Cleaning composition and use thereof

Abstract

The present invention relates to compositions, such as cleaning compositions comprising a mixture of enzymes. The invention further relates to the use of a composition comprising such an enzyme in a cleaning process and / or for deep cleaning of organic soils, a method for removing or reducing components of organic matter.

Description

[0001] References to sequence listings

[0002] This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference. Background of the Invention

[0004] The present invention relates to compositions, such as cleaning compositions, comprising a mixture of enzymes. The invention further relates to the use of compositions comprising such enzymes in cleaning processes and / or for deep cleaning of organic soils, for methods of removing or reducing the fraction of organic matter. Background Art

[0005] Enzymes have been used in detergents for decades. Typically, a cocktail of enzymes is added to detergent compositions. This cocktail typically contains multiple enzymes, each targeting its own specific substrate—for example, amylases active on starch stains, proteases active on protein stains, and so on. Textile surfaces and hard surfaces (such as dishes or the interior of a washing machine) soiled with many different types of soils (which can be composed of proteins, grease, starch, and more) are subjected to multiple wash cycles.

[0006] The ability of a detergent to release soil and keep it suspended is crucial to its efficiency. Particulate soil that is not suspended by the detergent will be redeposited on the fabric. It is known that redeposited soil is generally more difficult to remove than the original soil, partly because of its smaller particle size. The surfactants in detergents are generally not capable of releasing soil and keeping it suspended, so polymers are added to detergents. The addition of polymers helps prevent graying, dulling, and yellowing of garments, which are obviously of concern from a consumer perspective.

[0007] Detergent compositions have been described, but there is an ongoing need for more sustainable detergent compositions in which enzymes remain active and improved sustainability profiles, which can be achieved by adding enzymes to partially or even completely replace the polymers in the detergent. It is therefore an object of the present invention to provide such detergent compositions. Summary of the Invention

[0008] The present invention relates to a cleaning composition comprising:

[0009] (i) at least one xyloglucanase, wherein the xyloglucanase is selected from the group consisting of:

[0010] a) having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 1,

[0011] b) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 2,

[0012] c) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 3,

[0013] d) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 4,

[0014] e) having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 5,

[0015] f) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 6, or

[0016] g) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide shown in SEQ ID NO: 7; and

[0017] (ii) at least one DNA enzyme.

[0018] The present invention also relates to the use of a cleaning composition according to any one of the embodiments described herein in laundry, manual dishwashing or automatic dishwashing.

[0019] The present invention also relates to a method of washing comprising washing fabrics with a cleaning composition according to any one of the embodiments described herein, preferably at a temperature of 40°C or lower.

[0020] The present invention also relates to a method for washing dishes in an automatic dishwasher using a cleaning composition according to any one of the embodiments described herein, the method comprising the steps of adding the cleaning composition to a detergent composition chamber in the automatic dishwasher, and releasing the cleaning composition during a main wash cycle.

[0021] definition

[0022] In light of this detailed description, the following definitions apply. Note that the singular forms "a," "an," and "the" include plural referents unless the context clearly dictates otherwise.

[0023] Reference herein to "about" a value or parameter includes aspects directed to the value or parameter itself. For example, description referring to "about X" includes the aspect "X."

[0024] Unless defined otherwise or clearly indicated by the context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs.

[0025] Amino acids: As used herein, the term "amino acid" refers to the standard twenty genetically encoded amino acids and their corresponding stereoisomers in the "d" form (as opposed to the natural "l" form), ω-amino acids, other naturally occurring amino acids, unconventional amino acids (e.g., α,α-disubstituted amino acids, N-alkyl amino acids, etc.), and chemically derivatized amino acids. Chemical derivatives of one or more amino acids can be achieved by reaction with functional side groups. Such derivatized molecules include, for example, those in which free amino groups have been derivatized to form amine hydrochlorides, p-toluenesulfonyl groups, carboxyphenoxy groups, tert-butoxycarbonyl groups, chloroacetyl groups, or formyl groups. Free carboxyl groups can be derivatized to form salts, methyl and ethyl esters or other types of esters and hydrazides. Free hydroxyl groups can be derivatized to form O-acyl or O-alkyl derivatives. Also included as chemical derivatives are peptides containing naturally occurring amino acid derivatives of the twenty standard amino acids. For example, 4-hydroxyproline can be substituted for proline; 5-hydroxylysine can be substituted for lysine; 3-methylhistidine can be substituted for histidine; homoserine can be substituted for serine, and ornithine can be substituted for lysine. Derivatives also include peptides containing one or more additions or deletions, as long as the necessary activity is maintained. Other modifications include amidation, amino-terminal acylation (e.g., acetylation or thioglycolic acid amidation), terminal carboxyl amidation (e.g., with ammonia or methylamine), and similar terminal modifications.

[0026] When an amino acid is explicitly listed, such as "alanine" or "Ala" or "A," the term refers to both l-alanine and d-alanine, unless expressly stated otherwise. Other unconventional amino acids may also be suitable components of the polypeptides of the invention, as long as the desired functional properties are retained by the polypeptide. For the peptides shown, each encoded amino acid residue is represented by a single-letter designation, corresponding to the common name of the conventional amino acid, where appropriate. In one embodiment, the polypeptides of the invention comprise or consist of l-amino acids.

[0027] Anti-redeposition polymers: In the context of the present invention, polymers include, but are not limited to, polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose, and / or combinations thereof.

[0028] Allelic variants: The term "allelic variant" refers to any of two or more alternative forms of a gene occupying the same chromosomal locus. Allelic variation arises naturally through mutation and can lead to polymorphism within a population. Gene mutations can be silent (no change in the encoded polypeptide) or can encode a polypeptide with an altered amino acid sequence. An allelic variant of a polypeptide is a polypeptide encoded by an allelic variant of a gene.

[0029] bacterial: The term "bacterial" with respect to polypeptides (such as enzymes, for example, xyloglucanase) refers to polypeptides encoded by the bacterial genome and therefore directly derived from the bacterial genome, wherein such bacteria have not been genetically modified to encode the polypeptide, for example, by introducing the coding sequence into the genome through recombinant DNA technology. Therefore, in the context of the present invention, the term "bacterial xyloglucanase" or "polypeptide with xyloglucanase activity obtained from a bacterial source" or "polypeptide of bacterial origin" refers to cellulases encoded by the genome of a bacterial species and therefore directly derived from the genome of a bacterial species, wherein these bacterial species have not been genetically modified by introducing recombinant DNA encoding the xyloglucanase. Therefore, the nucleotide sequence encoding the bacterial polypeptide with xyloglucanase activity is a sequence naturally present in the genetic background of the bacterial species. The sequence encoding the bacterial polypeptide with cellulase activity can also be referred to as a wild-type xyloglucanase (or parent xyloglucanase). Bacterial polypeptides with xyloglucanase activity include wild-type recombinantly produced polypeptides. In another aspect, the invention provides polypeptides with xyloglucanase activity, wherein the polypeptide is substantially homologous to a bacterial cellulase. In the context of the present invention, the term "substantially homologous" means that the polypeptide having cellulase activity has at least 80%, preferably at least 85%, more preferably at least 90%, more preferably at least 95%, even more preferably at least 96%, 97%, 98%, and most preferably at least 99% identity with the amino acid sequence of the selected bacterial cellulase.

[0030] Cellulolytic enzymes or cellulases : The term "cellulolytic enzyme" or "cellulase" means one or more (e.g., several) enzymes that hydrolyze cellulosic material. Such enzymes include one or more endoglucanases (e.g., EC 3.2.1.4), one or more cellobiohydrolases, one or more β-glucosidases, or a combination thereof. Two basic methods for measuring cellulolytic enzyme activity include: (1) measuring total cellulolytic enzyme activity, and (2) measuring individual cellulolytic enzyme activities (endoglucanase, cellobiohydrolase, and β-glucosidase), as described in Zhang et al., 2006, Biotechnology Advances 24: 452-481. Total cellulolytic enzyme activity can be measured using insoluble substrates including Whatman No. 1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, and the like. The most common total cellulolytic activity assay is the filter paper assay using Whatman No. 1 filter paper as the substrate. This assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Pure Appl. Chem. 59: 257-68).

[0031] Cellulosic materials : The term "cellulosic material" means any material containing cellulose. The main polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemicellulose, and the third most abundant is pectin. The secondary cell wall, which is produced after the cells stop growing, also contains polysaccharides and is reinforced by polymeric lignin that is covalently cross-linked with the hemicellulose. Cellulose is a homopolymer of dehydrocellobiose and is therefore a linear β-(1-4)-D-glucan, while hemicellulose includes a variety of compounds such as xylans, xyloglucans, arabinoxylans, and mannans that have a series of substituents in a complex branched structure. Although cellulose is generally polymorphic, it is found in plant tissues primarily as an insoluble crystalline matrix of parallel glucan chains. Hemicellulose is typically hydrogen-bonded to cellulose and other hemicelluloses, which helps stabilize the cell wall matrix.

[0032] cDNA : The term "cDNA" means a DNA molecule that can be prepared by reverse transcription from a mature, spliced mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial primary RNA transcript is a precursor to mRNA, which is processed through a series of steps (including splicing) and then present as mature spliced mRNA.

[0033] Coding sequence : The term "coding sequence" means a polynucleotide that directly specifies the amino acid sequence of a variant. The boundaries of a coding sequence are usually determined by an open reading frame that begins with a start codon (such as ATG, GTG, or TTG) and ends with a stop codon (such as TAA, TAG, or TGA). The coding sequence can be genomic DNA, cDNA, synthetic DNA, or a combination thereof.

[0034] Control Sequence : The term "control sequence" means the nucleic acid sequence necessary for expressing the polynucleotide encoding the variant of the present invention. Each control sequence can be native (i.e., from the same gene) or exogenous (i.e., from different genes) to the polynucleotide encoding the variant, or native or exogenous relative to each other. Such control sequences include, but are not limited to, leader sequences, polyadenylation sequences, propeptide sequences, promoters, signal peptide sequences, and transcription terminators. At a minimum, the control sequence includes a promoter and transcription and translation termination signals. The control sequence can be provided with a linker for the purpose of introducing specific restriction sites that facilitate connection of the control sequence to the coding region of the polynucleotide encoding the variant.

[0035] Dishwashing composition:As used herein, the term "dishwashing composition" refers to all forms of compositions used to clean hard surfaces. The present invention is not limited to any particular type of dishwashing composition or any particular detergent. Thus, in one embodiment, the dishwashing composition is a liquid dishwashing composition, a powder dishwashing composition, wherein the composition may optionally be in the form of a unit dose.

[0036] Detergent ingredients The term "detergent components" is defined herein to mean the types of chemicals that can be used in detergent compositions. Examples of detergent components are surfactants, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching systems or bleaching components, polymers, fabric hueing agents, fabric softeners, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, fluorescent whitening agents, perfumes, optical brighteners, bactericides, fungicides, soil-suspending agents, soil-release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizing agents. The detergent composition may contain one or more detergent components of any type.

[0037] Detergent or cleaning composition:The term "detergent or cleaning composition" refers to a composition for removing undesirable compounds from items to be cleaned, such as textiles, dishes, and hard surfaces. Detergent compositions can be used, for example, to clean textiles, dishes, and hard surfaces, for both domestic and industrial cleaning, and / or for fabric care. These terms encompass any material / compound selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granular, paste, or spray composition), and include, but are not limited to, detergent compositions (e.g., liquid and / or solid laundry detergents and delicate fabric detergents; hard surface cleaning formulations, such as for glass, wood, plastic, ceramic, and metal countertops and windows; carpet cleaners; oven cleaners; fabric refreshers; fabric softeners; and textile and clothing pre-stain removers, as well as dishwashing detergents). In addition to the enzymes of the present invention, the detergent formulations may also contain one or more additional enzymes (e.g., amylases, proteases, peroxidases, cellulases, β-glucanases, xyloglucanases, hemicellulases, xanthanases, xanthan lyases, lipases, acyltransferases, phospholipases, esterases, laccases, catalases, arylesterases, amylases, α-amylases, glucoamylases, cutinases, pectinases, pectin lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, carrageenanases, pullulanases, tannases, arabinosidases, hyaluronidases, chondroitinases, xyloglucanases, xylanases, pectin acetylesterases, polygalacturons, rhamnogalacturons, endo- β-mannanases, exo-β-mannanases (GH5 and / or GH26), licheninases, phosphodiesterases, pectin methylesterases, cellobiohydrolases, transglutaminases, nucleases, and combinations thereof, or any mixtures thereof), and / or components such as surfactants, builders, chelants or sequestrants, bleaching systems or bleaching components, polymers, fabric softeners, foam boosters, suds suppressors, dyes, perfumes, tarnish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, corrosion inhibitors, enzyme inhibitors or stabilizers, enzyme activators, one or more transferases, hydrolases, oxidoreductases, bluing agents and fluorescent dyes, antioxidants and solubilizers.

[0038] Dishwashing : The term "warewashing" refers to all forms of dishwashing, such as manual dishwashing (HDW) or automatic dishwashing (ADW). Dishwashing includes, but is not limited to, cleaning all forms of tableware, such as plates, cups, glasses, bowls, all forms of cutlery (e.g., spoons, knives, forks), and serving utensils including ceramic, plastic, metal, porcelain, glass, and acrylic.

[0039] Enzyme Cleaning BenefitsThe term "enzyme washing benefit" is defined in this article as the advantageous effect of adding enzyme to the detergent compared with the same detergent without the enzyme. The important washing benefit that can be provided by enzyme is that stain removal is accompanied by no visible dirt or visible dirt very little after washing and / or cleaning, prevents or reduces the redeposition of the dirt discharged in the washing process (also known as the effect of anti-redeposition), recovers the whiteness of textiles (also known as the effect of bleaching) wholly or in part, the textiles being originally white, but obtaining light grey or light yellow outward appearance after repeated use and washing. The textile care benefits that are not directly relevant to catalysis stain removal or preventing dirt from redeposition are also important for enzyme washing benefits. The example of such textile care benefits is to prevent or reduce dye from transferring to another part of another fabric or same fabric (also known as dye transfer inhibition or anti-backstaining effect) from a fabric surface, remove prominent or broken fibers to reduce pilling tendency or remove existing balls or fuzz (also known as the effect of anti-pilling) from the fabric surface, improve fabric softness, make the color of fabric clarified and remove the particulate dirt trapped in the fiber of fabric or clothing. Enzyme bleaching is another enzymatic detergent benefit where the catalytic activity is typically used to catalyze the formation of a bleaching component such as hydrogen peroxide or other peroxides.

[0040] Express : The term "expression" includes any step involved in the production of the variant including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion.

[0041] expression vector : The term "expression vector" means a linear or circular DNA molecule that contains a polynucleotide encoding a variant and is operably linked to control sequences that provide for its expression.

[0042] snippet : The term "fragment" means a polypeptide that lacks one or more (e.g., several) amino acids at the amino and / or carboxyl termini of a mature polypeptide; wherein the fragment has xyloglucanase activity. On the one hand, the fragment contains at least 445 amino acid residues, at least 471 amino acid residues, or at least 497 amino acid residues.

[0043] Fusion peptideThe term "fusion polypeptide" refers to a polypeptide in which one polypeptide is fused to the N-terminus or C-terminus of a variant of the present invention. Fusion polypeptides are produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention. Techniques for producing fusion polypeptides are known in the art and include ligating the coding sequences encoding the polypeptides so that they are in frame and expression of the fusion polypeptide is under the control of one or more identical promoters and terminators. Fusion polypeptides can also be constructed using intein technology, in which the fusion polypeptide is produced post-translationally (Cooper et al., 1993, EMBO J. 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779). The fusion polypeptide may further comprise a cleavage site between the two polypeptides. Upon secretion of the fusion protein, this site is cleaved, thereby releasing both polypeptides. Examples of cleavage sites include, but are not limited to, those disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000, J. Biotechnol. 76:245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381. 1995, Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6: 240-248; and Stevens, 2003, Drug Discovery World 4: 35-48.

[0044] Hard surface cleaningThe term "hard surface cleaning" is defined herein as cleaning hard surfaces, which can include floors, tables, walls, roofs, etc., as well as the surfaces of hard objects such as cars (car washing) and tableware (dishwashing). Dishwashing includes, but is not limited to, cleaning plates, cups, glasses, bowls, cutlery (e.g., spoons, knives, forks), serving utensils, ceramics, plastics, metals, porcelain, glass, and acrylics.

[0045] host cells : The term "host cell" means any cell type that is susceptible to transformation, transfection, transduction, etc. with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term "host cell" encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.

[0046] Hybrid peptide: The term "hybrid polypeptide" means a polypeptide comprising domains from two or more polypeptides of different origins (e.g., a binding module from one polypeptide and a catalytic domain from another polypeptide). The domains can be fused at the N-terminus or the C-terminus. Of particular interest herein are polypeptides comprising a binding module from one polypeptide (which may be naturally occurring or further modified), an engineered linker region (e.g., a proline-rich linker region (which is a synthetic construct)), and a catalytic domain from another polypeptide (which may be naturally occurring or further modified).

[0047] Hybridization:The term "hybridization" means using standard Southern blotting procedures with substantially complementary strands of nucleic acid paired. Hybridization can be carried out under medium, medium-high, high or very high stringency conditions. Medium stringency conditions mean 5X SSPE, 0.3% SDS, 200 micrograms / ml shearing and denatured salmon sperm DNA and 35% formamide in 42°C prehybridization and hybridization for 12 to 24 hours, then using 0.2X SSC, 0.2% SDS, 55°C washing 3 times, each 15 minutes. Medium-high stringency conditions mean 5X SSPE, 0.3% SDS, 200 micrograms / ml shearing and denatured salmon sperm DNA and 35% formamide in 42°C prehybridization and hybridization for 12 to 24 hours, then using 0.2X SSC, 0.2% SDS, 60°C washing 3 times, each 15 minutes. High stringency conditions mean prehybridization and hybridization in 5X SSPE, 0.3% SDS, 200 μg / ml sheared and denatured salmon sperm DNA, and 50% formamide at 42°C for 12 to 24 hours, followed by three 15-minute washes in 0.2X SSC, 0.2% SDS at 65°C. Very high stringency conditions mean prehybridization and hybridization in 5X SSPE, 0.3% SDS, 200 μg / ml sheared and denatured salmon sperm DNA, and 50% formamide at 42°C for 12 to 24 hours, followed by three 15-minute washes in 0.2X SSC, 0.2% SDS at 70°C.

[0048] Improved characteristics : The term "improved properties" means a feature associated with an improved variant compared to a reference enzyme / parent enzyme. Such improved properties include, but are not limited to, improved wash performance, improved enzyme wash benefit, improved stability, and / or improved whiteness.

[0049] Improved stability Term " improved stability " means that variant enzyme shows as retention enzymatic activity after hatching for a period of time under the existence of the chemical of the enzymic activity of one or more naturally occurring or synthetic, that reduces the parent enzyme.Improved stability means the stability with respect to reference enzyme / parent enzyme, and variant enzyme has better stability under the existence of protease, and for example comprises, storage stability in protein hydrolysis stability, detergent, storage stability in the detergent under chelating agent or chelating agent exists, stability and stability in the washing during detergent composition production.Especially, improved detergent stability is, when xyloglucanase variant of the present invention is mixed in liquid detergent formulation or unit dose detergent formulation, then when the temperature between 15 ℃ and 50 ℃ is stored, the stability of the improvement of xyloglucanase activity.

[0050] In the present invention, liquid detergents are particularly useful as liquid laundry detergents and / or unit dose laundry detergents.

[0051] Improved washing performance : The term "improved wash performance" is defined herein as an enzyme in a detergent composition that exhibits increased wash performance, e.g., by increased color clarification and / or anti-pilling effect, relative to the wash performance of a reference enzyme / parent enzyme when evaluated on a fresh sample and / or after storage of the sample under the same conditions. The term "improved wash performance" includes wash performance in laundry and also in, for example, hard surface cleaning such as automated dishwashing (ADW).

[0052] Separated The term "isolated" means a polypeptide, nucleic acid, cell, or other specific material or component that is separated from at least one other material or component with which it is naturally associated in nature (including, but not limited to, other proteins, nucleic acids, cells, etc.). An isolated polypeptide includes, but is not limited to, a culture medium containing a secreted polypeptide.

[0053] Clothes washing: The term "laundry" refers to both domestic and industrial laundry and means the process of treating textiles with a solution containing the cleaning or detergent composition of the present invention. The laundry process can be carried out, for example, using a domestic or industrial washing machine, or can be carried out manually.

[0054] Mature peptide : The term "mature polypeptide" means a polypeptide in its mature form after N-terminal processing (eg, removal of the signal peptide).

[0055] Mature polypeptide coding sequence : The term "mature polypeptide coding sequence" means a polynucleotide encoding a mature polypeptide having xyloglucanase activity.

[0056] mutant : The term "mutant" means a polynucleotide encoding a variant.

[0057] Modification: In the context of the polypeptides of the present invention, the term "modification" means changing one or more amino acids within a reference amino acid sequence (i.e., SEQ ID NO: 1, 2, or 3) by substitution with a different amino acid, by insertion of an amino acid, or by deletion (preferably by at least one deletion). The terms "modification," "alteration," and "mutation" are used interchangeably and have the same meaning and purpose.

[0058] Nucleic acid constructs: The term "nucleic acid construct" means a single-stranded or double-stranded nucleic acid molecule that is isolated from a naturally occurring gene, or modified to contain a nucleic acid segment in a manner not originally present in nature, or is synthetic, and contains one or more control sequences.

[0059] Operatively connected: The term "operably linked" means a configuration in which a control sequence is placed at an appropriate position relative to the coding sequence of a polynucleotide such that the control sequence directs the expression of the coding sequence.

[0060] Purified The term "purified" means a nucleic acid or polypeptide that is substantially free of other components, as determined by analytical techniques well known in the art (e.g., a purified polypeptide or nucleic acid can form discrete bands in an electrophoretic gel, a chromatography eluate, and / or a culture medium subjected to density gradient centrifugation). A purified nucleic acid or polypeptide is at least about 50% pure, typically at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percentages by weight on a molar basis). In a related sense, a composition is enriched for a molecule when the concentration of the molecule is substantially increased following application of a purification or enrichment technique. The term "enriched" refers to the presence of a compound, polypeptide, cell, nucleic acid, amino acid or other designated material or component in a composition at a relative or absolute concentration greater than that of the starting composition.

[0061] Reorganization : The term "recombinant" when used in reference to a cell, nucleic acid, protein, or vector means that it has been modified from its native state. Thus, for example, a recombinant cell expresses genes not found in the native (non-recombinant) form of the cell, or expresses native genes at different levels or under different conditions than they are found in nature. A recombinant nucleic acid differs from a native sequence by one or more nucleotides and / or is operably linked to a heterologous sequence (e.g., a heterologous promoter in an expression vector). A recombinant protein can differ from a native sequence by one or more amino acids and / or be fused to a heterologous sequence. A vector containing a nucleic acid encoding a polypeptide is a recombinant vector. The term "recombinant" is synonymous with "genetically modified" and "transgenic."

[0062] Sequence identity : The degree of relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity".

[0063] For purposes of the present invention, use Needleman-Wunsch algorithm (Needleman-Wunsch algorithm) (Needleman and Wunsch, 1970, J. Mol. Biol. [Journal of Molecular Biology] 48: 443-453) to determine the sequence identity between two amino acid sequences, this algorithm is as EMBOSS software package (EMBOSS:The European Molecular Biology Open Software Suite [European Molecular Biology Open Software Suite], people such as Rice, 2000, Trends Genet. [Genetics trend] 16: 276-277, preferred 5.0.0 version or more recent version) Needle program is implemented.Employed parameter is gap opening penalty 10, gap extension penalty 0.5 and EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.Use the output (using non-simplification (-nobrief) option to obtain) of " the longest identity " of Needle mark as identity percentage and as follows and calculate:

[0064] (identical residues x 100) / (alignment length - total number of gaps in the alignment)

[0065] For purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented by the Needle program of the EMBOSS software package (EMBOSS:TheEuropean Molecular Biology Open Software Suite [European Molecular Biology Open Software Suite], Rice et al., 2000, supra) (preferred 5.0.0 version or later). The parameters employed are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The output of the "longest identity" mark (obtained using the non-simplified (-nobrief) option) is used as percent identity and is calculated as follows:

[0066] (number of identical deoxyribonucleotides x 100) / (length of alignment – total number of gaps in the alignment)

[0067] subsequence : The term "subsequence" means a polynucleotide having one or more nucleotides deleted from the 5' end and / or 3' end of the mature polypeptide coding sequence; wherein the subsequence encodes a fragment having xyloglucanase activity.

[0068] Sustainability: Sustainability and sustainable mean using renewable resources that cause little or no damage to the environment and are biodegradable.

[0069] Sustainability Features: In the context of the present invention, the term sustainability profile is used to compare the sustainability of ingredients (e.g. in a detergent composition), where one or more ingredients can replace other less sustainable ingredients while maintaining the performance of the system (e.g. the performance of the detergent composition during the washing of items).

[0070] textile : Term " textile " means any textile material, and this any textile material comprises yarn, yarn intermediate, fiber, non-woven material, natural material, synthetic material and any other textile material, the fabric made by these materials and the product (for example, clothing and other goods) made by fabric.Textile or fabric can be in the form of knitwear, woven fabric, denim (denim), non-woven fabric, felt, yarn and toweling.Textile can be based on cellulose, for example natural cellulose product, comprises cotton, flax / linen, jute, ramie, sisal or coconut fiber, or artificial cellulose product (for example, deriving from wood pulp), comprises viscose / rayon, cellulose acetate fiber (tricell (tricell)), lyocell fiber (lyocell) or its blend. Textiles or fabrics can also be non-cellulose based, such as natural polyamides, including wool, camel hair, cashmere, mohair, rabbit hair and silk, or synthetic polymers such as nylon, aramid, polyester, acrylate, 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 accompanying materials, such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) and / or cellulose-containing fibers (e.g., rayon / viscose fibers, ramie, flax / linen, jute, cellulose acetate fibers, lyocell fibers). Fabrics can be conventional washable clothing, such as household clothing with stains. When the term fabric or clothing is used, it is intended to also include the broad term textiles.

[0071] VariantsTerm " variant " means to have xyloglucanase activity, comprise change at one or more (for example, several) positions and retain parent's active polypeptide.Replacement means to replace the amino acid that occupies a certain position with different amino acids.Variant of the present invention has at least 20% of the xyloglucanase activity of the polypeptide of SEQ ID NO:1, for example at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100%.

[0072] detergent : The term "wash liquor" refers to an aqueous solution containing a detergent composition in a diluted form, for example, but not limited to, a detergent solution containing a laundry detergent composition in a diluted form, such as the wash liquor in a laundry washing process.

[0073] Whiteness The term "whiteness" is defined herein as a broad term with different meanings in different fields and for different customers. Loss of whiteness can be due, for example, to graying, yellowing, or removal of optical brighteners / toners. Graying and yellowing can be due to soil redeposition, body soils, coloration from, for example, iron and copper ions, or dye transfer. Whiteness can include one or more issues from the following list: colorant or dye action; incomplete stain removal (e.g., body soils, sebum, etc.); redeposition (graying, yellowing, or other discoloration of an object) (re-association of removed soil with other parts of the textile, soiled or unsoiled); chemical changes in the textile during application; and clarification or brightening of color.

[0074] Wash cycle: The term "wash cycle" is defined herein as a washing operation in which a textile is immersed in a wash liquor, some mechanical action is applied to the textile to release stains and assist the flow of the wash liquor into and out of the textile, and ultimately remove excess wash liquor. After one or more wash cycles, the textile is generally rinsed and dried.

[0075] Washing performance : The term "wash performance" is used as the ability of a detergent composition, enzyme or polymer to remove stains present on an object to be cleaned or to maintain the color and whiteness of textiles during washing. The improvement in wash performance can be quantified by calculating the so-called ΔREM as described in the experimental part.

[0076] Weight Percentage: Abbreviations are w / w%, wt% or w%. These abbreviations are used interchangeably.

[0077] Washing time: The term "wash time" is defined herein as the time taken for a complete wash process; that is, the time for one or more wash cycles and one or more rinse cycles together.

[0078] wild type : The term "wild-type" when referring to an amino acid sequence or a nucleic acid sequence means that the amino acid sequence or nucleic acid sequence is a native or naturally occurring sequence. As used herein, the term "naturally occurring" refers to any substance (e.g., a protein, amino acid, or nucleic acid sequence) found in nature. In contrast, the term "non-naturally occurring" refers to any substance not found in nature (e.g., recombinant nucleic acid and protein sequences produced in a laboratory, or modifications of a wild-type sequence).

[0079] Xyloglucanase activity The term "xyloglucanase activity" is defined herein as the enzyme-catalyzed hydrolysis of xyloglucan. This reaction involves the endohydrolysis of 1,4-β-D-glucosidic bonds in xyloglucan. For the purposes of the present invention, xyloglucanase activity is determined using AZCL-xyloglucan (from Megazyme) as the reaction substrate. The assay can be performed in several ways, for example, as described in WO 01 / 62903. One xyloglucanase activity unit (XyloU) is defined with reference to the assay method described in WO 01 / 62903, page 60, lines 3-17.

[0080] Sequence review

[0081] SEQ ID NO: 1 is a xyloglucanase obtained from Paenibacillus polymyxa.

[0082] SEQ ID NO: 2 is a xyloglucanase obtained from Paenibacillus polymyxa.

[0083] SEQ ID NO: 3 is a xyloglucanase obtained from Paenibacillus polymyxa.

[0084] SEQ ID NO: 4 is a xyloglucanase obtained from Paenibacillus polymyxa.

[0085] SEQ ID NO: 5 is a xyloglucanase obtained from Paenibacillus polymyxa.

[0086] SEQ ID NO: 6 is a xyloglucanase obtained from Paenibacillus polymyxa

[0087] SEQ ID NO: 7 is a xyloglucanase obtained from Paenibacillus polymyxa

[0088] SEQ ID NO: 8 is a DNA enzyme obtained from Metabacillus indicus

[0089] SEQ ID NO: 9 is a DNA enzyme obtained from Aspergillus oryzae

[0090] SEQ ID NO: 10 is a DNA enzyme obtained from Bacillus proteus in India

[0091] SEQ ID NO: 11 is a DNA enzyme obtained from Bacillus licheniformis

[0092] SEQ ID NO: 12 is a DNA enzyme obtained from Bacillus subtilis

[0093] SEQ ID NO: 13 is a DNA enzyme obtained from Aspergillus oryzae

[0094] SEQ ID NO: 14 is a DNA enzyme obtained from Trichoderma harzianum

[0095] SEQ ID NO: 15 is a DNA enzyme obtained from Terribacillus saccharophilus

[0096] SEQ ID NO: 16 is a DNA enzyme obtained from Trichoderma reesei

[0097] SEQ ID NO: 17 is a DNA enzyme obtained from Tolypocladium inflatum

[0098] SEQ ID NO: 18 is a DNA enzyme obtained from Blastomyces gilchristii

[0099] SEQ ID NO: 19 is a DNA enzyme obtained from Gelasinospora tetrasperma

[0100] SEQ ID NO: 20 is a DNA enzyme obtained from Streptococcus dysgalactiae

[0101] SEQ ID NO: 21 is a DNA enzyme obtained from Thermobifida cellulosilytica

[0102] SEQ ID NO: 22 is a DNA enzyme obtained from Rasamsonia composticola

[0103] SEQ ID NO: 23 is a DNA enzyme obtained from Chaetosartorya cremea

[0104] SEQ ID NO: 24 is a DNA enzyme obtained from Aspergillus bisporus

[0105] SEQ ID NO: 25 is a DNA enzyme obtained from Aspergillus clavatus

[0106] SEQ ID NO: 26 is a DNA enzyme obtained from Metarhizium acridum

[0107] SEQ ID NO: 27 is a DNA enzyme obtained from Aspergillus ochraceoroseus DETAILED DESCRIPTION

[0108] The present invention relates to a cleaning composition comprising at least one xyloglucanase and at least one DNase.

[0109] The composition of the present invention is preferably a cleaning composition, the composition of the present invention comprising at least one xyloglucanase and at least one DNase.

[0110] The present invention relates to a cleaning composition comprising:

[0111] (i) at least one xyloglucanase, wherein the xyloglucanase is selected from the group consisting of:

[0112] a) having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 1,

[0113] h) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 2,

[0114] i) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 3,

[0115] j) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 4,

[0116] k) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 5,

[0117] 1) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 6, or

[0118] m) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 7; and

[0119] (iii) at least one DNA enzyme.

[0120] The present inventors have surprisingly found that more sustainable cleaning compositions (i.e. cleaning compositions with improved sustainability profiles) can be achieved by partially or even completely (totally) replacing the anti-redeposition polymers in a detergent by adding at least one xyloglucanase and at least one DNase, while maintaining the washing performance of the detergent.

[0121] As shown in the Examples section, while anti-redeposition polymers show benefits to textiles in the wash, xyloglucanases and DNAses can show competitive advantages, thus improving the sustainability profile by replacing petrochemically derived polymers with enzymes.

[0122] Thus, in an embodiment, the present invention relates to the use of at least one xyloglucanase and at least one DNase for improving the sustainability profile of a detergent composition by maintaining or improving the wash performance of the detergent while reducing the level of anti-redeposition polymers, particularly selected from the group consisting of: polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose and / or combinations thereof.

[0123] In an embodiment, the present invention relates to the use of at least one xyloglucanase and at least one DNA enzyme for improving the sustainability profile of a detergent composition by preventing, reducing, or removing soil redeposition onto textiles during a wash cycle while reducing the level of anti-redeposition polymers, particularly polymers selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or a combination thereof. When the soil is not adhered to the article, the textile appears cleaner.

[0124] In one embodiment, the present invention is directed to a detergent composition with improved sustainability characteristics, the detergent composition comprising at least one xyloglucanase, at least one DNase and at least one detergent adjunct ingredient, wherein the composition comprises less than 1%, e.g., less than 0,8%, less than 0,7%, less than 0,6%, less than 0,5%, less than 0,4%, less than 0,3%, less than 0,2%, less than 0,1%, less than 0,05%, less than 0,025% by weight of an anti-redeposition polymer, in particular an anti-redeposition polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or a combination thereof.

[0125] In another embodiment, the present invention is directed to a detergent composition with improved sustainability characteristics, comprising at least one xyloglucanase, at least one DNase, an anti-redeposition polymer, and at least one detergent adjunct ingredient, wherein the ratio (w / w) of anti-redeposition polymer to formulated xyloglucanase is in the range of 0.5 to 20; such as 0.5 to 10; such as 0.5 to 5; such as 0.5 to 2.5; such as 0.5 to 1, wherein the specific polymer is selected from the group consisting of: polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or a combination thereof.

[0126] In yet another embodiment, the present invention is directed to a detergent composition with improved sustainability characteristics, the detergent composition comprising at least one xyloglucanase, at least one DNase, an anti-redeposition polymer in the range of 0%-0.5% (w / w), and at least one detergent adjunct ingredient, wherein the formulated xyloglucanase is added in an amount of 0,15% – 0.5% (w / w); 0,2% – 0.5% (w / w); 0.3% – 0.5% (w / w); or 0.4% – 0.5% (w / w), wherein the anti-redeposition polymer is selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, or combinations thereof.

[0127] In yet another embodiment, the present invention is directed to a detergent composition with improved sustainability characteristics, the detergent composition comprising at least one xyloglucanase, at least one DNase, an anti-redeposition polymer and at least one detergent adjunct ingredient, wherein the ratio between the anti-redeposition polymer and the polypeptide having xyloglucanase activity (active enzyme protein) is in the range of 0-20, such as 2-20, 5-20, 5-15, 5-10, such as 5, 6, 7, 8, 9 or 10.

[0128] As demonstrated in Example 2, the combined use of two enzymes, xyloglucanase and DNase, can be used to increase perfume deposition from detergents during washing. Thus, one aspect of the present invention is the use of a detergent composition comprising xyloglucanase and DNase for increasing the overall perfume intensity on fabrics.

[0129] A further aspect is a method for increasing the overall fragrance intensity on a fabric, the method comprising contacting the fabric with a detergent composition comprising a xyloglucanase and a DNase.

[0130] The present invention further relates to a method for washing items, comprising the steps of:

[0131] a) exposing the items to a wash solution comprising at least one xyloglucanase and at least one DNase, or to a detergent composition comprising at least one xyloglucanase, at least one DNase and a reduced level of an anti-redeposition polymer, particularly a polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or a combination thereof;

[0132] b) complete at least one wash cycle;

[0133] c) optionally adding additional soil; and

[0134] d) optionally rinsing the article,

[0135] The article is a textile.

[0136] In an embodiment, a washing method with at least one xyloglucanase and at least one DNA enzyme provides the same or better whiteness of items compared to a washing method with a detergent composition that does not contain xyloglucanase but comprises a larger amount of an anti-redeposition polymer (such as a polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or a combination thereof).

[0137] The pH of the liquid solution is in the range of 1 to 11, such as in the range of 5.5 to 11, such as in the range of 7 to 9, in the range of 7 to 8 or in the range of 7 to 8.5 at 25°C. The pH of the powder detergent in demineralized water is measured at 1 g / L and is preferably in the range of 1-12; such as 5.5-11.5; such as 7.5-11.5; such as 8-11.

[0138] The wash liquid may have a temperature in the range of 5° C. to 95° C., or in the range of 10° C. to 80° C., in the range of 10° C. to 70° C., in the range of 10° C. to 60° C., in the range of 10° C. to 50° C., in the range of 15° C. to 40° C., or in the range of 20° C. to 40° C. In one embodiment, the temperature of the wash liquid is 30° C.

[0139] In one embodiment of the invention, the method for washing articles further comprises draining the washing liquid or part of the washing liquid after completing the wash cycle. The washing liquid can then be reused in a subsequent wash cycle or in a subsequent rinse cycle. During the first and optionally second or third wash cycle, the articles can be exposed to the washing liquid. In one embodiment, after being exposed to the washing liquid, the articles are rinsed. The articles can be rinsed with water or with water that contains a softener.

[0140] Xyloglucanases suitable for the uses as described herein are preferably microbial xyloglucanases, such as Bacillus or fungal xyloglucanases.

[0141] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 1, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 1 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0142] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 2 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 2 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0143] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 3 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 3 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0144] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 4 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 4 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0145] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 5 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 5 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0146] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 6 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 6 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0147] In an embodiment, the xyloglucanase is obtained from Paenibacillus, particularly Paenibacillus polymyxa. In an embodiment, the xyloglucanase comprises the amino acid sequence of SEQ ID NO: 6 or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 7 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0148] In an embodiment, the xyloglucanase of SEQ ID NO: 1 or the xyloglucanase of SEQ ID NO: 2, SEQ ID NO: 3 or the xyloglucanase of SEQ ID NO: 4 or the xyloglucanase of SEQ ID NO: 5 or the xyloglucanase of SEQ ID NO: 6 or the xyloglucanase of SEQ ID NO: 7 comprises a substitution, deletion and / or insertion at one or more (e.g., several) positions. In an embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the xyloglucanase of SEQ ID NO: 1 or the xyloglucanase of SEQ ID NO: 2, SEQ ID NO: 3 or the xyloglucanase of SEQ ID NO: 4 or the xyloglucanase of SEQ ID NO: 5 or the xyloglucanase of SEQ ID NO: 6 or the xyloglucanase of SEQ ID NO: 7 is no more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding domain.

[0149] Nuclease

[0150] Nuclease is a general term for enzymes that cleave the phosphodiester bonds between nucleic acid monomers. Exonucleases digest nucleic acids from the ends. Endonucleases target regions within the target molecule. Nucleases are further divided into deoxyribonucleases, which act on DNA, and ribonucleases, which act on RNA.

[0151] The present invention relates to compositions, such as cleaning compositions, comprising at least one polypeptide having DNase activity (DNase).

[0152] An example of a nuclease with DNase activity is the endonuclease from Serratia marcescens, which is commercially available under the name Benzonase® (available from Sigma-Aldrich). Thus, the compositions of the invention may include a nuclease selected from EC 3.1.30.1 or EC 3.1.30.2.

[0153] Some suitable nucleases for inclusion in the compositions of the present invention are listed below. Suitable nucleases include, but are not limited to, those listed below.

[0154] Some suitable nucleases for inclusion in the compositions of the present invention are listed below. Suitable nucleases include, but are not limited to, those listed below.

[0155] Peptides with DNase activity (DNase)

[0156] The term "DNA enzyme" refers to a polypeptide having DNA enzyme (deoxyribonuclease) activity, which catalyzes the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, thereby degrading the DNA. Exodeoxyribonucleases cleave or cut residues at the ends of the DNA backbone, whereas endo-deoxyribonucleases cleave or cut within the DNA backbone. DNA enzymes can cleave only double-stranded DNA or can cleave both double-stranded and single-stranded DNA. The term "DNA enzyme" and the expression "polypeptide having DNA enzyme activity" are used interchangeably throughout this application.

[0157] Preferably the DNase is selected from any one of the enzyme classes EC 3.1, preferably EC 3.1.21, such as, for example, EC 3.1.21.X (wherein X = 1, 2, 3, 4, 5, 6, 7, 8 or 9), or such as deoxyribonuclease I, deoxyribonuclease IV, type I site-specific deoxyribonuclease, type II site-specific deoxyribonuclease, type III site-specific deoxyribonuclease, CC-preferring endonuclease, deoxyribonuclease V, T(4) deoxyribonuclease II, T(4) deoxyribonuclease IV, or EC 3.1.22.Y (wherein Y = 1, 2, 4 or 5), such as deoxyribonuclease II, Aspergillus deoxyribonuclease K(1), cross-linking endonuclease, deoxyribonuclease X.

[0158] Preferably, the polypeptide having DNase activity is obtained from a microorganism, and the DNase is a microbial enzyme. The DNase is preferably of fungal or bacterial origin.

[0159] DNase can be obtained from Bacillus, for example, Bacillus species, such as Bacillus licheniformis, Bacillus subtilis, Bacillus species-62451, Bacillus horikoshii, Bacillus species-62451, Bacillus species-16840, Bacillus species-62668, Bacillus species-13395, Bacillus horneckiae, Bacillus species-11238, Bacillus agriculturae, Bacillus proteus, Bacillus idriensis, Bacillus species-62520, Bacillus species-16840, Bacillus species-62668, Bacillus algicola, Bacillus vietnamensis, Bacillus truncatum ... hwajinpoensis), Bacillus indica, Bacillus marisflavi, Bacillus luciferensis, and Bacillus species SA2-6.

[0160] DNase can also be obtained from any of the following: Pseudomonas sp., Vibrissea flavovirens, Setosphaeria rostrate, Endophragmiella valdina, Corynespora multilocus, Paraphoma sp. XZ1965, Monilinia fructicola, Curvularia lunata, Penicillium reticulisporum, Penicillium quercetorum, Setophaeosphaeria sp., Alternaria, Alternaria sp. XZ2545, Trichoderma reesei, Chaetomium thermophilum, Scytalidium thermophilum, Metapochonia suchlasporia), Daldinia fissa, Acremonium sp. XZ2007, Acremonium sp. XZ2414, Acremonium dichromosporum, Sarocladium sp. XZ2014, Metarhizium sp. HNA15-2, Isaria tenuipes, Scytalidium circinatum, Metarhizium lepidiotae, Thermobispora bispora, Sporormia fimetaria, Pycnidiophora cf. dispera, environmental sample D, environmental sample O, Clavicipitaceae species sp)-70249, Westerdykella sp.) AS85-2, Humicolopsis cephalosporioides, Neosartorya massa, Roussoella intermedia, Pleosporales, Phaeosphaeria, or Didymosphaeria futilis.

[0161] In an embodiment, the DNA enzyme is obtained from Bacillus proteus, particularly Bacillus proteus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 8, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 8. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 8 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0162] In an embodiment, the DNA enzyme is obtained from Aspergillus, particularly Aspergillus oryzae. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 9, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 9. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 9 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10) amino acids.

[0163] In an embodiment, the DNA enzyme is obtained from Bacillus proteus, particularly Bacillus proteus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 10, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 10. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 10 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0164] In an embodiment, the DNA enzyme is obtained from Bacillus, particularly Bacillus licheniformis. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 11, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 11. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 11 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0165] In an embodiment, the DNA enzyme is obtained from Bacillus, particularly Bacillus subtilis. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 12, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 12. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 12 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0166] In an embodiment, the DNA enzyme is obtained from Aspergillus, particularly Aspergillus oryzae. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 13, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 13. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 13 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10) amino acids.

[0167] In an embodiment, the DNA enzyme is obtained from Trichoderma, particularly Trichoderma harzianum. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 14, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 14. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 14 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0168] In an embodiment, the DNA enzyme is obtained from Bacillus terrestris, particularly Bacillus terrestris. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 15, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 15. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 15 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0169] In an embodiment, the DNA enzyme is obtained from Trichoderma, particularly Trichoderma reesei. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 16, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 16. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 16 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0170] In an embodiment, the DNA enzyme is obtained from Toxoplasma, particularly Toxoplasma swollensis. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 17, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 17. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 17 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0171] In an embodiment, the DNA enzyme is obtained from Blastomyces, particularly Blastomyces gibberellin. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 18, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 18. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 18 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0172] In an embodiment, the DNA enzyme is obtained from Gelasinospora, particularly Gelasinospora tetraspora. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 19, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 19. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 19 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0173] In an embodiment, the DNA enzyme is obtained from Streptococcus, particularly Streptococcus dysgalactiae. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 20, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 20. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 20 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0174] In an embodiment, the DNA enzyme is obtained from Thermobifida, particularly Thermobifida cellulolyticus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 21, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 21. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 21 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0175] In an embodiment, the DNA enzyme is obtained from Rasamsonia, in particular Rasamsonia composting. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 22, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 22. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 22 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0176] In an embodiment, the DNA enzyme is obtained from Sartorius spp., particularly Sartorius lactis. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 23, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the polypeptide of SEQ ID NO: 23. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 23 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0177] In an embodiment, the DNA enzyme is obtained from Aspergillus, particularly Aspergillus bisporus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 24, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 24. In one aspect, these polypeptides differ from the polypeptide comprising SEQ ID NO: 24 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0178] In an embodiment, the DNA enzyme is obtained from Aspergillus, particularly Aspergillus clavatus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 25, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 25. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 25 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0179] In an embodiment, the DNA enzyme is obtained from Metarhizium, particularly Metarhizium anisopliae. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 26, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 26. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 26 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0180] In an embodiment, the DNA enzyme is obtained from Aspergillus, particularly Aspergillus ochraceus. In an embodiment, the DNA enzyme comprises the amino acid sequence of SEQ ID NO: 27, or comprises an amino acid sequence having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the polypeptide of SEQ ID NO: 27. On the one hand, these polypeptides differ from the polypeptide comprising SEQ ID NO: 27 by up to 10 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10) amino acids.

[0181] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0182] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0183] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0184] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0185] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0186] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0187] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 8.

[0188] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0189] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0190] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0191] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0192] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0193] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0194] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 9.

[0195] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0196] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0197] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0198] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0199] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0200] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0201] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10.

[0202] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0203] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0204] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0205] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0206] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0207] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0208] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11.

[0209] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0210] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0211] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0212] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0213] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0214] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0215] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12.

[0216] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0217] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0218] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0219] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0220] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0221] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0222] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13.

[0223] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0224] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0225] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0226] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0227] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0228] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0229] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 14.

[0230] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0231] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0232] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0233] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0234] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0235] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0236] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 15.

[0237] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0238] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0239] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0240] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0241] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0242] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0243] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 16.

[0244] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0245] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0246] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0247] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0248] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0249] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0250] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 17.

[0251] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0252] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0253] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0254] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0255] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0256] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0257] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 18.

[0258] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0259] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0260] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0261] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0262] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNA enzyme having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0263] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 19.

[0264] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0265] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0266] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0267] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0268] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0269] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0270] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 20.

[0271] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0272] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0273] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0274] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0275] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0276] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0277] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 21.

[0278] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0279] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0280] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0281] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0282] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0283] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0284] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 22.

[0285] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0286] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0287] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0288] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0289] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0290] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0291] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 23.

[0292] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0293] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0294] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0295] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0296] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0297] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0298] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 24.

[0299] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0300] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0301] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0302] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0303] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0304] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0305] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 25.

[0306] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0307] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0308] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0309] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0310] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0311] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0312] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 26.

[0313] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0314] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 2, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0315] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0316] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 4, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0317] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 5, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0318] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 6, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0319] In embodiments, the cleaning composition comprises a xyloglucanase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 7, and a DNase having an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 27.

[0320] The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding domain.

[0321] Examples of conservative substitutions are within the group consisting of basic amino acids (arginine, lysine, and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, and valine), aromatic amino acids (phenylalanine, tryptophan, and tyrosine), and small amino acids (glycine, alanine, serine, threonine, and methionine). Amino acid substitutions that generally do not alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, in The Proteins, Academic Press, New York. Common substitutions are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly.

[0322] Alternatively, these amino acid changes have such a property that the physicochemical properties of the polypeptide are altered. For example, amino acid changes can improve the thermal stability of the polypeptide, change substrate specificity, change the optimal pH, etc.

[0323] Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resulting mutant molecules are tested for enzymatic activity to identify amino acid residues that are critical for the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. Mutations in putative contact site amino acids can also be combined with physical analysis of the structure, as determined by techniques such as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, to determine the active site of an enzyme or other biological interaction. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identities of essential amino acids can also be inferred from alignments with related polypeptides.

[0324] Single or multiple amino acid substitutions, deletions and / or insertions can be made and tested using known mutagenesis, recombination and / or shuffling methods, followed by relevant screening procedures, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95 / 17413; or WO 95 / 22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; U.S. Patent No. 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127).

[0325] Mutagenesis / shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules encoding active polypeptides can be recovered from host cells and rapidly sequenced using standard methods in the art. These methods allow for the rapid determination of the importance of individual amino acid residues in a polypeptide.

[0326] The polypeptide may be a hybrid polypeptide in which a region of one polypeptide is fused at the N-terminus or C-terminus of a region of another polypeptide.

[0327] The polypeptide can be a fusion polypeptide or a cleavable fusion polypeptide, in which another polypeptide is fused to the N-terminus or C-terminus of the polypeptide of the present invention. A fusion polypeptide is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention. Techniques for producing fusion polypeptides are known in the art and include ligating the coding sequences encoding the polypeptides so that they are in frame and expression of the fusion polypeptide is under the control of one or more identical promoters and terminators. Fusion polypeptides can also be constructed using intein technology, in which the fusion polypeptide is produced after translation (Cooper et al., 1993, EMBO J. [Journal of the European Molecular Biology Association] 12: 2575-2583; Dawson et al., 1994, Science [Science] 266: 776-779).

[0328] The fusion polypeptide may further comprise a cleavage site between the two polypeptides. When the fusion protein is secreted, the site is cleaved, thereby releasing the two polypeptides. Examples of cleavage sites include, but are not limited to, those disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000, J. Biotechnol. 76: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1997, Appl. Environ. Microbiol. 1995, Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6: 240-248; and Stevens, 2003, Drug Discovery World 4: 35-48.

[0329] General methods of PCR, cloning, ligation, etc. of nucleotides are well known to those skilled in the art and can be found, for example, in: "Molecular cloning: A laboratory manual", Sambrook et al. (1989), Cold Spring Harbor lab., Cold Spring Harbor, NY; Ausubel, FM et al. (eds.); "Current protocols in Molecular Biology", John Wiley and Sons, (1995); Harwood, CR and Cutting, SM (eds.); "DNA Cloning: A Practical Approach, Volumes I and II", DN Glover, ed. (1985); "Oligonucleotide Synthesis", MJ Gait, ed. (1984); "Nucleic Acid Hybridization", BD Hames and SJ Higgins, eds. (1985); “A Practical Guide To Molecular Cloning”, B. Perbal, (1984).

[0330] The concentration of enzymes (xyloglucanase and other enzymes present) in the wash liquor is typically in the range of 0.00004-100 ppm enzyme protein, such as in the range of 0.00008-100, in the range of 0.0001-100, in the range of 0.0002-100, in the range of 0.0004-100, in the range of 0.0008-100, in the range of 0.001-100 ppm enzyme protein, 0.01-100 ppm enzyme protein, preferably 0.05-50 ppm enzyme protein, more preferably 0.1-50 ppm enzyme protein, more preferably 0.1-30 ppm enzyme protein, more preferably 0.5-20 ppm enzyme protein, and most preferably 0.5-10 ppm enzyme protein.

[0331] The enzymes (xyloglucanases and other enzymes present) of the detergent compositions of the present invention can be stabilized using conventional stabilizers, such as polyols, for example propylene glycol or glycerol, sugars or sugar alcohols, lactic acid, boric acid or boric acid derivatives, for example aromatic borate esters, or phenylboronic acid derivatives, for example 4-formylphenylboronic acid, and the compositions can be formulated as described in, for example, WO 92 / 19709 and WO 92 / 19708.

[0332] The polypeptides of the present invention may also be incorporated into detergent formulations as disclosed in WO 97 / 07202, which is hereby incorporated by reference.

[0333] Liquid enzyme preparations

[0334] Enzymes (xyloglucanase, DNA enzyme and other enzymes present) can be formulated into liquid enzyme formulations, which are typically pourable compositions, although they may also have high viscosities. The physical appearance and properties of liquid enzyme formulations may vary greatly - for example, they may have different viscosities (gel-like to water-like), be colored, uncolored, transparent, fuzzy, and even have solid particles (such as in slurries and suspensions). The minimum ingredients are the enzyme (xyloglucanase, DNA enzyme and other enzymes present) and the solvent system that make it liquid.

[0335] The solvent system may comprise water, a polyol (e.g., glycerol, (mono-, di-, or tri-)propylene glycol, (mono-, di-, or tri-)ethylene glycol, a sugar alcohol (e.g., sorbitol, mannitol, erythritol, galactitol, inositol, xylitol, or ribitol), polypropylene glycol, and / or polyethylene glycol), ethanol, a sugar, and a salt. Typically, the solvent system also includes a preservative and / or other stabilizer.

[0336] Liquid enzyme formulations can be prepared by mixing a solvent system and an enzyme concentrate (or enzyme particles to obtain a slurry / suspension) of the desired purity.

[0337] In an embodiment, the liquid enzyme composition comprises:

[0338] (a) at least 0.01% w / w active enzyme protein,

[0339] (b) at least 0.5% w / w polyol,

[0340] (c) water, and

[0341] (d) optionally a preservative.

[0342] Conventional stabilizers can be used to stabilize the enzymes (xyloglucanase, DNA enzyme, and other enzymes present) in the liquid composition of the present invention. Examples of stabilizers include, but are not limited to, sugars such as glucose, fructose, sucrose, or trehalose; polyols (such as glycerol, propylene glycol); salts added to increase ionic strength; divalent cations (e.g., Ca 2+ or Mg 2+ ); as well as enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP). Selecting the optimal pH for the formulation can be very important for enzyme stability. The optimal pH depends on the specific enzyme but is typically in the pH range of 4-9. In some cases, surfactants, such as nonionic surfactants (e.g., alcohol ethoxylates), can improve the physical stability of the enzyme formulation.

[0343] One embodiment of the present invention relates to a composition comprising xyloglucanase and DNase, wherein the composition further comprises:

[0344] (i) a polyol, preferably selected from glycerol, (mono-, di- or tri-)propylene glycol, (mono-, di- or tri-)ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol and ribitol;

[0345] (ii) optionally further enzymes, preferably selected from proteases, amylases or lipases, DNases; mannanases;

[0346] (iii) optionally a surfactant, preferably selected from anionic and nonionic surfactants,

[0347] (iv) optionally a salt, a divalent cation, a polymer, or an enzyme inhibitor;

[0348] (v) optionally having a pH in the range of pH 4-9; and

[0349] (vi) Water.

[0350] Slurries or dispersions of the enzyme are typically prepared by dispersing small particles of the enzyme (e.g., spray-dried particles) in a liquid medium (e.g., a liquid nonionic surfactant or liquid polyethylene glycol) in which the enzyme is slightly soluble. Powders can also be added to aqueous systems in amounts so that not all of the enzyme goes into solution (above the solubility limit). Another form is a crystalline suspension, which can also be an aqueous liquid (see, for example, WO 2019 / 002356). Another method for preparing such a dispersant is by preparing a water-in-oil emulsion in which the enzyme is in the aqueous phase and evaporating the water from the droplets. Such slurries / suspensions can be physically stabilized (to reduce or avoid sedimentation) by adding rheology modifiers (e.g., fumed silica or xanthan gum), typically to achieve shear-thinning rheology.

[0351] Granzyme preparations

[0352] Enzymes (xyloglucanase and other enzymes present) can also be formulated into solid / granular enzyme formulations. Dust-free granules can be produced, for example, as disclosed in US 4,106,991 and US 4,661,452, and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) with an average molecular weight of 1000 to 20,000; ethoxylated nonylphenols with 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, wherein the alcohol contains 12 to 20 carbon atoms and wherein there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and monoglycerides, diglycerides, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for use by fluidized bed technology are given in GB 1483591.

[0353] Xyloglucanase can be formulated as granule, for example, is formulated as co-granule or the benefit agent (for example MnTACN or other bleaching components) in conjunction with one or more enzymes.The example of such other enzyme comprises lipase, xyloglucanase, perhydrolase, peroxidase, lipoxygenase, laccase, hemicellulase, protease, nursing cellulase, cellulase, cellobiose dehydrogenase, xylanase, phospholipase, esterase, cutinase, pectinase, mannanase, pectin lyase, keratinase, reductase, oxidase, phenoloxidase, ligninase, pullulanase, tannase, pentosanase, lichenase, glucanase, arabinosidase, hyaluronidase, chondroitinase, amylase, DNA enzyme, and composition thereof.Then, every kind of enzyme will be present in multiple granules, and these granules guarantee that the distribution of enzyme in detergent is more even.This has also reduced the physical isolation of the different enzymes that cause owing to different granularities. A process for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0354] Embodiments of the present invention relate to enzyme granules / particles comprising xyloglucanase. The granules are composed of a core and optionally one or more coatings (outer layers) surrounding the core. Typically, the granules have a particle size (measured as an equivalent spherical diameter (average particle size based on volume)) of 20-2000 μm, particularly 50-1500 μm, 100-1500 μm, or 250-1200 μm.

[0355] The core can comprise other material such as filler, fibrous material (cellulose or synthetic fiber), stabilizing agent, solubilizing agent, suspending agent, viscosity modifier, light sphere, plasticizer, salt, lubricant and aromatic.This core can comprise binding agent, such as synthetic polymer, wax, fat or carbohydrate.This core typically can comprise salt, reducing agent, antioxidant, peroxide decomposition catalyst and / or acidic buffer component of multivalent cation as uniform blend.This core can be made up of inert particle, and wherein enzyme is adsorbed within this inert particle, perhaps is applied (for example by fluidized bed coating) on the surface of this inert particle.The diameter of this core can be 20-2000 μ m, particularly 50-1500 μ m, 100-1500 μ m or 250-1200 μ m. The core can be prepared by granulating a blend of ingredients, for example, by methods including granulation techniques such as crystallization, precipitation, pan coating, fluidized bed coating, fluidized bed agglomeration, rotary atomization, extrusion, prilling, spheronization, particle size reduction, drum granulation, and / or high shear granulation. Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by CE Capes; Vol. 1; 1980; Elsevier. These methods are well known in the art and are also described in International Patent Application WO 2015 / 028567, pp. 3-5, which is incorporated by reference.

[0356] The core of the enzyme granule / particle may be surrounded by at least one coating, for example, to improve storage stability, to reduce dust formation during handling or to color the granule. Optional one or more coatings may include a salt coating or other suitable coating materials, such as polyethylene glycol (PEG), methylhydroxy-propylcellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93 / 07263 and WO 97 / 23606.

[0357] Such coatings are well known in the art and have been described earlier in, for example, WO 00 / 01793, WO 2001 / 025412 and WO 2015 / 028567, which are incorporated by reference.

[0358] In one aspect, the present invention provides a particle comprising:

[0359] (a) a core comprising a xyloglucanase according to the invention; and

[0360] (b) optionally a (salt) coating consisting of one or more layers surrounding the core.

[0361] Another aspect of the present invention relates to a stratified particle comprising:

[0362] (a) (non-enzyme) core;

[0363] (b) a coating surrounding the core, wherein the coating comprises a xyloglucanase; and

[0364] (c) optionally a (salt) coating consisting of one or more layers surrounding the enzyme-containing coating.

[0365] Encapsulated enzyme formulations

[0366] The enzymes (xyloglucanases and other enzymes present) can also be formulated as encapsulated enzyme formulations ("encapsulates"). This is particularly useful for isolating the enzymes from other ingredients when adding them to, for example, (liquid) cleaning compositions such as detergent compositions described below.

[0367] Physical separation can be used to resolve incompatibilities between one or more enzymes and other components. Incompatibility can arise if the other components react with the enzyme or if the other components are substrates for the enzyme. Other enzymes can be substrates for proteases.

[0368] The enzyme can be encapsulated in a matrix, preferably a water-soluble or water-dispersible matrix (e.g., water-soluble polymer particles), such as described in WO 2016 / 023685. An example of a water-soluble polymer matrix is a matrix composition comprising polyvinyl alcohol. Such compositions are also used to encapsulate detergent compositions in unit dosage form.

[0369] Enzymes may also be encapsulated in core-shell microcapsules, for example as described in WO 2015 / 144784, or in IP.com disclosure IPCOM000239419D.

[0370] Such core-shell capsules can be prepared using a variety of techniques known in the art, for example, using interfacial polymerization of water-in-oil or oil-in-water emulsions, where the polymer crosslinks at the surface of the droplets in the emulsion (the interface between water and oil), thereby forming a wall / membrane around each droplet / capsule.

[0371] Preparation of enzymes in co-granules

[0372] Enzymes (xyloglucanase, DNAse, and other enzymes present) can be formulated as granules, for example, as co-granules combining one or more enzymes. Each enzyme is then present in multiple granules, which ensure a more uniform distribution of the enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0373] Another example of formulation of enzymes by using co-granules is disclosed in WO 2013 / 188331, which relates to a detergent composition comprising: (a) a multi-enzyme co-granule; (b) less than 10 wt% zeolite (on an anhydrous basis); and (c) less than 10 wt% phosphate (on an anhydrous basis), wherein the enzyme co-granule comprises from 10 wt% to 98 wt% of a moisture sink component, and the composition further comprises from 20 wt% to 80 wt% of a detergent moisture sink component.

[0374] WO 2013 / 188331 also relates to a method for treating and / or cleaning a surface, preferably a textile surface, comprising the steps of: (i) contacting the surface in an aqueous wash liquor with a detergent composition as claimed and described herein, (ii) rinsing and / or drying the surface.

[0375] The multi-enzyme co-granule can comprise a xyloglucanase and (a) one or more enzymes selected from the group consisting of a lipase, a cellulase, a xyloglucanase, a perhydrolase, a peroxidase, a lipoxygenase, a laccase, and mixtures thereof; and (b) one or more enzymes selected from the group consisting of a hemicellulase, a protease, a care cellulase, a cellulase, a cellobiose dehydrogenase, a xylanase, a phospholipase, an esterase, a cutinase, a pectinase, a mannanase, a pectin lyase, a keratinase, a reductase, an oxidase, a phenoloxidase, a ligninase, a pullulanase, a tannase, a pentosanase, a lichenase, a glucanase, an arabinosidase, a hyaluronidase, a chondroitinase, an amylase, a DNase, and mixtures thereof.

[0376] Purification of enzymes from formulations

[0377] The enzymes used in the above-mentioned enzyme preparations (xyloglucanase, DNA enzyme and other enzymes present) can be purified to any desired purity. This includes high-level purification, for example, by using a crystallization method, but also includes no purification or low-level purification, for example, by using a crude fermentation broth, as described in WO 2001 / 025411 or WO 2009 / 152176.

[0378] microorganism

[0379] Enzyme formulations, as well as the detergent formulations described below, may contain one or more microorganisms or microorganisms. Generally, any one or more microorganisms may be used in any suitable amount / concentration in the enzyme / detergent formulation. Microorganisms may be used as the sole biologically active ingredient, but they may also be used in combination with one or more enzymes described above.

[0380] The purpose of adding one or more microorganisms may be to reduce malodors, for example as described in WO 2012 / 112718. Other purposes may include the in situ production of desirable biocompounds, or to inoculate / occupy a site with one or more microorganisms to competitively prevent other undesirable microbial forms from occupying the same site (competitive exclusion).

[0381] The term "microorganism" generally refers to a small organism visible through a microscope. Microorganisms typically exist as single cells or cell colonies. Some microorganisms may be multicellular. Microorganisms include prokaryotes (e.g., bacteria and archaea) and eukaryotes (e.g., some fungi, algae, protozoa). Examples of bacteria can be gram-positive bacteria or gram-negative bacteria. Example forms of bacteria include vegetative cells and spores. Examples of fungi can be yeasts, molds, and mushrooms. Example forms of fungi include hyphae and spores. For purposes of this document, viruses may be considered microorganisms.

[0382] Microorganisms can be recombinant or non-recombinant. In some instances, microorganisms can produce various substances (e.g., enzymes) that can be included in detergent compositions. Extracts or fractions of extracts from microorganisms can be used in detergents. Culture media in which microorganisms are cultured, or extracts or isolates from these cultures, can also be used in detergents. In some specific instances of microorganisms, substances produced by the microorganisms, their extracts, cultures, and fractions can be specifically excluded from the detergent. In some instances, the microorganisms or substances produced or extracted by the microorganisms can activate, enhance, preserve, or prolong the activity of the detergent or the activity of the components contained in the detergent.

[0383] Typically, methods known in the art can be used to cultivate microorganisms. The microorganisms can then be processed or prepared in various ways. In some instances, the microorganism can be dry (e.g., freeze-dried). In some instances, the microorganism can be encapsulated (e.g., spray-dried). Many other processes or preparations are also possible. These processes or preparations are conducive to retaining microbial activity over time and / or in the presence of detergent components. However, in some instances, the microorganisms in the detergent may be non-viable. The processed / prepared microorganisms can be added to the detergent before use or when using the detergent.

[0384] In one embodiment, the microorganism is a Bacillus species, such as at least one Bacillus species selected from the group consisting of Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus atrophaeus, Bacillus pumilus, Bacillus megaterium, or a combination thereof. In a preferred embodiment, the aforementioned Bacillus species are all in spore form, which significantly improves storage stability.

[0385] Detergent composition

[0386] In one embodiment, the present invention relates to a detergent composition comprising a combination of a xyloglucanase and one or more other cleaning composition components. In one embodiment, the detergent composition comprises a combination of a polypeptide with xyloglucanase activity and a polypeptide with DNase activity, the polypeptide with xyloglucanase activity having at least 60% identity, such as 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% or even 100% identity to the amino acid sequence listed in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6 and SEQ ID NO: 7. Preferably, the polypeptide with DNA enzymatic activity has at least 60% identity to the amino acid sequence listed in SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, such as 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% or even 100% identity. In one embodiment, the detergent composition is in solid form. In another embodiment, the detergent composition is in liquid or gel form. In another embodiment, the detergent composition is in strip form. In one embodiment, the detergent can be wrapped in a water-soluble PVOH film. The selection of other components is within the capabilities of technicians and includes conventional ingredients, including the exemplary non-limiting components set forth below.

[0387] Liquid detergent compositions

[0388] The liquid detergent composition may comprise the microcapsules of the present invention and thus form part of any detergent composition in any form, such as liquid and powder detergents, as well as soaps and detergent bars.

[0389] In one embodiment, the present invention is directed to liquid detergent compositions comprising microcapsules (as described above) in combination with one or more additional cleaning composition components.

[0390] Microcapsules (as described above) may be added to the liquid detergent composition in an amount corresponding to from 0.0001% to 5% (w / w) active enzyme protein (AEP); preferably from 0.001% to 5%, more preferably from 0.005% to 5%, more preferably from 0.005% to 4%, more preferably from 0.005% to 3%, more preferably from 0.005% to 2%, even more preferably from 0.01% to 2%, and most preferably from 0.01% to 1% (w / w) active enzyme protein.

[0391] Liquid detergent compositions have a physical form; they are not solid (or gas). They can be pourable liquids, pastes, pourable gels, or non-pourable gels. They can be isotropic or structural, preferably isotropic. They can be formulations for washing in automatic washing machines or for hand washing. They can also be personal care products, such as shampoo, toothpaste, or hand soap.

[0392] The liquid detergent composition can be aqueous, typically contains by weight at least 20% and up to 95% water, for example up to 70% water, up to 50% water, up to 40% water, up to 30% water or up to 20% water. The liquid of other types including but not limited to alkanol, amine, glycol, ether and polyvalent alcohol can be included in the aqueous liquid detergent. The aqueous liquid detergent can contain the organic solvent from 0%-30%. The liquid detergent can even be non-aqueous, and wherein water-content is lower than 10%, preferably lower than 5%.

[0393] The detergent ingredients can be physically separated from each other by the chambers in the water-soluble bag. Therefore, bad storage interactions between the components can be avoided. In the washing solution, the different dissolution curves of each chamber can also cause the delayed dissolution of the selected components.

[0394] Detergent compositions can be in the form of unit dose products. Unit dose products are single doses packaged in a non-reusable container. They are increasingly used in laundry detergents. Detergent unit dose products are packages (e.g., in a bag made of a water-soluble film) containing the amount of detergent needed for a single wash.

[0395] The bag can have any form, shape, and material suitable for holding the composition, for example, to prevent the composition from being released from the bag prior to contact with water. The bag is made of a water-soluble film that encloses an internal volume. The internal volume can be divided into the chambers of the bag. The preferred film is a polymeric material, preferably a polymer that forms a film or sheet. Preferred polymers, copolymers, or derivatives thereof are selected polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropyl methylcellulose, maltodextrin, polymethacrylates, and most preferably polyvinyl alcohol copolymers and hydroxypropyl methylcellulose (HPMC). Preferably, the level of polymer in the film, such as PVA, is at least about 60%. The preferred average molecular weight will typically be from about 20,000 to about 150,000. The film can also be a blend composition comprising a hydrolytically degradable and water-soluble polymer blend, such as polylactic acid and polyvinyl alcohol (known under trade reference number M8630, such as sold by Chris Craft Industrial Products, Gary, Indiana, USA) plus a plasticizer such as glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain a solid laundry cleaning composition or partial components and / or a liquid cleaning composition or partial components separated by a water-soluble film. The composition can have a compartment for the liquid component that is distinct from the compartment containing the solid component (see, for example, US 2009 / 0011970).

[0396] The selection of detergent components may include (for textile care) considerations of the type of textile to be cleaned, the type and / or degree of soiling, the temperature at which cleaning is to be performed, and the formulation of the detergent product. Although the components mentioned below are categorized under general headings according to specific functionality, this is not to be construed as limiting, as a component may contain additional functionality, as will be understood by the skilled artisan.

[0397] The selection of additional components is within the purview of the skilled artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.

[0398] surfactants

[0399] Cleaning compositions can comprise one or more surfactants, which can be anionic and / or cationic and / or nonionic and / or semipolar and / or zwitterionic, or a mixture thereof. In a specific embodiment, the detergent composition comprises a surfactant system (comprising more than one surfactant), for example a mixture of one or more nonionic surfactants and one or more anionic surfactants. In one embodiment, the detergent comprises at least one anionic surfactant and at least one nonionic surfactant, and the weight ratio of the anionic surfactant to the nonionic surfactant can be 20: 1 to 1: 20. In one embodiment, the amount of the anionic surfactant is higher than the amount of the nonionic surfactant, for example, the weight ratio of the anionic surfactant to the nonionic surfactant can be 10: 1 to 1.1: 1 or 5: 1 to 1.5: 1. The amount of the anionic surfactant and the nonionic surfactant can also be equal and the weight ratio is 1: 1. In one embodiment, the amount of the nonionic surfactant is higher than the amount of the anionic surfactant, and the weight ratio can be 1: 10 to 1: 1.1. The weight ratio of anionic surfactant and nonionic surfactant is preferably 10: 1 to 1: 10, as 5: 1 to 1: 5, or 5: 1 to 1: 1.2.Preferably, the weight fraction of nonionic surfactant and anionic surfactant is 0 to 0.5 or 0 to 0.2, so if weight fraction is 0, then can exist or not exist nonionic surfactant, but if there is nonionic surfactant, then the weight fraction of nonionic surfactant is preferably anionic surfactant and nonionic surfactant total weight at the most 50% or at the most 20%.Light-duty detergent comprises the nonionic surfactant more than anionic surfactant usually, and wherein the fraction of nonionic surfactant and anionic surfactant is preferably 0.5 to 0.9. The gross weight of one or more surfactants typically with by weight approximately 0.1% to approximately 60%, for example approximately 1% to approximately 40%, or approximately 3% to approximately 20%, or approximately 3% to approximately 10% level exists.Select these one or more surfactants based on desired cleaning application, and these one or more surfactants can comprise any one or more conventional surfactants as known in the art. When included therein, the detergent will typically contain from about 1% to about 40% by weight anionic surfactant, for example from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% anionic surfactant.Non-limiting examples of anionic surfactants include sulfates and sulfonates, typically available as sodium or potassium salts, or monoethanolamine (MEA, 2-aminoethan-1-ol) or triethanolamine (TEA, 2,2',2''-nitrilotriethane-1-ol); in particular linear alkylbenzenesulfonates (LAS), isomers of LAS, such as branched alkylbenzenesulfonates (BABS) and phenylalkanesulfonates; olefinsulfonates, in particular alpha-olefinsulfonates (AOS); alkyl sulfates (AS), in particular fatty alcohol sulfates (FAS), i.e., primary alcohol sulfates ( Examples of surfactants include paraffin sulfonates (PS), such as lauryl sulfate (SLS); alcohol ether sulfates (AES, AEOS, or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates); paraffin sulfonates (PS), including alkane-1-sulfonates and secondary alkane sulfonates (SAS); ester sulfonates, including sulfonated fatty acid glycerides and α-sulfo fatty acid methyl esters (α-SFMe, SES, or MES); alkyl or alkenyl succinic acids, such as dodecenyl / tetradecenyl succinic acid (DTSA); diesters and monoesters of sulfosuccinic acid; and fatty acid derivatives of amino acids. Anionic surfactants can be added as acids, salts, or ethanolamine derivatives.

[0400] When included therein, the detergent will typically contain from about 0.1% to about 40% by weight of a cationic surfactant, for example from about 0.5% to about 30%, particularly from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyl dimethylethanol quaternary ammonium (ADMEAQ), cetyl trimethyl ammonium bromide (CTAB), dimethyl distearylammonium chloride (DSDMAC), as well as alkyl benzyl dimethyl ammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quaternary ammonium, and combinations thereof.

[0401] When included therein, the detergent will typically contain from about 0.2% to about 40% by weight of nonionic surfactant, for example from about 0.5% to about 30%, especially from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO) (e.g., the AEO series such as AEO-7), alcohol propoxylates (particularly propoxylated fatty alcohols (PFA), ethoxylated alcohols, and propoxylated alcohols), alkoxylated fatty acid alkyl esters (such as ethoxylated and / or propoxylated fatty acid alkyl esters (particularly ethoxymethyl ester, MEE)), alkyl polyglycosides (APGs), alkoxylated amines, fatty acid monoethanolamide (FAM), fatty acid diethanolamide (FADA), ethoxylated fatty acid monoethanolamide (EFAM), propoxylated fatty acid monoethanolamide (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamide (GA), or fatty acid glucamide (FAGA)), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.

[0402] When included therein, the detergent will typically contain from about 0.01% to about 10% by weight of a semi-polar surfactant. Non-limiting examples of semi-polar surfactants include amine oxides (AOs), such as alkyldimethylamine oxides, particularly N-(cocoylalkyl)-N,N-dimethylamine oxide and N-(tallowalkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof.

[0403] When included therein, the detergent will typically contain from about 0.01% to about 10% by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines, such as alkyl dimethyl betaines, sulfobetaines, and combinations thereof.

[0404] Additional bio-based surfactants may be used, for example where the surfactant is a sugar-based non-ionic surfactant, which may be hexyl-β-D-maltopyranoside, thiomaltopyranoside or cyclic maltopyranoside, such as described in EP 2 516 606 B1. Other biosurfactants may include rhamnolipids and sophorolipids.

[0405] hydrotrope

[0406] Hydrotropes are compounds that dissolve hydrophobic compounds in aqueous solutions (or conversely, polar substances in a nonpolar environment). Typically, hydrotropes possess both hydrophilic and hydrophobic properties (so-called amphiphilic properties, as known from surfactants); however, the molecular structure of hydrotropes is generally not conducive to spontaneous self-aggregation, as reviewed, for example, by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not exhibit a critical concentration above which self-aggregation occurs, as observed for surfactants, and lipids form micelles, lamellae, or other well-defined mesophases. Instead, many hydrotropes exhibit a continuous type of aggregation process, in which the size of aggregates increases with increasing concentration. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances with both polar and nonpolar characteristics, including mixtures of water, oils, surfactants, and polymers. Hydrotropes are routinely used in various industries ranging from pharmaceuticals, personal care, food to technical applications. The use of hydrotropes in detergent compositions allows, for example, more concentrated surfactant formulations (such as in the process of compacting liquid detergents by removing water) without causing undesirable phenomena such as phase separation or high viscosity.

[0407] The detergent may contain 0% to 10% by weight, such as 0% to 5% by weight, such as from about 0.5% to about 5%, or from about 3% to about 5% of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluenesulfonate (STS), sodium xylenesulfonate (SXS), sodium cumenesulfonate (SCS), sodium cymenesulfonate, amine oxides, alcohols and polyethylene glycol ethers, sodium hydroxynaphthoate, sodium hydroxynaphthalenesulfonate, sodium ethylhexylsulfonate, and combinations thereof.

[0408] Builders and co-builders

[0409] The detergent composition can contain about 0% to 65% (e.g., about 5% to about 50%) by weight of a detergent builder or co-builder, or a mixture thereof. The builder and / or co-builder can be, in particular, a chelating agent that forms a water-soluble complex with Ca and Mg. Any builder and / or co-builder known in the art for use in cleaning detergents can be utilized.

[0410] Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Clariant), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-iminodiethanol-1-ol), triethanolamine (TEA, also known as 2,2',2''-nitrilotriethanol-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

[0411] The detergent composition can also contain by weight from about 0%-50%, such as about 5% to about 30% detergent co-builder. The detergent composition can include a co-builder alone or in combination with a builder (e.g., zeolite builder). Non-limiting examples of co-builders include or copolymers thereof, such as poly(acrylic acid) (PAA) or co-poly(acrylic acid / maleic acid) (PAA / PMA). According to the present invention, these components can be included at a level lower than that in currently available detergent compositions. Further non-limiting examples include citrate, chelating agents (e.g., aminocarboxylates, aminopolycarboxylates, and phosphonates), and alkyl succinic acid or alkenyl succinic acid. Further specific examples include 2,2',2''-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid) (HEDP), ethylenediaminetetramethylenetetra(phosphonic acid) (EDTMPA), diethylenetriaminepentamethylene(phosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (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-(2-hydroxyethyl)ethylenediamine-N,N',N''-triacetic acid (HEDTA), diethanolglycine (DEG), aminotrimethylene (phosphonic acid) (ATMP), and combinations and salts thereof. Additional exemplary builders and / or co-builders are described, for example, in WO09 / 102854, US 5977053 in.

[0412] bleaching system

[0413] The cleaning composition may contain 0% to 50% (e.g., 1% to 40%, such as 1% to 30%, such as from about 1% to about 20%) of a bleaching system by weight. Any oxygen-based bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include a hydrogen peroxide source; a peracid and a peracid source (bleach activator); and a bleach catalyst or accelerator.

[0414] Hydrogen peroxide source:

[0415] Suitable sources of hydrogen peroxide are inorganic persalts, including the alkali metal salts such as sodium percarbonate and sodium perborate (usually monohydrate or tetrahydrate), and hydrogen peroxide-urea (1 / 1).

[0416] Peracid sources:

[0417] The peracid may be (a) incorporated directly as a preformed peracid, 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 enzyme and a suitable substrate for the latter (e.g. an ester).

[0418] a) Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids (such as perbenzoic acid) and ring-substituted derivatives thereof, peroxy-α-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, ε-phthalimidoperoxycaproic acid [phthalimidoperoxycaproic acid (PAP)], and o-carboxybenzoylaminoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids, such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassyl acid, 2-decyldiperoxysuccinic acid, as well as diperoxyphthalic acid, -isophthalic acid, and -terephthalic acid; perimidic acid; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of said compounds. It will be appreciated that in some cases the peracids mentioned may best be added as suitable salts, such as alkali metal salts (e.g. Oxone®) or alkaline earth metal salts.

[0419] b) Suitable bleach activators include those belonging to the classes of esters, amides, imides, nitriles, or anhydrides, and, where applicable, their salts. Suitable examples include tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), sodium 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO 98 / 17767. A particular family of bleach activators of interest is disclosed in EP 624154, and acetyl triethyl citrate (ATC) is particularly preferred within this family. ATC or short-chain triglycerides (such as triacetin) have the advantage that they are environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin have good hydrolytic stability in the product upon storage and are effective bleach activators. Finally, ATC is multifunctional in that the citrate released in the perhydrolysis reaction can function as a builder.

[0420] Bleach catalysts and accelerators

[0421] The bleaching system may also include a bleaching catalyst or accelerator.

[0422] Some non-limiting examples of bleaching catalysts that can be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese collagen, cobalt-amine catalysts, and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Me4-TACN), especially Me3-TACN, such as the binuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2, and [2,2',2''-nitrilotri(ethane-1,2-diylazanylidene-κN-methylidene)triphenol-κ3O]manganese(III). These bleaching catalysts can also be other metal compounds, such as iron or cobalt complexes.

[0423] In some embodiments where a peracid source is included, an organic bleach catalyst or bleach booster having one of the following formulae may be used:

[0424]

[0425] (iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or a straight chain alkyl group containing from 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or a straight chain alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.

[0426] Further exemplary bleaching systems are described in, for example, WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259, EP 1867708 (Vitamin K) and WO 2007 / 087242. Suitable photobleaches may, for example, be sulfonated zinc or aluminum phthalocyanines.

[0427] Polymers and dispersants

[0428] In some embodiments, the detergent composition can contain 0%-10% by weight, such as 0.5%-5%, 2%-5%, 0.5%-2% or 0.2%-1% polymer. Any polymer used for using in detergents as known in the art can be utilized. Polymer can be used as a co-builder as mentioned above to work, or anti-redeposition, fiber protection, dirt release, dye transfer inhibition, grease cleaning and / or defoaming properties can be provided. Some polymers can have more than one above-mentioned character and / or more than one motif mentioned below. Exemplary polymers include poly(vinyl alcohol) (PVA), poly(vinyl pyrrolidone) (PVP), poly(ethylene glycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethylene imine), carboxymethyl inulin (CMI), and silicones, copolymers of terephthalic acid and oligoethylene glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethylene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO), and polyvinylpyrrolidone-vinylimidazole (PVPVI). Further exemplary polymers include polyethylene oxide and polypropylene oxide (PEO-PPO), diquaternary ammonium salts of ethoxysulfate, styrene / acrylic acid copolymers, and fragrance capsules. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the above-mentioned polymers are also contemplated.

[0429] The detergent compositions of the present invention may also contain a dispersant. In particular, powdered detergents may contain a dispersant. Suitable water-soluble organic materials include homopolymeric or copolymeric acids or salts thereof, wherein the polycarboxylic acid comprises at least two carboxyl groups separated from each other by no more than two carbon atoms. Suitable dispersants are described, for example, in Powdered Detergents, Surfactant science series, Vol. 71, Marcel Dekker, Inc.

[0430] However, according to the present invention, certain of the above polymers (i.e., polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose and / or combinations thereof) may be included at lower levels than in currently available detergent compositions, or even more preferably, may be excluded entirely.

[0431] fabric toner

[0432] The detergent compositions of the present invention may also include fabric hueing agents, such as dyes or pigments, which, when formulated in the detergent compositions, can be deposited on the fabric when the fabric is in contact with a wash solution comprising the detergent compositions and which, therefore, changes the color of the fabric by absorption / reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, when fabric hueing agents absorb at least a portion of the visible spectrum, they change the color of the surface. 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 the following dyes classified as falling within the Color Index (CI): direct blue, direct red, direct violet, acid blue, acid red, acid violet, basic blue, basic violet and basic red, or mixtures thereof, such as described in WO 2005 / 03274, WO 2005 / 03275, WO 2005 / 03276 and EP 1876226 (incorporated herein by reference). The detergent composition preferably comprises from about 0.00003 wt % to about 0.2 wt %, from about 0.00008 wt % to about 0.05 wt %, or even from about 0.0001 wt % to about 0.04 wt % of the fabric hueing agent. The composition can comprise from 0.0001 wt % to 0.2 wt % of the fabric hueing agent, which can be particularly preferred when the composition is in the form of a unit dose bag. Suitable hueing agents are also disclosed in, for example, WO 2007 / 087257 and WO 2007 / 087243.

[0433] Additional enzymes

[0434] The detergent additive together with the detergent composition may comprise one or more [additional] enzymes, such as proteases, lipases, cutinases, amylases, carbohydrases, DNases, pectinases, mannanases, arabinases, galactanases, xylanases, oxidases, such as laccases, and / or peroxidases.

[0435] Generally, the properties of the enzyme(s) selected should be compatible with the chosen detergent (ie, pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in an effective amount.

[0436] Nuclease

[0437] Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases), which are any enzymes that catalyze the hydrolytic cleavage of phosphodiester bonds in the DNA or RNA backbone, thereby degrading DNA and RNA, respectively. There are two main classifications based on the site of activity. Exonucleases digest nucleic acids from the ends. Endonucleases act on regions within the target molecule. The nuclease is preferably a DNase, which is preferably obtainable from a microorganism, preferably a fungus or a bacterium. In particular, DNases obtainable from species of the genus Bacillus are preferred; in particular, DNases obtainable from Bacillus alginate, Bacillus proteus, Bacillus subtilis, or Bacillus licheniformis are preferred. Examples of these DNases are described in WO 2011 / 098579, WO 2014 / 087011, and WO 2017 / 060475. Also particularly preferred are DNases obtainable from species of the genus Aspergillus; in particular, DNases obtainable from Aspergillus oryzae, such as the DNase described in WO 2015 / 155350.

[0438] Cellulase

[0439] Suitable cellulases include those of bacterial or fungal origin. Include chemically modified mutants or protein engineered mutants. Suitable cellulases include cellulases from Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, such as those disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757 and WO 89 / 09259, produced by Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum.

[0440] Suitable cellulases include alkaline cellulases or neutral cellulases, which provide or maintain whiteness and prevent redeposition or have color care benefits. Examples of such cellulases are the cellulases described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are those cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307 and WO 99 / 001544.

[0441] Other cellulases are endo-β-1,4-glucanases having a sequence that is at least 97% identical to the amino acid sequence from position 1 to position 773 of SEQ ID NO: 2 of WO 2002 / 099091, or Family 44 xyloglucanases having a sequence that is at least 60% identical to positions 40-559 of SEQ ID NO: 2 of WO 2001 / 062903.

[0442] 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-500(B)™ (Kao Corporation).

[0443] Mannanase

[0444] Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are also included. The mannanase may be an alkaline mannanase from family 5 or 26. It may be a wild-type from the genus Bacillus or Humicola, particularly from B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or Humicola insolens. Suitable mannanases are described in WO 1999 / 064619. A commercially available mannanase is Mannaway (Novozymes).

[0445] Protease

[0446] Suitable proteases can be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants. The protease can be an alkaline protease, such as a serine protease, or a metalloprotease. The serine protease can be, for example, of the S1 family (such as trypsin) or the S8 family (such as subtilisin). The metalloprotease can be, for example, a thermolysin, such as a thermolysin from the M4 family, or another metalloprotease, such as those from the M5, M7, or M8 families.

[0447] The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with the substrate. Subtilases can be divided into six subclasses: the subtilisin family, the thermophilic protease family, the proteinase K family, the lanthionine antibiotic peptidase family, the Kexin family, and the pyrolysin family.

[0448] Although proteases suitable for detergent use can be obtained from a variety of organisms (including fungi such as Aspergillus), detergent proteases have generally been obtained from bacteria (particularly from the genus Bacillus). Examples of Bacillus species from which subtilases are derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus, and Bacillus gibsonii. Particular subtilisins include subtilisinlentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN', subtilisin 309, subtilisin 147, and subtilisin 168, as well as, for example, protease PD138 (described in WO 93 / 18140). Other useful proteases are those described, for example, in WO 01 / 16285 and WO 02 / 16547.

[0449] Examples of trypsin-like proteases include the Fusarium protease (described in WO 94 / 25583 and WO 2005 / 040372), and the chymotrypsin derived from Cellumonas (described in WO 2005 / 052161 and WO 2005 / 052146).

[0450] Examples of metalloproteases include neutral metalloproteases described in WO 2007 / 044993 (such as those derived from Bacillus amyloliquefaciens), and metalloproteases described, for example, in WO 2015 / 158723 and WO 2016 / 075078.

[0451] Examples of useful proteases are the protease variants described in WO 89 / 06279, WO 92 / 19729, WO 96 / 34946, WO 98 / 20115, WO 98 / 20116, WO 99 / 11768, WO 01 / 44452, WO 03 / 006602, WO 2004 / 003186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2014 / 207227, WO 2016 / 087617 and WO 2016 / 174234. Preferred protease variants may, for example, comprise one or more 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, P1 27Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Q200L, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256DT268A, and R269H, where the position numbers correspond to WO 2016 / 001449. Protease variants having one or more of these mutations are preferably variants of the protease Bacillus lentus (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016 / 001449 or variants of the protease Bacillus amyloliquefaciens (BPN') shown in SEQ ID NO: 2 of WO 2016 / 001449. Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2 of WO 2016 / 001449.

[0452] Another protease of interest is the alkaline protease from Bacillus lentus DSM 5483 (as described, for example, in WO 91 / 02792) and variants thereof (these variants are described, for example, in WO 92 / 21760, WO 95 / 23221, EP 1921147, EP 1921148 and WO 2016 / 096711).

[0453] Alternatively, the protease may be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004 / 067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 111, 171, 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004 / 067737, wherein the protease variant has at least 75% but less than 100% sequence identity to SEQ ID NO: 1 of WO 2004 / 067737. TY145 variants of interest are described, for example, in WO 2015 / 014790, WO 2015 / 014803, WO 2015 / 014804, WO 2016 / 097350, WO 2016 / 097352, WO 2016 / 097357 and WO 2016 / 097354.

[0454] Examples of preferred proteases include:

[0455] (a) a variant of SEQ ID NO: 1 of WO 2016 / 001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D and L262E, such as a variant having the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261W and L262E, or having the substitutions S9E, N43R, N76D, N185E, S188E, Q191N, A194P, Q206L, Y209W, S259D and L262E, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0456] (b) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the mutation S99SE, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0457] (c) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the mutation S99AD, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0458] (d) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions Y167A+R170S+A194P, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0459] (e) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+V68A+N218D+Q245R, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0460] (f) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0461] (g) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S99D+S101R / E+S103A+V104I+G160S; for example, a variant of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S3T+V4I+S99D+S101E+S103A+V104I+G160S+V205I, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0462] (h) a variant of the polypeptide of SEQ ID NO: 2 of WO 2016 / 001449 having the substitutions S24G+S53G+S78N+S101N+G128A / S+Y217Q, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0463] (i) the polypeptide disclosed in GENESEQP with accession number BER84782, which corresponds to SEQ ID NO: 302 in WO 2017 / 210295;

[0464] (j) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S99D+S101E+S103A+V104I+S156D+G160S+L262E, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0465] (k) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+G61E+V68A+N76D+S99G+N218D+Q245R, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449;

[0466] (1) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitution V68A+S106A, wherein the position numbering is based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449; and

[0467] (m) A variant of the polypeptide of SEQ ID NO: 1 of WO 2004 / 067737 having the substitutions S27K+N109K+S111E+S171E+S173P+G174K+S175P+F180Y+G182A+L184F+ Q198E+N199+T297P, wherein the position numbering is based on the numbering of SEQ ID NO: 1 of WO 2004 / 067737.

[0468] Suitable commercially available proteases include those sold under the following trade names: Alcalase®, Duralase TM 、Durazym TM , Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase TM, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In, and Progress® Excel (Novozymes), those sold under the following trade names: Maxatase TM 、Maxacal TM , Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2 TM 、FN3 TM 、FN4 exTM 、Excellase®、Excellenz TM P1000、Excellenz TM P1250、Eraser TM , Preferenz® P100, Purafect Prime, Preferenz P110 TM 、Effectenz P1000 TM , Purafect®, Effectenz P1050 TM 、Purafect® Ox、Effectenz TM P2000, Purafast TM 、Properase®、Opticlean TM and Optimase® (Danisco / DuPont), BLAP (sequence shown in FIG. 29 of US 5352604) and its variants (Henkel AG), and KAP (alkalophilic Bacillus subtilisin) from Kao Corporation.

[0469] Lipase and cutinase

[0470] Suitable lipases and cutinases include those of bacterial or fungal origin, including chemically modified mutant enzymes or protein engineered mutant enzymes. Examples include lipases from thermophilic fungi, such as T. lanuginosus (formerly named Humicola lanuginosa) as described in EP 258068 and EP 305216; cutinases from Humicola, such as Humicola insolens (WO 96 / 13580); lipases from strains of Pseudomonas (some of these are now renamed Burkholderia), such as P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331376), Pseudomonas strain SD705 (WO 95 / 06720 and WO 95 / 06721). 96 / 27002), P. wisconsinensis (WO 96 / 12012); GDSL-type Streptomyces lipase (WO 10 / 065455); cutinase from Magnaporthe grisea (WO 10 / 107560); cutinase from Pseudomonas mendocina (US 5,389,536); lipase from Thermobifida fusca (WO 11 / 084412); Geobacillus stearothermophilus lipase (WO 11 / 084417); lipase from Bacillus subtilis (WO 11 / 084599); and lipase from Streptomyces griseus (WO 11 / 084599). 11 / 150157) and lipases from Streptomyces pristinaespiralis (WO 12 / 137147).

[0471] Other examples are lipase variants as described in EP 407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO 97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 07 / 87508 and WO 09 / 109500.

[0472] Preferred commercial lipase products include Lipolase TM 、Lipex™;Lipolex TM and Lipoclean TM (Novozymes), Lumafast (DuPont), and Lipomax (Gist-Brocades).

[0473] Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, such as the acyltransferase with homology to Candida antarctica lipase A (WO 10 / 111143), the acyltransferase from Mycobacterium smegmatis (WO 05 / 56782), the perhydrolases from the CE 7 family (WO 09 / 67279) and variants of the M. smegmatis perhydrolase, in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 10 / 100028).

[0474] amylase

[0475] Suitable amylases include alpha-amylases or glucoamylases and may be of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, for example, a special strain of Bacillus licheniformis (described in more detail in GB 1,296,839).

[0476] Suitable amylases include those having SEQ ID NO: 2 in WO 95 / 10603 or variants thereof having 90% sequence identity to SEQ ID NO: 3. Preferred variants are described in WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and in SEQ ID NO 4 of WO 99 / 019467, such as variants having substitutions at one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

[0477] Various suitable amylases include those having SEQ ID NO: 6 in WO 02 / 010355 or a variant thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having deletions at positions 181 and 182 and a substitution at position 193.

[0478] Other suitable amylases are hybrid alpha-amylases comprising residues 1-33 of an alpha-amylase derived from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of a Bacillus licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006 / 066594, or variants thereof having 90% sequence identity. Preferred variants of the hybrid alpha-amylase are those having a substitution, deletion, or insertion at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, 1201, A209, and Q264. The most preferred variant of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 is a variant having the following substitutions:

[0479] M197T;

[0480] H156Y+A181T+N190F+A209V+Q264S; or

[0481] G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

[0482] Another suitable amylase is an amylase having SEQ ID NO: 6 in WO 99 / 019467 or a variant thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having substitutions, deletions, or insertions at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those having deletions at positions R181 and G182, or positions H183 and G184.

[0483] Additional amylases that can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96 / 023873, or variants thereof having 90% sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 of WO 96 / 023873. Preferred variants of the foregoing SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, deletion, or insertion at one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476, using SEQ ID 2 of WO 96 / 023873 for numbering. More preferred variants are those having deletions in two positions selected from 181, 182, 183, and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. The most preferred amylase variants of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7 are those having deletions at positions 183 and 184 and substitutions at one or more of positions 140, 195, 206, 243, 260, 304, and 476.

[0484] Other amylases that can be used are those having SEQ ID NO: 2 of WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712, or a variant thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08 / 153815, or a variant thereof having 90% sequence identity to SEQ ID NO: 10 in WO 01 / 66712. Preferred variants of SEQ ID NO: 10 in WO 01 / 66712 are those having a substitution, deletion or insertion at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

[0485] Additional suitable amylases are those having SEQ ID NO: 2 of WO 09 / 061380, or variants thereof having 90% sequence identity to SEQ ID NO: 2. Preferred variants of SEQ ID NO: 2 are those having a C-terminal truncation, and / or substitution, deletion, or insertion at one or more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444, and G475. More preferred variants of SEQ ID NO: 2 are those having substitutions at one or 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 deletions at positions R180 and / or S181 or T182 and / or G183. The most preferred amylase variants of SEQ ID NO: 2 are those having the following substitutions:

[0486] N128C+K178L+T182G+Y305R+G475K;

[0487] N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

[0488] S125A+N128C+K178L+T182G+Y305R+G475K; or

[0489] S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K, wherein the variants are C-terminally truncated and optionally further comprise a substitution at position 243 and / or a deletion at position 180 and / or position 181.

[0490] Additional suitable amylases are amylases having SEQ ID NO: 1 of WO13184577, or variants thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 are those having substitutions, deletions or insertions at one or more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, 1203, S241, R458, T459, D460, G476, and G477. More preferred variants of SEQ ID NO: 1 are those having substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K, and / or deletions at positions R178 and / or S179 or T180 and / or G181. The most preferred amylase variants of SEQ ID NO: 1 are those having the following substitutions:

[0491] E187P+I203Y+G476K

[0492] E187P+I203Y+R458N+T459S+D460T+G476K

[0493] wherein the variants optionally further comprise a substitution at position 241 and / or a deletion at position 178 and / or position 179.

[0494] Another suitable amylase is an amylase having SEQ ID NO: 1 of WO10104675 or a variant thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 are those having substitutions, deletions or insertions at one or more of the following positions: N21, D97, V128, K177, R179, S180, I181, G182, M200, L204, E242, G477, and G478. More preferred variants of SEQ ID NO: 1 are those having substitutions at one or more of the following positions: N21D, D97N, V128I, K177L, M200L, L204YF, E242QA, G477K, and G478K, and / or deletions at positions R179 and / or S180 or I181 and / or G182. The most preferred amylase variants of SEQ ID NO: 1 are those having the following substitutions:

[0495] N21D+D97N+V128I

[0496] wherein the variants optionally further comprise a substitution at position 200 and / or a deletion at position 180 and / or position 181.

[0497] Other suitable amylases are alpha-amylases having SEQ ID NO: 12 in WO 01 / 66712, or variants having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, deletion or insertion at one or more of the following positions of SEQ ID NO: 12 in WO 01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and having substitutions R118K, N195F, R320K, and R458K, as well as variants additionally having substitutions at one or more positions selected from the group consisting of M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, with variants additionally having substitutions in all of these positions being most preferred.

[0498] Further examples are amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078 and WO 2013 / 001087.

[0499] Commercially available amylase is Duramyl TM Termamyl TM 、Fungamyl TM 、Stainzyme TM 、StainzymePlus TM 、Natalase TM , Liquozyme X and BAN TM Amplify; Amplify Prime; (from Novozymes), and Rapidase TM 、Purastar TM / Effectenz TM , Powerase, Preferenz S1000, Preferenz S100, and Preferenz S110 (from Genencor International Ltd. / DuPont).

[0500] Peroxidase / oxidase

[0501] Suitable peroxidases / oxidases include those of plant, bacterial, or fungal origin. Examples include chemically modified mutants or protein engineered mutants. Examples of useful peroxidases include peroxidases from Coprinus, for example from C. cinereus, and variants thereof, such as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercially available peroxidases include Guardzyme (Novozymes).

[0502] Suitable peroxidases are preferably peroxidases of enzyme classification EC 1.11.1.7 as stated by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragments derived therefrom that exhibit peroxidase activity.

[0503] Suitable peroxidases also include haloperoxidases, such as chloroperoxidase, bromoperoxidase, and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidase (EC 1.11.1.10) catalyzes the formation of hypochlorite from chloride ions. The haloperoxidase can be a chloroperoxidase. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In a preferred method, the vanadate-containing haloperoxidase is combined with a chloride ion source.

[0504] Haloperoxidases have been isolated from many different fungi, particularly from the dematiaceous hyphomycetes group, such as Caldariomyces (e.g., C. fumago), Alternaria, Curvularia (e.g., C. verruculosa and C. inaequalis), Drechslera, Ulocladium, and Botrytis.

[0505] Haloperoxidases have also been isolated from bacteria such as Pseudomonas (eg, P. pyrrocinia) and Streptomyces (eg, S. aureofaciens).

[0506] The haloperoxidase may be derived from a Curvularia species, in particular Curvularia verrucosa or Curvularia inaequalis, such as Curvularia inaequalis CBS 102.42 as described in WO 95 / 27046; or Curvularia verrucosa CBS 147.63 or Curvularia verrucosa CBS 444.70 as described in WO 97 / 04102; or from Drechslera hartlebii as described in WO 01 / 79459, Dendryphiella salina as described in WO 01 / 79458, Phaeotrichoconiscrotalarie as described in WO 01 / 79461, or Geniculosporium species as described in WO 01 / 79460.

[0507] Suitable oxidases include in particular any laccase consisting of enzyme classification EC 1.10.3.2 or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as catechol oxidase (EC 1.10.3.1), o-aminophenol oxidase (EC 1.10.3.4) or bilirubin oxidase (EC 1.3.3.5).

[0508] Preferred laccases are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).

[0509] Suitable examples of fungi include laccases derived from strains 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., Myceliophthora thermophila), Schytalidium (e.g., S. thermophilum), Polyporus (e.g., P. pinsitus), Pseudomonas (e.g., P. radiata) (WO 92 / 01046) or Coriolus (e.g., C. hirsutus) (JP 2238885).

[0510] Suitable examples from bacteria include laccases derivable from strains of the genus Bacillus.

[0511] Preferred are laccases derived from Coprinus or Myceliophthora; in particular laccases derived from Coprinus cinerea, as disclosed in WO 97 / 08325; or from Myceliophthora thermophila, as disclosed in WO 95 / 33836.

[0512] Lichenase

[0513] Suitable lichenases (lichenases) include enzymes that catalyze the hydrolysis of β-1,4-glycosidic bonds to produce β-glucans. Lichenases (or lichenases) (e.g., EC 3.2.1.73) hydrolyze (1,4)-β-D-glycosidic bonds in β-D-glucans containing both (1,3)- and (1,4)-linkages and can act on lichen starch and cereal β-D-glucans, but not on β-D-glucans containing only 1,3-linkages or 1,4-linkages. Examples of such lichenases are described in patent applications WO 2017 / 097866 and WO 2017 / 129754.

[0514] Other Materials

[0515] Can also use any detergent component that is used for using in detergent as known in the art.Other optional detergent components comprise corrosion inhibitor, shrink-proofing agent, anti-soil redeposition agent, wrinkle-resistant agent, bactericide, tackiness agent, corrosion inhibitor, disintegrating agent / disintegrating agent, dyestuff, enzyme stabilizer (comprising boric acid, borate and / or polyvalent alcohol, as propylene glycol), fabric softener (comprising clay), filler / processing aid, fluorescent whitening agent / optical brightener, foam accelerator, foam (bubble) conditioning agent, spices, dirt suspending agent, softening agent, suds suppressor, dark inhibitor and wicking agent, alone or in combination.Can utilize any composition that is used for using in detergent as known in the art.The selection of such composition is fully within the technical range of technician.

[0516] Dye transfer inhibitors

[0517] Detergent compositions of the present invention can also include one or more dye transfer inhibitors.Suitable polymer dye transfer inhibitor includes but is not limited to copolymer, polyvinyl oxazolidone and polyvinyl imidazole or its mixture of polyvinyl pyrrolidone polymers, polyamine N-oxide polymers, N-vinyl pyrrolidone and N-vinylimidazole.When in subject composition, when existing, dye transfer inhibitor can exist with from about 0.0001% to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% level by the weight of said composition.

[0518] fluorescent brightener

[0519] The detergent compositions of the present invention will preferably also contain additional components that can color the articles being cleaned, such as fluorescent whitening agents or optical brighteners. When present, the level of brightening agent is preferably from about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in laundry detergent compositions can be used in the compositions of the present invention. The most commonly used fluorescent whitening agents are those belonging to the following categories: diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives, and diphenyl-distyryl derivatives. Examples of diaminostilbene-sulfonic acid derivatives of the fluorescent whitening agent include the sodium salts of 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1,2,3-triazol-2-yl)stilbene-2,2'-disulfonate, and sodium 5-(2H-naphtho[1,2-d][1,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS, available from Ciba-Geigy AG (Basel, Switzerland). Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate. Another preferred fluorescent whitening agent is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals of Mumbai, India. Tinopal CBS-X is the disodium salt of 4,4'-bis-(sulfostyryl)-biphenyl, also known as distyrylbiphenyl disulfonic acid. Other fluorescent agents suitable for use in the present invention include 1-3-diarylpyrazolines and 7-alkylaminocoumarins.

[0520] Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1, or even from about 0.2 wt % to higher levels of 0.5 or even 0.75 wt %.

[0521] Soil release polymers

[0522] Detergent compositions of the present invention can also comprise one or more soil-releasing polymers, and these polymers help to remove dirt from fabric (as cotton and based on polyester fabric), particularly from the hydrophobic dirt removal based on polyester fabric.Soil-releasing polymers can for example be based on the polymer of nonionic or anionic terephthalic acid, polyvinyl caprolactam and related copolymer, vinyl graft copolymer, polyester polyamide, referring to for example Powdered Detergents [powder detergent], Surfactant science series [surfactant science series], the 71st volume, the 7th chapter, MarcelDekker, Inc. [Marcel Dekker company].Another type of soil-releasing polymer is the amphiphilic alkoxylated grease cleaning polymer that comprises core structure and the multiple alkoxylated groups that are attached to this core structure.Core structure can comprise polyalkyl imine structure or polyalkanolamine structure, as described in detail in WO 2009 / 087523 (being incorporated herewith by reference).In addition, random graft copolymer is suitable soil-releasing polymer. Suitable graft copolymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856 and WO 2006 / 113314 (incorporated herein by reference).

[0523] Anti-redeposition agents

[0524] The detergent compositions of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyoxyethylene and / or polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid. The cellulose-based polymers described above under soil release polymers may also function as anti-redeposition agents.

[0525] However, according to the present invention, certain of the above-mentioned polymers (i.e., polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose, and / or combinations thereof) can be included at lower levels than in currently available detergent compositions, or excluded entirely, thereby improving the sustainability profile of the detergent composition.

[0526] Rheology modifiers

[0527] Detergent compositions of the present invention can also comprise one or more rheology modifiers, structurants or thickening agents, are different from viscosity reducers.Rheology modifier is selected from the group consisting of: non-polymer crystallization, hydroxyl functional materials, polymer rheology modifiers, which give shear-thinning characteristics to the aqueous liquid phase matrix of the liquid detergent composition. The rheology and the viscosity of the detergent can be modified and adjusted by methods known in the art, for example, as shown in EP 2169040.

[0528] Other suitable excipients These include, but are not limited to, shrink-proofing agents, anti-wrinkle agents, bactericides, adhesives, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, fragrances, pigments, foam suppressants, solvents, and structurants and / or structural elastic agents for liquid detergents.

[0529] Preparation of detergent products

[0530] The detergent compositions of the present invention may be in any conventional form, such as a bar, a uniform tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compressed powder, granules, a paste, a gel, or a regular, compressed or concentrated liquid.

[0531] The bag can be configured as a single chamber or multiple chambers. It can have any form, shape, and material suitable for containing the composition, for example, preventing the composition from being released from the bag prior to contact with water. The bag is made of a water-soluble film that encloses an internal volume. The internal volume can be divided into the chambers of the bag. The preferred film is a polymeric material, preferably a polymer that forms a film or sheet. Preferred polymers, copolymers, or derivatives thereof are selected polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropyl methylcellulose, maltodextrin, polymethacrylates, and most preferably polyvinyl alcohol copolymers and hydroxypropyl methylcellulose (HPMC). Preferably, the level of polymer in the film, such as PVA, is at least about 60%. The preferred average molecular weight will typically be about 20,000 to about 150,000. The film can also be a blended composition comprising a hydrolytically degradable and water-soluble polymer blend, such as polylactic acid and polyvinyl alcohol (known under trade reference M8630, as sold by MonoSol LLC, Indiana, USA), plus a plasticizer such as glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. The bag can contain a solid laundry cleaning composition or partial components and / or a liquid cleaning composition or partial components separated by a water-soluble film. The chamber for the liquid component can be different in composition from the chamber containing the solid component: US 2009 / 0011970 A1.

[0532] The detergent ingredients can be physically separated from each other by different layers of compartments or tablets in water-soluble bags. Thus, adverse storage interactions between the components can be avoided. In the washing solution, the different dissolution profiles of each compartment can also cause delayed dissolution of the selected component.

[0533] Non-unit dose liquid or gel detergents can be aqueous, typically containing at least 20% and up to 95% water by weight, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids including but not limited to alkanols, amines, glycols, ethers, and polyols can be included in the aqueous liquid or gel. The aqueous liquid or gel detergent can contain from 0% to 30% organic solvent. The liquid or gel detergent can be non-aqueous.

[0534] laundry soap bars

[0535] Xyloglucanase of the present invention can be added into laundry soap bar and be used for hand-washing clothes, fabric, and / or textile.Term laundry soap bar comprises laundry bar, soap bar, combination bar (combo bar), synthetic detergent bar and detergent bar.The usual difference of the type of bar is the type of surfactant they contain, and term laundry soap bar comprises those containing soap and / or synthetic soap from fatty acid.Laundry soap bar has the physical form that is solid rather than liquid, gel or powder at room temperature.Term solid is defined as the physical form that does not change significantly over time, that is, if solid object (for example laundry soap bar) is placed in container, this solid object can not change in order to fill its placed container.When this bar is solid, it is typically the form of bar but also can be other solid shapes such as circle or oval.

[0536] The laundry soap bar may comprise one or more additional enzymes, protease inhibitors such as peptide aldehydes (or sulfoxylate adducts or hemiacetal adducts), boric acid, borate, borax and / or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerol, pH control compounds such as fatty acids, citric acid, acetic acid and / or formic acid, and / or salts of monovalent cations and organic anions, wherein the monovalent cation may be, for example, Na + , K + or NH4 + And the organic anion may be, for example, formate, acetate, citrate or lactate, so that the salt of the monovalent cation and the organic anion may be, for example, sodium formate.

[0537] Laundry soap bars may also contain complexing agents like EDTA and HEDP, perfumes and / or different types of fillers, surfactants such as anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelants, stabilizers, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, suds suppressors, structurants, binders, leaching agents, bleach activators, clay soil release agents, anti-redeposition agents, polymeric dispersants, brighteners, fabric softeners, perfumes and / or other compounds known in the art.

[0538] The laundry soap bars can be processed using conventional laundry soap bar manufacturing equipment, such as, but not limited to, mixers, plodders, e.g., two-stage vacuum plodders, extruders, cutters, logo stampers, cooling tunnels, and packaging machines. The present invention is not limited to making laundry soap bars by any single method. The premix of the present invention can be added to the soap at various stages of the process. For example, a premix containing soap, xyloglucanase, optionally one or more additional enzymes, a protease inhibitor, and salts of monovalent cations and organic anions can be prepared, and the mixture can then be plodded. The xyloglucanase and optional additional enzymes can be added simultaneously, e.g., in liquid form, to act as protease inhibitors. In addition to the mixing and plodding steps, the process can further include the steps of grinding, extruding, cutting, compression molding, cooling, and / or packaging.

[0539] Examples

[0540] Materials and Methods

[0541] Composition of Standard Detergent A (Liquid)

[0542] Composition of Detergent A (Liquid): Ingredients: 12% LAS, 11% AEO Biosoft N25-7 (NI), 5% AEOS (SLES), 6% MPG (monopropylene glycol), 2.7% ethanol, 3.3% TEA, 5.5% cocoa soap, 1.7% glycerin, 2% sodium hydroxide, 2% sodium citrate, 1% sodium formate, 0.2% DTMPA (diethylenetriamine penta(methylenephosphonic acid)) and 0.2% PCA (polycarboxylate polymer), water to 100% (all percentages are w / w).

[0543] Composition of standard detergent A2 (liquid)

[0544] Composition of Detergent A2 (Liquid): Ingredients: 12% LAS, 12% AEO Biosoft N25-7 (NI), 4% AEOS (SLES), 2% MPG (monopropylene glycol), 3.1% ethanol, 2% TEA (triethylamine), 3% soap, 0.5% sodium hydroxide, 3.9% sodium citrate, 1.5% DTMPA-Na7 (diethylenetriamine penta(methylene)penta(phosphonic acid), heptasodium salt), 0.5% phenoxyethanol, water to 100% (all percentages are w / w).

[0545] Composition of Standard Detergent J (Liquid)

[0546] Composition of Detergent J (Liquid): Ingredients: 5% LAS, 5% alkyl sulfate, 5% AEO Biosoft N25-7 (NI), 10% AEOS (SLES), 1% soap, 3% MPG (monopropylene glycol), 1.5% ethanol, 0.3% MEA (monoethanolamine), 0.5% sodium hydroxide, 4% sodium citrate, 0.1% DTPA, 1% sodium formate, water to 100% (all percentages are w / w).

[0547] Example 1: Synergistic Effect of Xyloglucanase and DNase for Partial or Complete Polymer Replacement

[0548] Washing assay

[0549] Terg-O-Tometer (TOM) washing assay

[0550] The Terg-O-Meter (TOM) is a medium-scale standard wash system that can be used to simultaneously test 12 different wash conditions. Essentially, the TOM is a large, temperature-controlled water bath that holds up to 12 open metal beakers. Each beaker acts as a small top-loading washing machine. During an experiment, each beaker contains a solution of a specific detergent / enzyme system, and its performance is tested on soiled and unsoiled fabrics. Mechanical stress is applied by a rotating stirring arm, which agitates the liquid within each beaker. Because the TOM beakers lack lids, samples can be withdrawn during a TOM experiment and the information analyzed online during the wash cycle.

[0551] The TOM standard wash system is primarily designed for medium-scale testing of detergents and enzymes under US or LA / AP wash conditions. Factors such as the ballast-to-soil ratio and the fabric-to-wash liquor ratio can be varied in TOM experiments. Thus, the TOM provides a link between small-scale experiments (such as AMSA and mini-wash) and more time-consuming full-scale experiments in top-loading washing machines.

[0552] Equipment: The water bath has 12 steel beakers and a rotating arm per beaker. Each beaker holds 500 or 1200 mL of detergent solution. The temperature range is from 5°C to 80°C. The water bath must be filled with deionized water. The speed can be set from 70 to 120 rpm / min.

[0553] Procedure: Set the temperature in the Terg-O-Tometer and start the rotation in the water bath. Wait for the temperature to adjust (tolerance is + / - 0.5°C). All beakers should be clean and free of traces of the previously tested substance.

[0554] Prepare a wash solution in a bucket with the desired amount of detergent, temperature, and water hardness. Allow the detergent to dissolve while magnetically stirring for 10 minutes. The wash solution should be used within 30 to 60 minutes of preparation.

[0555] 800 ml washing solution is added to the TOM beaker. Washing solution is stirred under 120 rpm, and optionally one or more enzymes are added to this beaker. Small pieces of cloth are sprinkled in the beaker and then ballast loading. Start time measurement when small pieces of cloth and ballast are added in the beaker. The small pieces of cloth are washed for 20 minutes, after which, stop stirring. Subsequently, the washing loading is transferred to a sieve from the TOM beaker and rinsed with cold tap water. The small pieces of cloth that are soiled are separated from the ballast loading. Under flowing water, the dirty small pieces of cloth are transferred to a 5L beaker containing cold tap water, lasting 5 minutes. For the inactivation that is about to be carried out, ballast is stored separately. Gently squeeze out the water in the small pieces of cloth with your hand, and be placed on a tray covered with paper. Another piece of paper is placed on the top of the small pieces of cloth. Before the small pieces of cloth are subjected to analysis, allow the small pieces of cloth to dry overnight, for example, use DataColor to measure color intensity.

[0556]

[0557] Table 1: Combinations of xyloglucanase and DNase

[0558]

[0559] From Table 1, improved wash performance was observed with partial / complete replacement of polymer in the presence of xyloglucanase and DNase.

[0560] Example 2: Effect of a mixture of xyloglucanase and DNase on the enhancement of fragrance in malodorous cloth swatches

[0561] fabric

[0562] Knitted cotton fabric (CN-42, Center for Test materials BV, The Netherlands) was pre-washed as described below and cut into 5 x 5 cm swatches.

[0563] Pre-wash

[0564] Pre-washing of textiles is mainly to remove starch, carboxymethyl cellulose (CMC) and other additives from textiles. As shown in Table 2, proteases, amylases and cellulases are added to the pre-washing to remove these additives.

[0565] The textiles were washed three times in 86.1 g / wash of detergent W-ECE-2 (wfk Testgewebe GmbH, Germany) using water with a water hardness of 15° dH (3.00 mL of 0.713 mol / L CaCl2, 1.50 mL of 0.357 mol / L MgCl2, and 0.3371 g of NaHCO3 in 1 L of deionized water) and containing the following enzymes:

[0566] Table 2. Pre-wash components

[0567]

[0568] stench

[0569] All malodorous compounds (Table 3) were purchased from Sigma-Aldrich. They were diluted in dipropylene glycol (CAS No. 25265-71-8, Sigma-Aldrich) and mixed to a final concentration of 5 mM for compounds 1-8 and 80 mM for compound 9.

[0570] Table 3. Malodorous compounds used to prepare odor stains

[0571]

[0572] Preparation of odor swatches

[0573] 1. Preparation of DNA and Sebum Stains

[0574] Deoxyribonucleic acid (DNA) sodium salt from salmon testicles (Sigma-Aldrich) was dissolved in MilliQ water in a glass beaker with a magnetic stirrer for 1 hour to prepare a 1% DNA solution. While stirring the DNA solution, artificial sebum (BEY Sebum, wfk Testing Material GmbH, Germany) was melted in a 70°C water bath in the glass beaker. After the DNA was completely dissolved, the DNA solution was heated in a 70°C water bath in the glass beaker, and 0.02% (v / v) Tween® 80 (Sigma-Aldrich) was added to the DNA solution. After the sebum melted, 533 µL of sebum was transferred to 10 mL of the 1% DNA solution in a glass beaker and magnetically stirred at 70°C. The glass beaker was placed in a water bath on a heated stirrer at 400 rpm. To prevent water evaporation during stirring, the glass beaker was covered with tin foil. The sebum and DNA solutions were mixed by vigorous pipetting to form an emulsion.

[0575] DNA and sebum stains were then prepared by applying 400 µl of the DNA and sebum emulsion to the center of a square cotton swatch (5 x 5 cm) and subsequently drying it at room temperature overnight out of direct sunlight.

[0576] 2. Adding malodorous compounds to DNA and sebum stains

[0577] After drying overnight, the DNA and sebum stains were placed in a fume hood, and 80 μl of the malodor mixture was added to the center of each DNA and sebum stain to prepare the odor stains, which were left in the fume hood for 1 h before washing.

[0578] detergent

[0579] The detergent used in the experiment was Tide Pods® ColdwaterClean (Procter & Gamble, USA) purchased from Amazon. The detergent dosage was one pod per 47 liters of water (assuming an average water intake of 47 liters in a typical US top-loading washing machine).

[0580] enzymes

[0581] In this experiment, two enzymes, xyloglucanase (SEQ ID NO: 7) and DNase (a variant of SEQ ID NO: 8 with substitutions S25P, K33L, I56D, T77Y, V127T, G149N, and S181L), were tested. They were tested as an enzyme mixture containing both enzymes.

[0582] Washing assay

[0583] 1. Terg-O-tometer (TOM) Washing

[0584] The Terg-O-tometer in this example consists of sixteen 2 L metal beakers, each equipped with an agitator that rotates back and forth at a controlled speed (120 rpm) to simulate the agitation pattern occurring in a commercial top-loading washing machine. The beakers are partially submerged in a thermostatic water bath maintained at 30°C. Three stains are washed in one beaker filled with 1 L of detergent solution (6° dH water and Tide detergent at the dosages described above). Washing conditions are: 1) detergent without enzymes, and 2) detergent with 0.07 ppm xyloglucanase and 1.0 ppm DNase. Three replicates (1 replicate per beaker) are used for each condition (without or with enzymes).

[0585] After the 20 minute wash period, the stain was quickly removed from the beaker and placed back into the same beaker and rinsed with 1 L of 6° dH water for 8 minutes.

[0586] 2. Drying of stains

[0587] After washing and rinsing, the three odor stains from the same beaker were centrifuged at 4000 g for 5 min in a falcon tube containing two filters (HOZELOCKK3 Kaldness filters, Aquacadabra, eBay) to remove excess water. The plastic filters separated excess water from the small pieces of cloth after centrifugation.

[0588] 3. Evaluation by Headspace SPME-GC-MS Analysis

[0589] To analyze the fragrance remaining on odor stains after washing, three centrifuged stains from the same tube were placed in a 20 mL GC-MS vial (Mikrolab Aarhus A / S, Aarhus, Denmark) and capped with a silicone screw-top cap (Mikrolab Aarhus A / S, Aarhus, Denmark). Samples were analyzed in random order, and the headspace of each vial was analyzed on an Agilent 7890 GC with a split / splitless injector and a 5977 MS with an extractor ion source, coupled to a Gerstel MPS2 sampler with HS / SPME and an SPME needle heater.

[0590] The methods used are:

[0591] GC oven temperature: Initial 40°C; hold for 2 minutes; rate 5°C / min to 180°C; rate 30°C / min to 240°C; hold for 0 minutes. Front SS inlet He: Mode Split; Tª 230°C, split ratio 10:1; split flow rate 15 mL / min. Column: Agilent 19091F-433: FFAP-01 HP-FFAP 30 m x 250 μm x 0.25 μm.

[0592] Gerstel MPS SPME incubator: agitator. Incubation temperature: 60°C; incubation time: 10.00 min; agitator speed: 250 rpm; sample parameters: extraction time: 2.00 min; injection-desorption time: 120 s.

[0593] • Fiber type: Carbon molecular sieve (Carboxen) / polydimethylsiloxane (CAR / PDMS)

[0594] • MS Information: Acquisition Mode: Scan. Solvent Delay (min): 1. Scan Parameters: Start Time: 1. Low Mass: 35. High Mass: 350. Threshold: 100. A / D Samples: 4. MS Zone: MS Source: 230°C. MS Quadrupole: 150°C

[0595] result

[0596] The data in Table 4 below show that the overall fragrance intensity on the odor stain was increased using a combination of two enzymes, xyloglucanase and DNase.

[0597] Table 4. Fragrance Intensity on Odor Stains After Washing with Tide Pods® Coldwater Clean Detergent Without Enzymes or with a Mix of Xyloglucanase and DNase

[0598]

[0599] The invention described and claimed herein is not limited in scope to the specific aspects disclosed herein, as these aspects are intended to serve as illustrations of several aspects of the invention. Any equivalent aspects are intended to be within the scope of the invention. Indeed, various modifications of the invention, in addition to those shown and described herein, will become apparent to those skilled in the art from the foregoing description. Such modifications are also intended to fall within the scope of the appended claims. In the event of a conflict, the present disclosure, including definitions, will prevail.

Claims

1. A cleaning composition comprising (i) at least one xyloglucanase, wherein the xyloglucanase is selected from the group consisting of: n) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 1, o) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 2, p) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 3, q) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 4, r) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 5, s) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 6, or t) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide shown in SEQ ID NO: 7; and (ii) at least one DNA enzyme.

2. The cleaning composition according to claim 1, wherein the DNA enzyme is selected from the group consisting of: I. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 8; II. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 9; III. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 10; IV. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 11; V. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 12; VI. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 13; VII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 14; VIII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 15; IX. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 16; X. a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 17; XI. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 18; XII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 19; XIII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 20; XIV. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 21; XV. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 22; XVI. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 23; XVII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 24; XVIII. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 25; XIX. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 26; or XX. A polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO:

27.

3. The cleaning composition according to claim 1, further comprising a cleaning component.

4. The cleaning composition of claim 3, wherein the cleaning component is selected from the group consisting of surfactants, builders, chelants or sequestrants, bleaching systems or bleaching components, polymers, foam boosters, suds suppressors, dyes, perfumes, tarnish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, corrosion inhibitors, enzyme stabilizers, enzyme inhibitors or activators, one or more transferases, hydrolases, oxidoreductases, bluing agents and fluorescent dyes, antioxidants and solubilizers.

5. The composition according to any one of the preceding claims, wherein the composition further comprises an additional enzyme.

6. The composition of claim 5, wherein the additional enzyme is selected from the group consisting of a protease, a lipase, a cutinase, a second amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, a lichenase, a laccase and / or a peroxidase.

7. The composition according to any one of the preceding claims, wherein the composition is a detergent, and wherein the detergent composition is a liquid laundry detergent composition, a powder laundry detergent composition, a liquid dishwashing detergent composition, or a powder dishwashing detergent composition.

8. The composition of any one of the preceding claims, wherein the composition is in the form of a strip, a uniform tablet, a tablet having two or more layers, a unit dose product such as a bag having one or more compartments, a regular or compressed powder, granules, a paste, a gel, or a regular, compressed or concentrated liquid.

9. A cleaning composition according to any preceding claim, wherein the amount of DNase in the composition is from 0.01 to 1000 ppm and the amount of xyloglucanase is from 0.01 to 1000 ppm.

10. Use of a composition according to any one of claims 1 to 9 in a domestic or industrial cleaning process.

11. Use of the composition according to any one of claims 1 to 9 for partial or complete replacement of anti-redeposition polymers.

12. A method for removing soil from a fabric or hard surface, the method comprising contacting the fabric or hard surface contaminated with soil with a composition according to any one of claims 1 to 9.

13. A method for washing dishes in an automatic dishwasher using the composition according to any one of claims 1 to 9, the method comprising the steps of: The detergent composition is added to a detergent composition chamber in the automatic dishwasher and released during a main wash cycle.

14. A method for deep cleaning an item, the method comprising the following steps: a) contacting the article with a cleaning composition according to any one of claims 1 to 9; and b) optionally rinsing the item, wherein the item is preferably a textile.

15. A method for treating a surface, the method comprising a. Forming an aqueous washing solution using a composition according to any one of claims 1 to 9, b. treating the surface with the aqueous washing solution, preferably at a temperature in the range of 5 ° C-60 ° C, and c. Rinse the surface.

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