Patent Description:
The present invention relates to compositions such as cleaning compositions comprising a mix of enzymes. The invention further relates to use of compositions comprising such enzymes in cleaning processes and/or for deep cleaning of biofilm soiling, and methods for removal or reduction of biofilm related soiling.

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 its specific substrate e.g. amylases are active towards starch stains, proteases on protein stains and so forth. Textiles surface and hard surfaces, such as dishes or the inner space of a laundry machine enduring a number of wash cycles, become soiled with many different types of soiling which may comprise proteins, grease, starch etc. One type of soiling may be organic matter, such as biofilm, EPS, etc. Organic matter comprises different molecules such as polysaccharides, extracellular DNA (eDNA), and proteins. Some organic matter forms an extracellular polymeric matrix, which may be sticky or glueing, which when present on textile, attracts soils and may cause redeposition or backstaining of soil resulting in a greying of the textile. Additionally, organic matters such as biofilms often cause malodor issue as various malodor molecules can be adhered by the polysaccharides, extracellular DNA (eDNA), and proteins in the complex extracellular matrix and be slowly released to cause consumer noticeable malodor issue.

Enzymes having hexosaminidase activity include Dispersins such as Dispersin B (DspB), which as described is β-N-acetylglucosaminidases belonging to the Glycoside Hydrolase <NUM> family. Enzymes having hexosaminidase activity include chitinase and the use of such enzymes is described in <CIT>). <CIT>) describes compositions comprising DspB for reducing and preventing biofilm caused by poly-N-acetylglucosamine-producing bacteria and describes the use of the compositions comprising DspB for reducing / removing biofilm on medical devices and for wound care.

<CIT> discloses the use of a polypeptide having DNase activity for preventing, reducing or removing a biofilm component e.g. DNA from an item, wherein the polypeptide is obtained from a fungal source, such as A. oryzae and the item is a textile.

<CIT> discloses the use of a polypeptide having DNase activity for preventing, reducing or removing a biofilm component e.g. DNA from an item, wherein the polypeptide is obtained from a bacterial source such as Bacillus.

<CIT> discloses the use of a polypeptide having DNase activity for preventing, reducing or removing a biofilm component e.g. DNA from an item.

<CIT>, <CIT> and <CIT> disclose cleaning compositions comprising a nuclease enzyme as well as e.g. methods of treating a textile using a nuclease. These documents include formulation examples disclosing recipes for detergent compositions comprising a nuclease, where it is indicated that some of them may contain Dispersin B.

There is still a need for cleaning compositions which effectively prevent, reduce or remove components of organic soiling, an effect also described in the present application as "deep cleaning. The present invention provides new compositions fulfilling such need.

In a first aspect, the present invention relates to a cleaning composition comprising <NUM>-<NUM> ppm DNase, <NUM>-<NUM> ppm hexosaminidase, and at least one cleaning component,.

The invention further relates to the use of the cleaning composition for cleaning of an item, wherein the item is a textile or a surface, as well as a method of formulating a cleaning composition, a kit intended for deep cleaning, and a method of deep cleaning of an item, as set forth in the claims.

Various enzymes are applied in cleaning processes, each targeting specific types of soiling such as protein, starch and grease soiling. Enzymes are now standard ingredients in detergents for laundry and dish wash. The effectiveness of these commercial enzymes provides cleaning compositions such as detergents which removes much of the soiling. However, organic matters such as EPS (extracellular polymeric substance) comprised in much biofilm constitute a challenging type of soiling due to the complex nature of such organic matters. None of the commercially available cleaning compositions effectively remove or reduce EPS and/or biofilm related soiling. Biofilm may be produced when a group of microorganisms' 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), which constitutes <NUM>% to <NUM>% of the biofilm's total organic matter. EPS is mostly composed of polysaccharides (exopolysaccharides) and proteins, but includes other macro-molecules such as eDNA, lipids and other organic substances. Organic matter like biofilm 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. Another drawback of organic matter e.g. biofilm is malodor as various malodor related molecules are often associated with organic matter e.g. biofilm. Further, when dirty laundry items are washed together with less dirty laundry items the dirt present in the wash liquor tends to stick to organic matter e.g. biofilm or biofilm components as a result, thus the laundry item is more "soiled" after wash than before wash. This is effect may also be termed re-deposition.

The compositions of the invention are effective in reducing or removing organic components and soiling from organic matter.

The term "DNase" means a polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA. The term "DNases" and the expression "a polypeptide with DNase activity" are used interchangeably throughout the application. For purposes of the present invention, DNase activity is determined according to the procedure described in the Assay I or IV.

The DNase to be added in the cleaning composition of the invention may be a polypeptide obtainable from Aspergillus, e.g. obtainable from Aspergillus oryzae, having a sequence identity to the polypeptide shown in SEQ ID NO: <NUM> of at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, or <NUM>% and which have DNase activity. The polypeptide may differ by up to <NUM> amino acids, e.g., <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, or <NUM>, from the mature polypeptide shown in SEQ ID NO: <NUM>.

The preparation of the polypeptide having DNase activity as described under this section can refer to the description in the Nucleic acid Construct, Expression Vectors, Host Cells, Methods of Production and Fermentation Broth Formulations sections in <CIT>.

The DNase can be included in the cleaning composition of the present invention at a level of from <NUM> to <NUM> ppm, from 1ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm.

The DNase above may be combined with hexosaminidase to form a blend to be added to the wash liquor solution according to the invention. The concentration of the DNase in the wash liquor solution is typically in the range of wash liquor from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, <NUM> ppm to <NUM> ppm, from <NUM>. 2ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm.

The term hexosaminidase includes "dispersin" and the abbreviation "Dsp", which means a polypeptide having hexosaminidase activity, EC <NUM>. - that catalyzes the hydrolysis of β-<NUM>,<NUM>-glycosidic linkages of N-acetyl-glucosamine polymers found e.g. in biofilm. The term hexosaminidase includes polypeptides having N-acetylglucosaminidase activity and β-N-acetylglucosaminidase activity. The term "polypeptide having hexosaminidase activity" may be used interchangeably with the term hexosaminidases and similarly the term "polypeptide having β-N-acetylglucosaminidase activity" may be used interchangeably with the term β-N-acetylglucosaminidases. For purposes of the present invention, hexosaminidase activity is determined according to the procedure described in Assay II. In a preferred embodiment, the polypeptide having hexosaminidase activity is a dispersin. In a preferred embodiment, the polypeptide having hexosaminidase activity is a β-N-acetylglucosaminidase targeting poly-β-<NUM>,<NUM>-N-acetylglucosamine.

In one embodiment, the invention relates to a composition comprising a DNase, a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin, and a cleaning component.

One embodiment of the invention relates to a composition comprising a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin, polypeptide wherein the polypeptide is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>. The polypeptide preferably cleaves β-substituted N-acetyl glucosaminide.

A polypeptide having hexosaminidase activity may be obtained from microorganisms of any genus. Preferably the hexosaminidase or the β-N-acetylglucosaminidase targeting poly-β-<NUM>,<NUM>-N-acetylglucosamine e.g. a dispersin is obtained from Terribacillus.

In one aspect, the polypeptide is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus saccharophilus. In a preferred aspect, the polypeptide is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to SEQ ID NO: <NUM> and is obtained from Terribacillus, preferably Terribacillus saccharophilus.

The hexosaminidase polypeptides useful in the present invention belong to the Glycoside Hydrolase family <NUM> (GH20, www. This family includes dispersins such as Dispersin B (DspB) which is β-N-acetylglucosaminidases belonging to the Glycoside Hydrolase <NUM> family.

The preparation of the polypeptide having hexosaminidase activity as described under this section can refer to the description in the Nucleic acid Construct, Expression Vectors, Host Cells,.

The hexosaminidase can be included in the cleaning composition of the present invention at a level of from <NUM> to <NUM> ppm, from 1ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm.

The hexosaminidase can be included in the wash liquor solution of the present invention at a level of from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM>. 0001ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm, from <NUM> ppm to <NUM> ppm.

The invention relates to cleaning compositions comprising at least one DNase and at least one hexosaminidase in combination with one or more additional cleaning components. The choice of additional components is within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.

The hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin is preferably selected from the genus Terribacillus, preferably Terribacillus saccharophilus.

The DNase may be fungal, one embodiment of the invention relates to a cleaning composition comprising a DNase, a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin and a cleaning component, wherein the DNase is fungal, preferably obtained from Aspergillus and even more preferably from Aspergillus oryzae and wherein the DNase has at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the amino acid sequence shown in SEQ ID NO: <NUM>.

One embodiment of the invention relates to a cleaning composition comprising a DNase, a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin and a cleaning component, wherein the DNase has at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the amino acid sequence shown in SEQ ID NO <NUM> and wherein the hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin has at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>.

One embodiment of the present invention relates to a cleaning composition comprising;.

One preferred embodiment relates to a cleaning composition comprising;.

The choice of cleaning components may include, for textile care, the consideration of the type of textile to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.

The cleaning composition may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant(s) is typically present at a level of from about <NUM>% to <NUM>% by weight, such as about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>%. The surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.

When included therein the detergent will usually contain from about <NUM>% to about <NUM>% by weight of an anionic surfactant, such as from about <NUM>% to about <NUM>%, including from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, or from about <NUM>% to about <NUM>%, or from about <NUM>% to about <NUM>% 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-<NUM>,<NUM>-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.

When included therein the detergent will usually contain from about <NUM>% to about <NUM>% by weigh of a cationic surfactant, for example from about <NUM>% to about <NUM>%, in particular from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, such as from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>% or from about <NUM>% to about <NUM>%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.

When included therein the detergent will usually contain from about <NUM>% to about <NUM>% by weight of a nonionic surfactant, for example from about <NUM>% to about <NUM>%, in particular from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, such as from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, or from about <NUM>% to about <NUM>%. 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.

When included therein the detergent will usually contain from about <NUM> to about <NUM> % by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N-(tallow-alkyl)-N,N-bis(<NUM>-hydroxyethyl)amine oxide, , and combinations thereof.

When included therein the detergent will usually contain from about <NUM> % to about <NUM> % by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.

The detergent composition may contain about <NUM>-<NUM>% by weight, such as from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, of a detergent builder or co-builder, or a mixture thereof. In a dish wash detergent, the level of builder is typically <NUM>-<NUM>%, particularly <NUM>-<NUM>%. 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-<NUM> from Hoechst), ethanolamines such as <NUM>-aminoethan-<NUM>-ol (MEA), diethanolamine (DEA, also known as <NUM>,<NUM>'-iminodiethan-<NUM>-ol), triethanolamine (TEA, also known as <NUM>,<NUM>',<NUM>"-nitrilotriethan-<NUM>-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

The detergent composition may also contain <NUM>-<NUM>% by weight, such as about <NUM>% to about <NUM>%, of a detergent co-builder. The detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include <NUM>,<NUM>',<NUM>"-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), <NUM>-hydroxyethane-<NUM>,<NUM>-diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTMPA or DTPMPA), N-(<NUM>-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(<NUM>-sulfomethyl)-aspartic acid (SMAS), N-(<NUM>-sulfoethyl)-aspartic acid (SEAS), N-(<NUM>-sulfomethyl)-glutamic acid (SMGL), N-(<NUM>-sulfoethyl)-glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA) , taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(<NUM>-hydroxyethyl)ethylenediamine-N,N',N"-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and/or co-builders are described in, e.g., <CIT>, <CIT>.

The cleaning composition may contain <NUM>-<NUM>% by weight, such as from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, from about <NUM>% to about <NUM>%, of a bleaching system. Any bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.

Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide-urea (<NUM>/<NUM>).

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.

Some non-limiting examples of bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with <NUM>,<NUM>,<NUM>-trimethyl-<NUM>,<NUM>,<NUM>-triazacyclononane (Me3-TACN) or <NUM>,<NUM>,<NUM>,<NUM>-tetramethyl-<NUM>,<NUM>,<NUM>-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)<NUM>, and [<NUM>,<NUM>',<NUM>"-nitrilotris(ethane-<NUM>,<NUM>-diylazanylylidene-κN-methanylylidene)triphenolato-κ3O]manganese(III). The bleach catalysts may also be other metal compounds; such as iron or cobalt complexes.

In some embodiments, where a source of a peracid is included, an organic bleach catalyst or bleach booster may be used having one of the following formulae:.

Other exemplary bleaching systems are described, e.g. in <CIT>, <CIT>, <CIT>, <CIT>) and <CIT>. Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.

Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:.

Further suitable organic and inorganic redox-active substances that act as silver/copper corrosion inhibitors are disclosed in <CIT> and <CIT>. Preferably the composition of the invention comprises from <NUM> to <NUM>% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.

The cleaning composition may contain <NUM>-<NUM>% by weight, for example <NUM>-<NUM>% by weight, such as about <NUM> to about <NUM>%, or about <NUM>% to about <NUM>%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.

The cleaning composition may contain <NUM>-<NUM>% by weight, such as <NUM>-<NUM>%, <NUM>-<NUM>%, <NUM>-<NUM>% or <NUM>-<NUM>% of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide anti redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-<NUM>, ChromaBond S- 403E and Chromabond S-<NUM> from Ashland Aqualon, and Sokalan® HP <NUM>, Sokalan® HP <NUM> (Dispersing agent), Sokalan® HP <NUM> (Dispersing agent), Sokalan® HP <NUM> (Dispersing agent), Sokalan® HP <NUM> (dye transfer inhibitor), Sokalan® HP <NUM> (dye transfer inhibitor) from BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., <CIT>. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP <NUM> from BASF, which helps to prevent redeposition of soil in the wash liquor.

The 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. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C. ) 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 <CIT>, <CIT>, <CIT> and <CIT>. The detergent composition preferably comprises from about <NUM> wt% to about <NUM> wt%, from about <NUM> wt% to about <NUM> wt%, or even from about <NUM> wt% to about <NUM> wt% fabric hueing agent. The composition may comprise from <NUM> wt% to <NUM> 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. <CIT> and <CIT>.

The 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.

In general, 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.

Examples of subtilases are those derived from Bacillus such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; <CIT> and <CIT>. Subtilisin lentus, Subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin <NUM>, subtilisin <NUM> and subtilisin <NUM> and e.g. protease PD138 described in (<CIT>). Other useful proteases may be those described in <CIT> and <CIT>. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in <CIT> and <CIT>, and the chymotrypsin proteases derived from Cellumonas described in <CIT> and <CIT>.

A further preferred protease is the alkaline protease from Bacillus lentus DSM <NUM>, as described for example in <CIT>, and variants thereof which are described in <CIT>, <CIT>, <CIT> and <CIT>.

Examples of metalloproteases are the neutral metalloprotease as described in <CIT> such as those derived from Bacillus amyloliquefaciens.

Examples of useful proteases are the variants described in: <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, especially the variants with substitutions in one or more of the following positions: <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM> and <NUM> wherein the positions correspond to the positions of the Bacillus lentus protease shown in SEQ ID NO <NUM>. More preferred the 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, N198D, V199I, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, N255W, N255D, N255E, L256E, L256D T268A and R269H. The protease variants are preferably variants of the Bacillus lentus protease (Savinase®) shown in SEQ ID NO <NUM>, the Bacillus amylolichenifaciens protease (BPN') shown in SEQ ID NO <NUM>. The protease variants preferably have at least <NUM> % sequence identity to SEQ ID NO <NUM> or SEQ ID NO <NUM> of <CIT>.

A protease variant comprising a substitution at one or more positions corresponding to positions <NUM>, <NUM>, <NUM>, <NUM>, or <NUM> of SEQ ID NO: <NUM>, wherein said protease variant has a sequence identity of at least <NUM>% but less than <NUM>% to SEQ ID NO: <NUM>.

Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect Ox®, Purafect OxP®, Puramax®, FN2®, FN3®, FN4®, Excellase®, Excellenz P1000™, Excellenz P1250™, Eraser®, Preferenz P100™, Purafect Prime®, Preferenz P110™, Effectenz P1000™, Purafect®™, Effectenz P1050™, Purafect Ox®™, Effectenz P2000™, Purafast®, Properase®, Opticlean® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N. ), BLAP (sequence shown in Figure <NUM> of <CIT>) and variants hereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.

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 <CIT>, <CIT>, <CIT>, <CIT> and <CIT>.

Especially suitable cellulases are the alkaline or neutral cellulases having colour care benefits. Examples of such cellulases are cellulases described in <CIT>, <CIT>, <CIT>, <CIT>, <CIT>. Other examples are cellulase variants such as those described in <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT> and <CIT>.

Other cellulases are endo-beta-<NUM>,<NUM>-glucanase enzyme having a sequence of at least <NUM>% identity to the amino acid sequence of position <NUM> to position <NUM> of SEQ ID NO:<NUM> of <CIT> or a family <NUM> xyloglucanase, which a xyloglucanase enzyme having a sequence of at least <NUM>% identity to positions <NUM>-<NUM> of SEQ ID NO: <NUM> of <CIT>.

Commercially available cellulases include Celluzyme™, and Carezyme™ (Novozymes A/S) Carezyme Premium™ (Novozymes A/S), Celluclean ™ (Novozymes A/S), Celluclean Classic™ (Novozymes A/S), Cellusoft™ (Novozymes A/S), Whitezyme™ (Novozymes A/S), Clazinase™, and Puradax HA™ (Genencor International Inc. ), and KAC-<NUM>(B)™ (Kao Corporation).

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 <NUM> or <NUM>. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. Suitable mannanases are described in <CIT>. A commercially available mannanase is Mannaway (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 <CIT> and <CIT>, cutinase from Humicola, e.g. H. insolens (<CIT>), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (<CIT>), P. cepacia (<CIT>), P. strain SD705 (<CIT> & <CIT>), P. wisconsinensis (<CIT>), GDSL-type Streptomyces lipases (<CIT>), cutinase from Magnaporthe grisea (<CIT>), cutinase from Pseudomonas mendocina (<CIT>), lipase from Thermobifida fusca (<CIT>), Geobacillus stearothermophilus lipase (<CIT>), lipase from Bacillus subtilis (<CIT>), and lipase from Streptomyces griseus (<CIT>) and S. pristinaespiralis (<CIT>).

Other examples are lipase variants such as those described in <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT>, <CIT> and <CIT>.

Preferred commercial lipase products include LipolaseTM, Lipex™; LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).

Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (<CIT>), acyltransferase from Mycobacterium smegmatis (<CIT>), perhydrolases from the CE <NUM> family (<CIT>), 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 (<CIT>).

Suitable 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 <CIT>.

Suitable amylases include amylases having SEQ ID NO: <NUM> in <CIT> or variants having <NUM>% sequence identity to SEQ ID NO: <NUM> thereof. Preferred variants are described in <CIT>, <CIT>, <CIT> and SEQ ID NO: <NUM> of <CIT>, such as variants with substitutions in one or more of the following positions: <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, and <NUM>.

Different suitable amylases include amylases having SEQ ID NO: <NUM> in <CIT> or variants thereof having <NUM>% sequence identity to SEQ ID NO: <NUM>. Preferred variants of SEQ ID NO: <NUM> are those having a deletion in positions <NUM> and <NUM> and a substitution in position <NUM>.

Other amylases which are suitable are hybrid alpha-amylase comprising residues <NUM>-<NUM> of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: <NUM> of <CIT> and residues <NUM>-<NUM> of the B. licheniformis alpha-amylase shown in SEQ ID NO: <NUM> of <CIT> or variants having <NUM>% 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. Most preferred variants of the hybrid alpha-amylase comprising residues <NUM>-<NUM> of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: <NUM> of <CIT> and residues <NUM>-<NUM> of SEQ ID NO: <NUM> are those having the substitutions:.

Further amylases which are suitable are amylases having SEQ ID NO: <NUM> in <CIT> or variants thereof having <NUM>% sequence identity to SEQ ID NO: <NUM>. Preferred variants of SEQ ID NO: <NUM> 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: <NUM>, SEQ ID NO: <NUM>, SEQ ID NO: <NUM> or SEQ ID NO: <NUM> of <CIT> or variants thereof having <NUM>% sequence identity to SEQ ID NO: <NUM>, SEQ ID NO: <NUM>, SEQ ID NO: <NUM> or SEQ ID NO: <NUM>. Preferred variants of SEQ ID NO: <NUM>, SEQ ID NO: <NUM>, SEQ ID NO: <NUM> or SEQ ID NO: <NUM> are those having a substitution, a deletion or an insertion in one or more of the following positions: <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM> and <NUM>, using SEQ ID <NUM> of <CIT> for numbering. More preferred variants are those having a deletion in two positions selected from <NUM>, <NUM>, <NUM> and <NUM>, such as <NUM> and <NUM>, <NUM> and <NUM>, or positions <NUM> and <NUM>. Most preferred amylase variants of SEQ ID NO: <NUM>, SEQ ID NO: <NUM> or SEQ ID NO: <NUM> are those having a deletion in positions <NUM> and <NUM> and a substitution in one or more of positions <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM> and <NUM>.

Other amylases which can be used are amylases having SEQ ID NO: <NUM> of <CIT>, SEQ ID NO: <NUM> in <CIT> or variants thereof having <NUM>% sequence identity to SEQ ID NO: <NUM> of <CIT> or <NUM>% sequence identity to SEQ ID NO: <NUM> in <CIT>. Preferred variants of SEQ ID NO: <NUM> in <CIT> are those having a substitution, a deletion or an insertion in one of more of the following positions: <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM>, <NUM> and <NUM>.

Further suitable amylases are amylases having SEQ ID NO: <NUM> of <CIT> or variants having <NUM>% sequence identity to SEQ ID NO: <NUM> thereof. Preferred variants of SEQ ID NO: <NUM> 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: <NUM> 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: <NUM> are those having the substitutions:.

Further suitable amylases are amylases having SEQ ID NO: <NUM> of <CIT> or variants having <NUM>% sequence identity to SEQ ID NO: <NUM> thereof. Preferred variants of SEQ ID NO: <NUM> 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: <NUM> 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: <NUM> are those having the substitutions:.

Further suitable amylases are amylases having SEQ ID NO: <NUM> of <CIT> or variants having <NUM>% sequence identity to SEQ ID NO: <NUM> thereof. Preferred variants of SEQ ID NO: <NUM> 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: <NUM> 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: <NUM> are those having the substitutions:.

Other suitable amylases are the alpha-amylase having SEQ ID NO: <NUM> in <CIT> or a variant having at least <NUM>% sequence identity to SEQ ID NO: <NUM>. 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: <NUM> in <CIT>: 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.

Other examples are amylase variants such as those described in <CIT>, <CIT> and <CIT>.

Commercially available amylases are DuramylTM, TermamylTM, FungamylTM, Stainzyme TM, Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM/EffectenzTM, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc.

A peroxidase according to the invention is a peroxidase enzyme comprised by the enzyme classification EC <NUM>. <NUM>, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.

Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (<CIT>), and variants thereof as those described in <CIT>, <CIT>, and <CIT>. Commercially available peroxidases include Guardzyme™ (Novozymes A/S).

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. <NUM>) catalyze formation of hypochlorite from chloride ions. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.

Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.

A suitable oxidase includes in particular, any laccase enzyme comprised by the enzyme classification EC <NUM>. <NUM>, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC <NUM>. <NUM>), an o-aminophenol oxidase (EC <NUM>. <NUM>), or a bilirubin oxidase (EC <NUM>. Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (<CIT>), or Coriolus, e.g., C. hirsutus (<CIT>). 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 <CIT>; or from Myceliophthora thermophila, as disclosed in <CIT>.

The cleaning composition of the present invention can also contain dispersants. In particular, powdered detergents may comprise dispersants. Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in <NPL>.

The 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. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about <NUM> % to about <NUM>%, from about <NUM>% to about <NUM>% or even from about <NUM>% to about <NUM>% by weight of the composition.

The cleaning 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 <NUM>% to about <NUM>%. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: <NUM>,<NUM>'-bis-(<NUM>-diethanolamino-<NUM>-anilino-s-triazin-<NUM>-ylamino) stilbene-<NUM>,<NUM>'-disulfonate, <NUM>,<NUM>'-bis-(<NUM>,<NUM>-dianilino-s-triazin-<NUM>-ylamino) stilbene-<NUM>'-disulfonate, <NUM>,<NUM>'-bis-(<NUM>-anilino-<NUM>-(N-methyl-N-<NUM>-hydroxy-ethylamino)-s-triazin-<NUM>-ylamino) stilbene-<NUM>,<NUM>'-disulfonate, <NUM>,<NUM>'-bis-(<NUM>-phenyl-<NUM>,<NUM>,<NUM>-triazol-<NUM>-yl)stilbene-<NUM>,<NUM>'-disulfonate and sodium <NUM>-(<NUM>-naphtho[<NUM>,<NUM>-d][<NUM>,<NUM>,<NUM>]triazol-<NUM>-yl)-<NUM>-[(E)-<NUM>-phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of <NUM>,<NUM>'-bis-(<NUM>-morpholino-<NUM>-anilino-s-triazin-<NUM>-ylamino) stilbene-<NUM>,<NUM>'-disulfonate. Tinopal CBS is the disodium salt of <NUM>,<NUM>'-bis-(phenyl-styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the <NUM>-<NUM>-diaryl pyrazolines and the <NUM>-alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about <NUM>, from <NUM>, from about <NUM> or even from about <NUM> wt % to upper levels of <NUM> or even <NUM> wt%.

The cleaning 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 <NPL>. 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 <CIT>. Furthermore, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in <CIT>, <CIT> and <CIT>. 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, CI-C <NUM> 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 <NUM>,<NUM> Da to <NUM>,<NUM> Da, or from <NUM>,<NUM> Da to <NUM>,<NUM> Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from <NUM>: <NUM> to <NUM>:<NUM>, or from <NUM>: <NUM> to <NUM>:<NUM>. The average number of graft sites per ethylene oxide units can be less than <NUM>, or less than <NUM>, the average number of graft sites per ethylene oxide units can be in the range of from <NUM> to <NUM>, or the average number of graft sites per ethylene oxide units can be in the range of from <NUM> to <NUM>, or from <NUM> to <NUM>. A suitable polyethylene glycol polymer is Sokalan HP22. Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in <CIT> or <CIT>. Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.

The cleaning 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. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.

The cleaning 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 <CIT>.

Other suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.

The cleaning composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.

Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about <NUM>%. Preferred average molecular weight will typically be about <NUM>,<NUM> to about <NUM>,<NUM>. 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: <CIT>.

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 <NUM>% by weight and up to <NUM>% water, such as up to about <NUM>% water, up to about <NUM>% water, up to about <NUM>% water, up to about <NUM>% water, up to about <NUM>% 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 <NUM>-<NUM>% organic solvent. A liquid or gel detergent may be non-aqueous.

The composition(s) of the invention may be formulated as a granule for example as a co-granule that combines one or more enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates for the detergent industry are disclosed in the IP. com disclosure IPCOM000200739D.

Another example of formulation of enzymes by the use of co-granulates are disclosed in <CIT>, which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than <NUM> wt zeolite (anhydrous basis); and (c) less than <NUM> wt phosphate salt (anhydrous basis), and the composition additionally comprises from <NUM> to <NUM> wt% detergent moisture sink component. The multi-enzyme co-granule may comprise an enzyme blend i.e. at least one DNase and at least one hexosaminidase and one or more enzymes selected from the group consisting of proteases, lipases, cellulases, xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases, hemicellulases, proteases, cellulases, cellobiose dehydrogenases, xylanases, phospho lipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase, amylases, and mixtures thereof.

<CIT> also relates to a method of treating and/or cleaning a surface, preferably a fabric surface comprising the steps of (i) contacting said surface with the detergent composition as claimed and described herein in aqueous wash liquor, (ii) rinsing and/or drying the surface.

An embodiment of the invention relates to an enzyme granule/particle comprising the DNase and hexosaminidase. The granule is composed of a core, and optionally one or more coatings (outer layers) surrounding the core. Typically, the granule/particle size, measured as equivalent spherical diameter (volume based average particle size), of the granule is <NUM>-<NUM>, particularly <NUM>-<NUM>, <NUM>-<NUM> or <NUM>-<NUM>. 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 <NUM>-<NUM>, particularly <NUM>-<NUM>, <NUM>-<NUM> or <NUM>-<NUM>. 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<NPL>.

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 <CIT> and <CIT>. The coating may be applied in an amount of at least <NUM>% by weight of the core, e.g., at least <NUM>%, <NUM>% or <NUM>%. The amount may be at most <NUM>%, <NUM>%, <NUM>%, <NUM>% or <NUM>%. The coating is preferably at least <NUM> thick, particularly at least <NUM>, at least <NUM> or at least <NUM>. In a one embodiment, the thickness of the coating is below <NUM>. In another embodiment, the thickness of the coating is below <NUM>. In an even more particular embodiment the total thickness of the coating is below <NUM>. 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 no uncoated areas. The layer or coating should be homogeneous in thickness. The coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc. A salt coating may comprise at least <NUM>% by weight w/w of a salt, e.g., at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or at least <NUM>% 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 <NUM>, such as less than <NUM> or less than <NUM>. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, and may have a solubility at least <NUM> grams in <NUM> of water at <NUM>, preferably at least <NUM> per <NUM> water, e.g., at least <NUM> per <NUM> water, e.g., at least <NUM> per <NUM> 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 <NUM> carbon atoms, e.g., <NUM> or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminium. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used. The salt in the coating may have a constant humidity at <NUM> above <NUM>%, particularly above <NUM>%, above <NUM>% or above <NUM>%, or it may be another hydrate form of such a salt (e.g., anhydrate). The salt coating may be as described in <CIT> or <CIT>. Specific examples of suitable salts are NaCl (CH<NUM>=<NUM>%), Na<NUM>CO<NUM> (CH<NUM>=<NUM>%), NaNO<NUM> (CH<NUM>=<NUM>%), Na<NUM>HPO<NUM> (CH<NUM>=<NUM>%), Na<NUM>PO<NUM> (CH<NUM>=<NUM>%), NH<NUM>Cl (CH<NUM> = <NUM>%), (NH<NUM>)<NUM>HPO<NUM> (CH<NUM> = <NUM>,<NUM>%), NH<NUM>H<NUM>PO<NUM> (CH<NUM> = <NUM>%), (NH<NUM>)<NUM>SO<NUM> (CH<NUM>=<NUM>%), KCI (CH<NUM>=<NUM>%), K<NUM>HPO<NUM> (CH<NUM>=<NUM>%), KH<NUM>PO<NUM> (CH<NUM>=<NUM>%), KNO<NUM> (CH<NUM>=<NUM>%), Na<NUM>SO<NUM> (CH<NUM>=<NUM>%), K<NUM>SO<NUM> (CH<NUM>=<NUM>%), KHSO<NUM> (CH<NUM>=<NUM>%), MgSO<NUM> (CH<NUM>=<NUM>%), ZnSO<NUM> (CH<NUM>=<NUM>%) and sodium citrate (CH<NUM>=<NUM>%). Other examples include NaH<NUM>PO<NUM>, (NH<NUM>)H<NUM>PO<NUM>, CuSO<NUM>, Mg(NO<NUM>)<NUM> and magnesium acetate. The salt may be in anhydrous form, or it may be a hydrated salt, i.e. a crystalline salt hydrate with bound water(s) of crystallization, such as described in <CIT>. Specific examples include anhydrous sodium sulfate (Na<NUM>SO<NUM>), anhydrous magnesium sulfate (MgSO<NUM>), magnesium sulfate heptahydrate (MgSO<NUM>·<NUM><NUM>O), zinc sulfate heptahydrate (ZnSO<NUM>·<NUM><NUM>O), sodium phosphate dibasic heptahydrate (Na<NUM>HPO<NUM>·<NUM><NUM>O), magnesium nitrate hexahydrate (Mg(NO<NUM>)<NUM>(<NUM><NUM>O)), sodium citrate dihydrate and magnesium acetate tetrahydrate. Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed.

One embodiment of the present invention provides a granule, which comprises:.

One embodiment of the invention relates to a granule, which comprises:.

The present invention is also directed to methods for using the cleaning composition in laundry/textile/fabric (Household laundry washing, Industrial laundry washing) or hard surface cleaning (ADW, car wash, Industrial surface).

The cleaning composition of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for 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. In a specific aspect, the present invention provides a detergent additive comprising enzymes as described herein.

The present invention is directed to methods for using the compositions thereof. Laundry/textile/fabric (Household laundry washing, Industrial laundry washing). Hard surface cleaning (ADW, car wash, Industrial surface). The compositions of the invention comprise a blend of DNase and a hexosaminidase, and effectively reduce or remove organic components, such as polysaccharide and DNA from surfaces such as textiles and hard surfaces e.g. dishes.

One embodiment of the invention relates to the use of a cleaning composition comprising a DNase, a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin, and at least one cleaning component for reduction or removal of components e.g. of biofilm, such as polysaccharides, e.g. N-acetyl-glucosaminide e.g. poly-N-acetylglucosamine (PNAG) and DNA, of an item, wherein the item is a textile or a hard surface.

One embodiment of the invention relates to the use of a cleaning composition comprising a DNase, at least one hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin, and a cleaning component for deep cleaning of an item, wherein the item is a textile or a surface.

One embodiment of the invention relates to the use of a composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction or removal of biofilm and/or compounds such as polysaccharide, e.g. N-acetyl-glucosaminide e.g. poly-N-acetylglucosamine (PNAG) and/or DNA of an item. One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction or removal of biofilm and/or compounds such as polysaccharide, e.g. N-acetyl-glucosaminide e.g. poly-N-acetylglucosamine (PNAG) and/or DNA of an item such as textile. One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for deep cleaning when the cleaning composition is applied in e.g. laundry process.

One embodiment of the invention relates to the use of a composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction of redeposition or reduction of malodor. One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction of redeposition or reduction of malodor.

One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction of redeposition or reduction of malodor when the cleaning composition is applied in e.g. laundry process. One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for reduction of redeposition or reduction of malodor on an item e.g. textile. In one embodiment, the composition is an anti-redeposition composition.

One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for deep cleaning of an item or reduction of redeposition or malodor, wherein the hexosaminidase is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>.

One embodiment of the invention relates to the use of a cleaning composition comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin for deep cleaning of an item or reduction of redeposition or malodor, wherein the hexosaminidase is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>; and
wherein the DNase has at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the amino acid sequence shown in SEQ ID NO <NUM>.

The invention further relates to a method of deep cleaning an item, comprising the steps of:.

The invention further relates to a kit intended for deep cleaning, wherein the kit comprises a solution of an enzyme mixture comprising a DNase and a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin.

The DNase is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the amino acid sequence shown in SEQ ID NO <NUM>, and the a hexosaminidase, preferably a β-N-acetylglucosaminidase e.g. a dispersin is a polypeptide having at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>%, at least <NUM>% or <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>;.

Biofilm is produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS). 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. On hard surfaces 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. In one aspect, the biofilm producing strain is Brevundimonas sp. In one aspect, the biofilm producing strain is Pseudomonas alcaliphila or Pseudomonas fluorescens. In one aspect, the biofilm producing strain is Staphylococcus aureus.

By the term "deep cleaning" is meant disruption, removal or reduction of components of organic matter, e.g. biofilm, such as polysaccharides, proteins, DNA, soil or other components present in the organic matter.

Cleaning component: The cleaning component is different from the DNase and hexosaminidase. The precise nature of these cleaning component, 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.

Cleaning Composition: The term "cleaning composition" refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles. The cleaning composition may be a detergent composition and 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). In addition to containing the enzyme of the invention, the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases 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. The term "cleaning composition" is used interchangeably with "detergent composition". The cleaning composition of the present invention can be diluted with water to form a wash liquor solution upon application.

The term "enzyme detergency benefit" is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme. Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and/or cleaning, prevention or reduction of redeposition of soils released in the washing process (an effect that also is termed anti-redeposition), restoring fully or partly the whiteness of textiles which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance (an effect that also is termed whitening). Textile care benefits, which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits. Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the fabric-softness, colour clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment. Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides. Textile care benefits, which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits. Examples of such textile care benefits are prevention or reduction of dye transfer from one textile to another textile or another part of the same textile (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a textile surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the textile-softness, colour clarification of the textile and removal of particulate soils which are trapped in the fibers of the textile. Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching component such as hydrogen peroxide or other peroxides or other bleaching species.

The term "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). Dishwashing includes but is not limited to cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.

The term "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.

The term "whiteness" is defined herein as a greying, yellowing of a textile. Loss of whiteness may be due to removal of optical brighteners/hueing agents. Greying and yellowing can be due to soil redeposition, body soils, colouring from e.g. iron and copper ions or dye transfer. Whiteness might include one or several issues from the list below: colourant or dye effects; incomplete stain removal (e.g. body soils, sebum etc.); redeposition (greying, yellowing or other discolourations of the object) (removed soils reassociate with other parts of textile, soiled or unsoiled); chemical changes in textile during application; and clarification or brightening of colours.

The term "laundering" relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention. The laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.

By the term "malodor" is meant an odor which is not desired on clean items. The cleaned item should smell fresh and clean without malodors adhered to the item. One example of malodor is compounds with an unpleasant smell, which may be produced by microorganisms. Another example is unpleasant smells can be sweat or body odor adhered to an item which has been in contact with human or animal. Another example of malodor can be the odor from spices, which sticks to items for example curry or other exotic spices which smells strongly.

The term "mature polypeptide" means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc..

The term "textile" means any textile material including yarns, yarn intermediates, fibers, nonwoven 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. Examples of blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing fiber (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fiber, lyocell). Fabric may be conventional washable laundry, for example stained household laundry. When the term fabric or garment is used it is intended to include the broader term textiles as well.

The term "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". For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (<NPL>) as implemented in the Needle program of the EMBOSS package (E<NPL>), preferably version <NUM>. <NUM> or later. The parameters used are a gap open penalty of <NUM>, a gap extension penalty of <NUM>, 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:<MAT>.

NUC1, NUC1A DNase: The term includes DNases comprising a certain domain. The domain termed NUC1 and polypeptides of this domain are in addition to having DNase activity, characterized by comprising certain motifs e.g. one or more of the motifs [F/L/Y/I]A[N/R]D[L/I/P/V] (SEQ ID NO: <NUM>) or C[D/N]T[A/R] (SEQ ID NO: <NUM>); the letters indicate amino acids in one letter code thus F is phenylalanine, L is leucine, A is alanine, N is asparagine, D is aspartic acid, I is isoleucine, V is valine, H is histidine, G is glycine, C cysteine, T is threonine, R is arginine and so forth. The brackets indicate that the amino acids within the bracket are alternatives. The NUC1_A domain share the common motif [D/Q][I/V]DH (SEQ ID NO <NUM>).

DNase activity was determined on DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which was prepared according to the manual from supplier. Briefly, <NUM> of agar was dissolved in <NUM> water and then autoclaved for <NUM> at <NUM>. Autoclaved agar was temperated to <NUM> in water bath, and <NUM> of agar was poured into petri dishes and allowed to solidify by incubation o/n at room temperature. On solidified agar plates, <NUM>µl of enzyme solutions are added and DNase activity is observed as colorless zones around the spotted enzyme solutions.

The hexosaminidase activity of the polypeptides listed in the table below was determined using <NUM>-nitrophenyl N-acetyl-β-D-glucosaminide (Sigma-Aldrich) as substrate. The enzymatic reaction was performed in triplicates in a <NUM> well flat bottom polystyrene microtiter plate (Thermo Scientific) with the following conditions: <NUM> <NUM>-(N-morpholino)ethanesulfonic acid pH <NUM> buffer, <NUM>/ml <NUM>-nitrophenyl N-acetyl-β-D-glucosaminide and <NUM>µg/ml purified enzyme sample in a total reaction volume of <NUM>µl. Blank samples without polypeptide were run in parallel. The reactions were carried out at <NUM> in a Thermomixer comfort (Eppendorf). After <NUM> minutes of incubation, <NUM>µl <NUM> NaOH was added to each reaction mixture to stop the enzymatic reaction. The absorbance was read at <NUM> using a POLARstar Omega plate reader (BMG LABTECH) to estimate the formation of <NUM>-nitrophenolate ion released because of enzymatic hydrolysis of the <NUM>-nitrophenyl N-acetyl-β-D-glucosaminide substrate.

Wash performance may be assessed in laundry wash experiment using a Mini wash assay, which is a test method where soiled textile is continuously lifted up and down into the test solution and subsequently rinsed.

The wash experiment is conducted under various experimental conditions, one example specified below:.

Test materials may be obtained from EMPA Testmaterials AG Mövenstrasse <NUM>, CH-<NUM> St. Gallen, Switzerland, from Center for Testmaterials BV, P. Box <NUM>, <NUM> KT Vlaardingen, the Netherlands, and WFK Testgewebe GmbH, Christenfeld <NUM>, D-<NUM> Brüggen, Germany. The textiles are subsequently air-dried and the wash performance is measured as the brightness of the colour of these textiles. Brightness can also be expressed as the Remission (R), which is a measure for the light reflected or emitted from the test material when illuminated with white light. The Remission (R) of the textiles is measured at <NUM> using a Zeiss MCS <NUM> VIS spectrophotometer. The measurements are done according to the manufacturer's protocol.

DNase activity was determined by using the DNaseAlert™ Kit (<NUM>-<NUM>-<NUM>-<NUM>, IDT Intergrated DNA Technologies) according to the supplier's manual. Briefly, <NUM>µl DNase sample was mixed with <NUM>µl substrate in a microtiter plate, and fluorescence was immediately measured using a Clariostar microtiter reader from BMG Labtech (<NUM> excitation, <NUM> emission).

Preparation of the biofilm swatches: A PNAG-producing Pseudomonas fluorescens isolate was used as model microorganism in the present example. Hexosaminidases such as dispersin have previously been shown to effectively target the PNAG in Pseudomonas fluorescens biofilms (<NPL>). The Pseudomonas fluorescens strain was restreaked on Tryptone Soya Agar (TSA) (pH <NUM>) (CM0131; Oxoid Ltd, Basingstoke, UK) and incubated for <NUM> days at ambient temperature. A single colony was inoculated into <NUM> of TSB and the culture was incubated for <NUM> hours at ambient temperature with shaking (Tetramax <NUM>, 460rpm). After propagation, the culture was diluted (<NUM>:<NUM>) in fresh TSB and <NUM> aliquots were added to the wells of <NUM>-well polystyrene flat-bottom microplates (<NUM>; Costar, Corning Incorporated, Corning, NY, USA), in which round swatches (diameter <NUM>) of sterile textile (WFK20A) had been placed. Sterile TSB was added to control wells. The biofilm swatches were cultivated for <NUM> at ambient temperature (static incubation).

The prepared biofilm swatches were then rinsed twice with <NUM>% (w/v) NaCl. Five rinsed swatches (sterile or with P. fluourescens) were placed in <NUM> test tubes, and <NUM> of wash liquor (<NUM>°dH water with <NUM>/L iron(III) oxide nanopowder (<NUM>; Sigma-Aldrich) with <NUM>/L liquid model A detergent and <NUM>. 2ppm enzyme(s) was added to each tube. Washes without enzyme were included as controls. The test tubes were placed in a Stuart rotator and incubated for <NUM> hour at <NUM> at 20rpm. The wash liquor was then removed, and the swatches were rinsed twice with <NUM>°dH water and dried on filter paper over night.

The tri-stimulus light intensity (Y) values of the swatches were measured using a DigiEYE colour measurement and imaging system (VeriVide) equipped with a Nikon D90 digital camera.

Delta values (Y(swatch washed with enzyme) - Y(swatch washed without enzyme)) are also indicated.

Table <NUM>. Synergistic effect between hexosaminidase and DNase on cleaning in model A detergent on wfk20A, swatches.

As seen in table <NUM>, the DNase is capable of boosting the effect of the hexosaminidase on the PNAG-containing biofilm. Thus, an enzyme blend comprising hexosaminidase and DNase provides superior cleaning e.g. deep properties in model A detergent as compared to the individual enzymes. Given that the wash performance of the enzyme blend (ΔYblend) clearly exceed the sum of the performances seen for of the individual enzymes (ΔYHexos + ΔYDNase), this suggests that there is a synergetic effect between the two enzymes on the deep-cleaning properties in a detergent (model A).

Example <NUM> was conducted essentially the same as described above for Example <NUM>, except that a different hexosaminidase (SEQ ID NO: <NUM>) was used.

The tristimulus light intensity (Y) values were measured using a DigiEYE colour measurement and imaging system (VeriVide) equipped with a Nikon D90 digital camera, and are displayed in table <NUM>.

As seen in table <NUM>, the DNase is capable of boosting the effect of the hexosaminidase (SEQ ID NO: <NUM>) on the PNAG containing biofilm. Thus, an enzyme blend comprising hexosaminidase and DNase provides superior cleaning e.g. deep properties in model A detergent as compared to the individual enzymes. Given that the wash performance of the enzyme blend (ΔYblend) clearly exceed the sum of the performances seen for of the individual enzymes (ΔYHexos + ΔYDNase), this suggests that there is a synergetic effect between the two enzymes on the deep-cleaning properties in a detergent (model A).

EPS from the PNAG-producing Pseudomonas fluorescens isolate was isolated and used as follows: The strain was restreaked on Tryptone Soya Agar (TSA) (pH <NUM>) (CM0131; Oxoid Ltd, Basingstoke, UK) and incubated at <NUM>. The strain was then inoculated into <NUM> DURAN® laboratory bottles containing T-broth (<NUM>/L Bacto™ Tryptone (<NUM>, BD), <NUM>/L sodium chloride (<NUM>, Sigma-Aldrich)) and incubated statically for <NUM> days at <NUM>. The biofilm pellicles were subsequently extracted, pelleted by centrifugation (<NUM>, <NUM>), resuspended in <NUM> NaCl and incubated for <NUM> at ambient temperature to extract the surface-associated EPS (extracellular polymeric substances). The EPS-containing supernatants obtained after centrifugation (<NUM>, <NUM>, <NUM>) were pooled and stored at -<NUM> until further use (termed crude EPS).

For testing wash performance, 50ul aliquots of the crude EPS were spotted on sterile textile swatches (WFK20A) and incubated for <NUM> at ambient temperature. Swatches spotted with sterile <NUM> NaCl were included as controls. The swatches (sterile or with EPS) were placed in <NUM> test tubes and <NUM> of wash liquor (<NUM>°dH water with <NUM>/L WFK 09V pigment soil (Wfk-Testgewebe GmbH, #<NUM>) and <NUM>/L liquid model A detergent (<NUM>% LAS, <NUM>% AEO Biosoft N25-<NUM> (NI), <NUM>% AEOS (SLES), <NUM>% MPG (monopropylene glycol), <NUM>% ethanol, <NUM>% TEA, <NUM>% coco soap, <NUM>% soya soap, <NUM>% glycerol, <NUM>% sodium hydroxide, <NUM>% sodium citrate, <NUM>% sodium formate, <NUM>% DTMPA and <NUM>% PCA (all percentages are w/w)) and <NUM>µg/ml enzyme(s) was added to each tube. Washes without enzyme were included as controls. The test tubes were placed in a Stuart rotator and incubated for <NUM> hour at <NUM> at 20rpm. The wash liquor was then removed, and the swatches were rinsed twice with <NUM>°dH water and dried on filter paper over night. The remisssion (REM<NUM>) values were measured using a Macbeth Color-Eye <NUM> (CE7000), and are displayed in table <NUM>. Delta values (REM<NUM>(swatch washed with enzyme) - REM<NUM>(swatch washed without enzyme)) and the wash performance synergies, WPsyn (ΔREM<NUM> (Blend) - ΔREM<NUM> (sum of individual enzyme treatments)) are also indicated.

Claim 1:
A cleaning composition comprising <NUM>-<NUM> ppm DNase, <NUM>-<NUM> ppm hexosaminidase, and at least one cleaning component,
wherein the cleaning component comprises at least a surfactant, optionally a builder, and optionally a bleach component;
wherein the DNase is a polypeptide having at least <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>; and
wherein the hexosaminidase is a polypeptide having at least <NUM>% sequence identity to the polypeptide shown in SEQ ID NO: <NUM>.