WO2022089571A1 - Composition détergente et procédé de nettoyage - Google Patents

Composition détergente et procédé de nettoyage Download PDF

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Publication number
WO2022089571A1
WO2022089571A1 PCT/CN2021/127306 CN2021127306W WO2022089571A1 WO 2022089571 A1 WO2022089571 A1 WO 2022089571A1 CN 2021127306 W CN2021127306 W CN 2021127306W WO 2022089571 A1 WO2022089571 A1 WO 2022089571A1
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alpha
seq
amylase
composition
detergent
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PCT/CN2021/127306
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English (en)
Inventor
Qiang Zhao
Cheng Zhang
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Novozymes A/S
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Priority to CN202180073222.4A priority Critical patent/CN116547366A/zh
Publication of WO2022089571A1 publication Critical patent/WO2022089571A1/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
    • C11D2111/14—

Definitions

  • the present invention relates to hard surface detergent composition for enhancing shine on hard surfaces and finds particular application in the cleaning of hard surfaces.
  • Dish washing is a well know activity that takes place in practically all places where food is prepared or consumed.
  • dish washing is done manually by immersing the soiled dishware in dishwater, brushing or other mechanical action to the dishware followed by rinsing and drying the cleaned dishware.
  • the inventors have developed a detergent composition and method for imparting or maintaining a glossy or shiny finish on a hard surface.
  • the present invention generally relates to detergent composition suitable for hand-dishwashing and comprising at least an alpha-amylase.
  • the detergent composition for shining surfaces wherein the composition comprises at least an alpha amylase.
  • the invention relates to a method for preparing a hand dishwashing detergent composition with glossy or shiny finish, the method comprising adding to the composition at least an alpha amylase.
  • the invention relates to use of a composition comprising an alpha amylase as disclosed herein in a cleaning process, e.g. for hand dishwashing.
  • the invention relates to a method of cleaning, e.g. for hand dishwashing or hard surface cleaning, comprising contacting dishes or a hard surface to be cleaned with a detergent composition comprising an alpha amylase as described herein under conditions suitable for cleaning the dishes or surface.
  • SEQ ID NO: 1 is the amino acid sequence of an alpha-amylase (AAI10)
  • SEQ ID NO: 2 is the amino acid sequence of a fusion alpha-amylase (LABM)
  • SEQ ID NO: 3 is the amino acid sequence of an alpha-amylase (AA560)
  • SEQ ID NO: 4 is the amino acid sequence of an alpha-amylase (AAI10)
  • SEQ ID NO: 5 is the amino acid sequence of a fusion alpha-amylase (LASB0000)
  • SEQ ID NO: 6 is the amino acid sequence of an alpha-amylase (TS23)
  • SEQ ID NO: 7 is the amino acid sequence of an alpha-amylase (Cytophaga sp)
  • SEQ ID NO: 8 is the amino acid sequence of an alpha-amylase (SP722)
  • SEQ ID NO: 9 is the amino acid sequence of an alpha-amylase (SP707)
  • SEQ ID NO: 10 is the amino acid sequence of an alpha-amylase (BAN)
  • SEQ ID NO: 11 is the amino acid sequence of an alpha-amylase (BspAmy24)
  • SEQ ID NO: 12 is the amino acid sequence of a fusion alpha-amylase (Alicyclobacillus)
  • SEQ ID NO: 13 is the amino acid sequence of an alpha-amylase (BSG)
  • references to “about” a value or parameter herein includes aspects that are directed to that value or parameter per se. For example, description referring to “about X” includes the aspect “X” .
  • alpha-amylases refers to (alpha-1, 4-glucan-4-glucanohydrolases, E.C. 3.2.1.1) constitute a group of enzymes, which catalyze hydrolysis of starch and other linear and branched 1, 4-glucosidic oligo-and polysaccharides.
  • alpha-amylase activity refers to the activity of an alpha-amylase wherein the activity is determined according to the procedure described in the Examples.
  • the alpha-amylase activity may be determined according to a method using the micro swatch assay which is described in the Examples.
  • amino acid refers to the standard twenty genetically-encoded amino acids and their corresponding stereoisomers in the ‘d’ form (as compared to the natural ‘l’ form) , omega-amino acids other naturally-occurring amino acids, unconventional amino acids (e.g. ⁇ , ⁇ -disubstituted amino acids, N-alkyl amino acids, etc. ) and chemically derivatised amino acids. Chemical derivatives of one or more amino acids may be achieved by reaction with a functional side group.
  • Such derivatised molecules include, for example, those molecules in which free amino groups have been derivatised to form amine hydrochlorides, p-toluene sulphonyl groups, carboxybenzoxy groups, t-butyloxycarbonyl groups, chloroacetyl groups or formyl groups.
  • Free carboxyl groups may be derivatised to form salts, methyl and ethyl esters or other types of esters and hydrazides.
  • Free hydroxyl groups may be derivatised to form O-acyl or O-alkyl derivatives.
  • chemical derivatives are those peptides which contain naturally occurring amino acid derivatives of the twenty standard amino acids.
  • 4-hydroxyproline may be substituted for proline; 5-hydroxylysine may be substituted for lysine; 3-methylhistidine may be substituted for histidine; homoserine may be substituted for serine and ornithine for lysine.
  • Derivatives also include peptides containing one or more additions or deletions as long as the requisite activity is maintained. Other included modifications are amidation, amino terminal acylation (e.g. acetylation or thioglycolic acid amidation) , terminal carboxylamidation (e.g. with ammonia or methylamine) , and the like terminal modifications.
  • polypeptides of the invention comprise or consist of l-amino acids.
  • dishware is intended to mean any form of kitchen utensil, dinner set or tableware such as but not limited to pans, plates, cops, knives, forks, spoons, porcelain etc.
  • greye or "greasy” as used herein means materials comprising at least in part (i.e., at least 0.5 wt%by weight of the grease) saturated and unsaturated fats and oils, preferably oils and fats derived from animal sources such as beef, pig and/or chicken.
  • wash refers to all forms of washing dishes, e.g. by hand (MDW) or automatic dish wash (ADW) .
  • Washing dishes includes, but is not limited to, the cleaning of all forms of crockery such as plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils as well as ceramics, plastics, metals, china, glass and acrylics.
  • dish washing composition refers to compositions intended for cleaning dishware such as plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics in a dishwashing machine.
  • the terms encompass any materials/compounds selected for household or industrial washing applications and the form of the product can be liquid, powder or granulate.
  • the automatic dishwashing composition contains detergent components such as polymers, bleaching systems, bleach activators, bleach catalysts, silicates, dyestuff and metal care agents.
  • the dishwashing composition can be use in manual dishwashing (MDW) or automatic dishwashing (ADW) .
  • the dish washing composition is a liquid dish washing composition, a powder dish washing composition, wherein the composition may optionally be in the form of a unit dose.
  • enzyme detergency benefit refers to 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 re-deposition 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 re-deposition 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 component such as hydrogen peroxide or other peroxides.
  • hard surface cleaning refers to 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.
  • improved wash performance is defined herein as displaying an alteration of the wash performance of an amylase of the present invention relative to the wash performance of the parent alpha-amylase or no amylase.
  • sequence identity is relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity” .
  • the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277) , preferably version 5.0.0 or later.
  • the parameters used may be gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled “longest identity” (obtained using the –nobrief option) is used as the percent identity and is calculated as follows:
  • the parameters used may be gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) 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:
  • detergent composition is not intended to be limited to compositions that contain surfactants. It is intended that in addition to the enzymes herein described, the detergents compositions may comprise, e.g. one or more additional components selected from stabilizing agents, surfactants, hydrotopes, builders, co-builders, chelating agents, bleaching systems, bleach activators, bleach catalysts, polymers, metal care agents, glass care agents, crystal growth inhibitors and fabric-hueing agents.
  • non-fabric detergent compositions include non-textile surface detergent compositions, including but not limited to compositions for hard surface cleaning, such as dishwashing detergent compositions, oral detergent compositions, denture detergent compositions, and personal cleansing compositions.
  • the term "effective amount of enzyme” refers to the quantity of enzyme necessary to achieve the enzymatic activity required in the specific application, e.g., in a defined detergent composition. Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many factors, such as the particular enzyme used, the cleaning application, the specific composition of the detergent composition, and whether a liquid or dry (e.g., granular, bar) composition is required, and the like.
  • the term "effective amount” of an enzyme refers to the quantity of enzyme described hereinbefore that achieves a desired level of enzymatic activity, e.g., in a defined detergent composition.
  • water hardness or “degree of hardness” or “dH” or “°dH” as used herein refers to German degrees of hardness. One degree is defined as 10 milligrams of calcium oxide per litre of water.
  • relevant washing conditions is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, detergent concentration, type of detergent and water hardness, actually used in households in a detergent market segment.
  • adjunct materials means any liquid, solid or gaseous material selected for the particular type of detergent composition desired and the form of the product (e.g., liquid, granule, powder, bar, paste, spray, tablet, gel, or foam composition) , which materials are also preferably compatible with the enzymes used in the composition.
  • granular compositions are in "compact” form, while in other embodiments, the liquid compositions are in a "concentrated” form.
  • stain removing enzyme describes an enzyme that aids the removal of a stain or soil from a fabric or a hard surface. Stain removing enzymes act on specific substrates, e.g., protease on protein, amylase on starch, lipase and cutinase on lipids (fats and oils) , pectinase on pectin and hemicellulases on hemicellulose. Stains are often depositions of complex mixtures of different components which either results in a local discolouration of the material by itself or which leaves a sticky surface on the object which may attract soils dissolved in the washing liquor thereby resulting in discolouration of the stained area.
  • an enzyme acts on its specific substrate present in a stain the enzyme degrades or partially degrades its substrate thereby aiding the removal of soils and stain components associated with the substrate during the washing process.
  • a protease acts on a grass stain it degrades the protein components in the grass and allows the green/brown colour to be released during washing.
  • reduced amount means in this context that the amount of the component is smaller than the amount which would be used in a reference process under otherwise the same conditions. In a preferred embodiment the amount is reduced by, e.g., at least 5%, such as at least 10%, at least 15%, at least 20%or as otherwise herein described.
  • liquid dishwash detergent composition refers to a detergent composition which is in a stabilized liquid form and used in dishwash.
  • Dishwash may be any kind of dishwash, such as manual dishwash and such as automated dishwash (ADW) .
  • ADW automated dishwash
  • powder dishwash detergent composition refers to a detergent composition which is in a solid form, such as a granulate, powder or compact unit and used in dishwash.
  • a powder dishwash detergent composition is typically used in automated dishwash, but the used is not limited to such ADW, and may also be intended for used in any other kind of dishwash, such as manual dishwash.
  • variant means a polypeptide having enzyme activity comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions.
  • a substitution means replacement of the amino acid occupying a position with a different amino acid;
  • a deletion means removal of the amino acid occupying a position; and
  • an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
  • detergent components is defined herein to mean the types of chemicals which can be used in detergent compositions.
  • detergent components are alkalis, surfactants, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching system or bleach components, polymers, fabric hueing agents, fabric conditioners, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, fluorescent whitening agents, perfume, optical brighteners, bactericides, fungicides, soil suspending agents, soil release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants and solubilizers.
  • wash cycle is defined herein as a washing operation wherein dishware are exposed to the wash liquor for a period of time by circulating the wash liquor and spraying the wash liquor onto the dishware in order to clean the dishware and finally the superfluous wash liquor is removed.
  • a wash cycle may be repeated one, two, three, four, five or even six times at the same or at different temperatures.
  • the dishware is generally rinsed and dried.
  • One of the wash cycles can be a soaking step, where the dishware is left soaking in the wash liquor for a period.
  • wash liquor is intended to mean the solution or mixture of water and detergents optionally including enzymes used for dishwashing.
  • compositions of the present invention can comprise, consist of, and consist essentially of the essential elements and limitations of the invention described herein, as well as any of the additional or optional ingredients, components, steps, or limitations described herein.
  • the polypeptides disclosed in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or 13 may be used to determine the corresponding amino acid residue in another polypeptide.
  • the amino acid sequence of another polypeptide is aligned with the polypeptide disclosed in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or 13 depending on whether it is an alpha-amylase, a protease or a lipase, and based on the alignment, the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or 13 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol.
  • EMBOSS The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • Identification of the corresponding amino acid residue in another enzyme may be determined by an alignment of multiple polypeptide sequences using several computer programs including, but not limited to, MUSCLE (multiple sequence comparison by log ⁇ expectation; version 3.5 or later; Edgar, 2004, Nucleic Acids Research 32: 1792-1797) , MAFFT (version 6.857 or later; Katoh and Kuma, 2002, Nucleic Acids Research 30: 3059-3066; Katoh et al., 2005, Nucleic Acids Research 33: 511-518; Katoh and Toh, 2007, Bioinformatics 23: 372-374; Katoh et al., 2009, Methods in Molecular Biology 537: 39-64; Katoh and Toh, 2010, Bioinformatics 26: 1899-1900) , and EMBOSS EMMA employing ClustalW (1.83 or later; Thompson et al., 1994, Nucleic Acids Research 22: 4673-4680) , using their respective default parameters.
  • MUSCLE multiple
  • proteins of known structure For proteins of known structure, several tools and resources are available for retrieving and generating structural alignments. For example the SCOP super families of proteins have been structurally aligned, and those alignments are accessible and downloadable.
  • Two or more protein structures can be aligned using a variety of algorithms such as the distance alignment matrix (Holm and Sander, 1998, Proteins 33: 88-96) or combinatorial extension (Shindyalov and Bourne, 1998, Protein Engineering 11: 739-747) , and implementation of these algorithms can additionally be utilized to query structure databases with a structure of interest in order to discover possible structural homologs (e.g., Holm and Park, 2000, Bioinformatics 16: 566-567) .
  • variants described herein comprises one or more modifications as compared to the parent polypeptide. Accordingly, variants may comprise conservative modifications, in particular, such conservative modifications may be conservative substitutions. Examples of conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine) , acidic amino acids (glutamic acid and aspartic acid) , polar amino acids (glutamine and asparagine) , hydrophobic amino acids (leucine, isoleucine and valine) , aromatic amino acids (phenylalanine, tryptophan and tyrosine) , and small amino acids (glycine, alanine, serine, threonine and methionine) .
  • conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine) , acidic amino acids (glutamic acid and aspartic acid) , polar amino acids (glutamine and asparagine) , hydrophobic amino acids (leucine, isoleu
  • Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala/Ser, Val/Ile, Asp/Glu, Asn/Gln, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Glu/Gln, Leu/Ile, Leu/Val, Ala/Glu, and Asp/Gly.
  • amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered.
  • amino acid changes may improve the thermal stability of the polypeptide, alter the substrate specificity, change the pH optimum, and the like.
  • substitutions For an amino acid substitution, the following nomenclature is used: Original amino acid, position, substituted amino acid. Accordingly, the substitution of glycine at position G109 with alanine is designated as “Gly109Ala” or “G109A” . Multiple mutations are separated by addition marks ( “+” ) or by commas ( “, ” ) , e.g., “Gly109Ala + Leu173Pro” or “G109A, L173P” , representing substitutions at positions 109 and 173 of glysine (G) with alanine (A) and leucine (L) with proline (P) , respectively.
  • X109A/P where the X in the present example indicates that different enzymes may be parent e.g. such as an alpha-amylase with SEQ ID NO: 1 or an alpha-amylase having at least 75%identity hereto.
  • the variants are represented as 109A/P or X109A/P indicating that the amino acids to be substituted vary depending on the parent enzyme.
  • Deletions For an amino acid deletion, the following nomenclature is used: Original amino acid, position, *. Accordingly, the deletion of arginie at position 181 is designated as “Arg181*” or “R181*” . Multiple deletions are separated by addition marks ( “+” ) or commas, e.g., “Arg181*+ Gly182*” or “R181*+G182*” or “R181*, G182*” .
  • Insertions The insertion of an additional amino acid residue such as e.g. a lysine after G# 1 may be indicated by: Gly# 1 GlyLys or G# 1 GK. Alternatively insertion of an additional amino acid residue such as lysine after G109 may be indicated by: *109aL. When more than one amino acid residue is inserted, such as e.g. a Lys, and Ala after 109 this may be indicated as: Gly109GlyLysAla or G109GKA. In such cases, the inserted amino acid residue (s) may also be numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue (s) , in this example: *109aK *109bA.
  • Variants comprising multiple modifications are separated by addition marks ( “+” ) , slash marks ( “/” ) , or by commas ( “, ” ) , e.g., “Gly109Pro+Lys391Ala” or “G109P, K391A” representing a substitution of glysine at position 109 and lysine at position 391 with proline and alanine, respectively as described above.
  • the original amino acid in any position may vary from one parent alpha-amylase to another when aligned. Accordingly, it is to be understood that the skilled person would be able to align any alpha-amylase sequence with the numbering sequence, i.e. SEQ ID NO: 1, of the present invention.
  • the original amino acids are designated to an “X” which would cover all the parent polypeptides. It is thus, to be understood that “X” is listed as a prefix for an amino acid position in the present invention. It is not to be understood in any limiting way.
  • the present invention relates to a detergent or cleaning composition and method for imparting or maintaining a glossy or shiny finish on a hard surface suitable for hand dishwashing, wherein the compositions comprise at least an alpha amylase.
  • composition of the invention that is suitable for hand dishwashing, although it is also contemplated that composition of the invention may also be used for other purposes such as hard surface cleaning or hand laundry.
  • Such compositions can simultaneously provide both a washing or cleaning function to remove dirt, grease, grime and other deposits from the painted metal exterior surface of the dishware, and a waxing or polishing function to impart a durable, high gloss finish to the clean surface.
  • the detergent or cleaning composition comprises an alpha-amylase, wherein the amylase variant is a variant of a parent amylase, said variant amylase or parent amylase 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%but less than 100%sequence identity to SEQ ID NO: 1 and further comprises an modification in one or more positions corresponding to positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391, 395, 439, 469, 444, 473, 476, or 477 of SEQ ID NO: 1.
  • the invention relates to a detergent or cleaning composition, wherein the at least an alpha-amylase comprises one or more amino acid modifications in the positions corresponding to positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391, 395, 439, 469, 444, 473, 476, or 477 of SEQ ID NO: 1, wherein the alpha-amylase variant 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%but less than 100%sequence identity to the parent alpha-amylase of SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or 13, e.g., at least 80%, at least 81%,
  • the alpha-amylase variant comprises one or more modifications selected from the group consisting of: X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E, X172K, X172G, X172N, X173P, X174*, X174S, X181*, X182*, X183*, X184*, X184T, X189Y, X189F, X189H, X189E, X189D, X189Q, X189N, X194D, X194N, X194S, X195F, X206L, X206F, X206Y
  • the alpha-amylase variant comprises at two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, or thirteen of the following modifications X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E, X172K, X172G, X172N, X173P, X174*, X174S, X181*, X182*, X183*, X184*, X184T, X189Y, X189F, X189H, X189E, X189D, X189Q, X189N, X194D, X194N, X194S
  • the alpha-amylase variant comprises a deletion and/or a substitution at two or more positions corresponding to positions 181, 182, 183, or 184 of SEQ ID NO: 1, wherein the alpha-amylase variant has at least 60%, at least 65%, at least 75%sequence identity to SEQ ID NO: 1, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, e.g. at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, but less than 100%.
  • the alpha-amylase variant comprises a deletion in the positions corresponding to 181+182; 181+183; 181+184; 182+183; 182+184; or 183+184 of SEQ ID NO: 1.
  • the alpha-amylase variant comprises a one or more of the following modifications: X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E, X172K, X172G, X172N, X173P, X174*, X174S, X181*, X182*, X183*, X184*, X184T, X189Y, X189F, X189H, X189E, X189D, X189Q, X189N, X194D, X194N, X194S, X195F, X206L, X206F, X206Y
  • the alpha-amylase variant is selected from the group consisting of:
  • said alpha-amylase variant has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 75%, such as at least 80%, such as at least 85%, such as at least 90%, such as at least 93%, such as at least 94%, such as at least 95%, such as at least 96%, such as at least 97%, such as at least 98%, but less than 100%sequence identity with the polypeptide of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 or 14, and wherein said alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant is a variant of SEQ ID NO: 1 or SEQ ID NO: 2 comprising the following modifications:
  • said alpha-amylase variant has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 75%, at least 80%, such as at least 85%, such as at least 90%, such as at least 93%, such as at least 94%, such as at least 95%, such as at least 96%, such as at least 97%, such as at least 98%, but less than 100%sequence identity with the polypeptide of SEQ ID NO: 1, or SEQ ID NO: 2, and wherein said alpha-amylase variant has alpha-amylase activity
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L +K391A+G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A +G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182* +D183*+G184T+N195F+V206L+K391A+P473R+G476K, wherein numbering is according to SEQ ID NO: 1, wherein the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least
  • the alpha-amylase variant comprises the modifications: H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F +V206L+A265G+K391A+P473R+G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%
  • the alpha-amylase variant comprises the modifications: H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183* +N195F+V206L+K391A+G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%,
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S +G182*+D183*+N195F+V206L+G255A+K391A+G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least at least 60%, such as at least 65%, such as at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 9
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S +G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, wherein numbering is according to SEQ ID NO: 1, the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 9
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A +G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least at least 95%
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+ K391A+G476K, wherein numbering according to SEQ ID NO: 1, the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%,
  • the alpha-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F +V206L+K391A+G476K, wherein numbering is according to SEQ ID NO: 1,
  • the alpha-amylase variant is an alpha-amylase variant of a parent alpha-amylase which has at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, such as at least 75%, e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 3, or a variant thereof having a sequence identity of at least 75%but less than 100%to SEQ ID NO: 3, and wherein said alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 4, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 5, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 6, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 7, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 8, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 9, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 10, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 11, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 12, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the alpha-amylase variant comprises an alpha-amylase having the amino acid sequence of SEQ ID NO: 13, or a variant thereof having a sequence identity of at least 75%e.g., at least 76%at least 77%at least 78%at least 79%at least 80%, at least 81%at least 82%at least 83%at least 84%at least 85%, at least 86%at least 87%at least 88%at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%e.g.
  • alpha-amylase variant has alpha-amylase activity.
  • the concentration of the alpha-amylase (the polypeptide having alpha-amylase activity) of the present invention is typically in the range of 0.005-200 ppm enzyme protein, such as in the range of 0.008-150, in the range of 0.01-100, in the range of 0.05-80, in the range of 0.1-50, in the range of 0.2-30, in the range of 0.5-20 ppm enzyme protein, in the range of 1-10 ppm enzyme protein, or in the range of 1.5-5 ppm enzyme protein in the wash liquor.
  • the alpha-amylase of the present invention may be added to a detergent composition in an amount corresponding to at least 0.002 mg of alpha-amylase protein, such as at least 0.005 mg of alpha-amylase protein, at least 0.08 mg of alpha-amylase protein, at least 0.1 mg of alpha-amylase protein, at least 0.2mg of alpha-amylase protein, at least 1 mg of protein, at least 5 mg of protein, at least 10 mg of protein, at least 15 mg of protein, at least 20 mg of protein, at least 25 mg of protein, at least 30 mg of protein, at least 50 mg of protein, per gram of detergent composition or the detergent composition may comprise at least 0.01%alpha-amylase protein, at least 0.02%, 0.03%, 0.04%, 0.05%, 0.06%, 0.08%, 0.1%, 0.2%, 0.3%, 0.4%, 0.5%, 0.8%, 1.0%, 2.0%, or 5.0%of alpha-amylase protein.
  • the detergent composition of the invention is typically formulated as a liquid detergent composition suitable for hand dishwashing as is well-known in the art.
  • the cleaning composition is a hand dishwashing cleaning composition in liquid form.
  • the cleaning composition is preferably an aqueous cleaning composition.
  • the composition can comprise from 50%to 85%, preferably from 50%to 75%, by weight of the total composition of water.
  • the compositions will typically contain from 30%to 90%by weight of an aqueous liquid carrier in which the other components of the composition are dissolved, dispersed or suspended.
  • the aqueous liquid carrier will comprise from 45%to 70%, more preferably from 45%to 65%by weight of the composition.
  • the aqueous liquid carrier is water.
  • the aqueous liquid carrier may contain other materials which are liquid, or which dissolve in the liquid carrier, at room temperature (about 20-25°C) and which may also serve other functions besides that of an inert filler. Such materials can include, for example, hydrotropes and solvents as discussed in more detail below.
  • the liquid dishwashing composition may have any suitable pH value.
  • the pH of the composition is adjusted to between about 2 and 14, preferably between about 3 and 9.
  • the pH of the composition can be adjusted using pH modifying ingredients known in the art.
  • the invention is directed to detergent or cleaning composition
  • additional cleaning components such as a surfactant.
  • compositions of the invention preferably comprise at least one surfactant selected from nonionic, anionic, cationic surfactants, amphoteric, zwitterionic, semi-polar nonionic surfactants, and mixtures thereof.
  • Surfactants may be included in an amount of from about 1%to about 50%by weight, preferably from about 5%to about 40%by weight, more preferably from about 5%to about 30%by weight, such as from about 10%to about 20%by weight of the liquid detergent composition.
  • an efficient but mild surfactant system may comprise from about 4%to about 40%, preferably about 6%to about 32%, more preferably about 11%to about 25%, and most preferably about 11%to about 18%by weight of the total composition of an anionic surfactant and optionally no more than about 15%, preferably no more than about 10%, more preferably no more than about 5%by weight of the total composition, of a sulfonate surfactant.
  • Suitable anionic surfactants to be used in the compositions and methods of the present invention include sulfate, sulfosuccinates, sulfonate, and/or alkyl ethoxy sulfates; more preferably a combination of alkyl sulfates and/or alkyl ethoxy sulfates with a combined ethoxylation degree less than about 5, preferably less than about 3, more preferably less than about 2.
  • the surfactant system may be based on high levels of nonionic surfactant (such as about 10%to about 45%, preferably about 15%to about 40%, more preferably about 20%to about 35%by weight of the total composition) , preferably combined with an amphoteric surfactant, and more preferably with a low level of anionic surfactant (such as less than 20%, preferably less than 10%, more preferably less than about 5%by weight of the total composition) .
  • high levels of nonionic surfactant such as about 10%to about 45%, preferably about 15%to about 40%, more preferably about 20%to about 35%by weight of the total composition
  • amphoteric surfactant preferably combined with an amphoteric surfactant
  • anionic surfactant such as less than 20%, preferably less than 10%, more preferably less than about 5%by weight of the total composition
  • Suitable sulfate surfactants for use in the compositions herein include water-soluble salts or acids of C 10 -C 14 alkyl or hydroxyalkyl sulfate and/or ether sulfate.
  • Suitable counterions include hydrogen, alkali metal cations or ammonium or substituted ammonium, preferably sodium.
  • hydrocarbyl chain is branched, it preferably comprises C 14 alkyl branching units.
  • the average percentage branching of the sulfate surfactant is preferably greater than 30%, more preferably from 35%to 80%and most preferably from 40%to 60%of the total hydrocarbyl chains.
  • the sulfate surfactants may be selected from C 8 -C 20 primary, branched-chain and random alkyl sulfates (AS) ; C 10 -C 18 secondary (2, 3) alkyl sulfates; C 10 -C 18 alkyl alkoxy sulfates (AExS) wherein x is preferably from 1 to 30; C 10 -C 18 alkyl alkoxy carboxylates, preferably comprising 1-5 ethoxy units; mid-chain branched alkyl sulfates as discussed in US 6,020,303 and US 6,060,443; and mid-chain branched alkyl alkoxy sulfates as discussed in US 6,008,181 and US 6,020,303.
  • AS branched-chain and random alkyl sulfates
  • AS branched-chain and random alkyl sulfates
  • AExS alkyl alkoxy sulfates
  • alkyl preferably dialkyl, sulfosuccinates and/or sulfoacetate.
  • the dialkyl sulfosuccinate may be a C 6-15 linear or branched dialkyl sulfosuccinate.
  • the alkyl moieties may be symmetrical (i.e., the same alkyl moieties) or asymmetrical (i.e., different alkyl moieties) .
  • the alkyl moiety is symmetrical.
  • compositions of the invention will preferably comprise no more than 15%by weight, preferably no more than 10%, even more preferably no more than 5%by weight of the total composition, of a sulfonate surfactant.
  • a sulfonate surfactant include water-soluble salts or acids of C 10- C 14 alkyl or hydroxyalkyl, sulfonates; C 11 -C 18 alkyl benzene sulfonates (LAS) , modified alkylbenzene sulfonate (MLAS) as discussed in WO 99/05243, WO 99/05242, WO 99/05244, WO 99/05082, WO 99/05084, WO 99/05241, WO 99/07656, WO 00/23549 and WO 00/23548; methyl ester sulfonate (MES) ; and alpha-olefin sulfonate (AOS) .
  • MES methyl ester sulfonate
  • paraffin sulfonates which may be monosulfonates and/or disulfonates, obtained by sulfonating paraffins of 10 to 20 carbon atoms.
  • the sulfonate surfactants also include the alkyl glyceryl sulfonate surfactants.
  • amphoteric and zwitterionic surfactant may be included in the compositions at a level of from 0.01%to 20%, preferably from 0.2%to 15%, more preferably 0.5%to 12%by weight.
  • Suitable amphoteric and zwitterionic surfactants are amine oxides and betaines.
  • amine oxides especially coco dimethyl amine oxide or coco amido propyl dimethyl amine oxide.
  • Amine oxides may have a linear or mid-branched alkyl moiety.
  • Typical linear amine oxides include water-soluble amine oxides of the formula R 1 -N (R 2 ) (R 3 ) ⁇ O, wherein R 1 is a C 8-18 alkyl moiety; R 2 and R 3 are independently selected from the group consisting of C 1-3 alkyl groups and C 1-3 hydroxyalkyl groups and preferably include methyl, ethyl, propyl, isopropyl, 2-hydroxethyl, 2-hydroxypropyl and 3-hydroxypropyl.
  • the linear amine oxide surfactants may in particular include linear C 10 -C 18 alkyl dimethyl amine oxides and linear C 8 -C 12 alkoxy ethyl dihydroxy ethyl amine oxides.
  • Preferred amine oxides include linear C 10 , linear C 10 -C 12 , and linear C 12 -C 14 alkyl dimethyl amine oxides.
  • mid-branched means that the amine oxide has one alkyl moiety having n1 carbon atoms with one alkyl branch on the alkyl moiety having n2 carbon atoms. The alkyl branch is located on the ⁇ carbon from the nitrogen on the alkyl moiety.
  • n1 and n2 are also known in the art as an internal amine oxide.
  • the total sum of n1 and n2 is from 10 to 24 carbon atoms, preferably from 12 to 20, and more preferably from 10 to 16.
  • the number of carbon atoms for the one alkyl moiety (n1) should be approximately the same number of carbon atoms as the one alkyl branch (n2) , such that the one alkyl moiety and the one alkyl branch are symmetric.
  • symmetric means that n1 -n2 is less than or equal to 5, preferably 4, most preferably from 0 to 4 carbon atoms in at least 50 wt%, more preferably at least 75 wt%to 100 wt%of the mid-branched amine oxides for use herein.
  • the amine oxide further comprises two moieties, independently selected from a C 1-3 alkyl, a C 1-3 hydroxyalkyl group, or a polyethylene oxide group containing an average of from about 1 to about 3 ethylene oxide groups.
  • the two moieties are selected from a C 1-3 alkyl, more preferably both are selected as a C 1 alkyl.
  • surfactants include betaines such alkyl betaines, alkylamidobetaine, amidazoliniumbetaine, sulfobetaine (INCI Sultaines) as well as phosphobetaines.
  • One preferred surfactant system is a mixture of anionic surfactant and amphoteric or zwiterionic surfactants in a ratio within the range of 1: 1 to 5: 1, preferably from 1: 1 to 3.5: 1.
  • a nonionic surfactant when present as a co-surfactant, may be in a typical amount of from 0.1%to 20%, preferably 0.5%to 15%, more preferably from 0.5%to 10%by weight of the liquid detergent composition. When present as the main surfactant, it may be in a typical amount of from 0.1%to 45%, preferably 15%to 40%, more preferably 20%to 35%by weight of the total composition.
  • Suitable nonionic surfactants include the condensation products of aliphatic alcohols with from 1 to 25 moles of ethylene oxide. The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from 8 to 22 carbon atoms.
  • alkylpolyglycosides e.g. as described in WO 2012/015852.
  • alkylpolyglycosides e.g. as described in WO 2012/015852.
  • Cationic surfactants when present in the composition, are present in an effective amount of e.g. 0.1%to 20%by weight of the liquid detergent composition.
  • Suitable cationic surfactants are quaternary ammonium surfactants. Suitable quaternary ammonium surfactants are selected from the group consisting of mono C 6 -C 16 , preferably C 6 -C 10 N-alkyl or alkenyl ammonium surfactants, wherein the remaining N positions are substituted by methyl, hydroxyethyl or hydroxypropyl groups.
  • Another preferred cationic surfactant is a C 6 -C 18 alkyl or alkenyl ester of a quaternary ammonium alcohol, such as quaternary chlorine esters.
  • the detergent compositions herein may comprise at least one cationic polymer for further enhanced skin benefits.
  • the cationic polymer may be present an amount of from 0.001%to 10%, preferably from 0.01%to 5%, more preferably from 0.05%to 1%, by weight of the total composition.
  • Suitable cationic polymers contain cationic nitrogen-containing moieties such as quaternary ammonium or cationic protonated amino moieties, and may have an average molecular weight of form about 5000 to about 10 million, preferably at least about 100,000, more preferably at least about 200,000, but preferably not more than about 3,000,000. See e.g. WO 2012/015852 for further information on the use of cationic polymers in liquid dishwashing compositions.
  • the detergent compositions may further comprise one or more humectants.
  • the compositions may be without a humectant.
  • the humectant may be used in an amount of from 0.1%to 50%, preferably from 1%to 20%, more preferably from 1%to 10%, even more preferably from 1%to 6%, and most preferably from 2%to 5%by weight of the total composition.
  • Suitable humectants include those substances that exhibit an affinity for water and help enhance the absorption of water onto a substrate, preferably skin.
  • Particular suitable humectants include glycerol, diglycerol, polyethyleneglycol (PEG-4) , propylene glycol, hexylene glycol, butylene glycol, (di) propylene glycol, glyceryl triacetate, polyalkyleneglycols, and mixtures thereof.
  • Others can be polyethylene glycol ether of methyl glucose, pyrrolidone carboxylic acid (PCA) and its salts, pidolic acid and salts such as sodium pidolate, polyols like sorbitol, xylitol and maltitol, or polymeric polyols like polydextrose or natural extracts like quillaia, or lactic acid or urea. Also included are alkyl polyglycosides, polybetaine polysiloxanes, and mixtures thereof.
  • PCA pyrrolidone carboxylic acid
  • pidolic acid and salts such as sodium pidolate, polyols like sorbitol, xylitol and maltitol, or polymeric polyols like polydextrose or natural extracts like quillaia, or lactic acid or urea.
  • alkyl polyglycosides polybetaine polysiloxanes, and mixtures thereof.
  • humectants are polymeric humectants of the family of water soluble and/or swellable polysaccharides such as hyaluronic acid, chitosan and/or a fructose rich polysaccharide which is e.g. available as 1000 (CAS-No. 178463-23-5) by SOLABIA S.
  • Humectants containing oxygen atoms are preferred over those containing nitrogen or sulphur atoms. More preferred humectants are polyols or are carboxyl-containing such as glycerol, diglycerol, sorbitol, propylene glycol, polyethylene glycol, butylene glycol; and/or pidolic acid and salts thereof, and most preferred are humectants selected from the group consisting of glycerol, sorbitol, sodium lactate and urea, or mixtures thereof.
  • the detergent compositions herein may optionally further comprise an alkoxylated polyethyleneimine polymer.
  • the composition may comprise from 0.01%to 10%, preferably from 0.01%to 2%, more preferably from 0.1%to 1.5%, even more preferably from 0.2%to 1.5%by weight of the total composition of an alkoxylated polyethyleneimine polymer e.g. as described in WO 2007/135645.
  • the alkoxylated polyethyleneimine polymer may have a polyethyleneimine backbone having from 400 to 10000 weight average molecular weight, preferably from 400 to 7000 weight average molecular weight, alternatively from 3000 to 7000 weight average molecular weight.
  • the alkoxylation of the polyethyleneimine backbone includes: (1) one or two alkoxylation modifications per nitrogen atom, depending on whether the modification occurs at an internal nitrogen atom or at an terminal nitrogen atom, in the polyethyleneimine backbone, the alkoxylation modification consisting of the replacement of a hydrogen atom by a polyalkoxylene chain having an average of about 1 to about 40 alkoxy moieties per modification, wherein the terminal alkoxy moiety of the alkoxylation modification is capped with hydrogen, a C 1 -C 4 alkyl or mixtures thereof; (2) a substitution of one C 1 -C 4 alkyl moiety or benzyl moiety and one or two alkoxylation modifications per nitrogen atom, depending on whether the substitution occurs at an internal nitrogen atom or at a terminal nitrogen atom in the polyethyleneimine backbone, the alkoxylation modification consisting of the replacement of a hydrogen atom by a polyalkoxylene chain having an average of about 1 to about 40 alkoxy moieties per modification wherein the terminal
  • composition may further comprise amphiphilic graft polymers based on water soluble polyalkylene oxides (A) as a graft base and side chains formed by polymerization of a vinyl ester component (B) , said polymers having an average of not more than 1 graft site per 50 alkylene oxide units and mean molar mass Mw of from 3,000 to 100,000 as described in WO 2007/138053.
  • A water soluble polyalkylene oxides
  • B vinyl ester component
  • magnesium ions may be utilized in the detergent composition when the compositions are used in softened water that contains few divalent ions.
  • the magnesium ions preferably are added as a hydroxide, chloride, acetate, sulfate, formate, oxide or nitrate salt to the compositions of the invention.
  • the magnesium ions are present at an active level of from 0.01%to 1.5%, preferably from 0.015%to 1%, more preferably from 0.025%to 0.5%, by weight of the detergent composition.
  • the detergent compositions may optionally comprise a solvent.
  • suitable solvents include C 4- C 14 ethers and diethers, glycols, alkoxylated glycols, C 6 -C 16 glycol ethers, alkoxylated aromatic alcohols, aromatic alcohols, aliphatic branched alcohols, alkoxylated aliphatic branched alcohols, alkoxylated linear C 1 -C 5 alcohols, linear C 1 -C 5 alcohols, amines, C 8 -C 14 alkyl and cycloalkyl hydrocarbons and halohydrocarbons, and mixtures thereof.
  • the liquid detergent composition When present, the liquid detergent composition will contain from 0.01%to 20%, preferably from 0.5%to 20%, more preferably from 1%to 10%by weight of the liquid detergent composition of a solvent.
  • solvents may be used in conjunction with an aqueous liquid carrier, such as water, or they may be used without any aqueous liquid carrier being present.
  • the detergent compositions of the invention may optionally comprise a hydrotrope in an effective amount so that the liquid detergent compositions are appropriately compatible in water.
  • Suitable hydrotropes for use herein include anionic-type hydrotropes, particularly sodium, potassium and ammonium xylene sulfonate, sodium, potassium and ammonium toluene sulfonate, sodium, potassium and ammonium cumene sulfonate, and mixtures thereof, and related compounds.
  • the liquid detergent compositions of the invention may comprise from 0%to 15%by weight of the total liquid detergent composition of a hydrotrope, or mixtures thereof, preferably from 1%to 10%, most preferably from 3%to 10%by weight of the total liquid hand dishwashing composition.
  • the detergent compositions of the invention may optionally contain a polymeric suds stabilizer. These polymeric suds stabilizers provide extended suds volume and suds duration of the liquid detergent compositions. These polymeric suds stabilizers may be selected from homopolymers of (N, N-dialkylamino) alkyl esters and (N, N-dialkylamino) alkyl acrylate esters.
  • the weight average molecular weight of the polymeric suds boosters is from 1,000 to 2,000,000, preferably from 5,000 to 1,000,000, more preferably from 10,000 to 750,000, more preferably from 20,000 to 500,000, even more preferably from 35,000 to 200,000.
  • the polymeric suds stabilizer can optionally be present in the form of a salt, either an inorganic or organic salt.
  • One preferred polymeric suds stabilizer is an (N, N-dimethylamino) alkyl acrylate ester.
  • Other preferred suds boosting polymers are copolymers of hydroxypropylacrylate/dimethyl aminoethylmethacrylate (copolymer of HPA/DMAM) .
  • the polymeric suds booster/stabilizer may be present from 0.01%to 15%, preferably from 0.05%to 10%, more preferably from 0.1%to 5%, by weight of the liquid detergent composition.
  • hydrophobically modified cellulosic polymers having a number average molecular weight (Mw) below 45,000; preferably between 10,000 and 40,000; more preferably between 13,000 and 25,000.
  • the hydrophobically modified cellulosic polymers include water soluble cellulose ether derivatives, such as nonionic and cationic cellulose derivatives.
  • Preferred cellulose derivatives include methylcellulose, hydroxypropyl methylcellulose, hydroxyethyl methylcellulose, and mixtures thereof.
  • Another optional ingredient of the detergent compositions of the invention is a diamine. Since liquid detergent compositions show considerable variation, the composition may contain 0%to 15%, preferably 0.1%to 15%, preferably 0.2%to 10%, more preferably 0.25%to 6%, more preferably 0.5%to 1.5%by weight of said composition of at least one diamine.
  • Preferred organic diamines are those in which pK1 and pK2 are in the range of 8.0 to 11.5, preferably in the range of 8.4 to 11, even more preferably from 8.6 to 10.75.
  • Other preferred materials include primary/primary diamines with alkylene spacers ranging from C 4 to C 5 .
  • the detergent compositions of the invention may comprise a linear or cyclic carboxylic acid or salt thereof to improve the rinse feel of the composition.
  • Carboxylic acids useful herein include C 1-6 linear or at least 3 carbon containing cyclic acids.
  • the linear or cyclic carbon-containing chain of the carboxylic acid or salt thereof may be substituted with a substituent group selected from the group consisting of hydroxyl, ester, ether, aliphatic groups having from 1 to 6, more preferably 1 to 4 carbon atoms, and mixtures thereof.
  • Preferred carboxylic acids are those selected from the group consisting of salicylic acid, maleic acid, acetyl salicylic acid, 3-methyl salicylic acid, 4-hydroxy isophthalic acid, dihydroxyfumaric acid, 1, 2, 4-benzene tricarboxylic acid, pentanoic acid and salts thereof and mixtures thereof.
  • the carboxylic acid is in the salt form, the cation of the salt is preferably selected from alkali metal, alkaline earth metal, monoethanolamine, diethanolamine or triethanolamine and mixtures thereof.
  • the carboxylic acid or salt thereof when present, is preferably present at the level of from 0.1%to 5%, more preferably from 0.2%to 1%and most preferably from 0.25%to 0.5%, by weight of the total composition.
  • the detegent composition may contain 0-50%by weight, such as 1-40%, such as 1-30%, such as about 1%to about 20%, of a bleaching system.
  • a bleaching system Any oxygen-based 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; peracids and sources of peracids (bleach activators) ; 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- ⁇ -naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, ⁇ -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;
  • 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-1-sulfonate, 4- (decanoyloxy) benzoic acid (DOBA) , sodium 4-(nonanoyloxy) benzene-1-sulfonate (NOBS) , and/or those disclosed in WO98/17767.
  • TAED tetraacetylethylenediamine
  • ISONOBS sodium 4- [ (3, 5, 5-trimethylhexanoyl) oxy]
  • ATC acetyl triethyl citrate
  • ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly.
  • acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators.
  • ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.
  • the bleaching system may also include a bleach catalyst or booster.
  • bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1, 4, 7-trimethyl-1, 4, 7-triazacyclononane (Me3-TACN) or 1, 2, 4, 7-tetramethyl-1, 4, 7-triazacyclononane (Me4-TACN) , in particular Me3-TACN, such as the dinuclear manganese complex [ (Me3-TACN) Mn (O) 3Mn (Me3-TACN) ] (PF6) 2, and [2, 2', 2” -nitrilotris (ethane-1, 2-diylazanylylidene- ⁇ N-methanylylidene) triphenolato- ⁇ 3O] manganese (III) .
  • the bleach catalysts include
  • 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 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.
  • Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
  • the detergent compositions may contain about 0-65%by weight, such as about 5%to about 50%, 20-60%of a detergent builder or co-builder, or a mixture thereof.
  • the level of builder is typically in the range 40-65%, particularly in the range 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 Clariant) , 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” -nitri
  • the detergent compositions may also contain from about 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) .
  • 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 ethylenediaminetetramethylenetetrakis
  • EDTMPA diethylenetriaminepentamethylenepentakis (phosphonic acid)
  • DTMPA or DTPMPA N- (2-hydroxyethyl) iminodiacetic acid
  • ASMA aspartic acid-N-monoacetic acid
  • the detergent compositions herein can further comprise various other optional ingredients suitable for use in liquid detergent compositions such as perfume, dyes, opacifiers, other enzymes, chelants, pH buffering means and rheology modifiers, including those of the polyacrylate, polysaccharide or polysaccharide derivative type and/or a combination of a solvent and a polycarboxylate polymer.
  • the detergent compositions herein are typically thickened and preferably have a viscosity from 50 to 5000 centipoises (50-5000 mPa*s) , more preferably from 100 to 4000 centipoises (100-4000 mPa*s) , even more preferably from 500-3500 centipoises (500-3500 mPa*s) , and most preferably from 800 to 3000 centipoises (800-3000 mPa*s) at 20 s-1 and 20°C.
  • Viscosity can be determined by conventional methods known in the art, for example measured using an AR 550 rheometer from TA Instruments using a plate steel spindle at 40 mm diameter and a gap size of 500 ⁇ m.
  • the high shear viscosity at 20 s-1 and low shear viscosity at 0.05 s-1 can be obtained from a logarithmic shear rate sweep from 0.1 s-1 to 25 s-1 in 3 minutes time at 20°C.
  • the preferred rheology may be achieved using internal existing structuring with detergent ingredients or by employing an external rheology modifier and/or a crystalline structurant, which provides the composition with a pseudoplastic or shear thinning rheology profile and with time-dependent recovery of viscosity after shearing (thixotropy) .
  • the detegent compositions of the invention may further comprise one or more crystalline structurants, which are materials that form a thread-like structuring system and/or an insoluble particle network throughout the matrix of the composition.
  • the crystalline structurants may be crystallized in situ within the aqueous liquid matrix of the composition or within a pre-mix which is used to form such an aqueous liquid matrix. It has been found that the network generated by the crystalline wax structurant prevents the hydrophobic emollient droplets from coalescing and phase splitting in the product, thereby providing excellent stability of a hand dishwashing liquid composition.
  • said crystalline structurant When present, said crystalline structurant will typically be comprised at a level of from 0.02%to 5%, preferably from 0.025%to 3%, more preferably from 0.05%to 2%, most preferably from 0.1%to 1.5%by weight of the total composition.
  • Preferred crystalline structurants are: hydroxyl-containing crystalline structuring agents such as a hydroxyl-containing fatty acid, fatty ester or fatty soap wax-like materials or the like such as the ones described in US 6,080,707.
  • Suitable crystalline structurants include C 10-22 ethylene glycol fatty acid esters.
  • C 10-22 ethylene glycol fatty acid esters can be used alone or in combination with another crystalline structurant such as hydrogenated castor oil.
  • Typical examples are monoesters and/or diesters of ethylene glycol, propylene glycol, diethylene glycol, dipropylene glycol, triethylene glycol or tetraethylene glycol with fatty acids containing from about 6 to about 22, preferably from about 12 to about 18 carbon atoms, such as caproic acid, caprylic acid, 2-ethyhexanoic acid, capric acid, lauric acid, isotridecanoic acid, myristic acid, palmitic acid, palmitoleic acid, stearic acid, isostearic acid, oleic acid, elaidic acid, petroselic acid, linoleic acid, linolenic acid, arachic acid, gadoleic acid, behe
  • the detergent compositions may contain 0.005-10%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.
  • Exemplary polymers include (carboxymethyl) cellulose (CMC) , poly (vinyl alcohol) (PVA) , poly (ethyleneglycol) or poly (ethylene oxide) (PEG or PEO) , ethoxylated poly (ethyleneimine) , (carboxymethyl) inulin (CMI) , carboxylate polymers and polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers, acrylate/styrene copolymers, poly (aspartic) acid, and lauryl methacrylate/acrylic acid copolymers, hydrophobically modified CMC (HM-CMC) , silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly (ethylene terephthalate) and poly (oxyethene terephthalate) (PET-POET) , poly (vinylpyrrolidone) (PVP) , poly (vinylimidazole)
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S-403E and Chromabond S-100 from Ashland Aqualon, and HP 165, HP 50 (Dispersing agent) , HP 53 (Dispersing agent) , HP 59 (Dispersing agent) , HP 56 (dye transfer inhibitor) , 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.
  • Particularly preferred polymer is ethoxylated homopolymer HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.
  • Further exemplary polymers include sulfonated polycarboxylates, ethylene oxide-propylene oxide copolymers (PEO-PPO) , copolymers of PEG with and vinyl acetate, and diquaternium ethoxy sulfate or quaternized sulfated ethoxylated hexamethylenediamine.
  • PEO-PPO ethylene oxide-propylene oxide copolymers
  • Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated.
  • the detergent compositions may also comprise one or more microorganisms, such as one or more fungi, yeast, or bacteria.
  • the one or more microorganisms are dehydrated (for example by lyophilization) bacteria or yeast, such as a strain of Lactobacillus.
  • the microrganisms are one or more microbial spores (as opposed to vegetative cells) , such as bacterial spores; or fungal spores, conidia, hypha.
  • the one or more spores are Bacillus endospores; even more preferably the one or more spores are endospores of Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus megaterium.
  • microrganisms may be included in the detergent composition or additive in the same way as enzymes (see below) .
  • the detergent 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.I.
  • 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 WO2007/087243.
  • any detergent components known in the art for use in laundry/ADW/hard surface cleaning detergents may also be utilized.
  • Other optional detergent components include anti-corrosion agents, anti-shrink agents, anti-soil redeposition agents, anti-wrinkling agents, bactericides, binders, corrosion inhibitors, disintegrants/disintegration agents, dyes, enzyme stabilizers (including boric acid, borates, CMC, and/or polyols such as propylene glycol) , fabric conditioners including clays, fillers/processing aids, fluorescent whitening agents/optical brighteners, foam boosters, foam (suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, tarnish inhibitors, and wicking agents, either alone or in combination.
  • Any ingredient known in the art for use in laundry/ADW/hard surface cleaning detergents may be utilized. The choice of such ingredients is well within the skill of the artisan.
  • the detergent 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 detergent 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 detergent 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%.
  • Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.
  • diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4, 4'-bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2, 2'-disulfonate, 4, 4'-bis- (2, 4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulfonate, 4, 4'-bis- (2-anilino-4- (N-methyl-N-2-hydroxy-ethylamino) -s-triazin-6-ylamino) stilbene-2, 2'-disulfonate, 4, 4'-bis- (4-phenyl-1, 2, 3-triazol-2-yl) stilbene-2, 2'-disulfonate and sodium 5- (2H-naphtho [1, 2-d] [1, 2, 3] triazol-2-yl) -2- [ (E) -2-phenylvinyl)
  • 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.
  • Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins.
  • Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt %to upper levels of 0.5 or even 0.75 wt%.
  • the detergent 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 are amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure.
  • the core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference) .
  • random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference) .
  • Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1867808 or WO 2003/040279 (both are hereby incorporated by reference) .
  • Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, 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 detergent 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
  • ethoxylated polyethyleneimines ethoxylated polyethyleneimines.
  • the cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.
  • the detergent 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.
  • adjunct materials 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 detergent composition as described above may comprise one or more microorganisms or microbes.
  • any microorganism (s) may be used in the enzyme/detergent formulations in any suitable amount (s) /concentration (s) .
  • Microorganisms may be used as the only biologically active ingredient, but they may also be used in conjunction with one or more of the enzymes described above.
  • the purpose of adding the microorganism (s) may, for example, be to reduce malodor as described in WO 2012/112718.
  • Other purposes could include in-situ production of desirable biological compounds, or inoculation/population of a locus with the microorganism (s) to competitively prevent other non-desirable microorganisms form populating the same locus (competitive exclusion) .
  • microorganism generally means small organisms that are visible through a microscope. Microorganisms often exist as single cells or as colonies of cells. Some microorganisms may be multicellular. Microorganisms include prokaryotic (e.g., bacteria and archaea) and eurkaryotic (e.g., some fungi, algae, protozoa) organisms. Examples of bacteria may be Gram-positive bacteria or Gram-negative bacteria. Example forms of bacteria include vegetative cells and endospores. Examples of fungi may be yeasts, molds and mushrooms. Example forms of fungi include hyphae and spores. Herein, viruses may be considered microorganisms.
  • prokaryotic e.g., bacteria and archaea
  • eurkaryotic e.g., some fungi, algae, protozoa
  • Examples of bacteria may be Gram-positive bacteria or Gram-negative bacteria.
  • Example forms of bacteria include vegetative cells and endospores. Examples of fungi may be yeasts
  • Microorganisms may be recombinant or non-recombinant.
  • the microorganisms may produce various substances (e.g., enzymes) that are useful for inclusion in detergent compositions. Extracts from microorganisms or fractions from the extracts may be used in the detergents. Media in which microorganisms are cultivated, or extracts or fractions from the media may also be used in detergents.
  • specific of the microorganisms, substances produced by the microorganisms, extracts, media, and fractions thereof, may be specifically excluded from the detergents.
  • the microorganisms, or substances produced by, or extracted from, the microorganisms may activate, enhance, preserve, prolong, and the like, detergent activity or components contained with detergents.
  • microorganisms may be cultivated using methods known in the art.
  • the microorganisms may then be processed or formulated in various ways.
  • the microorganisms may be desiccated (e.g., lyophilized) .
  • the microorganisms may be encapsulated (e.g., spray drying) .
  • Many other treatments or formulations are possible. These treatments or preparations may facilitate retention of microorganism viability over time and/or in the presence of detergent components.
  • microorganisms in detergents may not be viable.
  • the processed/formulated microorganisms may be added to detergents prior to, or at the time the detergents are used.
  • the microorganism is a species of Bacillus, for example, at least one species of Bacillus selected from the group consisting of Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus atrophaeus, Bacillus pumilus, Bacillus megaterium, or a combination thereof.
  • Bacillus subtilis Bacillus subtilis
  • Bacillus amyloliquefaciens Bacillus licheniformis
  • Bacillus atrophaeus Bacillus pumilus
  • Bacillus megaterium or a combination thereof.
  • the aforementioned Bacillus species are on an endospore form, which significantly improves the storage stability.
  • the detergent 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. They can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch.
  • Preferred films are polymeric materials preferably polymers which are formed into a film or sheet.
  • Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC) .
  • the level of polymer in the film for example PVA is at least about 60%.
  • Preferred average molecular weight will typically be about 20,000 to about 150,000.
  • Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water soluble film.
  • the compartment for liquid components can be different in composition than compartments containing solids: US2009/0011970 A1.
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
  • a liquid or gel detergent which is not unit dosed, may be aqueous, typically containing at least 20%by weight and up to 95%water, such as up to about 70%water, up to about 65%water, up to about 55%water, up to about 45%water, up to about 35%water.
  • Other types of liquids including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel.
  • An aqueous liquid or gel detergent may contain from 0-30%organic solvent.
  • a liquid or gel detergent may be non-aqueous.
  • the alpha-amylases of the invention may be added to soap bars and used for hand washing laundry, dishwash, surface, fabrics and/or textiles.
  • laundry soap bar includes laundry bars, soap bars, combo bars, syndet bars and detergent bars.
  • the types of bar usually differ in the type of surfactant they contain, and the term laundry soap bar includes those containing soaps from fatty acids and/or synthetic soaps.
  • the laundry soap bar has a physical form which is solid and not a liquid, gel or a powder at room temperature.
  • the term solid is defined as a physical form which does not significantly change over time, i.e. if a solid object (e.g. laundry soap bar) is placed inside a container, the solid object does not change to fill the container it is placed in.
  • the bar is a solid typically in bar form but can be in other solid shapes such as round or oval.
  • the laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hemiacetal adduct) , boric acid, borate, borax and/or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerine, pH controlling compounds such as fatty acids, citric acid, acetic acid and/or formic acid, and/or a salt of a monovalent cation and an organic anion wherein the monovalent cation may be for example Na + , K + or NH 4 + and the organic anion may be for example formate, acetate, citrate or lactate such that the salt of a monovalent cation and an organic anion may be, for example, sodium formate.
  • protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or
  • the laundry soap bar may also contain complexing agents like EDTA and HEDP, perfumes and/or different type of fillers, surfactants e.g. anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelators, stabilizing agents, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, suds suppressers, structurants, binders, leaching agents, bleaching activators, clay soil removal agents, anti-redeposition agents, polymeric dispersing agents, brighteners, fabric softeners, perfumes and/or other compounds known in the art.
  • the laundry soap bar may be processed in conventional laundry soap bar making equipment such as but not limited to: mixers, plodders, e.g a two stage vacuum plodder, extruders, cutters, logo-stampers, cooling tunnels and wrappers.
  • the invention is not limited to preparing the laundry soap bars by any single method.
  • the premix of the invention may be added to the soap at different stages of the process.
  • the premix containing a soap, alpha-amylases, optionally one or more additional enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion may be prepared and and the mixture is then plodded.
  • the alpha-amylases and optional additional enzymes may be added at the same time as the protease inhibitor for example in liquid form.
  • the process may further comprise the steps of milling, extruding, cutting, stamping, cooling and/or wrapping.
  • a granular detergent may be formulated as described in WO09/092699, EP1705241, EP1382668, WO07/001262, US6472364, WO04/074419 or WO09/102854.
  • Other useful detergent formulations are described in WO09/124162, WO09/124163, WO09/117340, WO09/117341, WO09/117342, WO09/072069, WO09/063355, WO09/132870, WO09/121757, WO09/112296, WO09/112298, WO09/103822, WO09/087033, WO09/050026, WO09/047125, WO09/047126, WO09/047127, WO09/047128, WO09/021784, WO09/010375, WO09/000605, WO09/122125, WO09/095645, WO09/040544, WO09/040545, WO09/0247
  • WO2011023716 WO2010142539, WO2010118959, WO2010115813, WO2010105942, WO2010105961, WO2010105962, WO2010094356, WO2010084203, WO2010078979, WO2010072456, WO2010069905, WO2010076165, WO2010072603, WO2010066486, WO2010066631, WO2010066632, WO2010063689, WO2010060821, WO2010049187, WO2010031607, WO2010000636.
  • the enzyme of the invention 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-granulates for the detergent industry are disclosed in the IP. com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes by the use of co-granulates 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.
  • 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 an aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • the multi-enzyme co-granule may comprise an enzyme of the invention and (a) one or more enzymes selected from the group consisting of first-wash lipases, cleaning cellulases, xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases and mixtures thereof; and (b) one or more enzymes selected from the group consisting of hemicellulases, proteases, care cellulases, cellobiose dehydrogenases, xylanases, phospho lipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase, amy
  • the enzyme may be formulated as a liquid enzyme formulation, which is generally a pourable composition, though it may also have a high viscosity.
  • the physical appearance and properties of a liquid enzyme formulation may vary a lot -for example, they may have different viscosities (gel to water-like) , be colored, not colored, clear, hazy, and even with solid particles like in slurries and suspensions.
  • the minimum ingredients are the enzyme and a solvent system to make it a liquid.
  • the liquid enzyme formulation may also comprise other enzyme activities, such as protease, amylase, lipase, cellulase, and/or nuclease (e.g., DNase, RNase) activities.
  • the solvent system may comprise water, polyols (such as glycerol, (mono, di, or tri) propylene glycol, (mono, di, or tri) ethylene glycol, sugar alcohol (e.g. sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol or adonitol) , polypropylene glycol, and/or polyethylene glycol) , ethanol, sugars, and salts.
  • polyols such as glycerol, (mono, di, or tri) propylene glycol, (mono, di, or tri) ethylene glycol
  • sugar alcohol e.g. sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol or adonitol
  • polypropylene glycol e.g. sorbitol, mannitol, ery
  • a liquid enzyme formulation may be prepared by mixing a solvent system and an enzyme concentrate with a desired degree of purity (or enzyme particles to obtain a slurry/suspension) .
  • liquid enzyme composition comprises:
  • the enzyme in the liquid composition of the invention may be stabilized using conventional stabilizing agents.
  • stabilizing agents include, but are not limited to, sugars like glucose, fructose, sucrose, or trehalose; addition of salt to increase the ionic strength; divalent cations (e.g., Ca 2+ or Mg 2+ ) ; and enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP) .
  • Selecting the optimal pH for the formulation may be very important for enzyme stability. The optimal pH depends on the specific enzyme but is typically in the range of pH 4-9.
  • surfactants like nonionic surfactant (e.g., alcohol ethoxylates) can improve the physical stability of the enzyme formulations.
  • composition comprising an enzyme, wherein the composition further comprises:
  • a polyol preferably selected from glycerol, (mono, di, or tri) propylene glycol, (mono, di, or tri) ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol and adonitol;
  • an additional enzyme preferably selected from protease, amylase, or lipase
  • a surfactant preferably selected from anionic and nonionic surfactants
  • Slurries or dispersions of enzymes are typically prepared by dispersing small particles of enzymes (e.g., spray-dried particles) in a liquid medium in which the enzyme is sparingly soluble, e.g., a liquid nonionic surfactant or a liquid polyethylene glycol. Powder can also be added to aqueous systems in an amount so not all go into solution (above the solubility limit) .
  • Another format is crystal suspensions which can also be aqueous liquids (see for example WO2019/002356) .
  • Another way to prepare such dispersion is by preparing water-in-oil emulsions, where the enzyme is in the water phase, and evaporate the water from the droplets.
  • Such slurries/suspension can be physically stabilized (to reduce or avoid sedimentation) by addition of rheology modifiers, such as fumed silica or xanthan gum, typically to get a shear thinning rheology.
  • the enzyme may also be formulated as a solid/granular enzyme formulation.
  • Non-dusting granulates may be produced, e.g. as disclosed in US 4,106,991 and US 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.
  • the enzyme may be formulated as a granule for example as a co-granule that combines one or more enzymes or benefit agents (such as MnTACN or other bleaching components) .
  • additional enzymes include proteases, amylases, lipases, cellulases, and/or nucleases (e.g., DNase, RNase) .
  • 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 are disclosed in the IP. com disclosure IPCOM000200739D.
  • An embodiment of the invention relates to an enzyme granule/particle comprising a enzyme.
  • 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 ⁇ m, particularly 50-1500 ⁇ m, 100-1500 ⁇ m or 250-1200 ⁇ m.
  • the core may include additional materials such as fillers, fibre materials (cellulose or synthetic fibres) , stabilizing agents, solubilising agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances.
  • the core may include binders, such as synthetic polymer, wax, fat, or carbohydrate.
  • the core may comprise a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend.
  • the core may consist of an inert particle with the enzyme absorbed into it, or applied onto the surface, e.g., by fluid bed coating.
  • the core may have a diameter of 20-2000 ⁇ m, particularly 50-1500 ⁇ m, 100-1500 ⁇ m or 250-1200 ⁇ m.
  • 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.
  • Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Volume 1; 1980; Elsevier. These methods are well-known in the art and have also been described in international patent application WO2015/028567, pages 3-5, which is incorporated by reference.
  • the core of the enzyme granule/particle may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule.
  • the optional coating (s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG) , methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA) . Examples of enzyme granules with multiple coatings are shown in WO 93/07263 and WO 97/23606.
  • Such coatings are well-known in the art, and have earlier been described in, for example, WO00/01793, WO2001/025412, and WO2015/028567, which are incorporated by reference.
  • the present invention provides a granule, which comprises:
  • Another aspect of the invention relates to a layered granule, comprising:
  • (c) optionally a (salt) coating consisting of one or more layer (s) surrounding the enzyme containing coating.
  • the enzyme may also be formulated as an encapsulated enzyme formulation (an ‘encapsulate’ ) . This is particularly useful for separating the enzyme from other ingredients when the enzyme is added into, for example, a (liquid) cleaning composition, such as the detergent compositions described below.
  • Physical separation can be used to solve incompatibility between the enzyme (s) and other components. Incompatibility can arise if the other components are either reactive against the enzyme, or if the other components are substrates of the enzyme. Other enzymes can be substrates of amylase.
  • the enzyme may be encapsulated in a matrix, preferably a water-soluble or water dispersible matrix (e.g., water-soluble polymer particles) , for example as described in WO 2016/023685.
  • a water-soluble polymeric matrix is a matrix composition comprising polyvinyl alcohol. Such compositions are also used for encapsulating detergent compositions in unit-dose formats.
  • the enzyme may also be encapsulated in core-shell microcapsules, for example as described in WO 2015/144784, or as described in the IP. com disclosure IPCOM000239419D.
  • Such core-shell capsules can be prepared using a number of technologies known in the art, e.g., by interfacial polymerization using either a water-in-oil or an oil-in-water emulsion, where polymers are crosslinked at the surface of the droplets in the emulsion (the interface between water and oil) , thus forming a wall/membrane around each droplet/capsule.
  • the detergent compositions may comprise one or more additional enzymes such as a protease, lipase, cutinase, second amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • additional enzymes such as a protease, lipase, cutinase, second amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • the detergent composition of the invention may further comprise one or more additional enzymes which provide cleaning and/or wash performance.
  • suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, ⁇ -glucanases, arabinosidases, nucleases, hyaluronidase, chondroitinase, laccase, chlorophyllases, other amylases, or mixtures thereof.
  • a typical combination is an enzyme cocktail that may comprise e.g. alpha-amylase and protease in conjunction with a mannanase.
  • the aforementioned additional enzymes may be present at levels from 0.00001 to 2wt%, from 0.0001 to 1wt%or from 0.001 to 0.5wt%enzyme protein by weight of the active components in the composition.
  • 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.
  • preferred enzymes includes a cellulase.
  • Suitable cellulases include mono-component and mixtures of enzymes of bacterial or fungal origin. Chemically modified or protein engineered mutants are also contemplated.
  • the cellulase may for example be a mono-component or a mixture of mono-component endo-1, 4-beta-glucanase also referred to as endoglucanase.
  • 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 96/11262, 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 are endo-beta-1, 4-glucanase enzyme having a sequence of at least 97%identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO: 2 of WO 2002/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60%identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.
  • cellulases include Carezyme Classic, (Novozymes A/S) , Puradax HA, and Puradax EG (available from Genencor International Inc. ) and KAC-500 (B) TM (Kao Corporation) .
  • preferred enzymes includes a mannanase.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes A/S) .
  • preferred enzymes includes a peroxidase.
  • a suitable peroxidase is preferably a peroxidase enzyme comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) , or any fragment derived therefrom, exhibiting peroxidase activity.
  • IUBMB 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.
  • Suitable peroxidases also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase may be a chloroperoxidase.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In a preferred method the vanadate-containing haloperoxidase is combined with a source of chloride ion.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Caldariomyces e.g., C. fumago
  • Alternaria Curvularia
  • Curvularia e.g., C. verruculosa and C. inaequalis
  • Drechslera Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • the haloperoxidase may be derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461, or Geniculosporium sp. as described in WO 01/79460.
  • Suitable oxidases include, 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 or fungi (including filamentous fungi and yeasts) .
  • Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, 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.
  • preferred enzymes includes a nucleases.
  • Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases) which are any enzyme that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA or RNA backbone respectively, thus degrading DNA and RNA.
  • DNases deoxyribonucleases
  • RNases ribonucleases
  • Exonucleases digest nucleic acids from the ends. Endonucleases act on regions in the middle of target molecules.
  • the nuclease is preferably a DNase, which is preferable is obtainable from a microorganism, preferably a fungi or bacterium.
  • a DNase which is obtainable from a species of Bacillus is preferred; in particular a DNase which is obtainable from Bacillus cibi, Bacillus subtilis or Bacillus licheniformis is preferred. Examples of such DNases are described in WO 2011/098579, WO2014/087011 and WO2017/060475. Particularly preferred is also a DNase obtainable from a species of Aspergillus; in particular a DNase which is obtainable from Aspergillus oryzae, such as a DNase described in WO 2015/155350.
  • the detergent enzyme (s) may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes.
  • a detergent additive of the invention i.e., a separate additive or a combined additive
  • Preferred detergent additive formulations are granulates, in particular non-dusting granulates as described above, liquids, in particular stabilized liquids, or slurries.
  • preferred enzymes includes a protease.
  • Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants.
  • the protease may be an alkaline protease, such as a serine protease or a metalloprotease.
  • a serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as a subtilisin.
  • a metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M8 families.
  • subtilases refers to a sub-group of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997) 501-523.
  • Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus
  • detergent proteases have generally been obtained from bacteria and in particular from Bacillus.
  • Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii.
  • Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’ , subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93/18140) .
  • Other useful proteases are e.g. those described in WO 01/16285 and WO 02/16547.
  • trypsin-like proteases examples include the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
  • metalloproteases include the neutral metalloproteases described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015/158723 and WO 2016/075078.
  • proteases examples include the protease variants described in WO 89/06279 WO 92/19729, WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 03/006602, WO 2004/003186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2014/207227, WO 2016/087617 and WO 2016/174234.
  • Preferred protease variants may, for example, comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V
  • Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Bacillus lentus protease also known as subtilisin 309
  • BPN Bacillus amyloliquefaciens protease
  • Such protease variants preferably have at least 80%sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016/001449.
  • protease of interest is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 91/02792, and variants thereof which are described for example in WO 92/21760, WO 95/23221, EP 1921147, EP 1921148 and WO 2016/096711.
  • the protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004/067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 111, 171, 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004/067737, wherein said protease variant has a sequence identity of at least 75%but less than 100%to SEQ ID NO: 1 of WO 2004/067737.
  • TY145 variants of interest are described in e.g. WO 2015/014790, WO 2015/014803, WO 2015/014804, WO 2016/097350, WO 2016/097352, WO 2016/097357 and WO 2016/097354.
  • proteases examples include:
  • variants of SEQ ID NO: 1 of WO 2016/001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D and L262E, for example a variant with the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261W and L262E, or with the substitutions S9E, N43R, N76D, N185E, S188E, Q191N, A194P, Q206L, Y209W, S259D and L262E, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
  • Suitable commercially available protease enzymes include those sold under the trade names Duralase TM , Durazym TM , Ultra, Ultra, Primase TM , Ultra, Ultra, Blaze 100T, Blaze 125T, Blaze 150T, Blaze 200T, Uno, In and Excel (Novozymes A/S) , those sold under the tradename Maxatase TM , Maxacal TM , Ox, OxP, FN2 TM , FN3 TM , FN4 exTM , Excellenz TM P1000, Excellenz TM P1250, Eraser TM , P100, Purafect Prime, Preferenz P110 TM , Effectenz P1000 TM , Effectenz P1050 TM , Ox, Effectenz TM P2000, Purafast TM , Opticlean TM and (Danisco/DuPont) , BLAP (sequence shown in Figure 29 of US 5352604) and variants here
  • preferred enzymes includes a lipase and/or cutinase.
  • Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580) , lipase from strains of Pseudomonas (some of these now renamed to Burkholderia) , e.g. P. alcaligenes or P.
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541, WO94/25578, WO95/14783, WO95/30744, WO95/35381, WO95/22615, WO96/00292, WO97/04079, WO97/07202, WO00/34450, WO00/60063, WO01/92502, WO07/87508 and WO09/109500.
  • Preferred commercial lipase products include include Lipolase TM , Lipex TM ; Lipolex TM and Lipoclean TM (Novozymes A/S) , Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades) .
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/111143) , acyltransferase from Mycobacterium smegmatis (WO05/56782) , perhydrolases from the CE 7 family (WO09/67279) , and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10/100028) .
  • preferred enzymes includes another (second) amylase.
  • Suitable amylases which can be used together with the compositions of the invention may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1,296,839.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90%sequence identity to SEQ ID NO: 3 thereof.
  • Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.
  • amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90%sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
  • amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90%sequence identity thereof.
  • Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209 and Q264.
  • hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of SEQ ID NO: 4 are those having the substitutions:
  • amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90%sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269.
  • Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
  • Additional amylases which can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90%sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7.
  • Preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering.
  • More preferred variants are those having a deletion in two positions selected from 181, 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184.
  • Most preferred amylase variants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
  • amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90%sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90%sequence identity to SEQ ID NO: 10 in WO 01/66712.
  • Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264.
  • amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90%sequence identity to SEQ ID NO: 2 thereof.
  • Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475.
  • More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E, R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E, R, N272E, R, S243Q, A, E, D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183.
  • Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
  • variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.
  • amylases having SEQ ID NO: 1 of WO13184577 or variants having 90%sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, I203, S241, R458, T459, D460, G476 and G477.
  • More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181.
  • Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.
  • amylases having SEQ ID NO: 1 of WO10104675 or variants having 90%sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477 and G478.
  • More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of I181 and/or G182.
  • Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.
  • amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90%sequence identity to SEQ ID NO: 12.
  • Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484.
  • Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R118K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
  • amylase variants such as those described in WO2011/098531, WO2013/001078 and WO2013/001087.
  • amylases are Amplify Prime TM , Atlantic TM , Arctic TM , Everest TM , Duramyl TM , Termamyl TM , Fungamyl TM , Stainzyme TM , Stainzyme Plus TM , Natalase TM , Liquozyme X and BAN TM (from Novozymes A/S) , and Rapidase TM , Purastar TM /Effectenz TM , Powerase, Preferenz S1000, Preferenz S100, Preferenz S110 and Preferenz S210 (from Genencor International Inc. /DuPont) .
  • the protease (s) may be stabilized using compounds that act by temporarily reducing the proteolytic activity (reversible inhibitors) .
  • composition of the invention may also include a protease inhibitor/stabilizer, which is a reversible inhibitor of protease activity, e.g., serine protease activity.
  • a protease inhibitor/stabilizer which is a reversible inhibitor of protease activity, e.g., serine protease activity.
  • the protease inhibitor is a (reversible) subtilisin protease inhibitor.
  • the protease inhibitor may be a peptide aldehyde, boric acid, or a boronic acid; or a derivative of any of these.
  • the protease inhibitor may be a boronic acid or a derivative thereof; preferably, a phenylboronic acid or a derivative thereof.
  • the phenyl boronic acid derivative is of the following formula:
  • R is selected from the group consisting of hydrogen, hydroxy, C1-C6 alkyl, substituted C1-C6 alkyl, C1-C6 alkenyl and substituted C1-C6 alkenyl.
  • R is hydrogen, CH 3 , CH 3 CH 2 or CH 3 CH 2 CH 2 .
  • the protease inhibitor (phenyl boronic acid derivative) is 4-formyl-phenyl boronic acid (4-FPBA) .
  • the protease inhibitor is selected from the group consisting of thiophene-2 boronic acid, thiophene-3 boronic acid, acetamidophenyl boronic acid, benzofuran-2 boronic acid, naphtalene-1 boronic acid, naphtalene-2 boronic acid, 2-FPBA, 3-FBPA, 4-FPBA, 1-thianthrene boronic acid, 4-dibenzofuran boronic acid, 5-methylthiophene-2 boronic, acid, thionaphtrene boronic acid, furan-2 boronic acid, furan-3 boronic acid, 4, 4 biphenyl-diborinic acid, 6-hydroxy-2-naphtalene, 4- (methylthio) phenyl boronic acid, 4 (trimethyl-silyl) phenyl boronic acid, 3-bromothiophene boronic acid, 4-methylthiophene boronic acid, 2-naphtyl
  • boronic acid derivatives suitable as protease inhibitors in the detergent composition are described in US 4,963,655, US 5,159,060, WO 95/12655, WO 95/29223, WO 92/19707, WO 94/04653, WO 94/04654, US 5442100, US 5488157 and US 5472628.
  • the protease stabilizer may have the formula: P-A-L-B-B0-R*wherein:
  • A is absent if L is absent, or is 1 or 2 amino acid residues connected to L via the N-terminal; thus, A may represent A1 or A2-A1, where A2 and A1 each represent one amino acid residue;
  • R is independently selected from the group consisting of C 1-6 alkyl, C 6-10 aryl or C 7-10 arylalkyl, optionally substituted with one or more, identical or different, substituents R’;
  • R is a C 1-6 alkyl group
  • P is selected from the group consisting of hydrogen, or -if L is absent -an N-terminal protection group;
  • B0 may be a single amino acid residue with L-or D-configuration, which is connected to H via the C-terminal of the amino acid.
  • B0 are the D-or L-form of arginine (Arg) , 3, 4-dihydroxyphenylalanine, isoleucine (Ile) , leucine (Leu) , methionine (Met) , norleucine (Nle) , norvaline (Nva) , phenylalanine (Phe) , m-tyrosine, p-tyrosine (Tyr) and valine (Val) .
  • a particular embodiment is when B0 is leucine, methionine, phenylalanine, p-tyrosine, or valine. Paticularly preferred is p-tyrosine.
  • B1 which is connected to B0 via the C-terminal of the amino acid, may be an aliphatic, hydrophobic and/or neutral amino acid.
  • B1 are alanine (Ala) , cysteine (Cys) , glycine (GIy) , isoleucine (Ile) , leucine (Leu) , norleucine (Nle) , norvaline (Nva) , proline (Pro) , serine (Ser) , threonine (Thr) and valine (VaI) .
  • Particular examples of B1 are alanine, glycine, isoleucine, leucine and valine. A particular embodiment is when B1 is alanine, glycine, or valine.
  • B2 if present, is connected to B1 via the C-terminal of the amino acid, and may be an aliphatic, hydrophobic, neutral and/or polar amino acid.
  • B2 are alanine (Ala) , arginine (Arg) , capreomycidine (Cpd) , cysteine (Cys) , glycine (GIy) , isoleucine (Ile) , leucine (Leu) , norleucine (Nle) , norvaline (Nva) , phenylalanine (Phe) , proline (Pro) , serine (Ser) , threonine (Thr) , and valine (VaI) .
  • B2 are alanine, arginine, capreomycidine, glycine, isoleucine, leucine, phenylalanine and valine.
  • a particular embodiment is when B2 is arginine, glycine, leucine, phenylalanine, or valine.
  • B3 if present, is connected to B2 via the C-terminal of the amino acid, and may be a large, aliphatic, aromatic, hydrophobic and/or neutral amino acid.
  • B3 isoleucine (Ile) , leucine (Leu) , norleucine (Nle) , norvaline (Nva) , phenylalanine (Phe) , phenylglycine, tyrosine (Tyr) , tryptophan (Trp) and valine (VaI) .
  • Particular examples of B3 are leucine, phenylalanine, tyrosine, and tryptophan.
  • A1 if present, is connected to L via the N-terminal of the amino acid, and may be an aliphatic, aromatic, hydrophobic, neutral and/or polar amino acid.
  • Examples of A1 are alanine (Ala) , arginine (Arg) , capreomycidine (Cpd) , glycine (GIy) , isoleucine (Ile) , leucine (Leu) , norleucine (Nle) , norvaline (Nva) , phenylalanine (Phe) , threonine (Thr) , tyrosine (Tyr) , tryptophan (Trp) and valine (VaI) .
  • A1 are alanine, arginine, glycine, leucine, phenylalanine, tyrosine, tryptophan and valine.
  • B2 is leucine, phenylalanine, tyrosine or tryptophan.
  • A2 if present, is connected to A1 via the N-terminal of the amino acid, and may be a large, aliphatic, aromatic, hydrophobic and/or neutral amino acid.
  • A2 are arginine (Arg) , isoleucine (Ile) , leucine (Leu) , norleucine (Nle) , norvaline (Nva) , phenylalanine (Phe) , phenylglycine, Tyrosine (Tyr) , tryptophan (Trp) and valine (VaI) .
  • Particular examples of A2 are phenylalanine and tyrosine.
  • the N-terminal protection group P may be selected from formyl, acetyl (Ac) , benzoyl (Bz) , trifluoroacetyl, methoxysuccinyl, aromatic and aliphatic urethane protecting groups such as fluorenylmethyloxycarbonyl (Fmoc) , methoxycarbonyl (Moc) , (fluoromethoxy) carbonyl, benzyloxycarbonyl (Cbz) , t-butyloxycarbonyl (Boc) and adamantyloxycarbonyl; p-methoxybenzyl carbonyl, benzyl (Bn) , p-methoxybenzyl (PMB) , p-methoxyphenyl (PMP) , methoxyacetyl, methylamino carbonyl, methylsulfonyl, ethylsulfonyl, benzylsulf
  • Suitable peptide aldehydes are described in WO94/04651, WO95/25791, WO98/13458, WO98/13459, WO98/13460, WO98/13461, WO98/13462, WO07/141736, WO07/145963, WO09/118375, WO10/055052 and WO11/036153.
  • the peptide aldehyde may be Cbz-Arg-Ala-Tyr-H, Ac-Gly-Ala-Tyr-H, Cbz-Gly-Ala-Tyr-H, Cbz-Gly-Ala-Tyr-CF 3 , Cbz-Gly-Ala-Leu-H, Cbz-Val-Ala-Leu-H, Cbz-Val-Ala-Leu-CF 3 , Moc-Val-Ala-Leu-CF 3 , Cbz-Gly-Ala-Phe-H, Cbz-Gly-Ala-Phe-CF 3 , Cbz-Gly-Ala-Val-H, Cbz-Gly-Gly-Tyr-H, Cbz-Gly-Gly-Phe-H, Cbz-Arg-Val-Tyr-H, Cbz-Leu-Val-Tyr-H, Ac-Leu-Gly-Ala-T
  • the protease stabilizer may be a hydrosulfite adduct of the peptide aldehyde or ketone described above, e.g., as described in WO 2013/004636.
  • the adduct may have the formula P-A-L-B-N (H) -CHR-CH (OH) -SO 3 M, wherein P, A, L, B, and R are defined as above, and M is H or an alkali metal, preferably Na or K.
  • An aqueous solution of the hydrosulfite adduct may be prepared by reacting the corresponding peptide aldehyde with an aqueous solution of sodium bisulfite (sodium hydrogen sulfite, NaHSO 3 ) ; potassium bisulfite (KHSO 3 ) by known methods, e.g., as described in WO 98/47523; US 6,500,802; US 5,436,229; J. Am. Chem. Soc. (1978) 100, 1228; Org. Synth., Coll. vol. 7: 361.
  • sodium bisulfite sodium hydrogen sulfite
  • KHSO 3 potassium bisulfite
  • Particularly preferred peptide aldehyde protease stabilizers have the formula P-B3-B2-B1-B0-H, or a hydrosulfite adduct having the formula P-B3-B2-B1-N (H) -CHR-CHOH-SO 3 M, wherein
  • B1 and B2 are independently single amino acid residues
  • iv) B3 is a single amino acid residue, or is absent
  • R is independently selected from the group consisting of C 1-6 alkyl, C 6-10 aryl or C 7-10 arylalkyl optionally substituted with one or more, identical or different, substituents R’;
  • R is a C 1-6 alkyl group
  • P is an N-terminal protection group, preferably methoxycarbonyl (Moc) or benzyloxycarbonyl (Cbz) ;
  • ix) M is H or an alkali metal, preferably Na or K.
  • the peptide aldehyde protease stabilizer has the formula P-B2-B1-B0-H or an adduct having the formula P-B2-B1-N (H) -CHR-CHOH-SO 3 M, wherein
  • B1 and B2 are independently single amino acid residues
  • R is independently selected from the group consisting of C 1-6 alkyl, C 6-10 aryl or C 7-10 arylalkyl optionally substituted with one or more, identical or different, substituents R’;
  • R is a C 1-6 alkyl group
  • P is an N-terminal protection group, preferably methoxycarbonyl (Moc) or benzyloxycarbonyl (Cbz) ;
  • M is H or an alkali metal, preferably Na or K.
  • B0, B1, B2, B3, and P are as described above.
  • P is preferably acetyl, methoxycarbonyl, benzyloxycarbonyl, methylamino carbonyl, methylsulfonyl, benzylsulfonyl and benzylphosphoramidyl.
  • P is preferably acetyl, methoxycarbonyl, methylsulfonyl, ethylsulfonyl and methylphosphoramidyl.
  • the molar ratio of the above-mentioned peptide aldehydes (or hydrosulfite adducts) to the protease may be at least 1: 1 or 1.5: 1, and it may be less than 1000: 1, more preferred less than 500: 1, even more preferred from 100: 1 to 2: 1 or from 20: 1 to 2: 1, or most preferred, the molar ratio is from 10: 1 to 2: 1.
  • Formate salts e.g., sodium formate
  • formic acid have also shown good effects as inhibitor of protease activity. Formate can be used synergistically with the above-mentioned protease inhibitors, as shown in WO 2013/004635.
  • the formate salts may be present in the composition in an amount of at least 0.1%w/w or 0.5%w/w, e.g., at least 1.0%, at least 1.2%or at least 1.5%. The amount is typically below 5%w/w, below 4%or below 3%.
  • the protease is a metalloprotease and the inhibitor is a metalloprotease inhibitor, e.g., a protein hydrolysate based inhibitor (e.g., as described in WO 2008/134343) .
  • a metalloprotease inhibitor e.g., a protein hydrolysate based inhibitor (e.g., as described in WO 2008/134343) .
  • the present invention is also directed to use of the detergent compositions for cleaning, in particular for hard surface cleaning such as dishwashing, in particular for hand dishwashing.
  • This aspect further relates to a method of cleaning, especially for cleaning hard surfaces or for dishwashing, comprising contacting the hard surface or dishes with the detergent composition under conditions suitable for cleaning the surface or dishes.
  • the method of cleaning is for hand dishwashing and comprises contacting dishes with a detergent composition comprising an amylase as described herein under conditions suitable for cleaning the dishes.
  • amylases for these uses and cleaning methods may be any of the proteases described in more detail elsewhere herein.
  • Amylase The alpha-amylase used was an alpha-amylase variant of SEQ ID NO: 2 having the following modifications: H1*+ N54S + V56T + K72R + G109A + F113Q + R116Q + W167F + Q172G + A174S + G182*+ D183*+ G184T + N195F + V206L + K391A + P473R + G476K
  • protease used was a protease variant of SEQ ID NO: 1 of WO 2016/001449 having the following substitutions: S9E + N43R + N76D + V205I + Q206L + Y209W + S259D +N261W + L262E, wherein position numbers are based on the numbering SEQ ID NO: 2 of WO 2016/001449.
  • Stain recipe (Porridge) : Add 80 grams of rice into 1 liter of boiling tap water and boil for 15 minutes (Taigroo multifunctional induction cooktop IC-A2102, 1000 Watts) and cool down to room temperature for a 1 hour. Pour cooked rice into a sieve to remove the water. Weigh out 100 grams of cooled rice into a household mixer (Media, MJ-PB80Easy218, vegetable mode) .
  • Amylase used in the detergent composition demonstrates shinning benefit compared with detergent only, even at soak and rinse condition, which can be seen in figure 1 (left: detergent only; right: with amylase) .
  • shininess e.g., less stains/spots/scratches, and brighter/glossier/more shinning
  • the shininess of plate washed with detergent only (without enzyme addition, i.e., the blank condition) was assigned with a shininess score of 1.
  • the plates washed with enzyme or enzyme mixtures were scored against the blank condition. The score ranges from 0-10. Score “0” indicates no difference compared to the blank condition. Score “10” indicates as shinning as a brand-new plate. The higher the score is, the better the shininess will be.

Abstract

L'invention concerne une composition détergente appropriée pour le lavage de vaisselle à la main. La composition comprend une alpha-amylase destinée à conférer ou à maintenir une finition lustrée ou brillante.
PCT/CN2021/127306 2020-10-30 2021-10-29 Composition détergente et procédé de nettoyage WO2022089571A1 (fr)

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WO2014106593A1 (fr) * 2013-01-03 2014-07-10 Novozymes A/S Variants d'alpha-amylase et polynucléotides les codant
WO2015189370A1 (fr) * 2014-06-12 2015-12-17 Novozymes A/S Variants d'alpha-amylase stable à l'oxydation
WO2016203064A2 (fr) * 2015-10-28 2016-12-22 Novozymes A/S Composition de détergent comprenant des variants de protéase et d'amylase
CN109312319A (zh) * 2016-05-09 2019-02-05 诺维信公司 具有改善的性能的变体多肽及其用途
WO2020188095A1 (fr) * 2019-03-21 2020-09-24 Novozymes A/S Variants d'alpha-amylase et polynucléotides codant pour ceux-ci

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WO2023225459A2 (fr) 2022-05-14 2023-11-23 Novozymes A/S Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes

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