. A laccase derived from Coprinopsis or Myceliophthora is preferred; in particular a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
Microorganisms
The detergent additive as well as the detergent composition may also comprise one or more microorganisms, such as one or more fungi, yeast, or bacteria. In an embodiment, the one or more microorganisms are dehydrated (for example by lyophilization) bacteria or yeast, such as a strain of Lactobacillus. In another embodiment, the microorganisms are one or more microbial spores (as opposed to vegetative cells), such as bacterial spores; or fungal spores, conidia, hypha. Preferably, the one or more spores are Bacillus endospores; even more preferably the one or more spores are endospores of Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus megaterium. The microorganisms may be included in the detergent composition or additive in the same way as enzymes (see above).
Formulation of detergent products
The cleaning composition of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for pretreatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations. In a specific aspect, the present invention provides a detergent additive comprising one or more enzymes as described herein. The cleaning composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.
Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about 60%. Preferred average molecular weight will typically be about 20,000 to about 150,000. Films can also be of blended compositions comprising hydrolytically degradable and water-soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water- soluble film. The compartment for liquid components can be different in composition than compartments containing solids: US2009/0011970 A1 .
Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
A liquid or gel detergent which is not unit dosed may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may also be non-aqueous.
Formulation of enzyme in granules
Non-dusting granulates may be produced e.g. as disclosed in US 4,106,991 and 4,661 ,452 and may optionally be coated by methods known in the art. Examples of waxy coating materials are polyethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591. Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods. Protected enzymes may be prepared according to the method disclosed in EP 238,216.
The compositions of the invention may be formulated as a granule, for example as a cogranule that combines one or more enzymes. Each enzyme will then be present in more granules, securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates for the detergent industry are disclosed in the IP.com disclosure IPCOM000200739D.
Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013/188331 , which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than 10 wt% zeolite (anhydrous basis); and (c) less than 10 wt% phosphate salt (anhydrous basis), wherein said enzyme co-granule comprises from 10 to 98 wt% moisture sink component and the composition additionally comprises from 20 to 80 wt% detergent moisture sink component. WO 2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a fabric surface comprising the steps of (i) contacting said surface with the detergent composition in aqueous wash liquor, (ii) rinsing and/or drying the surface.
A multi-enzyme co-granule may comprise an enzyme of the invention and one or more enzymes selected from the group consisting of proteases, lipases, cellulases, xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases, hemicellulases, proteases, cellulases, cellobiose dehydrogenases, xylanases, phospho lipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase, amylases, nucleases, hexosaminidases and mixtures thereof.
An embodiment of the invention relates to an enzyme granule/particle comprising the enzyme of the invention. The granule is composed of a core, and optionally one or more coatings (outer layers) surrounding the core. Typically, the granule/particle size, measured as equivalent spherical diameter (volume based average particle size), of the granule is 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250-1200 pm.
The core may include additional materials such as fillers, fibre materials (cellulose or synthetic fibres), stabilizing agents, solubilising agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances.
The core may include binders, such as synthetic polymer, wax, fat, or carbohydrate. The core may comprise a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend.
The core may consist of an inert particle with the enzyme absorbed into it, or applied onto the surface, e.g., by fluid bed coating.
The core may have a diameter of 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250- 1200 pm.
The core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheron ization, size reduction methods, drum granulation, and/or high shear granulation.
Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Volume 1 ; 1980; Elsevier.
The core of the enzyme granule/particle may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule. The optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93/07263 and WO 97/23606.
The coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, 1 % or 5%. The amount may be at most 100%, 70%, 50%, 40% or 30%.
The coating is preferably at least 0.1 pm thick, particularly at least 0.5 pm, at least 1 pm or at least 5 pm. In a particular embodiment, the thickness of the coating is below 100 pm. In a more particular embodiment the thickness of the coating is below 60 pm. In an even more particular embodiment the total thickness of the coating is below 40 pm.
The coating should encapsulate the core unit by forming a substantially continuous layer. A substantially continuous layer is to be understood as a coating having few or no holes, so that the core unit it is encapsulating/enclosing has few or none uncoated areas. The layer or coating should be homogeneous in thickness.
The coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc.
A salt coating may comprise at least 60% by weight w/w of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight w/w.
The salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles is less than 50 pm, such as less than 10 pm or less than 5 pm. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, in particular having a solubility at least 0.1 grams in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water.
The salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminium. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used.
The salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt e.g., anhydrate). The salt coating may be as described in WO 00/01793 or WO 2006/034710.
Specific examples of suitable salts are NaCI (CH20 C=76%), Na2CO3 (CH2o c=92%), NaNO3 (CH20 C=73%), Na2HPO4 (CH20 G=95%), Na3PO4 (CH25 G=92%), NH4CI (CH20 G = 79.5%), (NH4)2HPO4 (CH20 C = 93,0%), NH4H2PO4 (CH20 G = 93.1%), (NH4)2SO4 (CH20 G=81 .1%), KOI (CH20 C=85%), K2HPO4 (CH20 C=92%), KH2PO4 (CH20 G=96.5%), KNO3 (CH20 G=93.5%), Na2SO4 (CH20 C=93%), K2SO4 (CH20 C=98%), KHSO4 (CH20 G=86%), MgSO4 (CH20 G=90%), ZnSO4 (CH2O°C=9O%) and sodium citrate (CH25°c=86%). Other examples include NaH2PO4, (NH4)H2PO4, CuSO4, Mg(NO3)2 and magnesium acetate.
The salt may be in anhydrous form, or it may be a hydrated salt, i.e. a crystalline salt hydrate with bound water of crystallization, such as described in WO 99/32595. Specific examples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO4), magnesium sulfate heptahydrate (MgSO47H2O), zinc sulfate heptahydrate (ZnSO47H2O), sodium phosphate dibasic heptahydrate (Na2HPO47H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate. Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed.
Thus, in a further aspect, the present invention provides a granule comprising:
(a) a core comprising an enzyme according to the invention,
(b) optionally, a coating consisting of one or more layers surrounding the core; and (c) wherein the granule preferably is a co-granulate comprising one or more additional enzymes, preferably wherein at least one additional enzyme is selected from proteases, amylases and cellulases.
In one embodiment, the present invention provides a granule comprising:
(a) a core comprising a polypeptide having DNase degrading activity,
(b) optionally, a coating consisting of one or more layers surrounding the core; and
(c) wherein the granule preferably is a co-granulate comprising one or more additional enzymes, preferably wherein at least one additional enzyme is selected from proteases, amylases and cellulases.
Fabric softener compositions
Fabric softener compositions are well-known in the art. Such compositions include at least one fabric softener component, typically selected from the group consisting of cationic softener components, silicone softener components, paraffins, waxes, dispersible polyolefins and mixtures thereof. Preferred softener components include cationic surfactants, more preferably cationic surfactants of the quaternary ammonium type, for example in the form of a quaternary ammonium ester.
Uses
The present invention is directed to methods for using the compositions comprising a DNase as defined herein and at least one perfume compound, in particular for cleaning of laundry/textiles/fabrics, including household laundry and industrial laundry, and for hard surface cleaning, including automatic dishwashing (ADW), car washing and industrial surface cleaning.
Use of cleaning compositions
The detergent composition of the present invention may be formulated, for example, for use as a hand or machine laundry detergent composition, including as a laundry additive composition suitable for pre-treatment of stained fabrics or a rinse added to a fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing. Also provided herein is a detergent additive comprising a DNase and at least one perfume compound.
In one embodiment, the invention relates to use of a DNase in a detergent composition for increasing binding of a perfume to a textile during a laundry process, wherein the detergent composition comprises at least one perfume compound.
In one embodiment, the invention relates to use of a DNase in a detergent composition for increasing perfume retention on a textile after wash, wherein the detergent composition comprises at least one perfume compound. In one embodiment, the invention relates to use of a DNase for enhancing the effect of a perfume in a laundry detergent composition, wherein the detergent composition comprises at least one perfume compound.
Methods
In one embodiment, the invention provides a method for increasing binding of a perfume to a textile during a laundry process, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a DNase.
In one embodiment, the invention provides a method for increasing perfume retention on a textile after wash, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a DNase.
In one embodiment, the invention provides a method for enhancing the effect of a perfume in a laundry detergent composition, the method comprising preparing a detergent composition comprising at least one perfume compound and a DNase.
In one embodiment, the invention provides a method for preparing a detergent composition with reduced perfume content but with maintained perfume effect after wash relative to a comparable composition without DNase, the method comprising mixing at least one perfume compound, a polypeptide having DNase activity and at least one detergent component.
In one embodiment, the invention provides a method for cleaning an item, wherein the item is preferably a textile, comprising the steps of: a) contacting the item with a wash liquor comprising a detergent composition as defined herein comprising an enzyme having DNase activity and at least one perfume compound, and optionally b) rinsing the item.
The pH of the liquid wash liquor solution is typically in the range of from about 5.5 to about 12, such as from about 7 to about 1 1 , such as from about 7 to about 10, e.g. from about 7 to about 9.
The wash liquor may have a temperature in the range of 5eC to 95eC, such as in the range of 10eC to 80eC, in the range of 10eC to 70eC, in the range of 10eC to 60eC, in the range of 10eC to 50eC, in the range of 15eC to 40eC or in the range of 20eC to 30eC.
The present invention is further described by the following examples that should not be construed as limiting the scope of the invention. Examples
Assay 1 : Determination of DNase activity
DNase activity may be determined on DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which is prepared according to the manual from the supplier. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is tempered to 48°C in water bath, and 20 ml of agar is poured into petri dishes and allowed to solidify by incubation overnight at room temperature. On solidified agar plates, 5 pl of enzyme solutions are added and DNase activity is observed as colorless zones around the spotted enzyme solutions.
Assay 2: Determination of DNase activity
DNase activity may be determined using the DNaseAlert™ Kit (11 -02-01 -04, IDT Intergrated DNA Technologies) according to the supplier’s manual. Briefly, 95 pl DNase sample is mixed with 5 pl substrate in a microtiter plate, and fluorescence is immediately measured using a Clariostar microtiter reader from BMG Labtech (536 nm excitation, 556 nm emission).
Example 1 : Sensory evaluation of perfume retention after wash in a liquid detergent with DNase
The evaluation of this example included the following steps:
Step 1 . Preparation of test items
Step 2. Wash test in detergent with and without DNase
Step 3. Human panel evaluation of washed items
Subsequent to the sensory evaluation, GC-MS analysis of washed items was performed. This is described in Example 2.
1 . Preparation of test items
The test items were 100% polyester T-shirts weighing 130 g/m2. The T-shirts were preaged before being handed out to be used for exercise by test persons.
Pre-aging procedure: T-shirts weighing a total of 4 kg were added to a Wascator FOM 71 CLS washing machine from Electrolux together with 75 g of IEC* A detergent. The detergent was mixed with 50 g tap water plus 28 g of ballast soil with the following composition:
Figure imgf000055_0001
Figure imgf000056_0001
The above ingredients were mixed into a homogenous material by mixing melted lanolin and sebum (melted by heating at 50°C) with the mixed dry ingredients, followed by addition of glycerol and tryptone soy broth and stirring the mixture with a magnetic stirrer at 50°C for about two hours. The mixture was then cooled to room temperature and stored at 5°C.
The Wascator was programmed to wash for 12 hours without a final rinse. 75 g of new detergent IEC* A was then added, and a one-hour wash program with two rinses was performed, after which the T-shirts were tumble dried.
The T-shirts were then handed out for use by members of either a soccer team or a running team. They were worn for at least one hour of intensive training during two separate training sessions, drying the T-shirts in between. They were then returned to the laboratory and incubated in a safety cupboard for safety reasons for three days, after which they were moved to a climate chamber for a 24h incubation at 30°C and 95% relative humidity, followed by collecting all the T-shirts in a box with a lid and letting them incubate at 30°C for another 24h. All T-shirts were sorted by smell. Those without smell were discarded, while those with intense smell could be used as test material.
2. Wash test in detergent with and without DNase
Since left and right armpits can smell differently, cutouts from each were made using a 6x8 cm oval template. Cutout swatches from the left and right armpits of each T-shirt were cut into 4 pieces, resulting in a total of 8 pieces from each T-shirt. These were divided among 4 nylon stockings that were used as washing bags, such that pieces from the left and right armpit and from the front and back side of the armpit were divided into different stockings. Cutouts from 4 T- shirts were divided in this manner among 4 nylon stockings, i.e. each stocking contained a total of 8 pieces from 4 different T -shirts. The nylon stockings were sealed with a knot or a rubber band before wash and were discarded after wash.
The rest of the T-shirts were cut into two pieces each, with one half T-shirt being washed with DNase and the other half without DNase. The nylon stockings containing the armpit samples were washed together with the half T-shirts as well as ballast consisting of 1 kg of discarded household garments (each cut in two and divided equally between the two washing machines) and 1 .5 kg of clean ballast items in the form of 5 cotton T-shirts, 1 towel and 4-6 tea towels.
Three washes were performed in each round:
1 st wash: A clean T-shirt was washed using the same detergent as that used in the test. This functioned as a clean background sample to give a “pure fragrance impression”.
2nd wash: This was a blank test wash with detergent alone.
3rd wash: Test wash using detergent and DNase.
Washing was performed in a standard US top loader washing machine with the armpit samples, half T-shirts and ballast as described above, using the following wash program:
• Load Size: Medium
• Wash temp.: 30°C
• Extra Rinse: On
• Program: Normal, Regular
• Duration: approx. 55 min
The main wash cycle water volume was approx. 67 liters of water with a hardness of water 6e dH (2:1 :1 .5 Ca:Mg:NaHCO3). The detergent was Arm & Hammer Oxiclean (Church & Dwight, USA), added directly to the machine in a dose of 54.8 g/wash. For washes with DNase, the DNase of SEQ ID NO: 1 was added to the wash water at a concentration of 2 ppm. For the 1st wash with a clean T-shirt, a single T-shirt was washed in the same manner as the 2nd wash with detergent alone, but without ballast. All items were line dried overnight after wash.
3. Human panel evaluation of washed items
Swatches were transferred from the dried stockings to 60L Nalophan bags sealed at the bottom and filled with filtered air (swatches from one stocking per bag). Background samples from the 1 st wash were cut out with a similar weight as the test samples and added to 2 bags. The bags are then stored at 30°C for 2 hours, after which they are ready for the sensory evaluation.
The sensory evaluation was performed using a PureSniff III device from Olfasense GmbH, Germany. The device has three chambers for simultaneous evaluation. The first chamber contained the background sample, while the other two chambers contained the test samples washed with or without DNase in a blinded order.
Each test panel member senses (smells) first the background sample and then the two test samples. The test is rated as a simple preference test in which the test person chooses the sample that he/she prefers.
The test is repeated with the remaining 6 test samples from each wash, each time evaluating a sample washed without DNase and a sample washed with DNase in blinded order.
Each test was repeated 3 times using 8 T-shirts (2 subgroups of 4), i.e. testing a total of 24 T-shirts in 12 pools. Seven test persons participated in the evaluation, thus providing a total of 84 different individual evaluations. The results are provided in Table 1 below.
Table 1 . Sensory results for 3 wash tests in liquid detergent with and without DNase (SEQ ID NO: 1 )
Figure imgf000058_0001
The results in Table 1 show that overall, there was a clear preference among the panelists for the T-shirt samples that were washed using a DNase.
Example 2: Perfume retention on textile after wash in liquid detergent with a DNase
The T-shirt samples which were evaluated by the panelists as described in Example 1 were further used for GC-MS analysis. Headspace SPME-GC-MS analysis of fragrances from the commercial detergent on polyester T-shirts was performed using an Agilent 7890 gas chromatograph coupled to an Agilent 5977 mass spectrometry GC-MS system.
• GCMS Agilent 7890 GC with split/splitless injector and 5977 MS with extractor ion source coupled to a Gerstel MPS2 sampler with HS/SPME, SPME needle heater.
• The method used was: GC Oven Temperature: Initial 40°C; hold 2 min; Rate 5°C/min until 150°C; Rate 35°C/min until 240°C; Hold 3 min. Front SS Inlet He: Mode Split; Ta 230°C, Split Ratio 10:1 ; Split Flow 15 mL/min. Column: Agilent 19091 F-433: FFAP-01 HP-FFAP 30 m x 250 pm x 0.25 pm.
• Gerstel MPS SPME Incubator/ Agitator. Incubation Temperature: 60eC. Incubation Time: 10.00 min. Agitator Speed: 250 rpm. Sample parameters: Extraction Time: 2.00 min; Inj. Desorption Time: 120 s. • Fiber type: Carboxen/Polydimethylsiloxane (CAR/PDMS)
• MS Information: Acquisition Mode: Scan. Solvent Delay (minutes): 1. Scan Parameters: Start Time: 1 . Low Mass: 35. High Mass: 350. Threshold: 100. A/D Samples: 4. MSZones: MS Source: 230eC. MS Quad: 150eC
Table 2. Fragrance intensity on polyester T-shirts washed in a liquid detergent with or without
DNase (SEQ ID NO: 1 )
Figure imgf000059_0001
Example 3: Sensory evaluation of perfume retention after wash in a powder detergent with DNase
Polyester T-shirts were prepared in the same manner as described above in Example 1 . For this example, they were washed with a commercial powder detergent, Gut & Gunstig (McBride, Germany), in Ell front loader machines (Miele Novotronic, Model W 1935 WTL) using tap water from Bagsvaerd, Denmark with a water hardness of about 20°dH. The wash program, was Cotton, Short (1 h 49 min, 1600 rpm) with a wash temperature of 30°C. For washes with DNase, 2 ppm of the DNase (SEQ ID NO: 1 ) was added directly to the washing machine. After wash, all items were line dried overnight, and then stored refrigerated before analysis.
T-shirt armpit samples and remaining half T-shirts (weight 530g) prepared as described in Example 1 were washed together with 1400g of ballast consisting of 6 used half polyester T- shirts, 5 dirty half cotton pillowcases, 3 frotte wash cloths (20x20 cm), 3 half shirts (polyester), and 2 dirty half cotton T-shirts.
Three washes were performed as described in Example 1 , i.e. a blank wash with a clean T-shirt and detergent to provide a clean background sample, and washes with and without DNase. The sensory evaluation was performed as in Example 1 . The results of the sensory evaluation are provided in Table 3 below.
Table 3. Sensory results for 3 wash tests in powder detergent with and without DNase (SEQ ID NO: 1 )
Figure imgf000060_0001
Example 4: Perfume retention on textile after wash in powder detergent with a DNase
T-shirt samples that had been subjected to a sensory evaluated by test persons as described in Example 3 were further used for GC-MS analysis, which was performed as described in Example 2. The results are provided in Table 4 below. Table 4. Fragrance intensity on the polyester T-shirts washed with or without DNase in a powder detergent.
Figure imgf000061_0001
The sensory evaluation data provided above in Tables 1 and 3 demonstrates that test persons clearly preferred the fragrance of the polyester T-shirt samples that had been washed according to the invention with a detergent composition containing a DNase. This was the case for samples washed with both the liquid detergent under North American wash conditions and the powder detergent under European conditions.
Similarly, the GC-MS data in Tables 2 and 4 shows that that the fragrance intensity on polyester T-shirts was increased for a variety of different perfume compounds, and that this was the case using different detergents and different washing conditions, when the samples were washed according to the invention with a composition contained a DNase.
Example 5: Perfume retention on textile after rinse in fabric softeners containing a DNase
The evaluation of this example included the following steps:
Step 1 . Preparation of test items
Step 2. Rinse test in softeners with and without DNase
Step 3. GC-MS analysis of the rinsed items
Step 1 . Preparation of test items
Prewash
New polyester T-shirts as described above were first prewashed.
Prewash of textiles was done primarily to remove starch, carboxymethyl cellulose (CMC) and other additives from the textiles. Protease (Savinase® 16L, Novozymes A/S, Denmark), amylase (Stainzyme® 12L, Novozymes A/S) and cellulase (Celluclean® ST, Novozymes A/S) were added to the prewashes to remove these additives. The textiles were washed three times in 86.1 g/wash detergent W-ECE-2 (wfk Testgewebe GmbH, Germany) using water with 15°dH water hardness (3.00 mL of 0.713 mol/L CaCh, 1.50 mL of 0.357 mol/L MgCh and 0.3371 g of NaHCOs in 1 L deionized water) and containing the following enzymes:
Figure imgf000062_0001
Adding DNA to the swatches
The prewashed T-shirts were then cut into small round swatches with a diameter of 2 cm. To each swatch, 47 pl of 1% (w/v) deoxyribonucleic acid (DNA) solution was added at the center of the swatch. The DNA solution was made by dissolving 100 mg deoxyribonucleic acid sodium salt from salmon testes (Sigma Aldrich) in 10 ml MilliQ water in a 25 ml beaker with constant stirring for 1 h at room temperature.
The swatches containing the DNA solution were then dried overnight (16 h) at room temperature in a fume hood with constant air flow.
Step 2. Rinse test in softeners with and without DNase
Detergent
Model detergent A2 was used in the main wash of this experiment. A wash solution of liquid model detergent A2 was prepared by weighing out the detergent and dissolving in water with a hardness of 15°dH, with the model detergent A2 dosed at 3.33 g/L.
Model detergent A2 contains the following ingredients:
12% Sodium salt of linear alkylbenzene sulphonates (Na-LAS), 12% alcohol ethoxylate (AEG) Biosoft N25-7 (Nl), 4% alkyl ethoxysulfate / sodium laureth sulfate (AEOS/SLES), 2% MPG (monopropylene glycol), 3.1% ethanol, 2% triethanolamine (TEA), 3% palm kernel oil soap, 2% sodium hydroxide, 3.9% sodium citrate, 1.5% diethylenetriaminepenta(methylenephosphonic acid) (DTMPA) and 0.5% phenoxyethanol; remainder water (all percentages are w/w).
Softeners
Three representative commercial European fabric softeners were tested in this experiment: Dun-let Dream of Freshness (Colgate), Lenor Weichspuler Aprilfrisch (Procter & Gamble) and Bamseline Dugfrisk (Unilever). Lenor Weichspuler Aprilfrisch was purchased from amazon.de, and the other two softeners were purchased from a supermarket in Denmark.
Rinse solutions of the above three softeners were prepared by weighing out softeners and dissolving in water with 15°dH hardness. Dosing of the softeners was calculated according to the suggested dosage for each at standard conditions for a 4-5 kg wash load, which was 25 ml, 27 ml and 27 ml for Lenor Weichspuler Aprilfrisch, Dun-let Dream of Freshness and Bamseline Dugfrisk, respectively. Considering that the average volume of water used in one rinse step in a common Ell washing machine (machine size 3.5-5 kg laundry load) is 13.5 L, the dosing of each softener used in this experiment was 1.85 ml/L, 2.0 ml/L and 2.0 ml/L for Lenor Weichspuler Aprilfrisch, Dun-let Dream of Freshness and Bamseline Dugfrisk, respectively.
Main wash
The dried swatches from Step 1 were washed in a Mini Launder-O-Meter (MiniLOM) wash. The miniLOM assay is a small-scale version of the Launder-OMeter® (LOM). A miniLOM basically consists of closed test tubes being rotated in a heating cabinet for a given time and at a given temperature. Each test tube represents one small washing machine. It is mainly used in testing of detergents and enzymes at European wash conditions.
In this experiment, three swatches were placed in a 50-ml glass tube and 20 ml of wash solution (15° dH water with 3.15 g/L Model A2). To better mimic the wash performance of commercial detergents in Europe, an enzyme blend, Medley® Brilliant (Novozymes A/S, Denmark), was added to all glass tubes at a dosage of 2.5% of the detergent. The enzyme blend contains a variety of commonly used enzymes, including protease, amylase, lipase, mannanase, pectate lyase and two cellulases.
The glass tubes were then mounted in a Mini-Launder-O-Meter (a Stuart Tube Rotator SB3) and rotated at 30°C for 60 minutes at 30 rpm.
First rinse
After the main wash, the rotator was placed at room temperature, and the wash liquor was carefully poured out of each tube. 30 ml of hard water (15° dH water) was then added to each tube. The swatches were then rinsed in the miniLOM at room temperature for 30 min at 30 rpm.
Rinse test in softeners (second rinse)
After the first rinse, the rinse liquor was carefully poured out. 30 ml of rinse solution (softener dissolved in 15° dH water) was then added to each tube. Three replicates (one replicate/tube) were used for each rinse condition (softener/DNase combination). 1 .0 ppm DNase was added to the tubes, and tubes without DNase were included as controls. The swatches were then rinsed in the tubes in the miniLOM at room temperature for 30 min at 30 rpm.
Step 3. GC-MS analysis of the rinsed items
After washing and rinsing, each swatch was centrifuged in a falcon tube containing a filter (HOZELOCK K3 kaldness filters, Aquacadabra, eBay) at 4000g for 5 min to remove excess water. This plastic filter separated the excess water from the swatch after centrifuging.
The three swatches from the same glass tube were then placed in one 20 mL GC-MS vial (Mikrolab Aarhus A/S, Aarhus, Denmark) and capped with silicone screw top lids (Mikrolab Aarhus A/S, Aarhus, Denmark). All vials were then analyzed by GC-MS, as described in Example 2.
Results
This example showed that the fragrance intensity on polyester T-shirts was increased for a variety of different perfume compounds in all tested softeners when the samples were rinsed according to the invention with a composition contained a DNase (Tables 5, 6 and 7).
Table 5. Fragrance intensity on polyester T-shirts rinsed in Dun-let Dream of Freshness softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000064_0001
Figure imgf000065_0001
Figure imgf000066_0001
Table 6. Fragrance intensity on polyester T-shirts rinsed in Lenor Weichspuler Aprilfrisch softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000066_0002
Figure imgf000067_0001
Figure imgf000068_0001
Figure imgf000069_0001
Table 7. Fragrance intensity on polyester T-shirts rinsed in Bamseline Dugfrisk softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000069_0002
Figure imgf000070_0001
Figure imgf000071_0001
Figure imgf000072_0001
Figure imgf000073_0001
The above fragrances can be grouped into different perfume notes, i.e. top, heart or base notes based on their volatility as explained above in the description. It was found that the intensity of the heart note fragrances on polyester T-shirts was increased most in two of the three softeners, compared to the top notes and base notes, when the samples were rinsed according to the invention with a softener composition contained a DNase (Tables 8 and 9). As shown in Table, 9 however, this softener also resulted in a substantial increase in the top notes that was close to the increase observed for the heart notes. The third softener (Table 10) showed the largest increase in intensities in the top notes, compared to the heart notes and base notes, when the samples were rinsed in the softener containing a DNase.
Table 8. Fragrance intensity of different notes on polyester T-shirts rinsed in Dun-let Dream of
Freshness softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000073_0002
Table 9. Fragrance intensity of different notes on polyester T-shirts rinsed in Lenor Weichspuler
Aprilfrisch softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000073_0003
Table 10. Fragrance intensity of different notes on polyester T -shirts rinsed in Bamseline Dugfrisk softener with or without DNase (SEQ ID NO: 1 )
Figure imgf000074_0001

Claims

Claims
1 . Use of a polypeptide having DNase activity in a detergent composition for increasing binding of a perfume to a textile during a laundry process, for increasing perfume retention on a textile after wash, and/or for enhancing the effect of a perfume in a detergent composition, wherein the detergent composition comprises at least one perfume compound.
2. Use according claim 1 , wherein the polypeptide having DNase activity is selected from the group consisting of: a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3; b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to the polypeptide of SEQ ID NO: 6; c) a polypeptide comprising one or both of the motifs [D/M/L][S/T]GYSR[D/N] (SEQ ID
NO: 4) and/or ASXNRSKG (SEQ ID NO: 5) and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to any of the polypeptides of SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13,
SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18,
SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21 , SEQ ID NO: 22, SEQ ID NO: 23,
SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28,
SEQ ID NO: 29 or SEQ ID NO: 30; d) a polypeptide comprising one or both of the motifs [V/I]PL[S/A]NAWK (SEQ ID NO: 31 ) and/or NPQL (SEQ ID NO: 32) and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to any of the polypeptides of SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41 , SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44 or SEQ ID NO: 45; e) a polypeptide comprising one or both of the motifs P[Q/E]L[W/Y] (SEQ ID NO: 46) and/or [K/H/E]NAW (SEQ ID NO: 47) and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% sequence identity to any of the polypeptides of SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51 , SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59 or SEQ ID NO: 60; f) a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 61 ; and g) a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the polypeptide of SEQ ID NO: 62. Use according to claim 2, wherein the polypeptide having DNase activity has at least 80%, at least 85%, at least 90% or at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3; or at least 80%, at least 85%, at least 90% or at least 95% sequence identity to the polypeptide of SEQ ID NO: 6. Use according to claim 3, wherein the polypeptide having DNase activity comprises a substitution at one or more positions corresponding to positions 4, 17, 19, 36, 38, 39, 40, 41 , 45, 51 , 53, 54, 55, 57, 64, 66, 67, 68, 69, 70, 71 , 72, 74, 75, 77, 82, 83, 84, 85, 86, 88, 91 , 99, 101 , 105, 106, 115, 1 16, 135, 136, 138, 139, 140, 141 , 151 , 152, 153, 154, 162, 163, 164, 166, 168, 169, 173, 182, 183, 184, 185, 186, 189, 212 and 215 of SEQ ID NO: 1 , and wherein the polypeptide has at least 80%, at least 85%, at least 90% or at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3. Use according to claim 4, wherein the polypeptide having DNase activity comprises one or more substitutions selected from the group consisting of N4E, L17E, T19A, T19G, T19I, K36P, Q38P, S39V, S39R, A40P, A40H, L41 T, L41 H, V45H, L51 G, K53T, K53P, G54P, A55P, N57H, E64A, E64Q, E64R, E64T, E64I, E64S, T66H, K67A, K67T, N68V, N68P, N68I, N68H, S69A, S69D, S69E, S69K, S69L, S69W, S69Y, S69Q, N70T, N70H, N70G, R71 T, D72E, S74H, S74G, G75I, N77T, K82P, K82I, D83T, D83P, D83I, D83H, D83G, P84H, Q85T, Q85P, Q85H, K86T, K86P, K86H, G88P, G88H, A91 P, W99T, A101 W, K105E, K105N, K105T, K105D, S106T, S1 15T, L116I, Q135L, G136L, V138I, V138L, V138P, V138Q, L139A, N140R, N140L, N140A, G141 L, F151 R, D152Y, D152L, D152I, D152A, P153E, S154R, T162R, W163E, F164R, I166Y, I166R, K168N, F169R, F169E, A173I, A173R, A173T, S182R, N183E, D184I, K185Y, S186I, D189G, D189H, K212G, K212P and K215I, wherein numbering is based on SEQ ID NO: 1 , and wherein the polypeptide has at least 80%, at least 85%, at least 90% or at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 3. Use according to any of the preceding claims, wherein the detergent composition is a laundry detergent composition or a fabric softener.
75
7. Use according to any of the preceding claims, wherein the polypeptide having DNase activity results in an increase in binding and/or retention of top note and/or heart note perfume compounds on a textile compared to base note compounds.
8. A method for increasing binding of a perfume to a textile during a laundry process and/or for increasing perfume retention on a textile in a laundry process after washing, the method comprising washing the textile with a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity, wherein the polypeptide is as defined in any of claims 2-5.
9. A method for enhancing the effect of a perfume in a detergent composition, the method comprising preparing a detergent composition comprising at least one perfume compound and a polypeptide having DNase activity, wherein the polypeptide is as defined in any of claims 2-5.
10. A method for preparing a detergent composition with reduced perfume content but with maintained perfume effect after wash relative to a comparable composition without DNase, the method comprising mixing at least one perfume compound, a polypeptide having DNase activity and at least one detergent component, wherein the polypeptide is as defined in any of claims 2-5.
1 1 . The method of any of claims 8-10, wherein the detergent composition is a laundry detergent composition or a fabric softener.
12. The method of any of claims 8-11 , wherein the polypeptide having DNase activity results in an increase in binding and/or retention of top note and/or heart note perfume compounds compared to base note compounds.
13. A detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, wherein the polypeptide is as defined in any of claims 2-5, and wherein the composition has an increased perfume effect relative to a comparable detergent composition without a polypeptide having DNase activity.
14. The detergent composition of claim 13, wherein the composition is a laundry detergent composition, and wherein the composition has increased perfume retention on a textile after wash relative to a comparable detergent composition without a polypeptide having DNase
76 activity; or wherein the composition is a fabric softener, and wherein the composition has increased perfume retention on a textile after rinse relative to a comparable fabric softener without a polypeptide having DNase activity. 15. A method for cleaning an item, wherein the item is preferably a textile, comprising the steps of: a) contacting the item with a wash liquor comprising a detergent composition comprising a polypeptide having DNase activity and at least one perfume compound, wherein the polypeptide is as defined in any of claims 2-5, and optionally b) rinsing the item.
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CN117070394A (en) * 2023-04-20 2023-11-17 广东药科大学 Alkalophilic strain for producing alkaline protease, alkaline protease and application thereof
WO2024046952A1 (en) * 2022-08-30 2024-03-07 Novozymes A/S Improvements in or relating to organic compounds

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