EP3647398B1 - Compositions de nettoyage contenant des dispersines v - Google Patents

Compositions de nettoyage contenant des dispersines v Download PDF

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Publication number
EP3647398B1
EP3647398B1 EP18203740.8A EP18203740A EP3647398B1 EP 3647398 B1 EP3647398 B1 EP 3647398B1 EP 18203740 A EP18203740 A EP 18203740A EP 3647398 B1 EP3647398 B1 EP 3647398B1
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amount
acid
seq
composition
optionally
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EP3647398A1 (fr
Inventor
Mirko Weide
Susanne Wieland
Ulrike DENGUTH
Rebecca VEJBORG
Dorotea Raventos Segura
Jesper SALOMON
Johanne M. JENSEN
Rune Nygaard MONRAD
Anne Vindum Due
Martin GUDMAND
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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Priority to PCT/EP2019/078441 priority patent/WO2020088958A1/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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66—Non-ionic compounds
    • 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
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • C11D17/042—Water soluble or water disintegrable containers or substrates containing cleaning compositions or additives for cleaning compositions
    • 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
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/12—Water-insoluble compounds
    • C11D3/124—Silicon containing, e.g. silica, silex, quartz or glass beads
    • C11D3/1246—Silicates, e.g. diatomaceous earth
    • 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
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/12—Water-insoluble compounds
    • C11D3/124—Silicon containing, e.g. silica, silex, quartz or glass beads
    • C11D3/1246—Silicates, e.g. diatomaceous earth
    • C11D3/128—Aluminium silicates, e.g. zeolites
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
    • C11D3/227—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin with nitrogen-containing groups
    • 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
    • C11D3/36—Organic compounds containing phosphorus
    • C11D3/361—Phosphonates, phosphinates or phosphonites
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/373—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds containing silicones
    • C11D3/3742—Nitrogen containing silicones
    • 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
    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3769—(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles or amines
    • 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
    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3769—(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles or amines
    • C11D3/3776—Heterocyclic compounds, e.g. lactam
    • 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
    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/378—(Co)polymerised monomers containing sulfur, e.g. sulfonate
    • 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
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3902—Organic or inorganic per-compounds combined with specific additives
    • C11D3/3905—Bleach activators or bleach catalysts
    • 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
    • C11D3/40—Dyes ; Pigments
    • C11D3/42—Brightening agents ; Blueing agents
    • 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
    • C11D3/48—Medical, disinfecting agents, disinfecting, antibacterial, germicidal or antimicrobial compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/50—Perfumes

Definitions

  • the present invention relates to specific compositions, as defined herein, comprising enzymes having hexosaminidase activity comprising the motif D[IV]AR[TK] (SEQ ID NO 12) such as dispersins obtained from Staphylococcus.
  • the invention further relates to methods and use of said compositions comprising such enzymes in cleaning processes e.g. for stain removal.
  • Enzymes have been used in detergents for decades. Usually a cocktail of various enzymes is added to detergent compositions.
  • the enzyme cocktail often comprises various enzymes, wherein each enzyme targets it specific substrate e.g. amylases are active towards starch stains, proteases on protein stains and so forth.
  • One type of stain may compose of organic matter, such as cell debris, biofilm, EPS, etc.
  • Polypeptides having hexosaminidase activity include Dispersins such as Dispersin B (DspB), which are described as ⁇ -N-acetylglucosamininidases belonging to the Glycoside Hydrolase 20 family.
  • DspB Dispersin B
  • WO04061117 A2 Kane Biotech INC
  • Kane et al. describes the use of compositions comprising dispersins for reducing biofilm on medical devises and for wound care.
  • the application WO9850512 (Procter and Gamble) disclose laundry or cleaning products comprising one or more hexosaminidase enzymes.
  • the present invention provides suitable enzymes for use in detergents and for deep cleaning of items such as laundry and cleaning process.
  • WO 2017/186943 relates to polypeptides having hexosaminidase activity, and polynucleotides encoding the polypeptides.
  • it relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
  • WO 2017/186936 relates to polypeptides having hexosaminidase activity, and polynucleotides encoding the polypeptides.
  • it relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
  • WO 2017/186937 relates to polypeptides having hexosaminidase activity, and polynucleotides encoding the polypeptides.
  • it relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
  • the purified enzyme endo-beta-N-acetylglucosaminidase was found to give a single band on polyacrylamide-gel and cellulose acetate electrophoresis and was devoid of all 14 staphylococcal enzymes and toxins assayed for.
  • EP 0 425 019 relates to an antimicrobial composition
  • an antimicrobial composition comprising endo-beta-N-acetylglucosaminidase and/or endoglycopeptidase, and ruminant stomach lysozyme.
  • compositions of the invention or “compositions as described herein”
  • compositions (a)-(j) recited in claim 1 are meant.
  • all references to percentages in relation to the disclosed compositions relate to wt % relative to the total weight of the respective composition. It is understood that when reference is made to compositions that contain a hexosaminidase as defined herein, the respective composition contains at least one of said hexoaminidases but can also comprise two or more of them.
  • the hexosaminidase preferably has N-acetylglucosaminidase activity, preferably ⁇ -1,6 N-acetylglucosaminidase activity.
  • the present invention further relates to a composition, as defined herein, comprising at least 0.01 mg Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12) and optionally a further cleaning component, wherein the cleaning component is selected from
  • the invention further relates to a method of formulating a composition, as defined herein, comprising adding a Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12) and at least one cleaning component.
  • the invention further relates to a method of treating a fabric comprising;
  • the invention also relates to a method for cleaning or laundering an item comprising the steps of:
  • EPS extracellular polymeric substance
  • PNAG poly-N-acetylglucosamine
  • Organic stains like biofilm or components hereof, such as PNAG may be sticky or glueing, which when present on textile, may give rise to redeposition or backstaining of soil resulting in a greying of the textile. Further, when dirty laundry items are washed together with less dirty laundry items the dirt present in the wash liquor tend to stick to organic stains e.g. biofilm or biofilm components as a result, hereof the laundry item is more "soiled” after wash than before wash. This effect may also be termed re-deposition.
  • Another drawback of organic stains is the malodor as various malodor related molecules are often associated with organic stains such as biofilm.
  • the present invention relates to compositions comprising hexosaminidases comprising the motif D[IV]AR[TK] (SEQ ID NO 12) obtained from Staphylococcus, as defined herein, as well as the use and methods of use thereof.
  • the terms "Staphylococcus hexosaminidase” and “hexosaminidase obtained from Staphylococcus” are used interchangeably throughout.
  • the hexosaminidases are preferably dispersins and comprises N-acetylglucosaminidase and/or ⁇ -1,6-N-acetylglucosamininidase activity.
  • Dispersin and the abbreviation "Dsp” means a polypeptide having hexosaminidase activity, EC 3.2.1.- that catalyzes the hydrolysis of ⁇ -1,6-glycosidic linkages of N-acetyl-glucosamine polymers (poly-N-acetylglucosamine, PNAG) found e.g. in biofilm.
  • dispersins is an enzyme having beta-1,6 N-acetylglucosaminidase activity.
  • Hexosaminidase means a polypeptide having hexosaminidase activity (hexosaminidases), and includes EC 3.2.1. e.g. that catalyzes the hydrolysis of N-acetyl-D-hexosamine or N-acetyl-glucosamine polymers found e.g. in biofilm.
  • the term includes dispersins and includes polypeptides having N-acetylglucosaminidase activity and ⁇ -1,6 N-acetylglucosaminidase activity.
  • polypeptide having hexosaminidase activity may be used interchangeably with the term hexosaminidases and similar the term "polypeptide having beta-1,6-N-acetylglucosaminidase activity” may be used interchangeably with the term beta-1,6-N-acetylglucosamininidases.
  • hexosaminidase activity is determined according to the procedure described in Assay 1.
  • the polypeptide useful in accordance with the invention is comprised in a specific clade of hexosaminidases.
  • This clade is in the present context termed Staphylococcus as the hexosaminidases from the clade are obtained from bacteria within the taxonomic family Staphylococcaceae, preferably from the Staphylococcus genus.
  • the composition of the present invention comprises Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12).
  • the term "obtained from” as used herein in connection with a given source shall mean that the polypeptide encoded by a polynucleotide is produced by the source or by a strain in which the polynucleotide from the source has been inserted.
  • the polypeptide obtained from a given source is secreted extracellularly.
  • the phylogenetic tree of the Staphylococcus clade is shown in Figure 1 .
  • the polypeptides comprising in the Staphylococcus clade, which finds use in cleaning processes and compositions of the invention are listed in the table below.
  • the hexosaminidases of Table 1 have 1,6 N-acetylglucosaminidase activity and are thus dispersins.
  • the dispersins of this group have been found to be particularly useful in cleaning of organic stains e.g. PNAG from textiles.
  • dispersins of Table 1 may be formulated in cleaning composition, comprising a dispersin obtained from Staphylococcus and a detergent adjunct.
  • the Staphylococcus hexosaminidase comprises the motif D[IV]AR[TK] (SEQ ID NO 12).
  • the compositions of the invention are useful in cleaning processes such as laundry.
  • Table 1 The list of hexosaminidase polypeptides having beta-1,6 N-acetylglucosaminidase activity comprised in the Staphylococcus clade SEQ_ID_NO 3 Staphylococcus cohnii subsp.
  • the Glyco_hydro_20 domain includes the polypeptides having hexosaminidase, preferably beta-1,6 N-acetylglucosaminidase e.g. PNAG activity, these polypeptides are comprised in three specific clades which are the ENYA, VLG and/or DIARK clades as described below and in example 5 and figure 1 .
  • the polypeptide sequences containing a Glyco_hydro_20 domain comprises several motifs; one example is GXDE (SEQ ID NO 9), situated in positions 157 to 160 in Staphylococcus cohnii subsp. cohnii (SEQ ID NO 3). Residues D and E are the key catalytic residues of Glyco_hydro_20 enzymes (position 159 to 160 in SEQ ID NO 3).
  • the composition of the present invention comprises Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12).
  • the hexosaminidases e.g. the dispersins useful in the compositions of the invention may be divided into clades or domain groups characterized by having various motifs.
  • the composition of the present invention comprises Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12).
  • One clade (ENYA) was identified. This clade has not been described previously.
  • the clade is termed IES and polypeptides of this clade comprises Glyco_hydro_20 domain polypeptides of bacterial origin and are in addition to having beta-1,6 N-acetylglucosaminidase and PNAG activity, characterized by comprising certain motifs.
  • polypeptides of the clade comprise the motif example [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10), corresponding to ENYAIES at position 44 to 50 of SEQ ID NO 3.
  • VLG VLG
  • polypeptides of this clade comprise Glyco_hydro_20 domain polypeptides of bacterial origin and are in addition to having beta-1,6 N-acetylglucosaminidase and PNAG activity, characterized by comprising certain motifs.
  • the polypeptides of the clade comprise the motif example [VIMS][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO 11), corresponding to VLGGDEVP (positions 155 to 162 of SEQ ID NO 3), where G and DE (corresponding to positions 157 and 159-160 of SEQ ID NO 3) are fully conserved in VLG clade and part of the active site.
  • Residues D and E are the key catalytic residues of Glyco_hydro_20 enzymes (position 159 to 160 in SEQ ID NO 3).
  • DIARK comprises the hexosaminidases e.g. dispersins useful in the compositions of the invention.
  • the polypeptides of the clade comprise the motif example D[IV]AR[TK] (SEQ ID NO 12), corresponding to pos 10 to 14 of SEQ ID NO 3, where D and AR are fully conserved in DIARK clade (positions 10 and 12-13 in SEQ ID NO 3).
  • the Staphylococcus hexosaminidases e.g. dispersins comprise the motif D[IV]AR[TK] (SEQ ID NO 12).
  • the hexosaminidase e.g. dispersin comprises one or more of the following motifs GXDE (SEQ ID NO 9), [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10), or [VLIM][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO 11), in addition to D[IV]AR[TK] (SEQ ID NO 12).
  • GXDE SEQ ID NO 9
  • [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] SEQ ID NO 10
  • [VLIM][LIV]G[GAV]DE[VI][PSA] SEQ ID NO 11
  • D[IV]AR[TK] SEQ ID NO 12
  • dispersin comprises all four motifs GXDE (SEQ ID NO 9), [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10), [VLIM][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO 11), and D[IV]AR[TK] (SEQ ID NO 12).
  • the hexosaminidase e.g. dispersin comprises the three motifs GXDE (SEQ ID NO 9), [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10) and D[IV]AR[TK] (SEQ ID NO 12).
  • FIG. 2 An alignment of the polypeptides useful in the compositions of the invention is shown in Figure 2 .
  • Figure 1 A phylogenetic tree of the polypeptides useful in the compositions of the invention is shown in Figure 1 .
  • a polypeptide useful in the compositions of the present invention preferably has a sequence identity to the mature polypeptide sequence shown in SEQ ID NO: 3 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, 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%, or 100%, wherein the polypeptide has hexosaminidase, preferably 1,6 N-acetylglucosaminidase activity.
  • the polypeptide differs by up to 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10, from the polypeptide shown in SEQ ID NO: 3 and preferably has beta-1,6 N-acetylglucosaminidase activity.
  • a polypeptide useful in the compositions of the present invention preferably has a sequence identity to the mature polypeptide sequence shown in SEQ ID NO: 6 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, 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%, or 100%, wherein the polypeptide has hexosaminidase, preferably 1,6 N-acetylglucosaminidase activity.
  • the polypeptide differs by up to 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10, from the polypeptide shown in SEQ ID NO: 6 and preferably has beta-1,6 N-acetylglucosaminidase activity.
  • sequence identity The 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 are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled "longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: Identical Residues ⁇ 100 / Length of Alignment ⁇ Total Number of Gaps in Alignment .
  • Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis ( Cunningham and Wells, 1989, Science 244: 1081-1085 ). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resultant molecules are tested for hexosaminidase activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708 .
  • the active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312 ; Smith et al., 1992, J. Mol. Biol. 224: 899-904 ; Wlodaver et al., 1992, FEBS Lett. 309: 59-64 .
  • the identity of essential amino acids can also be inferred from an alignment with a related polypeptide
  • compositions as defined herein, comprising Staphylococcus hexosaminidases comprising the motif D[IV]AR[TK] (SEQ ID NO 12), preferably dispersins, as well as uses and methods of use thereof
  • the cleaning composition is a liquid composition, as defined herein.
  • the hexosaminidase 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(s) and a solvent system to make it a liquid.
  • the solvent system may comprise water, polyols (such as glycerol, (mono, di, ortri) propylene glycol, sugar alcohol (e.g. sorbitol), polypropylene glycol, and/or polyethylene glycol), ethanol, sugars, and salts.
  • polyols such as glycerol, (mono, di, ortri) propylene glycol, sugar alcohol (e.g. sorbitol), polypropylene glycol, and/or polyethylene glycol
  • ethanol e.g. sorbitol
  • sugars e.g. sorbitol
  • 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
  • hexosaminidases e.g. dispersins in the liquid composition of the invention may be stabilized using conventional stabilizing agents, e.g. a polyol such as propylene glycol or glycerol, ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol and adonitol.
  • a polyol such as propylene glycol or glycerol
  • ethylene glycol polyethylene glycol
  • polyethylene glycol polyethylene glycol
  • sugar alcohols sorbitol
  • mannitol mannitol
  • erythritol erythritol
  • dulcitol inositol
  • inositol xylitol
  • adonitol e.g. adonitol
  • composition comprising a Staphylococcus hexosaminidase, as defined herein, wherein the composition further comprises;
  • compositions comprising a Staphylococcus hexosaminidase, as defined herein, wherein the composition further comprises;
  • compositions comprising a Staphylococcus hexosaminidase, e.g. dispersin, as defined herein, wherein the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6 or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or such as at least 99% sequence identity hereto and wherein the composition optionally further comprises;
  • compositions comprising a Staphylococcus hexosaminidase, e.g. dispersin, as defined herein, wherein the Staphylococcus hexosaminidase is selected from the group shown in Table 1 comprising the motif D[IV]AR[TK] (SEQ ID NO 12) and wherein the composition optionally further comprises;
  • Non-dusting granulates may be produced, e.g. as disclosed in US 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art.
  • waxy coating materials are polyethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids.
  • Staphylococcus hexosaminidase for use in the compositions of the invention may be formulated as a granule for example as a co-granule that combines one or more enzymes or benefit agents such as MnTACN. Each enzyme will then be present in more granules securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes.
  • Methods for producing multi-enzyme co-granulate for the detergent industry is disclosed in the IP.com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes by the use of co-granulates are disclosed in WO 2013/188331 , which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than 10 wt zeolite (anhydrous basis); and (c) less than 10 wt phosphate salt (anhydrous basis), wherein said enzyme co-granule comprises from 10 to 98 wt% moisture sink components and the composition additionally comprises from 20 to 80 wt% detergent moisture sink components.
  • WO 2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a fabric surface comprising the steps of (i) contacting said surface with the detergent composition as claimed and described herein in aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • compositions comprising an enzyme granule/particle comprising a Staphylococcus hexosaminidase as described herein.
  • 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 .
  • the core of the enzyme granule/particle may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule.
  • the optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93/07263 and WO 97/23606 .
  • the coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, 1% or 5%.
  • the amount may be at most 100%, 70%, 50%, 40% or 30%.
  • the coating is preferably at least 0.1 ⁇ m thick, particularly at least 0.5 ⁇ m, at least 1 ⁇ m or at least 5 ⁇ m. In a one embodiment, the thickness of the coating is below 100 ⁇ m. In a more particular embodiment the thickness of the coating is below 60 ⁇ m. In an even more particular embodiment the total thickness of the coating is below 40 ⁇ m.
  • the coating should encapsulate the core unit by forming a substantially continuous layer.
  • a substantially continuous layer is to be understood as a coating having few or no holes, so that the core unit it is encapsulating/enclosing has few or none uncoated areas.
  • the layer or coating should in preferably be homogeneous in thickness.
  • the coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc.
  • a salt coating may comprise at least 60% by weight w/w of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight w/w.
  • the salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles is less than 50 ⁇ m, such as less than 10 ⁇ m or less than 5 ⁇ m.
  • the salt coating may comprise a single salt or a mixture of two or more salts.
  • the salt may be water soluble, preferably having a solubility at least 0.1 grams in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water.
  • the salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate.
  • simple organic acids e.g., 6 or less carbon atoms
  • Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminium.
  • anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate.
  • alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used.
  • the salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt (e.g., anhydrate).
  • the salt coating may be as described in WO 00/01793 or WO 2006/034710 .
  • the salt may be in anhydrous form, or it may be a hydrated salt, i.e. a crystalline salt hydrate with bound water(s) of crystallization, such as described in WO 99/32595 .
  • Specific examples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO4), magnesium sulfate heptahydrate (MgSO4.7H2O), zinc sulfate heptahydrate (ZnSO4.7H2O), sodium phosphate dibasic heptahydrate (Na2HPO4.7H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate.
  • the salt is applied as a solution of the salt, e.g., using a fluid bed.
  • the present invention provides a composition, as defined herein, comprising a granule, which comprises:
  • compositions as defined herein, comprising a granule, which comprises:
  • compositions as defined herein, comprising a granule, which comprises:
  • compositions as defined herein, comprising a layered granule comprising
  • compositions as defined herein, comprising a layered granule comprising
  • compositions as defined herein, comprising a layered granule comprising:
  • compositions of the invention are cleaning compositions comprising a Staphylococcus hexosaminidase e.g. dispersin comprising the motif D[IV]AR[TK] (SEQ ID NO 12) in combination with one or more additional cleaning composition components, as defined herein.
  • additional cleaning composition components as defined herein.
  • additional components is within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.
  • composition as defined herein, comprising;
  • composition as defined herein, comprising;
  • composition as defined herein, comprising;
  • the Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] may be included in the compositions e.g. cleaning e.g. detergent composition of the present invention at a level of at least 0.0001 to at least 100, at least 0.001 to at least 100, at least 0.01 to at least 100, at least 0.02 to at least 100, at least 0.01 to at least 100, at least 0.1 to at least 100, at least 0.2 to at least 100, at least 0.5 to at least 100 mg/mL, preferably, the concentration of said Staphylococcus hexosaminidase enzyme in the cleaning composition e.g.
  • the detergent composition may comprise at least 0.00008%, preferably at least 0.002%, 0.003%, 0.004%, 0.005%, 0.006%, 0.008%, 0.01%, 0.02%, 0.03%, 0.05%, 0.1%, 0.2%, 0.3%, 0.4%, 0.6%, 0.7%, 0.8%, 0.9% or 1.0% Staphylococcus hexosaminidase comprising the motif D[IV]AR[TK] (SEQ ID NO 12).
  • composition components for liquid and granular compositions and of cleaning components for cleaning composition as described above may include, any of the components mentioned below.
  • the cleaning compositions of the invention may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof.
  • the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants.
  • the surfactant(s) is typically present at a level of from about 0.1% to 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 3% to about 10%.
  • the surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.
  • compositions as defined herein may comprise from 0-65 wt %, from about 2 wt % to about 60 wt %, from about 5 wt % to about 50 wt %, from about 5 wt % to about 40 wt %, from about 5 wt % to about 30 wt %, from about 5 wt % to about 20 wt %, from about 5 wt % to about 10 wt % anionic surfactants, amphoteric and/or non-ionic surfactants.
  • "About”, as used herein in relation to a numerical value means said value ⁇ 10%, preferably ⁇ 5%.
  • “About 5 wt %” thus means from 4.5 to 5.5 wt %, preferably from 4.75 to 5.25 wt %.
  • the surfactant may be generally selected among nonionic, anionic and/or amphoteric surfactants.
  • bleach-stable surfactants are preferred.
  • Preferred anionic surfactants are sulphate surfactants and in particular alkyl ether sulphates, especially C9-C15 alcohol ether sulfates, preferably ethoxylates or mixed ethoxylates/propoxylates, such as those with 1 to 30 EO, C12-C15 primary alcohol ethoxylate, , such as those with 1 to 30 EO, C8-C16 ester sulphates and C10-C14 ester sulphates, such as mono dodecyl ester sulphates.
  • Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), in particular C12-C13 alkyl benzene sulfonates, isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates
  • the anionic surfactants are preferably added to the detergent in the form of salts.
  • Suitable cations in these salts are alkali metal ions, such as sodium, potassium and lithium and ammonium salts, for example (2-hydroxyethyl) ammonium, bis(2-hydroxyethyl) ammonium and tris(2-hydroxyethyl) ammonium salts.
  • Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof
  • said surfactant preferably comprises at least one alkyl ether sulfate.
  • Preferred alkyl ether sulfates are those of formula (I) R 1 -O-(AO) n -SO 3 - X + (I).
  • R 1 represents a linear or branched, substituted or unsubstituted alkyl group, preferably a linear, unsubstituted alkyl group, more preferably a fatty alcohol moiety.
  • Preferred R 1 moieties are selected from the group consisting of decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl moieties and mixtures thereof, wherein those groups with an even number of carbon atoms are preferred.
  • R 1 moieties are derived from C 10 -C 18 fatty alcohols, such as those derived from coconut oil alcohols, tallow fatty alcohols, lauryl, myristyl, cetyl or stearyl alcohol or from C 10 -C 20 oxoalcohols.
  • AO represents an ethyleneoxide (EO) or propyleneoxide (PO) group, preferably an ethyleneoxide group.
  • the index n represents an integer from 1 to 50, preferably from 1 to 20 and more preferably from 1 to 10. Particularly preferably, n is 1, 2, 3, 4, 5, 6, 7 or 8.
  • X represents a monovalent cation or the n-th part of an n-valent cation, preferred are alkali metal cations, specifically Na + and K + , most preferably Na + . Further cations X + may be selected from NH 4 + , 1 ⁇ 2 Zn 2+ ,1 ⁇ 2 Mg 2+ ,1 ⁇ 2 Ca 2+ ,1 ⁇ 2 Mn 2+ , and combinations thereof.
  • One specific embodiment thereof is lauryl ether sulfate sodium salt with 2 EO.
  • the level of ethoxylation is an average value and can, for a specific compound, be an integer or fractional number.
  • the surfactant comprises at least one alkyl benzene sulfonate.
  • Said alkyl benzene sulfonate may be present alternatively to the above alkyl ether sulfate or, preferably, in addition to it.
  • Exemplary alkyl benzene sulfonates include, but are not limited to linear and branched alkyl benzene sulfonates, preferably linear alkyl benzene sulfonates.
  • Exemplary compounds are those of formula (III) wherein R' and R" are independently H or alkyl and combined comprise 9 to 19, preferably 9 to 15 and more preferably 9 to 13 carbon atoms. Particularly preferred are dodecyl and tridecyl benzene sulfonates, in particular the sodium salts thereof.
  • compositions of the invention may further comprise one or more nonionic surfactants.
  • Preferred nonionic surfactants are those of formula (IV) R 2 -O-(AO) m -H (IV), wherein R 2 represents a linear or branched substituted or unsubstituted alkyl moiety, AO represents an ethylene oxide (EO) or propylene oxide (PO) group and m is an integer from 1 to 50.
  • R 2 preferably represents a linear or branched, substituted or unsubstited alkyl group, preferably a linear, unsubstituted alkyl group, particularly preferred a fatty alcohol group.
  • Preferred groups are R 2 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl groups and combinations thereof, wherein those groups with an even number of carbon atoms are preferred.
  • R 2 groups derived from C 12 -C 18 fatty alcohols such as coconut oil alcohol, tallow oil alcohol, lauryl, myristyl, cetyl or stearyl alcohol or from C 10 -C 20 oxoalcohols.
  • AO represents an ethyleneoxide (EO) or propyleneoxide (PO) group, preferably an ethyleneoxide group.
  • the index m represents an integer from 1 to 50, preferably from 1 to 20 and more preferably from 1 to 6. Particularly preferably, m is 1, 2, 3, 4 or 5, most preferably 3-5, as higher degrees of ethoxylation may negatively influence viscosity and stability.
  • the detergent compositions may further include other nonionic surfactants, such as alkyl glucosides of the general formula RO(G) x , where R is a primary linear or 2-methyl-branched aliphatic radical containing 8 to 22 and preferably 12 to 18 carbon atoms and G stands for a glucose unit.
  • R is a primary linear or 2-methyl-branched aliphatic radical containing 8 to 22 and preferably 12 to 18 carbon atoms and G stands for a glucose unit.
  • the degree of oligomerization x which indicates the distribution of monoglucosides and oligoglucosides, is a number of 1 to 10 and preferably a number of 1.2 to 1.4.
  • the composition comprises at least two anionic surfactants, e.g. at least one alkyl ether sulfate and preferably at least one alkyl benzene sulfonate, and optionally an alkyl ether.
  • anionic surfactants e.g. at least one alkyl ether sulfate and preferably at least one alkyl benzene sulfonate, and optionally an alkyl ether.
  • Suitable amphoteric surfactants comprise betains.
  • Preferred betaines are the alkylbetaines, the alkylamidobetaines, the imidazolinium betaines, the sulfobetaines (INCI Sultaines) and the phosphobetaines.
  • betaines and sulfobetaines are the following compounds designated as INCI: almondamidopropyl betaines, apricotam idopropyl betaines, avocadamidopropyl betaines, babassuamidopropyl betaines, behenamide idopropyl betaines, behenyl betaines, betaines, canola idopropyl betaines, caprylic / capram idopropyl betaines, carnitines, cetyl betaines, Cocamidoethyl betaines, cocamidopropyl betaines, cocam idopropyl hydroxysultaines, cocobetaines, coco-hydroxysultaines, coco / oleam idopropyl betaines, coco-sultaines, decyl betaines, dihydroxyethyl oleyl glycinates, dihydroxyethyl so
  • amine oxides suitable in accordance with the invention include alkylamine oxides, in particular alkyldimethylamine oxides, alkylamidoamine oxides and alkoxyalkylamine oxides.
  • suitable amine oxides are the following compounds designated as INCI: Almond amidopropylamine oxides, Babassu amidopropylamine oxides, Behenamine oxides, Cocamidopropyl Amine oxides, Cocamidopropylamine oxides, Cocamine oxides, Coco-Morpholine oxides, Decylamine oxides, Decyltetradecylamine oxides, Diaminopyrimidine oxides, Dihydroxyethyl C8-10 alkoxypropylamines oxides , Dihydroxyethyl C9-11 alkoxypropylamines oxides, dihydroxyethyl C12-15 alkoxypropylamines oxides, dihydroxyethyl cocamine oxides, dihydroxyethyl laur
  • low-foaming nonionic surfactants are preferably used, in particular alkoxylated, especially ethoxylated, low-foaming nonionic surfactants.
  • the automatic dishwashing detergents contain nonionic surfactants from the group of the alkoxylated alcohols. Particular preference is given to nonionic surfactants which have a melting point above room temperature. Nonionic surfactants having a melting point above 20 ° C, preferably above 25 ° C, more preferably between 25 and 60 ° C and especially between 26.6 and 43.3 ° C, are particularly preferred.
  • surfactants are those from the groups of alkoxylated nonionic surfactants, in particular the ethoxylated primary alcohols and mixtures of these surfactants with structurally more complex surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants).
  • Such (PO / EO / PO) nonionic surfactants are also characterized by good foam control.
  • Particularly preferred nonionic surfactants are those containing alternating ethylene oxide and different alkylene oxide units.
  • surfactants with EO-AO-EO-AO blocks are preferred, with one to ten EO or AO groups before one block from the other group follows.
  • nonionic surfactants are those having a C9-alkyl group with 1 to 4 ethylene oxide units followed by 1 to 4 propylene oxide units, followed by 1 to 4 ethylene oxide units followed by 1 to 4 propylene oxide units.
  • the alkyl groups may also comprise hydroxyl groups.
  • nonionic surfactants include, for example, the C4-22 fatty alcohol (EO) 10-50 -2- hydroxyalkyl ethers, in particular also the C8-12 fatty alcohol (EO) 22 -2-hydroxydecyl ethers and the C4-22 fatty alcohol (EO) 40-80 -2-hydroxyalkyl ethers.
  • the detergent When included therein the detergent will usually contain from about 1% to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • an anionic surfactant such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (
  • the detergent When included therein the detergent will usually contain from about 1% to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • a cationic surfactant for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.
  • ADMEAQ alkyldimethylethanolamine quat
  • CAB cetyltrimethylammonium bromide
  • DMDMAC dimethyldistearylammonium chloride
  • AQA alkoxylated quaternary ammonium
  • the detergent When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • a nonionic surfactant for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof
  • the detergent When included therein the detergent will usually contain from about 0.01 to about 10 % by weight of a semipolar surfactant.
  • semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N-(tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof.
  • AO amine oxides
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant.
  • zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.
  • the cleaning compositions of the invention may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof.
  • the level of builder is typically 40-65%, particularly 50-65%.
  • the builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized.
  • Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.
  • Co-builder as used herein, means that the respective component is used in combination with another builder. All compounds disclosed as co-builders herein may also be used as main builders and vice versa, unless indicated otherwise.
  • the composition may comprise, if not indicated otherwise, from 0-65 wt %, for example about 1 wt% to about 65 wt%, from about 5 wt% to about 50 wt%, preferably from about 40 wt% to 65 wt%, such as 50 - 65 wt %, particularly about 20 wt% to about 65 wt%, particularly from 10 wt% to 50 wt% of at least one builder.
  • the builder may be preferably selected from citrate, carbonate, silicate, aluminosilicate (zeolite) and combinations thereof. Suitable builders also include phosphonates, polyphosphonates, bicarbonates, borates, and further polycarboxylates. Citrate builders, e.g., citric acid and soluble salts thereof (particularly sodium salt), are particularly suitable water-soluble organic builders. Citrates can be used in combination with zeolite, silicates like the BRITESIL types, and/or layered silicate builders. The builder and/or co-builder may be any chelating agent that forms water-soluble complexes with Ca and Mg.
  • Non-limiting examples of builders include zeolites, in particular zeolite A or P or X, carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), and (carboxymethyl)inulin (CMI), and combinations thereof. Further non-limiting examples of builders include aminocarboxylates, aminopolycarboxylates, 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 glutamic acid-N,N-diacetic acid
  • GLDA glutamic acid-N,N-diacetic acid
  • GLDA 1-hydroxyethane-1,1-diphosphonic acid
  • EDG aspartic acid-N-monoacetic acid
  • ASMA aspartic acid-N,N-diacetic acid
  • ASMP aspartic acid-N-monopropionic acid
  • ASMP iminodisuccinic acid
  • IDA N-(sulfomethyl)aspartic acid
  • SMAS N-(2-sulfoethyl)-as
  • Phosphonates suitable for use herein include 1-hydroxyethane-1,1-diphosphonic acid (HEDP), ethylenediaminetetrakis (methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis (methylenephosphonic acid) (DTMPA or DTPMPA or DTPMP), nitrilotris (methylenephosphonic acid) (ATMP or NTMP), 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC), hexamethylenediaminetetrakis (methylenephosphonic acid) (HDTMP). Particularly preferred are HEDP and DTPMP.
  • HEDP 1-hydroxyethane-1,1-diphosphonic acid
  • EDTMPA ethylenediaminetetrakis
  • DTMPA or DTPMPA or DTPMP diethylenetriaminepentakis
  • nitrilotris methylenephosphonic acid
  • ATMP or NTMP 2-phosphonobutane-1,2,4-tricar
  • Suitable silicates are crystalline, layered sodium silicates of the general formula NaMSi x O 2+1 *yH 2 O, wherein M is sodium or H, x a number of from 1.9 to 4 and y a number of from 0 to 20 and x is preferably 2, 3 or 4.
  • Such silicates are for example disclosed in EP-A-0 164 514 .
  • Preferred are silicates in which M is sodium and is 2 or 3.
  • Particularly preferred are ⁇ - and ⁇ -sodium disilicate NazSizOs*yHzO.
  • compositions may also comprise phosphates, diphosphates (pyrophosphates) and/or triphosphates such as sodium triphosphate (STP or STPP). It is however preferred that all compositions disclosed herein are phosphate-free, i.e. do not contain deliberately added phosphate, in particular the phosphate content is below 1 wt %, more preferably less than 0.5 wt %, even more preferably less than 0.1 wt %, relative to the total weight of the composition.
  • the invention also relates to phosphate-free cleaning compositions in general that contain the polypeptides of the invention.
  • the invention thus features a phosphate-free cleaning composition comprising any one or more of the polypeptides having hexosaminidase activity disclosed herein.
  • the composition may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder.
  • the 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) or polyaspartic acid.
  • PAA poly (acrylic acid)
  • PAA/PMA copoly (acrylic acid/maleic acid)
  • Further exemplary builders and/or co-builders are described in, e.g., WO 09/102854 , US 5977053 .
  • co-builders are acrylate-containing water-soluble polymers, such as alkali metal salts of polyacrylic acid or polymethacrylic acid, for example those having a molecular weight M w in the range of 600 to 750,000 g / mol, as determined by gel permeation chromatography (GPC) according to DIN 55672-1:2007-08 with THF as an eluent.
  • GPC gel permeation chromatography
  • Preferred polymers are polyacrylates with a molecular weight M w of 1,000 to 15,000 g / mol, more preferred, due to their solubility, are short-chain polyacrylates with a molecular weight M w of 1,000 to 10,000 g / mol, most preferred from 1,000 to 5,000 g / mol.
  • Preferred acrylates for use in the present invention are alkali metal salts of polymers of acrylic acid, preferably the sodium salts, in particular those with molecular weights in the range of 1,000 to 10,000 g / mol or 1,000 to 5,000 g / mol.
  • Suitable acrylates are commercially available, for example under the tradename Acusol ® from Dow Chemical. Suitable are also copolymers of acrylates, in particular those of acrylic acid and methacrylic acid, and acrylic acid or methacrylic acid and maleic acid.
  • compositions of the invention comprise a sulfopolymer, preferably a copolymer comprising an ethylenically unsaturated sulfonate/sulfonic acid as a co-monomer.
  • a sulfopolymer preferably a copolymer comprising an ethylenically unsaturated sulfonate/sulfonic acid as a co-monomer.
  • Particularly suitable are monomers of allyl sulfonic acids, such as allyloxybenzene sulfonic acid and methallyl sulfonic acid.
  • Particularly preferred sulfonic acid group-containing monomers are 1-acrylamido propane sulfonic acid-1, 2-acrylamido-2-propanesulfonic acid, 2-acrylamido-2-methyl-1-propanesulfonic acid, 2-methacrylamido-2-methyl-1-propanesulfonic acid, 3- methacrylamido-2-hydroxy-propanesulfonic acid, allylsulfonic acid, methallylsulfonic acid, allyloxybenzenesulfonic acid, methallyloxybenzolsulfonkla, 2-hydroxy-3- (2-propenyloxy) propanesulfonic acid, 2-methyl-2-propenl-sulfonic acid, styrenesulfonic acid, vinylsulfonic acid, 3-sulfopropyl, 3-sulfo - propyl, sulfomethacrylamide, sulfomethylmethacrylamide and mixtures of said acids or their water-soluble salts.
  • the sulfopolymers are preferably copolymers of the afore-described monomers with unsaturated carboxylic acids, Especially preferred unsaturated carboxylic acids are acrylic acid, methacrylic acid, ethacrylic acid, chloroacrylic acid, alpha-cyanoacrylic acid, crotonic acid, alpha-phenyl-acrylic acid, maleic acid, maleic anhydride, fumaric acid, itaconic acid, citraconic acid, methylenemalonic acid, sorbic acid, cinnamic acid or mixtures thereof. Usable are of course also the unsaturated dicarboxylic acids. Preferred are copolymers with acrylates, in particular with acrylic acid and methacrylic acid, and acrylic acid or methacrylic acid and maleic acid.
  • Such polymers are, for example, commercially available under the trade names Acusol ® 590 or Acusol ® 588 from Dow Chemical.
  • the cleaning compositions of the invention comprise a polypeptide as defined herein and at least one sulfopolymer, as defined above.
  • Such compositions are preferably dishwashing compositions.
  • the builder is a non-phosphorus based builder such as citric acid and/or methylglycine-N,N-diacetic acid (MGDA) and/or glutamic-N,N-diacetic acid (GLDA) and / or salts thereof.
  • MGDA methylglycine-N,N-diacetic acid
  • GLDA glutamic-N,N-diacetic acid
  • co-builders include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid.
  • additional specific examples include 2,2',2"-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (N-(
  • compositions e.g. cleaning 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 comprising components known in the art for use in cleaning detergents may be utilized.
  • Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.
  • Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide-urea (1/1).
  • Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.
  • 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 may also be used in
  • an organic bleach catalyst or bleach booster may be used having one of the following formulae: (iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 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 bleaching systems are described, e.g. in WO2007/087258 , WO2007/087244 , WO2007/087259 , EP1867708 (Vitamin K) and WO2007/087242 .
  • Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
  • compositions may comprise metal care agents.
  • Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:
  • composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.
  • the composition may comprise e.g. one or more hydrotrope, which is a compound that solubilises hydrophobic compounds in aqueous solutions (or oppositely, polar substances in a non-polar environment).
  • hydrotropes have both hydrophilic and a hydrophobic character (so-called amphiphilic properties as known from surfactants), however the molecular structure of hydrotropes generally do not favor spontaneous self-aggregation, see e.g. review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128 .
  • Hydrotropes do not display a critical concentration above which self-aggregation occurs as found for surfactants and lipids forming miceller, lamellar or other well defined meso-phases. Instead, many hydrotropes show a continuous-type aggregation process where the sizes of aggregates grow as concentration increases. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances of polar and non-polar character, including mixtures of water, oil, surfactants, and polymers. Hydrotropes are classically used across industries from pharma, personal care, food, to technical applications. Use of hydrotropes in detergent compositions allow for example more concentrated formulations of surfactants (as in the process of compacting liquid detergents by removing water) without inducing undesired phenomena such as phase separation or high viscosity.
  • the cleaning composition may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope.
  • a hydrotrope Any hydrotrope known in the art for use in detergents may be utilized.
  • Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.
  • the composition e.g. cleaning composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1% of a polymer.
  • a polymer Any polymer known in the art for use in detergents may be utilized.
  • the polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties.
  • Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs.
  • Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aqualon, and Sokalan ® HP 165, Sokalan ® HP 50 (Dispersing agent), Sokalan ® HP 53 (Dispersing agent), Sokalan ® HP 59 (Dispersing agent), Sokalan ® HP 56 (dye transfer inhibitor), Sokalan ® HP 66 K (dye transfer inhibitor) from BASF.
  • Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate.
  • exemplary polymers are disclosed in, e.g., WO 2006/130575 . Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan ® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.
  • composition e.g. cleaning composition 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.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in WO2005/03274 , WO2005/03275 , WO2005/03276 and EP1876226 .
  • 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 .
  • composition e.g. cleaning composition may comprise one or more additional enzymes such as one or more lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • additional enzymes such as one or more lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • the properties of the selected 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.
  • Suitable proteases for the compositions of the invention include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It 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 subtilisin. A metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families.
  • subtilases are those derived from Bacillus such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09/021867 .
  • Other useful proteases may be those described in WO01/016285 and WO02/016547 .
  • trypsin-like proteases examples include trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO94/25583 and WO05/040372 , and the chymotrypsin proteases derived from Cellumonas described in WO05/052161 and WO05/052146 .
  • a further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO95/23221 , and variants thereof which are described in WO92/21760 , WO95/23221 , EP1921147 and EP1921148 .
  • metalloproteases are the neutral metalloprotease as described in WO07/044993 (Proctor & Gamble/Genencor Int.) such as those derived from Bacillus amyloliquefaciens.
  • Examples of useful proteases are the variants described in: WO89/06279 , WO92/19729 , WO96/034946 , WO98/20115 , WO98/20116 , WO99/011768 , WO01/44452 , WO03/006602 , WO04/03186 , WO04/041979 , WO07/006305 , WO11/036263 , WO11/036264 , especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101, 102, 104, 116, 118, 121, 126, 127, 128, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211, 212
  • protease variants may 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, V193M,
  • the protease variants are preferably variants of the Bacillus lentus protease (Savinase ® ) shown in SEQ ID NO 1 of WO 2016/001449 , the Bacillus amylolichenifaciens protease (BPN') shown in SEQ ID NO 2 of WO2016/001449 .
  • the protease variants preferably have at least 80 % sequence identity to SEQ ID NO 1 or SEQ ID NO 2 of WO 2016/001449 .
  • a protease variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO: 1 of WO2004/067737 , wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO2004/067737 .
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase ® , Duralase TM , Durazym TM , Relase ® , Relase ® Ultra, Savinase ® , Savinase ® Ultra, Primase ® , Polarzyme ® , Kannase ® , Liquanase ® , Liquanase ® Ultra, Ovozyme ® , Coronase ® , Coronase ® Ultra, Blaze ® , Blaze Evity ® 100T, Blaze Evity ® 125T, Blaze Evity ® 150T, Neutrase ® , Everlase ® and Esperase@ (Novozymes A/S), those sold under the tradename Maxatase ® , Maxacal ® , Maxapem ® , Purafect Ox ® , Purafect OxP ® , Puramax ® , FN2
  • the protease may be stabilized using conventional stabilizing agents, e.g., a polyol such as glycerol, (mono, di, or tri) propylene glycol, sugar alcohol, polypropylene glycol, and/or polyethylene glycol, preferably polyethylene glycol or polypropylene glycol with a molecular weight in the range of 200-1000; or compounds that act by temporarily reducing the activity of proteases (reversible inhibitors).
  • a polyol such as glycerol, (mono, di, or tri) propylene glycol, sugar alcohol, polypropylene glycol, and/or polyethylene glycol, preferably polyethylene glycol or polypropylene glycol with a molecular weight in the range of 200-1000; or compounds that act by temporarily reducing the activity of proteases (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 have an inhibition constant to a serine protease, Ki (mol/L) of from 1E-12 to 1E-03; more preferred from 1E-11 to 1E-04; even more preferred from 1E-10 to 1E-05; even more preferred from 1E-10 to 1E-06; and most preferred from 1E-09 to 1E-07.
  • Ki inhibition constant to a serine protease
  • 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: wherein 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, CH3, CH3CH2 or CH3CH2CH2.
  • 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)y-L-(B)x-B0-R* wherein:
  • 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).
  • Arg arginine
  • Ile isoleucine
  • Leu leucine
  • Met methionine
  • Nle norleucine
  • Nva norvaline
  • phenylalanine Phe
  • m-tyrosine p-tyrosine
  • Tyr valine
  • 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 (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), proline (Pro), serine (Ser), threonine (Thr) and valine (Val).
  • Particular examples of B1 are alanine, glycine, isoleucine, leucine and valine.
  • a particular embodiment is when B1 is alanine, glycine or valine.
  • B2 which is connected to B1 via the C-terminal of the amino acid, may be an aliphatic, hydrophobic, neutral and/or polar amino acid.
  • B2 are alanine (Ala), arginine (Arg), capreomycidine (Cpd), cysteine (Cys), glycine (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), proline (Pro), serine (Ser), threonine (Thr), and valine (Val).
  • 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 which if present is connected to B2 via the C-terminal of the amino acid, 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 (Val).
  • B3 isoleucine, leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), phenylglycine, tyrosine (Tyr), tryptophan (Trp) and valine (Val).
  • B3 isoleucine, leucine, norleucine (Nle), norvaline (Nva), phenylalanine (Phe), phenylglycine, tyrosine (Tyr
  • A1 which if present is connected to L via the N-terminal of the amino acid, may be an aliphatic, aromatic, hydrophobic, neutral and/or polar amino acid.
  • Examples of A1 are alanine (Ala), arginine (Arg), capreomycidine (Cpd), glycine (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), threonine (Thr), tyrosine (Tyr), tryptophan (Trp) and valine (Val).
  • A1 are alanine, arginine, glycine, leucine, phenylalanine, tyrosine, tryptophan and valine.
  • B2 is leucine, phenylalanine, tyrosine or tryptophan.
  • the A2 residue which if present is connected to A1 via the N-terminal of the amino acid, may be a large, aliphatic, aromatic, hydrophobic and/or neutral amino acid.
  • A2 arginine (Arg), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), phenylglycine, Tyrosine (Tyr), tryptophan (Trp) and valine (Val).
  • 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, benzylsulfonyl, methylphosphoramidyl (MeOP
  • P is preferably acetyl, methoxycarbonyl, benzyloxycarbonyl, methylamino carbonyl, methylsulfonyl, benzylsulfonyl and benzylphosphoramidyl.
  • P is preferably acetyl, methoxycarbonyl, methylsulfonyl, ethylsulfonyl and methylphosphoramidyl.
  • 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 described above, e.g. as described in WO 2013/004636 .
  • the adduct may have the formula P-(A)y-L-(B)x-N(H)-CHR-CH(OH)-SO 3 M, wherein P, A, y, L, B, x 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, NaHSOs); potassium bisulfite (KHSOs) 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
  • KHSOs 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
  • 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
  • B0, B1, B2, B3, and P are as described above.
  • 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 slurry 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 ).
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307 , US 5,648,263 , US 5,691,178 , US 5,776,757 and WO 89/09259 .
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257 , EP 0 531 372 , WO 96/11262 , WO 96/29397 , WO 98/08940 .
  • Other examples are cellulase variants such as those described in WO 94/07998 , EP 0 531 315 , US 5,457,046 , US 5,686,593 , US 5,763,254 , WO 95/24471 , WO 98/12307 and WO99/001544 .
  • 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 .
  • Celluzyme TM Commercially available cellulases include Celluzyme TM , and Carezyme TM (Novozymes A/S) Carezyme Premium TM (Novozymes A/S), Celluclean TM (Novozymes A/S), Celluclean Classic TM (Novozymes A/S), Cellusoft TM (Novozymes A/S), Whitezyme TM (Novozymes A/S), Clazinase TM , and Puradax HA TM (Genencor International Inc.), and KAC-500(B) TM (Kao Corporation).
  • Carezyme TM Novozymes A/S
  • Carezyme Premium TM Novozymes A/S
  • Celluclean TM Novozymes A/S
  • Celluclean Classic TM Novozymes A/S
  • Cellusoft TM Novozymes A/S
  • Whitezyme TM Novozymes A/S
  • Clazinase TM and Puradax HA TM (
  • 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 WO1999/064619 .
  • a commercially available mannanase is Mannaway (Novozymes A/S).
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618 , WO 95/10602 , and WO 98/15257 . Commercially available peroxidases include Guardzyme TM (Novozymes A/S).
  • Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa ) as described in EP258068 and EP305216 , cutinase from Humicola, e.g. H. insolens ( WO96/13580 ), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia ), e.g. P. alcaligenes or P. pseudoalcaligenes ( EP218272 ), P.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa ) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H. insolens ( WO96
  • 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 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 ).
  • amylases include alpha-amylases and/or a glucoamylases 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:
  • 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:
  • 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: N21D+D97N+V128I wherein the 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 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 and Preferenz S110 (from Genencor International Inc./DuPont).
  • a suitable peroxidase may be 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 Nomenclature Committee of the International Union of Biochemistry and Molecular Biology
  • Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea ( EP 179,486 ), and variants thereof as those described in WO 93/24618 , WO 95/10602 , and WO 98/15257 .
  • a suitable peroxidase includes a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • 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.
  • a suitable oxidase includes in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria 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. pin situs, 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 .
  • composition e.g. cleaning composition 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 composition e.g. cleaning composition 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 composition of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 0.5%.
  • fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.
  • diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1,2,3-triazol-2-yl)stilbene-2,2'-disulfonate and sodium 5-(2H-naphtho[1,2-d][1,2,3]triazol-2-yl)-2-[(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.
  • 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 composition of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics.
  • the soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71, Marcel Dekker, Inc.
  • Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure.
  • the core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 .
  • 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 .
  • Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1-C6 mono-carboxylic acid, Cl-C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof.
  • Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da.
  • the molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1: 1 to 1:5, or from 1: 1.2 to 1:2.
  • the average number of graft sites per ethylene oxide units can be less than 1, or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, or from 0.2 to 0.4.
  • a suitable polyethylene glycol polymer is Sokalan HP22.
  • Suitable soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1867808 or WO 2003/040279 .
  • 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.
  • composition of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines.
  • CMC carboxymethylcellulose
  • PVA polyvinyl alcohol
  • PVP polyvinylpyrrolidone
  • PEG polyethyleneglycol
  • homopolymers of acrylic acid copolymers of acrylic acid and maleic acid
  • the cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.
  • composition of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents.
  • the rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition.
  • the rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040 .
  • Suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sud suppressors, solvents, bittering agents, and structurants for liquid detergents and/or structure elasticizing agents.
  • the invention relates to compositions which comprise the polypeptides having hexosaminidase activity, as described herein, and any one or more of an adjunct ingredient selected from bittering agents and organic solvents, such as glycerol and 1,2-propane diol.
  • the cleaning composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, such as 2 or more, preferably 2, 3, 4 or 5 compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.
  • Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch.
  • Preferred films are polymeric materials preferably polymers which are formed into a film or sheet.
  • Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC).
  • the level of polymer in the film for example PVA is at least about 60%.
  • Preferred average molecular weight will typically be about 20,000 to about 150,000.
  • Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water soluble film.
  • the compartment for liquid components can be different in composition than compartments containing solids: US2009/0011970 A1 .
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
  • a liquid or gel detergent which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water.
  • Other types of liquids including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel.
  • An aqueous liquid or gel detergent may contain from 0-30% organic solvent.
  • a liquid or gel detergent may be non-aqueous.
  • the present invention is also directed to methods for using a composition, as defined herein, comprising a Staphylococcus hexosaminidase, e.g. dispersin of the invention and compositions hereof.
  • a Staphylococcus hexosaminidase of the invention is useful in cleaning processes typically in laundry/textile/fabric (House hold laundry washing, Industrial laundry washing) or hard surface cleaning (ADW, car wash, Industrial surface).
  • compositions as defined herein, comprising a Staphylococcus hexosaminidase e.g. dispersin comprising the motif D[IV]AR[TK] (SEQ ID NO 12) for cleaning of an item, wherein the item is a textile or a surface.
  • a Staphylococcus hexosaminidase e.g. dispersin comprising the motif D[IV]AR[TK] (SEQ ID NO 12) for cleaning of an item, wherein the item is a textile or a surface.
  • compositions comprising a Staphylococcus hexosaminidase e.g. dispersin for cleaning of an item, wherein the item is a textile or a surface, wherein the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or such as at least 99% sequence identity hereto.
  • a Staphylococcus hexosaminidase e.g. dispersin for cleaning of an item, wherein the item is a textile or a surface
  • the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%
  • compositions as defined herein, comprising a Staphylococcus hexosaminidase of the invention
  • compositions comprising a Staphylococcus hexosaminidase, wherein the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or such as at least 99% sequence identity hereto,
  • the detergent composition of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.
  • the present invention provides a detergent additive comprising one or more enzymes as described herein.
  • compositions as defined herein, preferably a detergent composition comprising a Staphylococcus hexosaminidase e.g. dispersin comprising the motif D[IV]AR[TK] (SEQ ID NO 12) for cleaning of an item, wherein the item is a textile or a surface.
  • a detergent composition comprising a Staphylococcus hexosaminidase e.g. dispersin comprising the motif D[IV]AR[TK] (SEQ ID NO 12) for cleaning of an item, wherein the item is a textile or a surface.
  • compositions as defined herein, preferably a detergent composition comprising a Staphylococcus hexosaminidase e.g. dispersin for cleaning of an item, wherein the item is a textile or a surface, wherein the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or such as at least 99% sequence identity hereto.
  • a detergent composition comprising a Staphylococcus hexosaminidase e.g. dispersin for cleaning of an item, wherein the item is a textile or a surface
  • Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at
  • compositions as defined herein, preferably a detergent composition comprising a Staphylococcus hexosaminidase e.g. dispersin of the invention,
  • compositions as defined herein, preferably a detergent composition comprising a Staphylococcus hexosaminidase, e.g. dispersin wherein the Staphylococcus hexosaminidase is selected from the group consisting of polypeptides shown in SEQ ID NO 3, SEQ ID NO 6, or polypeptides having at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or such as at least 99% sequence identity hereto,
  • the invention further relates to a method of treating a fabric comprising;
  • One aspect relates to a method of treating a fabric comprising;
  • the invention further relates to a method for cleaning or laundering an item comprising the steps of:
  • the invention further relates to a method for cleaning or laundering an item comprising the steps of:
  • Staphylococcus hexosaminidase e.g. dispersin comprises one or more of the following motifs GXDE (SEQ ID NO 9), [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10), or [VIMS][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO 11), in addition to D[IV]AR[TK] (SEQ ID NO 12).
  • the method wherein the Staphylococcus hexosaminidase comprises the motif D[IV]AR[TK] (SEQ ID NO 12).
  • the pH of the aqueous/liquid solution or wash liquor may be in the range of 1 to 11, such as in the range 5.5 to 11, such as in the range of 7 to 9, in the range of 7 to 8 or in the range of 7 to 8.5.
  • the wash liquor may have a temperature in the range of 5°C to 95°C, or in the range of 10°C to 80°C, in the range of 10°C to 70°C, in the range of 10°C to 60°C, in the range of 10°C to 50°C, in the range of 15°C to 40°C or in the range of 20°C to 30°C.
  • the temperature of the wash liquor is 30°C.
  • the concentration of the Staphylococcus hexosaminidase in the wash liquor is typically in the range of at least 0.00001 ppm to at least 10 ppm, at least 0.00002 ppm to at least 10 ppm, at least 0.0001 ppm to at least 10 ppm, at least 0.0002 ppm to at least 10 ppm, at least 0.001 ppm to at least 10 ppm, at least 0.002 ppm to at least 10 ppm, at least 0.01 ppm to at least 10 ppm, at least 0.02 ppm to at least 10 ppm, at least 0.1 ppm to at least 10 ppm, at least 0.2 ppm to at least 10 ppm, at least 0.5 ppm to at least 5 ppm.
  • Biofilm may be produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS).
  • EPS extracellular polymeric substance
  • Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides. Biofilms may form on living or non-living surfaces.
  • the microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium.
  • Bacteria living in a biofilm usually have significantly different properties from planktonic bacteria of the same species, as the dense and protected environment of the film allows them to cooperate and interact in various ways.
  • One benefit of this environment for the microorganisms is increased resistance to detergents and antibiotics, as the dense extracellular matrix and the outer layer of cells protect the interior of the community.
  • On laundry biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp.
  • biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, Staphylococcus aureus and Stenotrophomonas sp.
  • the biofilm producing strain is Brevundimonas sp.
  • the biofilm producing strain is Pseudomonas, e.g. Pseudomonas alcaliphila or Pseudomonas fluorescens.
  • the biofilm producing strain is Staphylococcus aureus.
  • deep cleaning disruption or removal of components of organic matter, e.g. biofilm, such as polysaccharides, e.g. PNAG, proteins, DNA, soil or other components present in the organic matter.
  • the Cleaning component or cleaning adjunct is different from the Staphylococcus hexosaminidase.
  • the precise nature of these cleaning (adjunct) components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used.
  • Suitable cleaning components include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric huing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • surfactants builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes,
  • cleaning composition refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles.
  • the detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning.
  • the terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment).
  • the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases and mannanases, or any mixture thereof), and/or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • additional enzymes such as proteases, am
  • hard surface cleaning is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash). Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.
  • wash performance is used as an enzyme's ability to remove stains present on the object to be cleaned during e.g. wash or hard surface cleaning.
  • whiteness is defined herein as the quality or state of a textile of being white. Loss of whiteness may be due to removal of optical brighteners/hueing agents and result in a greying or yellowing of the textiles. Greying and yellowing can be due to soil redeposition, body soils, colouring from e.g. iron and copper ions or dye transfer. Whiteness might include one or several issues from the list below: colourant or dye effects; incomplete stain removal (e.g. body soils, sebum etc.); redeposition (greying, yellowing or other discolourations of the object) (removed soils reassociate with other parts of textile, soiled or unsoiled); chemical changes in textile during application; and clarification or brightening of colours.
  • laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention.
  • the laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.
  • malodor an odor which is not desired on clean items.
  • the cleaned item should smell fresh and clean without malodors adhered to the item.
  • malodor is compounds with an unpleasant smell, which may be produced by microorganisms.
  • unpleasant smell can be sweat or body odor adhered to an item which has been in contact with human or animal.
  • malodor can be the odor from spices, which sticks to items for example curry or other exotic spices which smell strongly, tobacco, cooking smell (fried oil, fish etc.), scents of perfume such as deodorant and eau de cologne.
  • mature polypeptide means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminus processing, C-terminus truncation, glycosylation, phosphorylation, etc.
  • the term "textile” means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles).
  • the textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and towelling.
  • the textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose/rayon, cellulose acetate fibers (tricell), lyocell or blends thereof.
  • the textile or fabric may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing fiber (e.g.
  • Fabric may be conventional washable laundry, for example stained household laundry.
  • fabric or garment it is intended to include the broader term textiles as well.
  • variant means a polypeptide having the activity of the parent or precursor polypeptide and comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions compared to the precursor or parent polypeptide.
  • a substitution means replacement of the amino acid occupying a position with a different amino acid;
  • a deletion means removal of the amino acid occupying a position; and
  • an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity".
  • sequence identity is determined using the Needleman-Wunsch algorithm ( Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453 ) as implemented in the Needle program of the EMBOSS package ( EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277 ), preferably version 6.6.0 or later.
  • the parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled "longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: Identical Residues ⁇ 100 / Length of Alignment ⁇ Total Number of Gaps in Alignment .
  • Clade a group of polypeptides clustered together based on homologous features traced to a common ancestor. Polypeptide clades can be visualized as phylogenetic trees and a clade is a group of polypeptides that consists of a common ancestor and all its lineal descendants
  • the nomenclature [IV] or [I/V] means that the amino acid at this position may be isoleucine (Ile, I) or valine (Val, V).
  • the nomenclature [LVI] and [L/V/I] means that the amino acid at this position may be a leucine (Leu, L), valine (Val, V) or isoleucine (Ile, I), and so forth for other combinations as described herein.
  • the amino acid X is defined such that it may be any of the 20 natural amino acids.
  • MiniLOM Minimum Launder-O-Meter
  • MiniLOM is a mini wash system in which washes are performed in 50 ml test tubes placed in a Stuart rotator. Each tube simulates one small washing machine and during an experiment, each will contain a solution of a specific detergent/enzyme system to be tested along with the soiled and unsoiled fabrics it is tested on. Mechanical stress is achieved via rotation (typically 20rpm), and the temperature is controlled by placement of the rotator in a heating cabinet/room.
  • the hexosaminidase activity of the polypeptides listed in the table below was determined using 4-Methylumbelliferyl N-acetyl- ⁇ -D-glucosaminide (Sigma-Aldrich) as substrate.
  • the enzymatic reaction was performed in triplicates in a 96 well flat bottom polystyrene microtiter plate (Thermo Scientific) with the following conditions: 20 mM 3-(N-morpholino)propanesulfonic acid pH 7 buffer, 5 mM 4-Methylumbelliferyl N-acetyl- ⁇ -D-glucosaminide, 0.01 vol% Brij 35 (Polyoxyethylene lauryl ether, CAS 9002-92-0 ) detergent and 50 nM purified enzyme sample in a total reaction volume of 200 ⁇ l.
  • Triple-20 Nonionic Model Detergent was prepared by dissolving 3.33 g/l non-ionic detergent containing NaOH 0.87%, MPG (Monopropylenglycol) 6%, Glycerol 2%, Soap-soy 2.75%, Soap-coco 2.75%, PCA (Sokalon CP-5) 0.2%, AEO Biosoft N25-7(NI) 16%, Sodium formiate 1%, Sodium Citrate 2%, DTMPA 0.2%, Ethanol (96%) 3 %, adjustment of pH with NaOH or Citric acid ass water to 100% (all percentages are w/w (weight volume) in water with hardness 15 dH.
  • the gene sequence encoding the hexosaminidase polypeptides (SEQ ID 2 and 5) from the strains Staphylococcus cohnii subsp. cohnii and Staphylococcus fleurettii respectively were found in the public database (Accession number SWISSPROT:A0A0M2NYI1 and EMBLWGS:LAKJ01000034 for SEQ ID 1 and SWISSPROT:A0A1T1GHQ2 and EMBLWGS:MWJM01000007 for SEQ ID 4).
  • the codon optimized synthetic DNA encoding the mature peptide sequences of the two hexosaminidases were ordered from the company Geneart. The mature polypeptides are shown in SEQ ID 3 and 6. Table 1: SEQ ID donor country of origen SEQ ID 3 Staphylococcus cohnii subsp. cohnii United Kingdom SEQ ID 6 Staphylococcus fleurettii Germany
  • the codon optimized synthetic genes encoding the mature peptide sequences of the hexosaminidase with SEQ ID 3 and 6 were inserted into a Bacillus expression vector as described in WO12/025577 . Briefly, the DNA encoding the mature peptide of the glycol_hydro_20 hexosaminidase gene was cloned in frame to a Bacillus clausii secretion signal (BcSP; with the following amino acid sequence: MKKPLGKIVASTALLISVAFSSSIASA (SEQ ID NO: 7). BcSP replaced the native secretion signal in the gene.
  • BcSP Bacillus clausii secretion signal
  • an affinity tag sequence was introduced to ease the purification process (His-tag; with the following amino acid sequence: HHHHHHPR (SEQ ID NO: 8)
  • the gene that was expressed therefore comprised the BcSP sequence followed by the His-tag sequence followed by the mature wild type glycol_hydro_20 sequence.
  • the final expression plasmid (BcSP-His-tag- glycol_hydro_20) was transformed into a Bacillus subtilis expression host.
  • the glycol_hydro_20 BcSP-fusion gene was integrated by homologous recombination into the Bacillus subtilis host cell genome upon transformation.
  • the gene construct was expressed under the control of a triple promoter system (as described in WO99/43835 ).
  • the gene coding for chloramphenicol acetyltransferase was used as maker (as described in ( Diderichsen et al., 1993, Plasmid 30: 312-315 )). Transformants were selected on LB media agar supplemented with 6 micrograms of chloramphenicol per ml. One recombinant Bacillus subtilis clone containing the glycol_hydro_20 expression construct was selected and was cultivated on a rotary shaking table in 500 ml baffled Erlenmeyer flasks each containing 100 ml yeast extract-based media. After 3-5 days' cultivation time at 30 °C to 37°C, the enzyme containing supernatant was harvested by centrifugation and the enzymes was purified by His-tag purification.
  • the His-tagged glycol_hydro_20 hexosaminidase enzymes were purified by immobilized metal chromatography (IMAC) using Ni 2+ as the metal ion on 5 mL HisTrap Excel columns (GE Healthcare Life Sciences). The purification took place at pH 7 and the bound protein was eluted with imidazole. The purity of the purified enzymes was checked by SDS-PAGE and the concentration of the enzyme determined by Absorbance 280 nm after a buffer exchange in 50mM HEPES, 100mM NaCl pH7.0.
  • IMAC immobilized metal chromatography
  • Staphylococcus aureus 15981 was kindly provided by I ⁇ igo Lasa ( Valle et al., Mol Microbiol.2003 May; 48 (4):1075-87 ).
  • the strain was grown on trypticase soy agar (TSA) at 37°C overnight. Next day, a single colony was transferred to 15 ml tripticase soy broth (TSB) and incubated 5 hours at 37°C under shaking.
  • the culture was diluted 1:100 in TSB+1% glucose and 100 ⁇ L of the bacterial suspension was transferred to each well of a 96-well microtiter plates (Thermo Scientific, Nunclon Delta Surface, cat # 167008) and incubated 24 hours at 37°C without shaking.
  • EPS biofilm extracellular polymeric substances
  • the cells were pelleted by centrifugation (10min, 6000g, 25°C), pooled and resuspended in 4ml 3M NaCl. The suspension was vortexed vigorously and incubated for 15min at ambient temperature to extract the surface-associated EPS. The cells were then re-pelleted (10min, 5000g, 25°C) and the EPS-containing supernatant was retrieved. Milli-Q water was added (6ml) and the solution was sterile-filtered twice (0.45 ⁇ m followed by 0.2 ⁇ m). The crude extract was stored at -20°C until further use.
  • EPS sterile textile swatches
  • wash liquor 15 0 dH water with 0.2 g/L iron(III) oxide nano-powder (544884; Sigma-Aldrich) with 3.33g/L liquid model A detergent or 3.33 g/L nonionic model detergent
  • enzyme was added to each tube. Washes without enzyme were included as controls.
  • the test tubes were placed in a Stuart rotator and incubated for 1 hour at 37°C at 20rpm.
  • the wash liquor was then removed, and the swatches were rinsed twice with 15 0 dH water and left to dry on filter paper overnight.
  • the remisssion (REM 460nm ) values were measured using a Macbeth Color-Eye 7000 (CE7000), and are displayed in table 3. Delta values (REM 460nm (washed with enzyme) - REM 460nm (washed without enzyme) ) are also indicated.
  • the Glyco_hydro_20 domain includes the polypeptides having hexosaminidase e.g. PNAG activity and comprises the ENYA, VLG and/or DIARK clades.
  • the Staphylococcus hexosaminidase comprises the motif D[IV]AR[TK] (SEQ ID NO 12).
  • a phylogenetic tree was constructed, of polypeptide sequences containing a Glyco_hydro_20 domain, as defined in PFAM (PF00728, Pfam version 31.0 Finn (2016). Nucleic Acids Research, Database Issue 44:D279-D285 ).
  • the phylogenetic tree was constructed from a multiple alignment of mature polypeptide sequences containing at least one Glyco_hydro_20 domain. The sequences were aligned using the MUSCLE algorithm version 3.8.31 ( Edgar, 2004.
  • the polypeptide sequences containing a Glyco_hydro_20 domain comprises several motifs; one example is GXDE (SEQ ID NO 9), situated in positions 157 to 160 in Staphylococcus cohnii subsp. cohnii (SEQ ID NO 3). Residues D and E are the key catalytic residues of Glyco_hydro_20 enzymes (position 159 to 160 in SEQ ID NO 3).
  • polypeptides in Glyco_hydro_20 can be separated into multiple distinct sub-clusters, or clades as listed below.
  • the distinct motifs for each clade are described in detail below.
  • a clade preferably shared by the polypeptides of the invention, was identified. This clade has not been described previously.
  • the clade is termed IES and polypeptides of this clade comprises Glyco_hydro_20 domain polypeptides of bacterial origin and are in addition to having PNAG activity, characterized by comprising certain motifs.
  • the polypeptides of the clade comprise the motif example [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 10), corresponding to ENYAIES at position 44 to 50 of SEQ ID NO 3.
  • the clade is termed VLG and polypeptides of this clade comprise Glyco_hydro_20 domain polypeptides of bacterial origin and are in addition to having PNAG activity, characterized by comprising certain motifs.
  • the polypeptides of the clade comprise the motif example [VIMS][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO 11), corresponding to VLGGDEVP (positions 155 to 162 of SEQ ID NO 3), where G and DE (corresponding to positions 157 and 159-160 of SEQ ID NO 3) are fully conserved in VLG clade and part of the active site.
  • Residues D and E are the key catalytic residues of Glyco_hydro_20 enzymes (position 159 to 160 in SEQ ID NO 3).
  • the DIARK clade comprises VLG domain polypeptides of bacterial origin, having hexosaminidase e.g. PNAG activity.
  • the polypeptides of the clade comprise the motif example D[IV]AR[TK] (SEQ ID NO 12), corresponding to pos 10 to 14 of SEQ ID NO 3, where D and AR are fully conserved in DIARK clade (positions 10 and 12-13 in SEQ ID NO 3).
  • the Staphylococcus hexosaminidase comprises the motif D[IV]AR[TK] (SEQ ID NO 12).
  • FIG. 2 An alignment of the polypeptides of the invention is shown in Figure 2 .
  • FIG. 1 A phylogenetic tree of the polypeptides of the invention is shown in Figure 1 .
  • Activity assay The activity of the dispersin having SEQ ID NO 6 was measured with 4-Nitrophenyl N-acetyl- ⁇ -D-glucosaminide (4-NAG, CAS Number 3459-18-5 , CHE00244) as substrate as a function of pH (4-10 in 1-unit increments).
  • the concentrations of substrate and the dispersin having SEQ ID NO 6 were 1 mM and 1.0 ⁇ M, respectively, in all measurements.
  • the dilution buffers comprise: 50 mM MES ( CAS Number: 4432-31-9 ), 50 mM glycine (CAS Number: 56-40-6), 50 mM acetic acid ( CAS Number: 64-19-7 ) adjusted to pH 4-10.
  • the enzyme samples were incubated at the different pH-values in volumes of 200 ⁇ L in a thermomixer (in MTP) for 10 min and 500 rpm at 30 °C. After 10 min, the MTP was incubated at 95 °C and 500 rpm for 10 min in thermomixer to end the reaction. Then the samples were transferred to ice bath and cooled for 2 min. The samples were added 20 ⁇ L 4 M NaOH to deprotonate pNP (induce yellow color). Absorbance at 405 nm was measured for 2 min in 10 sec. intervals. All measurements were produced in triplicates and reference samples were produced for all conditions (buffer instead of enzyme).
  • results The following table display the average absorbance (activity) subtracted the average absorbance of the reference samples measured after 10 min incubation at different pH values: pH 4 5 6 7 8 9 10 A 405 0.370009 0.831697 0.911115 0.061912 -0.005915 -0.053345 -0.054276
  • the dilution buffers comprise: 50 mM MES (CAS Number: 4432-31-9 ), 50 mM glycine (CAS Number: 56-40-6), 50 mM acetic acid (CAS Number: 64-19-7) adjusted to pH 4, 6, 7, 8, or 10.
  • the enzyme samples were prepared by mixing a 5 M NaCl stock, buffer, water (MQ), and enzyme to obtain the desired concentrations. The total volume of each mixture was 100 ⁇ L. The samples were loaded in the instrument in duplicates and measured from 20 to 95 °C with temperature ramping of 2.0 °C/min.
  • the activity of the dispersin having SEQ ID NO 6 was measured with 4-Nitrophenyl N-acetyl- ⁇ -D-glucosaminide (4-NAG, CAS Number 3459-18-5 , CHE00244) as substrate at pH 7.
  • the concentrations of substrate and the dispersin having SEQ ID NO 6 were 1 mM and 0.5 ⁇ M, respectively, in all measurements.
  • the dilution buffer comprises: 50 mM MES ( CAS Number: 4432-31-9 ), 50 mM glycine ( CAS Number: 56-40-6 ), 50 mM acetic acid ( CAS Number: 64-19-7 ), pH 7.
  • the substrate solution (10 mM) was prepared by dissolving 35.9 mg 4-NAG in 10.482 mL water.
  • the reaction mixture comprised 15.9 ⁇ L enzyme (6.3 ⁇ M), 20 ⁇ L substrate, and 164.1 ⁇ L buffer.
  • the enzyme samples were incubated in volumes of 200 ⁇ L in a thermomixer for 10 min and 500 rpm at 20, 30, 40, 45, 50, 55, 60, or 70 °C. After 10 min, the samples were transferred to ice bath and cooled for 2 min. The samples were added 10 ⁇ L 4 M NaOH to deprotonate pNP (induce yellow color). 180 ⁇ L reaction mixture was transferred to a MT plate and absorbance at 405 nm was measured for 1 min in 10 sec. intervals. All measurements were produced in duplicates and reference samples were produced for all conditions (buffer instead of enzyme).
  • Results The following table display the average absorbance (activity) subtracted the average absorbance of the reference samples measured after 10 min incubation at different temperatures: 20 °C 30 °C 40 °C 45 °C 50 °C 55 °C 60 °C 70 °C A 405 0.121286 0.2024 0.294707 0.184157 0.054971 0.035657 0.02815 0.020007

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Claims (6)

  1. Composition comprenant une hexosaminidase de Staphylococcus, dans laquelle l'hexosaminidase de Staphylococcus comprend le motif D[IV]AR[TK] (SEQ ID NO 12) et dans laquelle la composition
    (a) est une composition solide, de préférence granulaire, de détergent à lessive et comprend en outre
    (a1) au moins un adjuvant zéolite, de préférence en une quantité de 10 à 50 % en poids, plus préférablement 20 à 30 % en poids ;
    (a2) au moins un adjuvant phosphonate, de préférence en une quantité de 0,1 à 5 % en poids, plus préférablement 0,4 à 1,5 % en poids ;
    (a3) au moins une enzyme supplémentaire, de préférence une cellulase, de préférence en une quantité d'enzyme active de 100 à 5000 ppb, plus préférablement 1000 à 2000 ppb ; et
    (a4) au moins un polymère, de préférence un polymère de polyvinylpyrrolidone, de préférence en une quantité de 0,01 à 1 % en poids, plus préférablement 0,1 à 0,3 % en poids ; ou
    (b) est une composition solide de détergent à lessive et comprend en outre
    (b1) au moins un adjuvant silicate, de préférence en une quantité de 2 à 20 % en poids, plus préférablement 5 à 10 % en poids ;
    (b2) facultativement de la carboxyméthylcellulose, de préférence en une quantité de 0,1 à 10 % en poids, plus préférablement 0,1 à 4 % en poids ;
    (b3) au moins une enzyme supplémentaire, de préférence une cellulase, de préférence en une quantité d'enzyme active de 0,1 à 100 ppm, plus préférablement 0,1 à 10 ppm ;
    (b4) facultativement au moins un polymère antisalissure, de préférence un polymère de polyvinylpyrrolidone, en une quantité de 0,1 à 3 % en poids, plus préférablement 0,1 à 1,0 % en poids ; et
    (b5) au moins un système de blanchiment, comprenant un agent de blanchiment, un activateur de blanchiment et un catalyseur de blanchiment, de préférence en une quantité de 0,1 à 50 % en poids, plus préférablement 0,1 à 30 % en poids ; ou
    (c) est une composition liquide de détergent à lessive et comprend en outre
    (c1) au moins un agent tensioactif, de préférence un agent tensioactif non ionique, de préférence en une quantité de 1 à 20 % en poids, de préférence 3 à 15 % en poids ;
    (c2) facultativement au moins un adjuvant phosphonate, de préférence en une quantité de 0,1 à 3 % en poids, plus préférablement 0,25 à 1,5 % en poids
    (c3) facultativement au moins une enzyme supplémentaire, de préférence une cellulase, de préférence en une quantité de composition enzymatique de 0,001 à 1 % en poids, plus préférablement 0,001 à 0,6 % en poids ; et
    (c4) facultativement au moins un solvant organique, de préférence du glycérol, de préférence en une quantité de 0,1 à 10 % en poids, plus préférablement 0,1 à 5 % en poids ; ou
    (d) est un détergent liquide à lessive sous forme de dose unitaire, de préférence un sachet comprenant un film hydrosoluble, et comprend en outre
    (d1) de l'eau en une quantité allant jusqu'à 20 % en poids, de préférence 5 à 15 % en poids ;
    (d2) facultativement au moins un agent amérisant, de préférence le benzoate de benzyldiéthyl(2,6-xylylcarbamoyl)-méthylammonium, de préférence en une quantité de 0,00001 à 0,04 % en poids ;
    (d3) facultativement au moins un azurant optique, de préférence en une quantité de 0,01 à 2 % en poids, plus préférablement 0,01 à 1 % en poids ; et
    (d4) facultativement au moins un polymère, de préférence en une quantité de 0,01 à 7 % en poids, plus préférablement 0,1 à 5 % en poids ; ou
    (e) est un finisseur de tissu et comprend en outre
    (e1) au moins une silicone adoucissante, de préférence une silicone à fonctionnalisation amino, de préférence en une quantité de 0,1 à 10 % en poids, plus préférablement 0,1 à 2 % en poids ;
    (e2) au moins un parfum, de préférence au moins partiellement encapsulé dans des microcapsules, plus préférablement au moins partiellement encapsulé dans des microcapsules de mélamine-formaldéhyde, de préférence en une quantité de 0,01 à 3 % en poids, plus préférablement 0,1 à 1 % en poids ;
    (e3) facultativement du polyquaternium 10 en une quantité de 0,1 à 20 % en poids, de préférence 0,1 à 13 % en poids ;
    (e4) facultativement du polyquaternium 37 en une quantité de 0,1 à 20 % en poids, de préférence 0,1 à 13 % en poids ;
    (e5) facultativement un esterquat d'origine végétale, de préférence un esterquat à base de canola ou de palme, en une quantité de 0,1 à 20 % en poids, de préférence 0,1 à 13 % en poids ; et
    (e6) facultativement de l'acide adipique, en une quantité de 0,1 à 20 % en poids, de préférence 0,1 à 13 % en poids ; ou
    (f) est un agent de nettoyage acide, ayant de préférence un pH inférieur à 6, et comprend en outre
    (f1) des agents tensioactifs d'origine végétale ou biologique, de préférence chacun en une quantité de 0,1 à 5, plus préférablement chacun en une quantité de 0,1 à 2 % en poids ;
    (f2) au moins un biocide acide, choisi de préférence parmi des acides, plus préférablement HCl et acide formique ; et
    (f3) au moins un polymère antisalissure, hydrofuge ou d'étalement d'eau, de préférence en une quantité de 0,01 à 3 % en poids, plus préférablement 0,01 à 0,5 % en poids ; ou
    (g) est un agent de nettoyage neutre, ayant de préférence un pH compris entre 6,0 et 7,5, et comprend en outre (g1) des agents tensioactifs d'origine végétale ou biologique, de préférence chacun en une quantité de 0,1 à 5, plus préférablement chacun en une quantité de 0,1 à 2 % en poids ;
    (g2) au moins un biocide, choisi de préférence parmi des composés d'ammonium quaternaire et des alcools ; et
    (g3) au moins un polymère antisalissure, hydrofuge ou d'étalement d'eau, de préférence en une quantité de 0,01 à 3 % en poids, plus préférablement 0,01 à 0,5 % en poids ; ou
    (h) est un agent de nettoyage alcalin, ayant de préférence un pH supérieur à 7,5, et comprend en outre (h1) des agents tensioactifs d'origine végétale ou biologique, de préférence chacun en une quantité de 0,1 à 5, plus préférablement chacun en une quantité de 0,1 à 2 % en poids ; ou
    (i) est un agent de lavage de vaisselle à la main, de préférence un agent liquide de lavage de vaisselle à la main, et comprend en outre
    (i1) au moins un agent tensioactif anionique, de préférence en une quantité de 0,1 à 40 % en poids, plus préférablement 5 à 30 % en poids ;
    (i2) au moins un agent tensioactif amphotère, de préférence la bétaïne, de préférence en une quantité de 0,1 à 25 % en poids, plus préférablement 1 à 15 % en poids ;
    (i3) au moins un agent tensioactif non ionique, de préférence en une quantité de 0,1 à 25 % en poids, plus préférablement 2 à 10 % en poids ;
    (i4) au moins une enzyme supplémentaire, choisie de préférence parmi protéases, amylases et combinaisons de celles-ci, de préférence en une quantité de composition enzymatique allant jusqu'à 1 % en poids, plus préférablement jusqu'à 0,6 % en poids ; ou
    (j) est une composition de lavage automatique de la vaisselle et comprend en outre
    (j1) au moins un adjuvant choisi parmi citrate, aminocarboxylates et combinaisons de ceux-ci, de préférence en une quantité de 5 à 30 % en poids, plus préférablement 10 à 20 % en poids ;
    (j2) au moins un adjuvant phosphonate, de préférence en une quantité de 0,1 à 5 % en poids, plus préférablement 0,4 à 1,5 % en poids ;
    (j3) au moins un agent tensioactif non ionique, de préférence en une quantité de 0,1 à 10 % en poids, plus préférablement 1 à 5 % en poids ;
    (j4) au moins un système de blanchiment, comprenant un agent de blanchiment, un activateur de blanchiment et un catalyseur de blanchiment, de préférence en une quantité de 0,1 à 50 % en poids, plus préférablement 0,1 à 30 % en poids ; et
    (j5) au moins un polymère choisi parmi sulfopolymères, polymères cationiques et polyacrylates, de préférence en une quantité de 0,01 à 15 % en poids, plus préférablement 2 à 10 % en poids.
  2. Composition selon la revendication 1, dans laquelle la composition comprend en outre ;
    (a)
    i. un ou plusieurs polyols, choisis de préférence parmi glycérol, (mono, di, ou tri) propylène glycol, éthylène glycol, polyéthylène glycol, alcools de sucre, sorbitol, mannitol, érythritol, dulcitol, inositol, xylitol et adoniol,
    ii. facultativement une ou plusieurs enzymes, choisies de préférence parmi protéases, amylases ou lipases,
    iii. facultativement un ou plusieurs agents tensioactifs, choisis de préférence parmi agents tensioactifs anioniques et non ioniques,
    iv. facultativement un ou plusieurs polymères ;
    ou
    (b) un granulé comprenant
    i. un noyau comprenant une hexosaminidase de Staphylococcus et facultativement,
    ii. un revêtement constitué d'une ou plusieurs couches entourant le noyau.
  3. Composition selon la revendication 1 ou la revendication 2, dans laquelle l'hexosaminidase a une activité N-acétylglucosaminidase, de préférence une activité β-1,6 N-acétyl-glucosaminidase.
  4. Composition selon l'une quelconque des revendications précédentes, dans laquelle le polypeptide ayant une activité hexosaminidase comprend la séquence d'acides aminés de SEQ ID NO 3 ou des polypeptides ayant au moins 60 %, par exemple 80 %, 85 %, 90 %, 95 %, 98 % ou 99 % d'identité de séquence avec celle-ci.
  5. Composition selon l'une quelconque des revendications précédentes, dans laquelle la composition comprend en outre une ou plusieurs enzymes choisies dans le groupe constitué de protéases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases, xylanases et oxydases
  6. Utilisation d'une composition selon l'une quelconque des revendications 1 à 5, de préférence une composition détergente comprenant une hexosaminidase de Staphylococcus,
    a) pour la prévention, la réduction ou l'élimination du caractère collant de l'article ;
    b) pour le prétraitement de taches sur l'article ;
    c) pour la prévention, la réduction ou l'élimination de redéposition de salissures pendant un cycle de lavage ;
    d) pour la prévention, la réduction ou l'élimination d'adhérence de salissures sur l'article ;
    e) pour le maintien ou l'amélioration de la blancheur de l'article ;
    f) pour la prévention, la réduction ou l'élimination des mauvaises odeurs de l'article, l'article étant un textile.
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