WO2020074498A1 - Compositions de nettoyage et leurs utilisations - Google Patents

Compositions de nettoyage et leurs utilisations Download PDF

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Publication number
WO2020074498A1
WO2020074498A1 PCT/EP2019/077196 EP2019077196W WO2020074498A1 WO 2020074498 A1 WO2020074498 A1 WO 2020074498A1 EP 2019077196 W EP2019077196 W EP 2019077196W WO 2020074498 A1 WO2020074498 A1 WO 2020074498A1
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Prior art keywords
seq
sequence identity
amylase
protease
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PCT/EP2019/077196
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English (en)
Inventor
Klaus GORI
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Novozymes A/S
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Priority to EP19782617.5A priority Critical patent/EP3864122A1/fr
Publication of WO2020074498A1 publication Critical patent/WO2020074498A1/fr

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    • 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
    • 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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase

Definitions

  • the present invention relates to compositions such as cleaning compositions comprising a mix of enzymes.
  • the invention further relates, use of compositions comprising such enzymes in cleaning processes and/or for deep cleaning of organic stains, methods for removal or reduction of components of organic matter.
  • Enzymes have been used in detergents for decades. Usually a cocktail of various enzymes is added to detergent compositions.
  • the enzyme cocktail often comprises various enzymes, wherein each enzyme targets it specific substrate e.g. amylases are active towards starch stains, proteases on protein stains and so forth.
  • One type of stains may be associated with organic matter such as stains from body soiling e.g. skin cell debris, sebum, sweat, biofilm, EPS, etc.
  • Organic matter or stains may compose of different organic molecules such as polysaccharides, extracellular DNA (exDNA), starch and proteins.
  • Organic matter may be poly-organic stains composing different organic stains.
  • Some organic matter or stains composes an extracellular polymeric matrix, which may be sticky or glueing, which when present on textile, attracts soils and may course redeposition or backstaining of soil resulting in a greying of the textile.
  • organic matters or stains such as biofilms often cause malodor issue as various malodor molecules can be adhered by the polysaccharides, extracellular DNA (exDNA), and proteins in the complex extracellular matrix and be slowly released to cause consumer noticeable malodor issue.
  • cleaning compositions which effectively prevent, reduce or remove stains e.g. associated with poly- organic stains e.g. biofilm, such as starch, mannan, protein and DNA.
  • the present invention provides new compositions fulfilling such need.
  • SEQ ID NO 2 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 3 mature polypeptide obtained from Cytophaga sp.
  • SEQ ID NO 4 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 5 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 7 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 8 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 10 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 14 mature polypeptide obtained from Thermomyces lanuginosus
  • SEQ ID NO 15 mature polypeptide obtained from Bacillus bogoriensis
  • SEQ ID NO 16 mature polypeptide obtained from Paenibacillus woosongensis
  • SEQ ID NO 17 mature polypeptide obtained from Paenibacillus illinoisensis
  • SEQ ID NO 18 mature polypeptide obtained from Neobulgaria sp.
  • SEQ ID NO 19 mature polypeptide obtained from Preussia aemulans
  • SEQ ID NO 21 mature polypeptide obtained from Myrothecium roridum
  • SEQ ID NO 23 mature polypeptide obtained from Ascobolus stictoideus
  • SEQ ID NO 24 mature polypeptide obtained from Chaetomium virescens
  • SEQ ID NO 25 mature polypeptide obtained from Bacillus lentus
  • SEQ ID NO 26 mature polypeptide obtained from Bacillus amyloliquefaciens
  • SEQ ID NO 27 mature polypeptide obtained from Bacillus sp.
  • SEQ ID NO 28 mature polypeptide obtained from Bacillus gibsonii
  • SEQ ID NO 29 mature polypeptide obtained from Bacillus lentus
  • SEQ ID NO 30 mature polypeptide obtained from Bacillus licheniformis
  • SEQ ID NO 31 mature polypeptide obtained from Paenibacillus polymyxa
  • SEQ ID NO 33 mature polypeptide obtained from Paenibacillus species
  • a first aspect of the invention relates to a cleaning composition
  • a cleaning composition comprising a DNase 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%, at least 98% or 100% sequence identity to the DNase shown in SEQ ID NO 1 , at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases, and at least one cleaning component.
  • a second aspect of the invention relates to the use of a cleaning composition
  • a cleaning composition comprising a DNase 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%, at least 98% or 100% sequence identity to the DNase shown in SEQ ID NO 1 , at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases, and at least one cleaning component for deep cleaning of an item, wherein the item is a textile or a surface.
  • a third aspect of the invention relates to a method of formulating a cleaning composition
  • a DNase 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%, at least 98% or 100% sequence identity to the DNase shown in SEQ ID NO 1 , at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases, and at least one cleaning component, comprising adding a DNase, at least one additional enzyme and at least one cleaning component.
  • a fourth aspect of the invention relates to a kit intended for deep cleaning, wherein the kit comprises a solution of an enzyme mixture comprising a DNase and at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases.
  • a fifth aspect a method of deep cleaning of an item, comprising the steps of:
  • a) contacting the item with a cleaning composition comprising a DNase 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%, at least 98% or 100% sequence identity to the DNase shown in SEQ ID NO 1 , at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases, and at least one cleaning component; and
  • Amylases are enzymes which catalyze the hydrolysis of starch, glycogen, and related polysaccharides to oligosaccharides, maltose, or glucose. Amylases are glycoside hydrolases and act on a-1 ,4-glycosidic bonds.
  • the amylases suitable in the cleaning compositions of the invention are preferably alpha amylases oamylases (EC 3.2.1 .1 ) includes 1 ,4-oD-glucan glucanohydrolase and glycogenase and are calcium metalloenzymes.
  • amylases of the present invention are preferably microbial e.g. obtained from bacterial or fungal sources.
  • alpha-amylase activity means the activity of alpha 1 ,4-glucan 4 glucanohydrolases, E.C. 3.2.1.1 , which constitute a group of enzymes, which catalyze hydrolysis of starch and other linear and branched 1 ,4 alpha-glucosidic oligo and poly-saccharides.
  • Alpha-amylase activity may be determined by Assay III as described in the Examples herein.
  • Biofilm is 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.
  • On laundry biofilm producing bacteria can be found among the following species: Acinetobactersp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp.
  • biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, Staphylococcus aureus and Stenotrophomonas sp.
  • Cellulolytic enzyme or cellulase means one or more
  • enzymes that hydrolyze a cellulosic material.
  • Such enzymes include endoglucanase(s), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof.
  • the two basic approaches for measuring cellulolytic activity include: (1 ) measuring the total cellulolytic activity, and (2) measuring the individual cellulolytic activities (endoglucanases, cellobiohydrolases, and beta-glucosidases) as reviewed in Zhang et al., Outlook for cellulase improvement: Screening and selection strategies, 2006, Biotechnology Advances 24: 452-481.
  • Total cellulolytic activity is usually measured using insoluble substrates, including Whatman N°1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc.
  • the most common total cellulolytic activity assay is the filter paper assay using Whatman N°1 filter paper as the substrate.
  • the assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Measurement of cellulase activities, Pure Appl. Chem. 59: 257-68).
  • Cellulases includes enzymes that catalyzes the hydrolysis of the 1 ,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans.
  • cellulase includes endo-1 ,4-beta-D-glucanase (beta-1 ,4-glucanase, beta-1 ,4-endoglucan hydrolase, endoglucanase D, 1 ,4-(1 ,3,1 ,4)-beta-D-glucan 4- glucanohydrolase) and carboxymethyl cellulase.
  • Cellulases includes endo-cellulases (EC 3.2.1 .4) which randomly cleave internal bonds at amorphous sites that create new chain ends and exocellulases (EC 3.2.1 .91 ) that cleave two to four units from the ends of the exposed chains produced by endocellulase, resulting in tetrasaccharides or disaccharides, such as cellobiose. Exocellulases are further classified into type I, that work processively from the reducing end of the cellulose chain, and type II, that work processively from the nonreducing end. 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.
  • Cellulases include enzymes having xyloglucanase activity Cellulase activity may be determined as described in Assay IV in the Examples herein.
  • Cellulosic material means any material containing cellulose.
  • the predominant polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemicellulose, and the third is pectin.
  • the secondary cell wall, produced after the cell has stopped growing, also contains polysaccharides and is strengthened by polymeric lignin covalently cross-linked to hemicellulose.
  • Cellulose is a homopolymer of anhydrocellobiose and thus a linear beta-(1 -4)-D-glucan, while hemicelluloses include a variety of compounds, such as xylans, xyloglucans, arabinoxylans, and mannans in complex branched structures with a spectrum of substituents. Although generally polymorphous, cellulose is found in plant tissue primarily as an insoluble crystalline matrix of parallel glucan chains. Hemicelluloses usually hydrogen bond to cellulose, as well as to other hemicelluloses, which help stabilize the cell wall matrix.
  • the cleaning component e.g. the detergent adjunct ingredient is different to the DNase and additional enzymes.
  • additional cleaning components e.g. 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 cleaning components e.g.
  • adjunct materials include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, 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, builders and co-builders, fabric huing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • surfactants builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, 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
  • cleaning composition refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles and hard surfaces.
  • the cleaning composition may be used to e.g. clean textiles or hard surfaces (e.g. dishes) for both household cleaning and industrial cleaning.
  • the terms encompass any materials/compounds selected for the particular type of cleaning 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 (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre- spotters/pretreatment).
  • the cleaning composition may contain e.g. 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, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • 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, transferase(s), hydrolytic enzymes, oxido
  • DNases are polypeptides with DNase (deoxyribonuclease) activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA. Exodeoxyribonuclease cut or cleaves residues at the end of the DNA back bone where endo- deoxyribonucleases cleaves or cut within the DNA backbone.
  • a DNase may cleave only double- stranded DNA or may cleave double stranded and single stranded DNA.
  • the term“DNases” and the expression“a polypeptide with DNase activity” may be used interchangeably throughout the application.
  • DNase activity is determined according to the procedure described in the Assay I or Assay II.
  • the DNase is selected from any of the enzyme classes E.C.3.1 , preferably E.C.3.1 .21.
  • the polypeptide having DNase activity is obtained from a microorganism and the DNase is a microbial enzyme.
  • the DNase is preferably of fungal or even more preferably of bacterial origin.
  • deep cleaning is meant reduction, disruption or removal of components, which may be comprised in organic matter, e.g. skin debris, dead cell material, sebum, sweat and biofilm, such as polysaccharides, grease, proteins, starch, DNA, soil or other components present in the organic matter.
  • organic matter e.g. skin debris, dead cell material, sebum, sweat and biofilm, such as polysaccharides, grease, proteins, starch, DNA, soil or other components present in the organic matter.
  • the organic matter may be termed poly-organic stains comprising more than one organic component such as starch, grease, protein, DNA and mannan.
  • enzyme detergency benefit is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme.
  • Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and/or cleaning, prevention or reduction of redeposition of soils released in the washing process (an effect that also is termed anti-redeposition), restoring fully or partly the whiteness of textiles which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance (an effect that also is termed whitening).
  • Textile care benefits which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits.
  • Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric (an effect that is also termed dye transfer inhibition or anti- backstaining), removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the fabric-softness, colour clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment.
  • Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.
  • Textile care benefits which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits.
  • textile care benefits are prevention or reduction of dye transfer from one textile to another textile or another part of the same textile (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a textile surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the textile- softness, colour clarification of the textile and removal of particulate soils which are trapped in the fibers of the textile.
  • Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching component such as hydrogen peroxide or other peroxides or other bleaching species.”
  • hard surface cleaning is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash). Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.
  • 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.
  • Lipases includes enzymes which catalyze the hydrolysis of fats (lipids). Lipases are a sub class of esterases. Lipases suitable in the present invention include phospholipases, acyltransferases or perhydrolases e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M.
  • acyltransferases with homology to Candida antarctica lipase A (WO10/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M.
  • 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 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 (W010/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W01 1/084412), Geobacillus stearothermophilus lipase (W01 1/084417), lipase from Bacillus subtilis (W01 1/084599), and lipase from Streptomyces griseus (W01 1/150157) and S. pristinaespiralis (W012/137147). Lipase activity may be determined as described in Assay V in the Examples herein.
  • malodor is meant an odor which is not desired on clean items.
  • malodor is compounds with an unpleasant smell, which may be produced by microorganisms.
  • unpleasant smells 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 sticks to items for example curry or other exotic spices which smells strongly.
  • Mannanases include enzymes that catalyzes the hydrolysis of mannans, which is a highly branched polymer of mannose.
  • the mannanases of the invention are preferably of microbial origin such as bacterial or fungal mannanases.
  • the mannanase preferably having mannan endo-1 ,4-beta-mannosidase activity (EC 3.2.1 .78) that catalyzes the hydrolysis of 1 ,4- 3-D-mannosidic linkages in mannans, galactomannans and/or glucomannans.
  • the mannanase may be a GH5 mannanase such as an endo-1 ,4-3-Mannanase or a GH26 endo-1 ,4 b- Mannanase. Mannanase activity may be determined as described in Assay VI in the Examples herein.
  • mature polypeptide means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc.
  • Proteases includes enzymes that hydrolyze peptide bonds and the term incudes peptidase and proteinase.
  • Serine proteases or serine endopeptidases
  • E.C. 3.4.21 are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the active site.
  • Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. Most relevant proteases for laundry may be the alkaline proteases, such as a serine protease.
  • a serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin.
  • a metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloproteases such as those from M5,
  • subtilases refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991 ) 719-737 and Siezen et al. Protein Science 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 6 sub- divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • Protease activity may be determined as described in Assay VII in the Examples herein.
  • 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 et al., 2000, Trends Genet. 16: 276-277), preferably version 6.6.0 or later.
  • the parameters used are a gap open penalty of 10, a 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:
  • 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).
  • 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.
  • 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. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing 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 the activity of the parent or precursor polypeptide and comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions compared to the precursor or parent polypeptide.
  • 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 performance is used as an enzyme’s ability to remove stains present on the object to be cleaned during e.g. wash or hard surface cleaning.
  • whiteness is defined herein as a greying, yellowing of a textile. Loss of whiteness may be due to removal of optical brighteners/hueing agents. Greying and yellowing can be due to soil redeposition, body soils, colouring from e.g. iron and copper ions or dye transfer. Whiteness might include one or several issues from the list below: colourant or dye effects; incomplete stain removal (e.g. body soils, sebum etc.); redeposition (greying, yellowing or other discolourations of the object) (removed soils reassociate with other parts of textile, soiled or unsoiled); chemical changes in textile during application; and clarification or brightening of colours.
  • the nomenclature“E/Q” or EQ means that the amino acid at a given 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 (Val, 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 amino acid present in a parent sequence), the position number, and the replacement amino acid.
  • A226V indicates that the alanine residue in position 226 has been replaced by a valine residue.
  • Different parent enzymes may have different amino acids in the position corresponding to position 226 of the parent sequence.
  • A226V is not limited to substitutions of alanine. Any amino acid may be replaced in the substitution, which may also be indicated with an X as X226V. Both annotations may be used interchangeably.
  • the substitution A226V may also be written e.g. enzyme X comprising valine at a position corresponding to position 226 of SEQ ID NO XX.
  • 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.
  • commas e.g. T51 I, S52Q, N54K, meaning that one or more maybe all of the listed mutations may be present. Thus, meaning the above example that either one, two or three (thus all) of the mutations may present compared to the parent enzyme.
  • mutations in alteration sets are separated by commas this means that all the alterations in the set are present and the selection is between the lists of alterations (alteration sets).
  • alteration sets E.g.“comprising one of the alterations sets selected from the group consisting of
  • SEQ ID NO XX + mutation(s) is to be understood as variants of an enzyme parent comprising specified mutations compared to the specific parent sequence.
  • corresponding to reflects the numbering system used and that various starting proteases (parent proteases) may have different length.
  • a given starting amylase is aligned with e.g. SEQ ID NO 2 and the position corresponding to e.g. pos 140 is determined.
  • parent enzyme includes terms such as reference enzyme, back bone or starting enzyme and is used to denote the enzyme into which to mutations e.g. substitutions are made.
  • the terms may be used interchangeably
  • the invention relates to cleaning compositions comprising a DNase and an additional cleaning enzyme e.g. an enzyme providing enzyme detergency benefit as described in“definitions” in combination with one or more cleaning composition component.
  • the DNase and the at least one additional enzyme preferably act synergistically to remove components such as skin debris, dead cells, components of biofilm, biofilm EPS and other organic components from e.g. poly-organic stains.
  • One embodiment of the invention relates to a cleaning composition comprising a DNase, a cleaning enzyme selected from the group consisting of an amylases, a cellulase, a lipase, a mannanase and a protease, and at least one cleaning component.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase 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%, at least 98% or 100% sequence identity to the DNase shown in SEQ ID NO 1 , at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases and proteases, and at least one cleaning component, wherein the amylases, cellulases, lipases, mannanases and proteases provide at least one enzyme detergency benefit.
  • Particularly useful DNases may be those of microbial origin.
  • the cleaning composition comprise a DNase from bacteria.
  • One embodiment of the invention relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cleaning enzyme selected from an amylase, a cellulase, a lipase, a mannanase and a protease and at least one cleaning component, wherein the DNase is obtained from Bacillus, preferably Bacillus cibi.
  • the term“obtained from” as used herein in connection with a given source shall mean that the enzyme of the invention is produced by the source or by a strain in which the polynucleotide encoding the enzyme of the invention from the source has been inserted. In one aspect, the enzyme obtained from a given source is secreted extracellularly.
  • One embodiment of the invention relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cleaning enzyme selected from an amylase, a cellulase, a lipase, a mannanase and a protease and at least one cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 .
  • the term cleaning enzyme means an enzyme with cleaning benefits e.g. enzyme detergency benefit.
  • One preferred cleaning enzyme to be combined with the DNase enzyme is an amylase in particular an alpha-amylase (alpha-1 ,4-glucan-4-glucanohydrolases, E.C. 3.2.1.1 ).
  • Amylases catalyzes hydrolysis of starch and other linear and branched 1 ,4-gluosidic oligo- and polysaccharides.
  • Amylases have several applications such as detergent, baking, brewing, starch liquefaction and saccharification e.g. in preparation of high fructose syrups or as part of ethanol production from starch.
  • An alpha-amylase useful in a cleaning composition of the invention is preferably an enzyme classified under EC 3.2.1.1.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an amylase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the amylase is classified under EC 3.2.1.1.
  • the alpha-amylase may be bacterial or fungal.
  • a bacterial alpha-amylase to be used in a composition according to the invention may, e.g., be derived from a strain of the genus Bacillus, which is sometimes also referred to as the genus Geobacillus.
  • Bacillus alpha-amylase is derived from a strain of B. amyloliquefaciens, B. licheniformis, B. stearothermophilus, B. halmapalus, or B. subtilis, but may also be derived from another Bacillus sp. e.g. Bacillus TS-23 is described in WO2014/195356.
  • the amylases may also be obtained from bacteria such as Cytophaga.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an amylase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the amylase is obtained from Bacillus e.g. B. amyloliquefaciens, B. licheniformis, B. stearothermophilus, B. halmapalus, or B. subtilis, Bacillus TS-23 or from Cytophaga.
  • Bacillus e.g. B. amyloliquefaciens, B. licheniformis, B. stearothermophilus, B. halmapalus, or B. subtilis, Bacillus TS-23 or from Cytophaga.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an amylase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the amylase is selected from the group consisting of;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 2 or SEQ ID NO 35, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 2 or SEQ ID NO 35 comprising one of the alterations set selected from the group consisting of:
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 3, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 3, comprising one of the alterations set selected from the group consisting of:
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 4, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 4, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184 compared to SEQ ID NO 4, wherein each position corresponds to the position in SEQ ID NO 4;
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 4, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 4 comprising an alteration at one or more, preferably at all of the position(s) selected from 3, 4, 5, 74, 1 18, 167, 170, 177, 195, 202, 204, 271 , 320, 330, 377, 385, 445, 458, 475, 476, 314, 315 or 316, compared to SEQ ID NO 4, wherein each position corresponds to the position in SEQ ID NO 4;
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 6, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 6, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184, compared to SEQ ID NO 6, wherein each position corresponds to the position in SEQ ID NO 6;
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 6, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 6, comprising one of the alterations set selected from the group consisting of
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 7, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 7, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184, compared to SEQ ID NO 7, wherein each position corresponds to the position in SEQ ID NO 7;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 8, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 8, comprising a two amino acid deletion in the sequence region R181 , G182, H183, G184, compared to SEQ ID NO 8, wherein each position corresponds to the position in SEQ ID NO 8;
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 8, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 8, comprising one of the alterations set selected from the group consisting of
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 9, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 9, comprising a two amino acid deletion in the sequence region R181 , G182, G182, D183, compared to SEQ ID NO 9, wherein each position corresponds to the position in SEQ ID NO 9;
  • an amylase 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%, at least 98% or 100% sequence identity to SEQ ID NO 9, or an amylase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 9, comprising one of the alterations set selected from the group consisting of
  • One preferred cleaning enzyme to be combined with the DNase enzyme is a cellulase in particular an enzyme exhibiting endo-beta-1 ,4-glucanase activity.
  • Cellulose is a polymer of glucose linked by beta-1 ,4-glucosidic bonds. Cellulose chains form numerous intra- and intermolecular hydrogen bonds, which results in the formation of insoluble cellulose micro-fibrils.
  • Microbial hydrolysis of cellulose to glucose involve three major classes of cellulases: (i) endo- glucanases (EC 3.2.1 .4) which cleave beta-1 ,4-glucosidic links randomly throughout cellulose molecules, also called endo-beta-1 ,4-glucanases; (ii) cellobiohydrolases (EC 3.2.1 .91 ) which digest cellulose from the non-reducing end, releasing cellobiose; and (iii) beta-glucosidases (EC
  • the cellulases useful in the cleaning composition of the invention are preferably endo- glucanases (EC 3.2.1 .4). Beta-1 ,4-glucosidic bonds are also present beta-glucans from plants such as barley and oats. In some cases, endo-glucanases also provide hydrolysis of such non- cellulose polymers.
  • the cellulases are placed into different families of glycosyl hydrolases; fungal and bacterial glycosyl hydrolases have been grouped into 35 families (Henrissat, B.: A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280
  • cellulases comprises or consists of a cellulose-binding domain (CBD) and a catalytic domain
  • CAD CAD separated by a linker which may be rich in proline and hydroxy amino acid residues.
  • CBDs (Gilkes et al. (1991 )) giving five families of glycosyl hydrolases (l-V).
  • Cellulases are synthesized by a large number of microorganisms which include fungi, actinomycetes, myxobacteria and true bacteria but also by plants. Especially endo-beta-1 ,4-glucanases of a wide variety of specificities have been identified. Many bacterial endo-glucanases have been described (Gilbert, H.J. and Hazlewood, G.P. (1993) J. Gen. Microbiol. 139:187-194. Henrissat, B., and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
  • One preferred cellulase includes endo-beta-1 ,4-glucanase activity (EC 3.2.1 .4), preferably obtained from Bacillus sp. AA349 (DSM 12648), as described in W02002/099091 .
  • Other cellulases that are endo-beta-1 ,4- glucanase enzyme includes the cellulase shown in SEQ ID NO 10
  • Other preferred cellulases include those described in W01996/029397, which discloses family 45 endoglucanases e.g.
  • Thielavia in particular a strain of Thielavia terrestris and the cellulases described in W01991/017243, which discloses endoglucanases from e.g. of Humicola such as Humicola insolens.
  • Suitable cellulases include those from the genera Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium.
  • Exemplary cellulases include a fungal cellulase from Humicola insolens (US 4,435,307) or from Trichoderma, e.g. T reesei or T viride.
  • Other suitable cellulases are from Thielavia e.g.
  • Thielavia terrestris as described in WO 96/29397 or the fungal cellulases produced from Myceliophthora thermophila and Fusarium oxysporum disclosed in US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89/09259 and WO 91/17244.
  • cellulases from Bacillus as described in WO 02/099091 and JP 2000210081. Suitable cellulases are alkaline or neutral cellulases having care benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96/1 1262, WO 96/29397, WO 98/08940.
  • 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.
  • Cellulases includes a family 44 xyloglucanase, which a xyloglucanase enzyme such as the xyloglucanase shown in SEQ ID NO 31.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase belongs to (EC 3.2.1 .4), (EC 3.2.1 .91 ) or (EC 3.2.1 .21 ).
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ I D NO 1 , wherein the cellulase is obtained from Thielavia, Humicola, Paenibacillus or Melanocarpus preferably Thielavia terrestris, Humicola insolens, Paenibacillus polymyxa or Melanocarpus albomyces
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase is selected from the group consisting of;
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 10;
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 1 1 ;
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 12
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 13,
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 31 , and
  • a cellulase 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%, at least 98% or 100% sequence identity to SEQ ID NO 32.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 10, and is preferably obtained from Bacillus.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 12, and is preferably obtained from Humicola e.g. Humicola insolens.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 13, and is preferably obtained from Thielavia e.g. Thielavia terrestris.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 31 , and is preferably obtained from Paenibacillus e.g. Paenibacillus polymyxa.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a cellulase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least
  • Melanocarpus e.g. Melanocarpus albomyces
  • One preferred cleaning enzyme to be combined with the DNase enzyme is a lipase.
  • Lipases are enzymes that catalyzes the hydrolysis of fats (lipids). Lipases are used in detergents for removal of grease stains. Lipases E.C. 3.1.1. are a subclass of the esterases E.C. 3.1 .
  • 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
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a lipase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the lipase belongs to E.C. 3.1.1 .
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a lipase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the lipase is obtained from Thermomyces, e.g. from T. lanuginosus, Pseudomonas e.g. P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. sp. strain SD705, P.
  • Thermomyces e.g. from T. lanuginosus
  • Pseudomonas e.g. P. alcaligenes or P. pseudoalcaligenes
  • P. cepacia P. sp. strain SD705, P.
  • wisconsinensis Pseudomonas mendocina, Streptomyces, Magnaporthe e.g. M. grisea, Thermobifida e.g. T. fusca, Geobacillus e.g. . G. stearothermophilus, Bacillus e.g. B. subtilis, Streptomyces e.g. S. griseus or S. pristinaespiralis.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an lipase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1
  • the lipase is a lipase 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%, at least 98% or 100% sequence identity to SEQ ID NO 14, or a lipase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 14 comprising one or more of the substitutions selected from the group consisting of D27R, G38A, G91A/Q,
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an lipase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the lipase is a lipase 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 14, wherein the lipase comprises one or both the substitutions T231 R and/or N233R, wherein the position corresponds to the positions of SEQ ID NO 14.
  • mannanases are enzyme catalyzing hydrolyses of 1 ,4-beta-D-mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans.
  • Mannans are a type of hemicellulose representing up to 25% of wood dry weight in softwoods, but are also found in other plant material, especially in a variety of seeds. Mannans are polysaccharides with a backbone of b-1 ,4-linked D-mannopyranosyl residues, which can contain galactose or acetyl substitutions and may have glucose residues in the backbone.
  • the main enzyme type participating in the degradation of mannans are endo-1 ,4-3-mannanases (EC 3.2.1 .78), which hydrolyze the internal glycoside bonds in the mannan backbone.
  • the present invention provides a cleaning composition comprising a DNase and a mannanase enzyme comprising a polypeptide having mannan endo-1 ,4-beta-mannosidase activity (EC 3.2.1 .78) that catalyzes the hydrolysis of 1 ,4-3-D-mannosidic linkages in mannans, galactomannans and/or glucomannans.
  • endo-1 ,4-3-mannanases can be found in glycoside hydrolyase families 5, 26 and 1 13.
  • Couturier et al. have reported a GH26 mannanase from Podospora anserina having 56.1 % and 76.4% identity to SEQ ID NO: 3 and 6 respectively in (2013),“Structural and Biochemical Analyses of Glycoside Hydrolase Families 5 and 26-(1 ,4)- Mannanases from Podospora anserina Reveal Differences upon Manno-oligosaccharide Catalysis”, J. Biol. Chem., 288(20): 14624-14635.
  • Preferred mannanases include the GH5 mannanase obtained from Bacillus bogoriensis described in W01999/064619 or any of the GH26 Mannanases, mannanase from Preussia aemulans WO 2017/021515 (SEQ ID NO 2), mannanase from Yunnania penicillata W02017/021516 (SEQ ID NO 2), mannanase from Myrothecium roridum W02017/021517 (SEQ ID NO 2), mannanase from Chaetomium brasiliense W02017/021518 (SEQ ID NO 2), mannanases from Ascobolus stictoideus or mannanase from Chaetomium virescens SEQ ID NO 3 and 6 from WO2015/040159.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase belongs to EC 3.2.1 .78.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase is a GH5 or a GH26 mannanase.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase is obtained from Bacillus e.g. B. bogoriensis or hemicellulosilyticus, Paenibacillus e.g. P. woosongensis or P. illinoisensis, Neobulgaria sp., Preussia e.g. P.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase is selected from the group consisting of;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 15;
  • mannanase wherein the mannanase preferably belongs to the Glycoside Hydrolase Family 26 mannanases;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 16;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 17;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 18;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 19;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 20;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 21 ;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 22;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 23;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 24;
  • x. a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 33;
  • a mannanase 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%, at least 98% or 100% sequence identity to SEQ ID NO 34.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 15, and preferably is obtained from Bacillus e.g. Bacillus bogoriensis.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 16, and preferably is obtained from Paenibacillus e.g. Paenibacillus woosongensis
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 17, and preferably is obtained from Paenibacillus e.g. Paenibacillus illinoisensis.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 18, and preferably is obtained from Neobulgaria sp.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 19, and preferably is obtained from Preussia e.g. Preussia aemulans.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 20, and preferably is obtained from Yunnania e.g. Yunnania penicillate.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 21 , and preferably is obtained from Myrothecium e.g. Myrothecium roridum.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 22, and preferably is obtained from Chaetomium e.g. Chaetomium Brasiliense.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 23, and preferably is obtained from Ascobolus e.g. Ascobolus stictoideus.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 24, and preferably is obtained from Chaetomium e.g. Chaetomium virescens.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 33, and preferably is obtained from Paenibacillus.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, an mannanase, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 34, and preferably is obtained from Bacillus e.g. Bacillus hemicellulosilyticus.
  • protease One preferred cleaning enzyme to be combined with the DNase enzyme is a protease.
  • protease are enzymes that hydrolyze peptide bonds.
  • the most frequently used protease for household care segment is the serine proteases (or serine endopeptidases), E.C. 3.4.21 , which are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the active site.
  • Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred.
  • the protease is a subtilase and even more preferably the protease belongs to the subtilisin sub group of subtilases.
  • proteases used in the cleaning industry today are obtained from Bacillus e.g. Bacillus lentus and Bacillus amyloliquefaciens.
  • One embodiment of the invention relates to a cleaning composition comprising a DNase, a protease and at least one cleaning component, wherein the protease is obtained from Bacillus preferably from Bacillus lentus, Bacillus amyloliquefaciens, Bacillus gibsonii, Bacillus licheniformis, Bacillus pumilus, Bacillus halodurans or Bacillus subtilis.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a protease, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the protease belongs to E.C. 3.4.21 .
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a protease, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the protease is obtained from Bacillus preferably from Bacillus lentus, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus, Bacillus halodurans or Bacillus subtilis.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, a protease, and a cleaning component, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 1 , wherein the protease is selected from the group consisting of;
  • a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • SEQ ID NO 26 preferably obtained from Bacillus amyloliquefaciens
  • a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • SEQ ID NO 28 preferably obtained from Bacillus gibsonir ' , e) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • SEQ ID NO 30 preferably obtained from Bacillus licheniformis ; g) or a protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises the substitution T22R or T22A compared to SEQ ID NO 25, wherein the position corresponds to the position of SEQ ID NO 25;
  • a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • protease comprises one or more, preferably all the substitutions selected from the group consisting of: S3T, V4I, A188P and V199I, compared to SEQ ID NO 25, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all the substitutions selected from the group consisting of N114L, T207A, A226V, and E265F, compared to SEQ ID NO 25, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all substitutions selected from the group consisting of: S97D, S101A, V102I and G157S compared to SEQ ID NO 25, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all the substitutions selected from the group consisting of: S85N, G116V, S126L, P127Q and S128A compared to SEQ ID NO 25, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all the substitutions selected from the group consisting of: Y161A, R164S and A188P, compared to SEQ ID NO 25, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all the substitutions selected from the group consisting of: S3T, R19L, and A188P, wherein the positions correspond to the positions of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises one or more, preferably all the substitutions selected from the group consisting of: S9R, R19L, and N60D, wherein the positions correspond to the positions of SEQ ID NO 25;
  • a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • protease comprises the amino acid Arginine (R), at a position corresponding to a position selected from the group consisting of: 9, 42 and 239 of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises the amino acid Glutamic acid (E) or Aspartic acid (D), at a position corresponding to a position selected from the group consisting of: 9, 42, 60, 61 , 74, 157, 176, 179, 182, 212, 250, 253 and 256 of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises an insertion of the amino acid Aspartic acid (D) or Glutamic acid (E) at a position corresponding to position 97 of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises the amino acid selected from the group consisting of: Glutamic acid (E), Aspartic acid (D), Glycine (G), Arginine (R) and Methionine (M) at a position corresponding to position 99 of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 25, wherein the protease comprises the amino acid selected from the group consisting of: Glutamic acid (E), Aspartic acid (D) and Glutamine (Q), at a position corresponding to position 21 1 of SEQ ID NO 25;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 26, wherein the protease comprises the amino acid selected from the group consisting of: Glutamic acid (E), Aspartic acid (D) and Glutamine (Q), at a position corresponding to position 217 of SEQ ID NO 26;
  • protease 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%, at least 98% but less than 100% sequence identity to SEQ ID NO 26, wherein the protease comprises one or more of the substitutions selected from the group consisting of: S24G/R, S53G, S78N, S101 N, G128A/S and Y217Q/L, compared to SEQ ID NO 26, wherein the positions correspond to the positions of SEQ ID NO 26.
  • the cleaning composition may comprise one or more additional enzymes such as one or more pectinase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • additional enzymes such as one or more pectinase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • the properties of the selected enzyme(s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
  • Peroxidases/Oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include GuardzymeTM (Novozymes A/S). A peroxidase is comprised by the enzyme classification EC 1 .1 1.1.7, 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.
  • IUBMB Nomenclature Committee of the International Union of Biochemistry and Molecular Biology
  • 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 suitable peroxidase includes 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.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase.
  • 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.
  • a suitable oxidase includes in particular, 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 orfungi (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, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, 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.
  • the enzymes may be included in the cleaning composition of the present invention at a level of from 0.01 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm s from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, from 250 ppm to 500 ppm.
  • the DNases above may be combined with enzymes to form a blend to be added to the wash liquor solution according to the invention.
  • the concentration of the DNase in the wash liquor solution is typically in the range of wash liquor from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm s from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, 0.1 ppm to 10 ppm, from 0.2 ppm to 10 ppm, from 0.5 ppm to 5 ppm.
  • concentration of the additional enzyme i.e.
  • the amylase, cellulase, lipase, mannanase or the protease in the wash liquor solution is typically in the range of wash liquor from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm s from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, 0.1 ppm to 10 ppm, from 0.2 ppm to 10 ppm, from 0.5 ppm to 5 ppm.
  • the DNases may be combined with any of the enzymes of the invention to form a blend to be added to a composition according to the invention.
  • One embodiment relates to a cleaning composition
  • a cleaning composition comprising a DNase, enzymes of the invention and at least one cleaning component, wherein the amount of DNase in the composition is from 0.01 to 1000 ppm and the amount of protease is from 0.01 to 1000 ppm.
  • the cleaning composition further comprises one or more cleaning component.
  • a cleaning composition comprising a DNase, an amylase, cellulase, lipase, mannanase or protease and at least one cleaning component, wherein the cleaning component is selected from surfactants, preferably anionic and/or nonionic, builders and bleach components.
  • 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(s) is typically present at a level of from about 0.1 % to 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 0.1 % to about 15% or about 3% to about 10%.
  • the surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.
  • the detergent When included therein the detergent will usually contain from about 1 % to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • an anionic surfactant such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, 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 (S
  • 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% to about 30%, in particular from about
  • Non-limiting 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
  • AE or AEO alcohol ethoxylates
  • 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.
  • 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.
  • Non-limiting 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)inul
  • 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 1-hydroxyethane-1 ,1 -diphosphonic acid
  • EDTMPA ethylenediaminetetra(methylenephosphonic acid)
  • DTMPA or DTPMPA diethylenetriaminepentakis(methylenephosphonic acid)
  • EDG N-(2- hydroxyethyl)iminodiacetic acid
  • ASMA aspartic acid-N-monoacetic acid
  • ASDA aspartic acid- N,N-diacetic acid
  • ASMP aspartic acid-N-monoprop
  • 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-onaphthoic 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 W098/17767.
  • TAED tetraacetylethylenediamine
  • ISONOBS sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1 - s
  • 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(0)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1 ,2-diylazanylylidene-KN-methanylylidene)triphenolato- K30]manganese(lll).
  • 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 1 1 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 poly(ethylene 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 poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aqualon, 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.l.) 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.
  • 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 agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01 % to about 0.5%.
  • 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-[(
  • 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 2006/1 13314 (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, orfrom 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, cationically 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 anti-redeposition 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 compositions of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre- treatment 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: US2009/001 1970 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 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 poly(ethylene 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- and 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.
  • the DNase may be formulated as a granule for example as a co-granule 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-granulate for the detergent industry is disclosed in the IP.com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes by the use of co-granulates are 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.
  • the multi-enzyme co-granule may comprise a DNase and an amylase, cellulase, lipase, mannanase or protease of the invention and one or more enzymes selected from the group consisting of xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases, hemicellulases, cellobiose dehydrogenases, xylanases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase and mixtures thereof.
  • 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 as claimed and described herein in aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • An embodiment of the invention relates to an enzyme granule/particle comprising the DNase an amylase, cellulase, lipase, mannanase or protease 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
  • 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, spheronization, 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, spheronization, 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).
  • PEG polyethylene glycol
  • MHPC methyl hydroxy-propyl cellulose
  • PVA polyvinyl alcohol
  • 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 one embodiment, the thickness of the coating is below 100 pm. In another 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 and may have 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(s) of crystallization, such as described in WO 99/32595.
  • anhydrous sodium sulfate Na 2 S0 4
  • anhydrous magnesium sulfate MgS0 4
  • magnesium sulfate heptahydrate MgS0 4 7H 2 0
  • zinc sulfate heptahydrate ZnS0 4 7H 2 0
  • sodium phosphate dibasic heptahydrate Na 2 HP0 4 7H 2 0
  • magnesium nitrate hexahydrate Mg(N0 3 ) 2 (6H 2 0)
  • sodium citrate dihydrate and magnesium acetate tetrahydrate Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed.
  • the present invention is also directed to methods for using the compositions thereof.
  • Laundry/textile/fabric House hold laundry washing, Industrial laundry washing).
  • Hard surface cleaning ADW, car wash, Industrial surface.
  • the cleaning e.g. detergent 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 pre-treatment 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.
  • compositions of the invention comprise a blend of DNase and amylase, cellulase, lipase, mannanase or protease and effectively reduce or remove organic components, such as starch, grease, protein and DNA stains from surfaces such as textiles and hard surfaces e.g. dishes.
  • One embodiment of the invention relates to the use of a composition comprising a DNase and an amylase, cellulase, lipase, mannanase or protease for reduction of redeposition.
  • One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and an amylase, cellulase, lipase, mannanase or protease for reduction of redeposition.
  • One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and an amylase, cellulase, lipase, mannanase or protease for reduction of redeposition when the cleaning composition is applied in e.g. laundry process.
  • a cleaning composition comprising a DNase and an amylase, cellulase, lipase, mannanase or protease for reduction of redeposition on an item e.g. textile.
  • the composition is an anti-redeposition composition.
  • DNase activity is determined on DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which is prepared according to the manual from supplier. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is temperated to 48°C in water bath, and 20 ml of agar is poured into petri dishes with and allowed to solidify by incubation o/n at room temperature. On solidified agar plates, 5 pi of enzyme solutions are added and DNase activity is observed as colorless zones around the spotted enzyme solutions
  • DNase activity is determined by using the DNaseAlertTM Kit (1 1 -02-01 -04, IDT Intergrated DNA Technologies) according to the supplier’s manual. Briefly, 95 mI DNase sample is mixed with 5 mI substrate in a microtiter plate, and fluorescence is immediately measured using a Clariostar microtiter reader from BMG Labtech (536 nm excitation, 556 nm emission).
  • the alpha-amylase activity may be determined by a method employing the G7-pNP substrate.
  • G7- pNP which is an abbreviation for 4,6-ethylidene(G 7 )-p-nitrophenyl(Gi)-a,D-maltoheptaoside, a blocked oligosaccharide which can be cleaved by an endo-amylase, such as an alpha-amylase.
  • Kits containing G7-pNP substrate and alpha- Glucosidase is manufactured by Roche/Hitachi (cat. No.1 1876473).
  • the G7-pNP substrate from this kit contains 22 mM 4,6-ethylidene- G7-pNP and 52.4 mM HEPES (2-[4-(2-hydroxyethyl)-1 - piperazinyl]-ethanesulfonic acid), pH 7.0).
  • the alpha-Glucosidase reagent contains 52.4 mM HEPES, 87 mM NaCI, 12.6 mM MgCh, 0.075 mM CaCh, > 4 kU/L alpha-glucosidase).
  • the substrate working solution is made by mixing 1 mL of the alpha-Glucosidase reagent with 0.2 mL of the G7-pNP substrate. This substrate working solution is made immediately before use.
  • the amylase sample to be analyzed is diluted in dilution buffer to ensure the pH in the diluted sample is 7.
  • the assay is performed by transferring 20 mI diluted enzyme samples to 96 well microtiter plate and adding 80mI substrate working solution. The solution is mixed and pre-incubated 1 minute at room temperature and absorption is measured every 20 sec. over 5 minutes at OD 405 nm. The slope (absorbance per minute) of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the alpha-amylase in question under the given set of conditions. The amylase sample should be diluted to a level where the slope is below 0.4 absorbance units per minute.
  • AZCL-He-cellulose azurine dye covalently cross-linked cellulose assay is used for detection of cellulase (endo-glucanase) activity.
  • AZCL-He-cellulose 75 mg is suspended in 15 mL detergent (e.g. Model detergent A).
  • detergent e.g. Model detergent A
  • enzyme 0.05 mg enzyme protein/mL
  • 250 pL of the solution is transferred to a micro-titer plate and the sample absorbance is measured at 590 nm.
  • Lipase is diluted with a buffer (10mM Succinic acid + 2mM CaCI2 + 0.02% Brij 35 adjusted to pH6.5) to the specified concentration. 10 uL of the 100 ppm lipase solution is added to a 90uL of detergent composition, stirred for 5 minutes and sealed. Samples are stored at 4°C in detergent D002 (unstressed) and in detergent D002 at 47°C (stressed). Storage time is 335.5 hours. After storage possible condensation liquid is collected by centrifugation.
  • a buffer 10mM Succinic acid + 2mM CaCI2 + 0.02% Brij 35 adjusted to pH6.5
  • this lipase dilution is mixed with four parts of 0.5 mM pNP-palmitate, 1 mM calcium chloride, 100 mM Tris (pH8.0), 6.5mM Deoxycholate, 1 .4g/L AOS and for 30 minutes release of the pNP chromophore is measured spectrophotometrically. This is used to determine activity via the initial linear slope of the reaction. Residual activity is calculated as the ratio of the measured velocities of stressed versus unstressed sample. The median value of the residual activity is calculated based on four replicates and normalized by a lipase variant reference run with each experimental set.
  • Mannanase activity may be tested according to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (carob), i.e. substrate for the assay of endo-1 ,4-beta-D- mannanase available as CatNo.l-AZGMA from the company Megazyme (Megazyme’s Internet address: http://www.megazyme.com/Purchase/index.html). Assay VII: testing of protease activity
  • Suc-AAPF-PNA is an abbreviation for N-Succinyl-Alanine-Alanine-Proline-Phenylalanine-p- Nitroanilide and is a blocked peptide which can be cleaved by endo-proteases. Following cleavage, a free PNA molecule is liberated, which has a yellow color and thus can be measured by visible spectrophotometry at wavelength 405 nm.
  • the Suc-AAPF-PNA substrate is manufactured by Bachem (cat. no. L1400, dissolved in DMSO).
  • the protease sample to be analyzed is diluted in residual activity buffer (100 mM Tris pH 8.6).
  • the assay is performed by transferring 3 0 mI of diluted enzyme samples to 96 well microtiter plate and adding 70 mI substrate working solution (0.72 mg/ml in 100 mM Tris pH8.6).
  • the solution is mixed at room temperature and absorption is measured every 20 seconds over 5 minutes at OD 405 nm.
  • the slope (absorbance per minute) of the time dependent absorption-curve is directly proportional to the activity of the protease in question under the given set of conditions.
  • the protease sample is diluted to a level where the slope is linear.
  • the below mentioned detergent composition can be used in combination with the enzyme combinations of the invention.
  • Anionic surfactants 5-15% Anionic surfactants, ⁇ 5% Nonionic surfactants, perfume, enzymes, DMDM and hydantoin.
  • composition of Ariel Sensitive White & Color liquid detergent composition
  • Ingredients 5-15% Anionic surfactants; ⁇ 5% Non-ionic surfactants, Phosphonates, Soap; Enzymes, Optical brighteners, Benzisothiazolinone, Methylisothiazolinone, Perfumes, Alpha-isomethyl ionone, Citronellol, Geraniol, Linalool.
  • Ingredients 5-15% Anionic surfactants; ⁇ 5% Non-ionic surfactants, Phosphonates, Soap; Enzymes, Perfumes, Benzisothiazolinone, Methylisothiazolinone, Alpha-isomethyl ionone, Butylphenyl methylpropional, Citronellol, Geraniol, Linalool.
  • Subtilisin Imidazolidinone, Hexyl Cinnamal, Sucrose, Sorbitol, Aluminum Silicate, Polyoxymethylene Melamine, Cl 61585, Cl 45100, Lipase, Amylase, Xanthan gum, Hydroxypropyl methyl cellulose, Cl 12490, Disodium Distyrylbiphenyl Disulfonate, Sodium Thiosulfate, Cl 42090, Mannanase, Cl 1 1680, Etidronic Acid, Tetrasodium EDTA.
  • Anilinomorpholinotriazinyl-aminostilbenesulfonate Sodium bicarbonate, Phenylpropyl Ethyl Methicone, Butylphenyl Methylpropional, Glyceryl Stearates, Calcium carbonate, Sodium Polyacrylate, Geraniol, Disodium Distyrylbiphenyl Disulfonate, Cellulose, Protease, PEG-75, Titanium dioxide, Dextrin, Sucrose, Sodium Polyaryl Sulphonate, Cl 12490, Cl 45100, Cl 42090, Sodium Thiosulfate, Cl 61585.
  • MEA-Dodecylbenzenesulfonate MEA-Hydrogenated Cocoate, C12-15 Pareth-7, Dipropylene Glycol, Aqua, Glycerin, Polyvinyl Alcohol, perfume, Aziridine homopolymer ethoxylated, Sodium Diethylenetriamine Pentamethylene Phosphonate, Propylene glycol, Sorbitol, MEA-Sulfate, Ethanolamine, Subtilisin, Glycol, Butylphenyl Methylpropional, Hexyl Cinnamal, Starch, Boronic acid, (4-formylphenyl), Limonene, Linalool, Disodium Distyrylbiphenyl Disulfonate, Alpha-Isomethyl lonone, Geraniol, Amylase, Talc, Polymeric Blue Colourant, Sodium chloride, Benzisothiazolinone, Denatonium Benzoate, Polymeric Yellow Colourant, Mannanase.
  • MEA-Dodecylbenzenesulfonate MEA-Hydrogenated Cocoate, C12-15 Pareth-7, Dipropylene Glycol, Aqua, Glycerin, Polyvinyl Alcohol, perfume, Aziridine homopolymer ethoxylated, Sodium Diethylenetriamine Pentamethylene Phosphonate, Propylene glycol, MEA- Sulfate, Ethanolamine, PVP, Sorbitol, Butylphenyl Methylpropional, Subtilisin, Hexyl Cinnamal, Starch, Limonene, Linalool, Boronic acid, (4-formylphenyl), Alpha-Isomethyl lonone, Geraniol, Talc, Polymeric Blue Colourant, Denatonium Benzoate, Polymeric Yellow Colourant.
  • Ingredients 5-15% Anionic surfactants, Oxygen-based bleaching agents, ⁇ 5% Non- ionic surfactants, Phosphonates, Polycarboxylates, Zeolites, Optical brightners, Enzymes, Perfumes, Butylphenyl Methylpropional, Coumarin, Hexyl Cinnamal
  • ingredients 15 - 30% of the following: anionic surfactants, oxygen-based bleaching agent and zeolites, less than 5% of the following: non-ionic surfactants, phosphonates, polycarboxylates, soap, Further ingredients: Perfumes, Hexyl cinnamal, Benzyl salicylate, Linalool, optical brighteners, Enzymes and Citronellol.
  • Alcoholethoxy sulfate diethylene glycol, monoethanolamine citrate, sodium formate, propylene glycol, linear alkylbenzene sulfonates, ethanolamine, ethanol, polyethyleneimine ethoxylate, amylase, benzisothiazolin, borax, calcium formate, citric acid, diethylenetriamine pentaacetate sodium, dimethicone, diquaternium ethoxysulfate, disodium diaminostilbene disulfonate, Laureth-9, mannanase, protease, sodium cumene sulfonate, sodium fatty acids.
  • Linear alkylbenzene sulfonates C12-16 Pareth-9, propylene glycol, alcoholethoxy sulfate, water, polyethyleneimine ethoxylate, glycerine, fatty acid salts, PEG-136 polyvinyl acetate, ethylene Diamine disuccinic salt, monoethanolamine citrate, sodium bisulfite, diethylenetriamine pentaacetate sodium, disodium distyrylbiphenyl disulfonate, calcium formate, mannanase, exyloglucanase, sodium formate, hydrogenated castor oil, natalase, dyes, termamyl, subtilisin, benzisothiazolin, perfume.
  • Liquid Ingredients Dipropylene Glycol, diquaternium Ethoxysulfate, Water, Glycerin, LiquitintTM Orange, Powder Ingredients: sodium percarbonate, nonanoyloxy benzene sulfonate, sodium carbonate, sodium sulfate, sodium aluminosilicate, sodium polyacrylate, sodium alkylbenzenesulfonate, maleic/acrylic copolymer, water, amylase, polyethylene glycol, sodium palmitate, modified starch, protease, glycerine, DTPA, fragrance.
  • Ethanol sodium cumene sulfonate, borax, fragrance, DTPA, Sodium bisulfate, disodium diaminostilbene disulfonate, Mannanase, cellulase, amylase, sodium formate, calcium formate, Lauramine oxide, LiquitintTM Blue, Dimethicone / polydimethyl silicone.
  • Lauramine oxide LiquitintTM Blue, Dimethicone / polydimethyl silicone.

Abstract

La présente invention concerne des compositions telles que des compositions de nettoyage comprenant un mélange d'enzymes. L'invention concerne en outre l'utilisation de compositions comprenant de telles enzymes dans des procédés de nettoyage.
PCT/EP2019/077196 2018-10-09 2019-10-08 Compositions de nettoyage et leurs utilisations WO2020074498A1 (fr)

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WO2021130167A1 (fr) * 2019-12-23 2021-07-01 Novozymes A/S Compositions enzymatiques et utilisations associées
WO2021133701A1 (fr) * 2019-12-23 2021-07-01 The Procter & Gamble Company Compositions comprenant des enzymes
WO2024061317A1 (fr) * 2022-09-21 2024-03-28 Novozymes A/S Utilisation d'une enzyme pour remplacer un agent de maintien de la blancheur dans une composition de nettoyage

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