Compositions comprising enzymes

Abstract

The present invention provides a cleaning composition comprising a deoxyribonuclease, an additional enzyme, and a cleaning adjunct; a method of preparing such a cleaning composition; and a method of treating a surface such as a fabric or a hard surface with an aqueous liquid comprising such a composition.

Description

[0001] Reference sequence list

[0002] This application contains a sequence listing in computer readable form. The computer readable form is incorporated herein by reference. Technical Field

[0003] The present invention relates to cleaning compositions comprising a mixture of enzymes, methods for their preparation and methods of use. The compositions and methods of the present invention are suitable for household cleaning or treatment compositions, particularly laundry cleaning and hard surface cleaning. The present invention is particularly useful for cleaning clothing. Background Art

[0004] Known enzymes are used for household cleaning compositions for many years. Enzyme mixtures are usually used, wherein each enzyme is selected to target a specific substrate. Fabric surfaces and hard surfaces (such as the inner surface of a dish, floor, shower, dishwashing or laundry washing machine, etc.) can be soiled by complex dirt, which can include one or more of protein, oily dirt, starch and / or other polysaccharides and extracellular DNA (exDNA). In addition, organic stains such as biofilms may cause odor problems because odor molecules can be adhered to polysaccharides, extracellular DNA (exDNA) and proteins in the composite extracellular matrix. These complex dirts are difficult to remove and may also cause fabrics to gray because they may attract other dirt such as particulate dirt, which causes further pollution and fabrics to gray. Therefore, there is still a need to provide a cleaning composition that is good at cleaning, prevents or reduces the above problems. Summary of the invention

[0005] The present invention relates to a cleaning composition comprising a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1; and at least one additional enzyme selected from the group consisting of mannanase, amylase, cellulase, lipase, protease and mixtures thereof, preferably including mannanase, most preferably comprising SEQ ID NO: 2. NO:15 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity; and a cleaning adjunct, which preferably includes a surfactant. The present invention also provides a cleaning composition, the cleaning composition comprising: a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1; and at least one additional enzyme selected from the group consisting of mannanase, amylase, cellulase, lipase, protease and mixtures thereof, preferably including mannanase, most preferably to the deoxyribonuclease shown in SEQ ID NO: 1. NO:15 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity; and a cleaning adjunct, wherein the cleaning adjunct preferably includes a surfactant, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO:36.

[0006] The present invention also provides a method for preparing a cleaning composition, the method comprising: obtaining a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, optionally with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36; at least one additional enzyme, the at least one additional enzyme selected from the group consisting of: mannanase, amylase, cellulase, lipase, protease and mixtures thereof; and a cleaning adjunct, the cleaning adjunct preferably comprising a surfactant; and mixing to prepare the cleaning composition.

[0007] The present invention also provides a method for treating a surface (preferably a fabric), the method comprising:

[0008] (i) forming an aqueous wash liquor comprising water, a deoxyribonuclease as described herein; at least one additional enzyme selected from the group consisting of mannanase, amylase, cellulase, lipase, protease, and mixtures thereof; and a cleaning adjunct, the cleaning adjunct preferably comprising a surfactant;

[0009] (ii) treating the surface with said aqueous washing liquid, preferably at a temperature of 5°C to 60°C, preferably 10°C to 40°C, or preferably at most 35°C, more preferably at a temperature of 30°C or less or at a temperature of 20°C or less; and optionally

[0010] (iii) rinsing the surface.

[0011] The present invention also provides the use of a composition as described herein for cleaning, such as deep cleaning, an item, wherein the item is a textile or a surface.

[0012] The present invention also provides a kit intended for cleaning, such as deep cleaning, wherein the kit comprises a solution or particles comprising one or more of: (i) a deoxyribonuclease as described herein; (ii) an additional enzyme as described herein; and (iii) a cleaning aid as described herein, for mixing with water to form an aqueous washing liquid for cleaning a surface.

[0013] The compositions, methods and kits herein are particularly useful for treating fabric surfaces comprising cotton and / or synthetic fibers (such as polyester, nylon, etc.), which can be in the form of fibers or fabrics, such as single fabrics or mixed fabrics, such as polyester-cotton fabrics. The compositions or methods described herein are also particularly useful for treating hard surfaces, such as floors, walls and / or surfaces in bathrooms and kitchens. DETAILED DESCRIPTION

[0014] Sequence Overview

[0015] SEQ ID NO: 1 Polypeptide obtained from Bacillus cibi

[0016] SEQ ID NO:2 Polypeptide obtained from Bacillus sp.

[0017] SEQ ID NO:3 Polypeptide obtained from Cytophaga sp.

[0018] SEQ ID NO:4 Polypeptide obtained from Bacillus sp.

[0019] SEQ ID NO:5 Polypeptide obtained from Bacillus sp.

[0020] SEQ ID NO:6 Polypeptide obtained from Bacillus subtilis

[0021] SEQ ID NO: 7 Polypeptide obtained from Bacillus sp.

[0022] SEQ ID NO:8 Polypeptide obtained from Bacillus sp.

[0023] SEQ ID NO:9 artificial sequence

[0024] SEQ ID NO: 10 Polypeptide obtained from Bacillus sp.

[0025] SEQ ID NO: 11 Polypeptide obtained from Humicola insolens

[0026] SEQ ID NO: 12 Polypeptide obtained from Humicola insolens

[0027] SEQ ID NO: 13 Polypeptide obtained from Thielavia terrestris

[0028] SEQ ID NO: 14 A polypeptide obtained from Thermomyces lanuginosus

[0029] SEQ ID NO: 15 Polypeptide obtained from Bacillus bogoriensis

[0030] SEQ ID NO: 16 Polypeptide obtained from Paenibacillus woosongensis

[0031] SEQ ID NO: 17 Polypeptide obtained from Paenibacillus illinoisensis

[0032] SEQ ID NO: 18 Polypeptide obtained from Neobulgaria sp.

[0033] SEQ ID NO: 19 A polypeptide obtained from Preussia aemulans

[0034] SEQ ID NO: 20 Polypeptide obtained from Yunnania penicillata

[0035] SEQ ID NO:21 A polypeptide obtained from Myrothecium roridum

[0036] SEQ ID NO:22 Polypeptide obtained from Chaetomium brasiliense

[0037] SEQ ID NO:23 Polypeptide obtained from Ascobolus stictoideus

[0038] SEQ ID NO:24 Polypeptide obtained from Chaetomium virescens

[0039] SEQ ID NO:25 Polypeptide obtained from Bacillus lentus

[0040] SEQ ID NO:26 Polypeptide obtained from Bacillus amyloliquefaciens

[0041] SEQ ID NO: 27 Polypeptide obtained from Bacillus sp.

[0042] SEQ ID NO:28 Polypeptide obtained from Bacillus gibsonii

[0043] SEQ ID NO: 29 Polypeptide obtained from Bacillus lentus

[0044] SEQ ID NO:30 Polypeptide obtained from Bacillus licheniformis

[0045] SEQ ID NO:31 Polypeptide obtained from Paenibacillus polymyxa

[0046] SEQ ID NO:32 Polypeptide obtained from Melanocarpus albomyces

[0047] SEQ ID NO:33 Polypeptide obtained from Paenibacillus species SEQ ID NO:34 Polypeptide obtained from Bacillus hemicellulosilyticus

[0048] SEQ ID NO:35 Polypeptide obtained from Bacillus sp.

[0049] SEQ ID NO:36 Polypeptide obtained from Bacillus spp.

[0050] definition

[0051] In light of this detailed description, the following definitions apply. It is noted that the singular forms "a," "an," and "the" include plural references unless the context clearly dictates otherwise.

[0052] References herein to "about" a value or parameter include aspects relating to the value or parameter itself. For example, description referring to "about X" includes the aspect "X".

[0053] 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.

[0054] Amino Acids: As used herein, the term "amino acid" includes the standard twenty genetically encoded amino acids and their corresponding stereoisomers in the 'd' form (compared 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 obtained by reaction with functional side groups. Such derived molecules include, for example, those in which free amino groups are derivatized to form amine hydrochlorides, p-toluenesulfonyl groups, carboxybenzyloxy 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. As chemical derivatives, peptides containing naturally occurring amino acid derivatives of the twenty standard amino acids are also included. 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 included are amidation, amino terminal acylation (e.g., acetylation or thioglycollic acid amidation), terminal carboxyl amidation (e.g., with ammonia or methylamine), and similar terminal modifications.

[0055] When an amino acid is specifically enumerated such as 'alanine' or 'Ala' or 'A', unless expressly stated otherwise, the term refers to both l-alanine and d-alanine. Other unconventional amino acids may also be suitable components of the polypeptides of the invention, so long as the polypeptide retains the desired functional properties. For the peptides shown, each encoded amino acid residue is represented by a single letter name corresponding to the common name of the conventional amino acid, where appropriate. In one embodiment, the polypeptide of the invention comprises or consists of an l-amino acid.

[0056] Amylase: Amylase (EC 3.2.1) is an enzyme that catalyzes the hydrolysis of starch, glycogen and related polysaccharides into oligosaccharides, maltose or glucose. Amylase is a glycoside hydrolase and acts on α-1,4-glycosidic bonds. Amylases suitable for use in the cleaning composition of the present invention are preferably alpha amylases. α-Amylase (EC3.2.1.1) includes 1,4-α-D-glucan glucanohydrolase and glycogenase, and is a calcium metalloenzyme. By acting at random positions along the starch chain, alpha-amylase breaks down long-chain carbohydrates, ultimately producing maltotriose and maltose from amylose, or maltose, glucose and "limit dextrins" from amylopectin. Suitable amylases of the present invention are preferably microorganisms, such as microorganisms obtained from bacterial or fungal sources. The term "α-amylase activity" means the activity of α1,4-glucan 4 glucanohydrolase EC 3.2.1.1, which constitutes a group of enzymes that catalyze the hydrolysis of starch and other linear and branched 1,4 α-glucosidic oligosaccharides and polysaccharides. The α-amylase activity can be determined by Assay III as described in the Examples herein.

[0057] The terms "alpha-amylase" and "amylase" are used interchangeably and constitute the same meaning and purpose herein.

[0058] Biofilm: The term "biofilm" refers to a sticky fouling usually produced by microorganisms that contains a matrix of extracellular polymeric substances (EPS). Biofilms can contain microbial cells that also adhere to each other. Biofilm EPS is usually a polymer aggregate composed of extracellular DNA, proteins and polysaccharides. Biofilms can form on the surface of living or non-living things. Microbial cells that can grow in biofilms are physiologically different from planktonic cells of the same organism, which are single cells that can float or swim in a liquid medium. Bacteria that can live in biofilms often have significantly different properties from planktonic bacteria of the same species because the dense and protected environment of the membrane enables them to cooperate and interact in various ways. One beneficial effect of this environment on microorganisms is increased resistance to detergents and antibiotics because the dense extracellular matrix and the outer layer of cells protect the interior of the community. In the case of laundry, examples of bacteria that produce biofilms are the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp. On hard surfaces, examples of bacteria that produce biofilms are the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, Staphylococcus aureus, and Stenotrophomonas sp.

[0059] Catalytic domain : The term "catalytic domain" means the region of an enzyme that contains the catalytic machinery of the enzyme.

[0060] cDNA : The term "cDNA" means a DNA molecule that can be prepared by reverse transcription of a mature mRNA molecule obtained from a eukaryotic cell through splicing. The cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial initial RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as a mature spliced ​​mRNA.

[0061] Cellulolytic enzymes or cellulose:The term "cellulolytic enzyme" or "cellulase" means one or more enzymes that hydrolyze cellulosic materials. Such enzymes include endoglucanases, cellobiohydrolases, beta-glucosidases, or combinations thereof. Two basic methods for measuring cellulolytic activity include: (1) measuring total cellulolytic activity, and (2) measuring individual cellulolytic activities (endoglucanases, cellobiohydrolases, and beta-glucosidases), as reviewed by Zhang et al., Outlook for cellulase improvement: Screening and selection strategies, 2006, Biotechnology Advances 24: 452-481. Total cellulolytic activity is typically measured using insoluble substrates, including Whatman No. 1 filter paper, microcrystalline cellulose, bacterial cellulose, algae cellulose, cotton, pretreated lignocellulose, and the like. The most common total cellulolytic activity assay is a filter paper assay using Whatman No. 1 filter paper as a substrate. The assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Measurement of cellulase activities, Pure Appl. Chem. 59: 257-68). Cellulase includes enzymes that catalyze the hydrolysis of 1,4-β-D-glycosidic bonds in cellulose, hemicellulose, lichenan, and cereal β-D-glucans. The term cellulase includes endo-1,4-β-D-glucanases (β-1,4-glucanases, β-1,4-endoglucanohydrolases, endoglucanase D, 1,4-(1,3,1,4)-β-D-glucan 4-glucanohydrolases) and carboxymethyl cellulase. Cellulase includes endocellulase (EC 3.2.1.4) and exocellulase (EC3.2.1.91), the endocellulase randomly cleaves internal bonds at amorphous sites forming new chain ends, and the exocellulase cleaves two to four units from the ends of the exposed chains produced by the endocellulase, thereby producing tetrasaccharides or disaccharides, such as cellobiose. Exocellulase is further classified into type I that gradually works from the reducing end of the cellulose chain and type II that gradually works from the non-reducing end. Suitable cellulase includes complete cellulase or monocomponent endoglucanase of bacterial or fungal origin. Including chemically modified or genetically modified mutants. Cellulase can be, for example, a mixture of monocomponent or monocomponent endo-1,4-β-glucanase, usually only referred to as endoglucanase. Cellulase includes an enzyme with xyloglucanase activity. Cellulase activity can be measured as described in assay IV in the embodiments herein.

[0062] 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 is pectin. The secondary cell wall produced after the cell has stopped growing also contains polysaccharides and is strengthened by polymeric lignin covalently cross-linked to hemicellulose. Cellulose is a homopolymer of dehydrated cellobiose and is therefore a linear β-(1-4)-D-glucan, while hemicellulose includes a variety of compounds such as xylan, xyloglucan, arabinan and mannan with a complex branched structure of a series of substituents. Although generally polycrystalline, cellulose is found in plant tissues mainly as an insoluble crystalline matrix of parallel glucan chains. Hemicellulose is usually hydrogen-bonded to cellulose and other hemicelluloses, which helps to stabilize the cell wall matrix.

[0063] Deoxyribonuclease :As used herein, the term deoxyribonuclease means a polypeptide with DNA enzyme (deoxyribonuclease) activity, which catalyzes the hydrolysis and cleavage of phosphodiester bonds in the DNA backbone, thereby degrading DNA. Deoxyribonucleases cut or cleave residues at the ends of the DNA backbone, wherein endodeoxyribonucleases cleave or cleave within the DNA backbone. Deoxyribonucleases can only cleave double-stranded DNA or can cleave double-stranded and single-stranded DNA. The term "deoxyribonuclease" and the expression "polypeptide with deoxyribonuclease activity" can be used interchangeably throughout the application. For the purposes of the present invention, the deoxyribonuclease activity is determined according to the steps described in assay method I or assay method II. Preferably, the deoxyribonuclease is selected from any enzyme class EC3.1, preferably EC3.1.21. Preferably, the polypeptide with deoxyribonuclease activity is obtained from a microorganism, and the deoxyribonuclease is a microbial enzyme. The deoxyribonuclease is preferably of fungal origin, or even more preferably of bacterial origin.

[0064] Deep Cleaning : The term "deep cleaning" means reducing, destroying or removing components that may be contained in organic matter, such as skin debris, dead cell matter, sebum, sweat and biofilm, such as polysaccharides, oils, proteins, starches, DNA, dirt or other components present in organic matter. Organic matter can be referred to as polyorganic stains containing more than one organic component, such as starch, oils, proteins, DNA and mannan.

[0065] Enzyme cleaning benefits: The term "enzyme detergency benefit" as used herein refers to the beneficial effect that an enzyme can add to a detergent compared to the same detergent without enzymes. Important detergency benefits that can be provided by enzymes are stain removal with no or very little visible stains after washing and / or cleaning; preventing or reducing the redeposition of stains released during the washing process (also known as the effect of anti-redeposition); completely or partially restoring the whiteness of textiles that were originally white but acquired a grayish or yellowish appearance after repeated use and washing (also known as the effect of whitening). Textile care benefits that are not directly related to catalytic stain removal or prevention of stain redeposition may also be important for enzyme detergency benefits. Examples of such textile care benefits are preventing or reducing dye transfer from one fabric to another fabric or another part of the same fabric (also known as the effect of dye transfer inhibition or anti-re-staining); removing protruding or broken fibers from the fabric surface to reduce the tendency to pilling or remove existing pills or fuzz (also known as the effect of anti-pilling); improving fabric softness; color clarification of fabrics; and removing particulate stains trapped in the fibers of fabrics or clothes. Enzymatic bleaching is another enzymatic detergency benefit wherein the catalytic activity is typically used to catalyze the formation of a bleaching component such as hydrogen peroxide or other peroxides.

[0066] Fabric : The term "fabric" can be used interchangeably with "textile", and means materials including yarn, yarn intermediates, fibers, nonwoven materials, natural materials, synthetic materials, and products made from fabrics (e.g., clothing and other articles). Textiles or fabrics can be in the form of knitted fabrics, woven fabrics, denim, nonwovens, felts, yarns, and towels. Textiles can be based on cellulose, such as natural cellulose, including cotton, flax / linen, jute, ramie, sisal, or coconut fiber, or artificial cellulose (e.g., derived from wood pulp), including viscose / rayon, cellulose acetate fibers (tricell), lyocell fibers, or blends thereof. Textiles or fabrics can also be based on non-cellulose, such as natural polyamides, including wool, camel, cashmere, mohair, and silk, or synthetic polymers, such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastic fibers, or blends thereof, as well as blends of cellulose-based fibers and non-cellulose-based fibers. Examples of blends are blends of cotton and / or rayon / viscose fibers 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).

[0067] Hard surface cleaning: As used herein, the term "hard surface cleaning" refers to cleaning any hard surface, including floors, roofs, cars, kitchen or bathroom surfaces and dish cleaning (dishwashing).

[0068] LipaseAs used herein, the term lipase includes enzymes that catalyze the hydrolysis of fats (lipids). Lipase is a subclass of esterase. Suitable lipases for use in the present invention include phospholipases, acyltransferases or perhydrolases, such as acyltransferases homologous to Candida antarctica lipase A (WO10 / 111143), acyltransferases from Mycobacterium smegmatis (WO05 / 56782), perhydrolases from CE 7 family (WO09 / 67279), and variants of Mycobacterium smegmatis perhydrolase, especially the S54V variant (WO10 / 100028) used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd. Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included.Examples include lipases from Thermomyces, e.g., from T. lanuginosus (formerly named Humicola lanuginosa) described in EP258068 and EP305216; cutinases from Humicola, e.g., H. insolens (WO96 / 13580); cutinases from strains of Pseudomonas (some of these now renamed Burkholderia), e.g., P. alcaligenes or P. pseudoalcaligenes (EP21 8272), Pseudomonas cepacia (EP331376), Pseudomonas sp. strain SD705 (WO95 / 06720 & WO96 / 27002), Pseudomonas wisconsinensis (WO96 / 12012); GDSL-type Streptomyces lipase (WO10 / 065455); lipase from Magnaporthe oryzae (Magnaporthe grisea) (WO10 / 107560); a cutinase from Pseudomonas mendocina (US5,389,536); a lipase from Thermobifida fusca (WO11 / 084412); a Geobacillus stearothermophilus lipase (WO11 / 084417), a lipase from Bacillus subtilis (WO11 / 084599); and a lipase from Streptomyces griseus (WO11 / 150157) and Streptomyces pristinae spiralis (WO12 / 137147). Lipase activity can be determined as described in Assay V in the Examples herein.

[0069] Low temperature "Low temperature" is a temperature of 5°C to 40°C, or 5°C to 35°C, or 5°C to 30°C, or even 5°C to 25°C, or 5°C to 20°C, or 5°C to 15°C, or 5°C to 10°C. Preferably, "low temperature" is a temperature of 10°C to 35°C, preferably 10°C to 30°C, or 10°C to 25°C, or 10°C to 20°C, or 10°C to 15°C.

[0070] Mannanase: The term as used herein includes enzymes that catalyze the hydrolysis of mannans, which are highly branched polymers of mannose. Mannanases as used herein are preferably of microbial origin, such as bacterial or fungal mannanases. Mannanases preferably have polypeptides of mannan endo-1,4-β-mannosidase activity (EC 3.2.1.78), which catalyze the hydrolysis of 1,4-3-D-mannosidic bonds in mannans, galactomannans and glucomannans. Mannanases can be GH5 mannanases, such as endo-1,4-β-mannanases or GH26 endo-1,4β-mannanases. Mannanase activity can be determined as described in assay VI in the examples herein.

[0071] Mature peptide : The term "mature polypeptide" refers to a polypeptide in its final form after translation and any post-translational modifications (such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc.). It is known in the art that a host cell can produce a mixture of two or more different mature polypeptides expressed by the same polynucleotide (i.e., having different C-terminal and / or N-terminal amino acids).

[0072] Mutants : The term "mutant" refers to a polynucleotide encoding a variant.

[0073] Protease:As used herein, the term protease includes enzymes that hydrolyze peptide bonds, and the term includes peptidases and proteases. Serine proteases (or serine endopeptidase), EC3.4.21 are enzymes that cleave peptide bonds in proteins, wherein serine is used as the nucleophilic amino acid at the active site. Suitable proteases include those of bacterial, fungal, plant, viral or animal origin, such as plant or microbial origin. Preferred microbial origin. Including chemically modified or protein engineered mutants. Most of the related proteases used for laundry washing can be alkaline proteases, such as serine proteases. Serine proteases can be, for example, S1 family (such as trypsin) or S8 family (such as subtilisin). Metalloprotease proteases can be, for example, thermophilic proteases or other metalloproteases from, for example, family M4, such as those from M5, M7 or M8 families. The term "subtilisin" refers to a subgroup of serine proteases, which is defined according to Siezen et al., Protein Engng. 4 (1991) 719-737 and Siezen et al. Protein Science 6 (1997) 501-523. Serine proteases are a subgroup of proteases, characterized in that they have serine in the active site, which forms a covalent adduct with the substrate. Subtilisin can be divided into 6 subclassifications, namely the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family, and the Pyrolysin family. Protease activity can be measured as described in the assay VII in the Examples herein.

[0074] Sequence identity : The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity".

[0075] For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J.Mol.Biol.48:443-453), as implemented in the Needle program of the EMBOSS program package (EMBOSS:The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet.16:276-277), preferably version 5.0.0 or later. The parameters used can be a gap opening penalty of 10, a gap extension penalty of 0.5, and an EBLOSUM62 (BLOSUM62 of the EMBOSS version) substitution matrix. The Needle output (obtained using the -nobrief option) labeled "longest identity" is used as a percentage identity, and is calculated as follows:

[0076] (identical residues × 100) / (sequence length - total number of gaps in the sequence)

[0077] Textile Care Benefits : As used herein, the term "textile care benefit" is defined as not directly related to catalytic stain removal or prevention of stain redeposition, but also important for enzyme detergency benefits. Examples of such textile care benefits are prevention or reduction of dye transfer from one textile to another textile or another part of the same textile (dye transfer inhibition); removal of protruding or broken fibers from the textile surface to reduce pilling tendency or remove existing pills or fuzz (anti-pilling); improvement of textile softness; color clarification of textiles; and removal of particulate stains entrapped in fibers of textiles. Enzyme bleaching is another enzyme detergency benefit, in which the catalytic activity is generally used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides or other bleaching substances.

[0078] Variants :As used herein, the term "variant" means a polypeptide having the activity of a parent or precursor polypeptide and including changes, i.e., substitutions, insertions and / or deletions, at one or more (e.g., several) positions compared to a precursor or parent polypeptide. Substitution refers to the replacement of an amino acid occupying a certain position by a different amino acid; deletion refers to the removal of an amino acid occupying a certain position; and insertion refers to the addition of an amino acid adjacent to and immediately after an amino acid occupying a certain position.

[0079] Washing performance:The term "detergent performance" is used to refer to the ability of a composition or enzyme to remove stains present on an object to be cleaned, for example during laundry or hard surface washing. The term "detergent performance" includes general cleaning, for example hard surface cleaning as in dishwashing, but also includes detergent performance on textiles such as clothing.

[0080] name

[0081] For the purposes of the present invention, the designation "E / Q" or EQ means that the amino acid at a given position can be glutamic acid (Glu, E) or glutamine (Gln, Q). Similarly, the designation "V / G / A / I" or VGAI means that the amino acid at this position can be valine (Val, V), glycine (Gly, G), alanine (Ala, A) or isoleucine (Ile, I), as well as other combinations as described herein, etc. Unless otherwise limited, amino acid X is defined so that it can be any of the 20 natural amino acids.

[0082] Substitution is usually represented by the original amino acid (amino acid present in the parent sequence), position number and alternative amino acid. For example, A226V represents that the alanine residue in position 226 has been replaced by a valine residue. Different parent enzymes can have different amino acids at the position corresponding to position 226 of the parent sequence. Therefore, A226V is not limited to the replacement of alanine. Any amino acid can be replaced in the replacement, which can also be represented by X as X226V. Two annotations can be used interchangeably. Replacing A226V can also be written as an enzyme X that, for example, comprises valine at the position corresponding to position 226 of SEQ ID NO:XX.

[0083] Deletions are indicated by an asterisk (*). For example, G184* indicates that the original glycine residue in position 184 has been deleted.

[0084] Insertions are indicated by listing the original amino acid, position number, the original amino acid, and the inserted amino acid. For example, S97SD indicates that the serine residue at position 97 is followed by an aspartic acid residue.

[0085] Multiple substitution mutations can be separated by commas, e.g. T51I, S52Q, N54K, which means that one or more of all possible listed mutations may be present. Thus, the above examples mean that one, two or three (thus all) mutations may be present compared to the parent enzyme.

[0086] When mutations in a change set are separated by commas, this means that all changes in the set are present and selected between the change lists (change sets). For example, "include a change set selected from the group consisting of:

[0087] a.H1*, D183*, G184*, N195F, V206Y;

[0088] b.H1*, D183*, G184*, N195F, M202L, V206L, R320K, R458K;...."

[0089] means choosing between a., b., etc. of said changeset. Thus, a set is a list of changes, all present but separated by commas.

[0090] SEQ ID NO: XX+mutation is to be understood as a variant of the enzyme parent comprising the specified mutation compared to the specific parent sequence.

[0091] The term "corresponding to" reflects the numbering system used, and various starting enzymes, such as starting proteases (parent proteases), may have different lengths. Thus, where the numbering of an amylase corresponds to, for example, SEQ ID NO: 2, a given starting amylase is aligned with SEQ ID NO: 2 and the position in the starting amylase corresponding to a given position in SEQ ID NO: 2, such as position 140, is determined.

[0092] The term parent enzyme includes terms such as reference enzyme, backbone or starting enzyme, and is used to refer to the enzyme to which the mutation (eg substitution) is made. The terms can be used interchangeably. DETAILED DESCRIPTION

[0094] Cleaning composition

[0095] The present invention relates to a cleaning composition comprising a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, optionally with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36; at least one additional enzyme, the at least one additional enzyme selected from the group consisting of: a mannanase, an amylase, a cellulase, a lipase and a protease; and a cleaning adjunct, the cleaning adjunct preferably comprising a surfactant.

[0096] The cleaning compositions of the present invention preferably relate to products for use in the following and / or to methods for use in the following and / or to uses of the claimed compositions for use in the following: air care, car care, dishwashing, laundry, care, (conditioning and / or softening), laundry and rinse additives, hard surface cleaning and / or treatment, and other cleaning for consumer or institutional use. Preferably, the composition comprises a laundry detergent or a hard surface cleaning composition for cleaning surfaces such as floors, walls or dishwashing compositions. The composition of the present invention may be a solid (e.g., a stick, tablet, powder, granules), a liquid, a gel and / or a paste, or may be in the form of a sheet. The preferred form is a unit dose form, which may be a tablet, a sheet or a pouch preferably containing a liquid and / or solid composition. Preferred are multi-compartment pouches. The composition may be a multi-purpose "heavy duty" detergent in powder form, a multi-purpose paste form, a heavy duty liquid type, a delicate fabric liquid, a hand dishwashing detergent, a light duty dishwashing detergent, a high foaming type, a machine dishwashing detergent. The dishwashing composition may be in the form of a liquid, gel or powder, and it may be in the form of a unit dose, such as a tablet or sachet, and is preferably a main wash composition or rinse aid type. The composition may also be present in unit dose packaging, including those known in the art and those that are water soluble, water insoluble and / or water permeable. Liquid detergents may be aqueous, typically containing up to 70% water and 0% to 30% organic solvent, or non-aqueous or containing greater than 0.5 g / L of a solution of the detergent composition.

[0097] The compositions of the present invention may, for example, be formulated as hand or machine laundry detergent compositions including a laundry detergent additive composition suitable for pre-treating stained fabrics and a rinse added fabric softener composition, or as detergent compositions for general household hard surface cleaning operations, or for hand or machine dishwashing operations.

[0098] Preferred unit dose compositions include solids (preferably in the form of powders) or liquids or combinations thereof, preferably in multi-compartment unit dose form. Particularly preferred are unit dose forms comprising a liquid detergent enclosed in a water-soluble material in the form of a pouch, optionally in the form of a multi-component pouch. Preferred unit doses include liquid laundry detergent / care compositions, optionally in unit dose form.

[0099] The cleaning composition of the present invention may be in the form of a soap bar, preferably a laundry soap bar, and may be used for hand washing of clothes, fabrics and / or textiles. The term laundry soap bar includes laundry soap bars, soap bars, combination soap bars, synthetic soap bars and detergent bars.

[0100] Deoxyribonuclease

[0101] Suitable deoxyribonucleases for use herein include deoxyribonucleases having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, preferably the deoxyribonuclease will be a deoxyribonuclease having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1.

[0102] In one embodiment, the deoxyribonuclease comprises a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO:1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO:36.

[0103] Preferred deoxyribonucleases for use herein include deoxyribonucleases having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, wherein the deoxyribonuclease comprises a tyrosine kinase at position 13. The invention further comprises the following: an amino acid at position 144, an amino acid at position 167, an amino acid at position 175, an amino acid at position 180, an amino acid at position 22, a proline at position 22, a leucine at position 27, a lysine at position 33, a proline at position 39, a glycine at position 42, an isoleucine at position 56, a valine at position 59, a valine at position 65, a leucine at position 76, an arginine at position 109, an aspartic acid at position 116, a valine at position 127, a proline at position 144, a leucine at position 167 and / or an aspartic acid at position 175, wherein the positions correspond to the positions of SEQ ID NO: 1 (numbered according to SEQ ID NO: 1).

[0104] In a preferred embodiment, the deoxyribonuclease further comprises isoleucine at position 1, lysine at position 4, proline at position 25, tryptophan at position 57, alanine at position 130 and / or histidine at position 147, wherein the positions correspond to the positions of SEQ ID NO: 1 (numbering according to SEQ ID NO: 1).

[0105] Preferred deoxyribonucleases for use herein include deoxyribonucleases having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, wherein the deoxyribonuclease comprises an isoleucine at position 1, a lysine at position 4, a tyrosine at position 13, a lysine at position 5, a tyrosine at position 6, a lysine at position 7, a tyrosine at position 8, a lysine at position 9, a tyrosine at position 10, a lysine at position 11, a tyrosine at position 12, a tyrosine at position 13, a tyrosine at position 14, a tyrosine at position 15, a tyrosine at position 16, a tyrosine at position 17, a tyrosine at position 18, a tyrosine at position 19, a tyrosine at position 20, a tyrosine at position 21, a tyrosine at position 23, a tyrosine at position 24, a tyrosine at position 25, a tyrosine at position 26, a tyrosine at position 27, a tyrosine at position 28, a tyrosine at position 29, a tyrosine at position 30, , proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, histidine at position 147, leucine at position 167 and / or aspartic acid at position 175.

[0106] In a preferred embodiment, the enzyme composition comprises a deoxyribonuclease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the deoxyribonuclease shown in SEQ ID NO: 1, wherein the deoxyribonuclease comprises:

[0107] i) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0108] ii) isoleucine at position 1, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175 Acid; lysine at position 4, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0109] iii) tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0110] iv) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57; valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0111] v) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0112] vi) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175;

[0113] vii) isoleucine at position 1, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0114] viii) isoleucine at position 1, lysine at position 4, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0115] ix) tyrosine at position 13, proline at position 22, leucine at position 27, proline at position 25, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0116] x) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0117] xi) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175;

[0118] xii) isoleucine at position 1, lysine at position 4, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0119] xiii) lysine at position 4, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0120] xiv) tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0121] xv) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175;

[0122] xvi) isoleucine at position 1, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0123] xvii) isoleucine at position 1, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0124] xviii) isoleucine at position 1, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175;

[0125] xix) lysine at position 4, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0126] xx) lysine at position 4, tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0127] xxi) lysine at position 4, tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175;

[0128] xxii) tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, leucine at position 167, and aspartic acid at position 175;

[0129] xxiii) tyrosine at position 13, proline at position 22, proline at position 25, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175; or xxiv) tyrosine at position 13, proline at position 22, leucine at position 27, lysine at position 33, proline at position 39, glycine at position 42, isoleucine at position 56, tryptophan at position 57, valine at position 59, valine at position 65, leucine at position 76, arginine at position 109, aspartic acid at position 116, valine at position 127, alanine at position 130, proline at position 144, histidine at position 147, leucine at position 167, and aspartic acid at position 175; wherein the positions correspond to the positions of SEQ ID NO: 1 (numbered according to SEQ ID NO: 1); and

[0130] xxv) mixtures thereof.

[0131] Particularly useful DNases may be those of microbial origin. In one embodiment, the composition comprises a DNase from bacteria. One embodiment of the invention relates to an enzyme composition, such as a cleaning composition, comprising a DNase; an enzyme selected from mannanase, amylase, cellulase, lipase and protease; and at least one cleaning aid, wherein the DNase is obtained from Bacillus, preferably Bacillus spp.

[0132] As used herein, the term "obtained from" in relation to a given source shall mean that the enzyme of the invention is produced by said source or by a strain into which a polynucleotide encoding an enzyme of the invention from said source has been inserted. In one aspect, the enzyme obtained from a given source is secreted extracellularly.

[0133] Additional enzyme

[0134] The composition comprises an additional enzyme selected from the group consisting of: mannanase, amylase, cellulase, lipase, protease and mixtures thereof. Such additional enzymes preferably include cleaning enzymes. As used herein, "cleaning enzymes" means enzymes that provide "enzyme cleaning benefits" (see definition). Preferably, such additional enzymes are combined with deoxyribonucleases to provide synergistic cleaning.

[0135] Amylase

[0136] A preferred enzyme to be combined with the deoxyribonuclease is an amylase, in particular an alpha-amylase (alpha-1,4-glucan-4-glucanohydrolase, EC 3.2.1.1). Amylases catalyze the hydrolysis of starch and other linear and branched 1,4-glucosidic oligosaccharides and polysaccharides. Amylases have several applications, such as detergents, baking, brewing, starch liquefaction and saccharification, for example in the preparation of high fructose syrup or as part of the production of ethanol from starch. The alpha-amylase useful in the cleaning composition of the present invention is preferably an enzyme classified as EC 3.2.1.1. One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, an amylase and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 90%, at least 91%, at least 92%, at 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 amino acid sequence shown in SEQ ID NO: 1, wherein the amylase is classified as EC 3.2.1.1. The alpha-amylase can be bacterial or fungal. The bacterial alpha-amylase used in the composition according to the invention can, for example, be derived from a strain of Bacillus, which is sometimes also referred to as Geobacillus. In one embodiment, the Bacillus alpha-amylase is derived from Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus stearothermophilus, Bacillus halmapalus or Bacillus subtilis, but may also be derived from another Bacillus, e.g. Bacillus TS-23 is described in WO2014 / 195356. Amylases may also be obtained from bacteria, such as Cellulophagus.

[0137] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a deoxyribonuclease, an amylase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the amylase is obtained from Bacillus, e.g., Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus stearothermophilus, Bacillus halosusceptus or Bacillus subtilis, Bacillus TS-23, or from Cellulophagus.

[0138] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a DNase, an amylase, and a cleaning aid, preferably a surfactant, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 and wherein the amylase is selected from the group consisting of:

[0139] an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 2 or SEQ ID NO: 35, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 2 or SEQ ID NO: 35, the amylase comprising two amino acid deletions in the sequence region R180, S181, T182, G183 compared to SEQ ID NO: 2, wherein each position corresponds to a position in SEQ ID NO: 2;

[0140] a) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:2 or SEQ ID NO:35, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:2 or SEQ ID NO:35, the amylase comprising one set of changes selected from the group consisting of:

[0141] a.R180*, S181*, S243Q, G475K;

[0142] b.R180*, T182*, S243Q, G475K;

[0143] c. R180*, T182*, G183S, S243Q, G475K; and

[0144] d. R180*, S181*, Y242F, S243Q, F266Y, G475K, wherein each position corresponds to a position in SEQ ID NO: 2;

[0145] b) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:3, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:3, said amylase comprising two amino acid deletions in the sequence region R178, G179, T180, G181 compared to SEQ ID NO:3, wherein each position corresponds to a position in SEQ ID NO:3;

[0146] c) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:3, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:3, said amylase comprising one set of changes selected from the group consisting of:

[0147] I.R178*, G179*, E187P, I203Y, G476K;

[0148] II.R178*, G179*, E187P, M199L, I203Y, G476K;

[0149] III.R178*, G179*, E187P, I203Y R458N, T459S, D460T, G476K;

[0150] IV.N126Y, F153W, R178*, G179*, T180H, I203Y, S241Q;

[0151] V.N126Y, F153W, R178*, G179*, T180H, I203Y, S241Q, S362A, R377Y;

[0152] VI. T38N, N126Y, T129I, F153W, R178*, G179*, T180D, E187P, I203Y, G476K, G477E; and

[0153] VII. N126Y, F153W, R178*, G179*, T180H, E187P, I203Y, S241Q, G476K, G477E, wherein each position corresponds to a position in SEQ ID NO: 3;

[0154] d) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:4, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:4, which comprises two amino acid deletions in the sequence region R181, G182, D183, G184 compared to SEQ ID NO:4, wherein each position corresponds to a position in SEQ ID NO:4;

[0155] e) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:4, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:4 comprising an alteration at one or more, preferably all, positions selected from 3, 4, 5, 74, 118, 167, 170, 177, 195, 202, 204, 271, 320, 330, 377, 385, 445, 458, 475, 476, 314, 315 or 316 compared to SEQ ID NO:4, wherein each position corresponds to a position in SEQ ID NO:4;

[0156] f) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:5, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:5, said amylase preferably comprising two amino acid deletions in the sequence region R181, G182, D183, G184 compared to SEQ ID NO:5, wherein each position corresponds to a position in SEQ ID NO:5;

[0157] g) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:5, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:5, said amylase comprising one set of changes selected from the group consisting of:

[0158] a.D183*, G184*, N195F, Y243F;

[0159] b.D183*, G184*, N195F, V206Y, Y243F;

[0160] c.W140Y, D183*, G184*, N195F, V206Y, Y243F, E260G, G304R, G476K;

[0161] d.W140Y, D183*, G184*, N195F, V206Y, Y243F, E260G, G477E;

[0162] e.W140Y, D183*, G184*, N195F, V206Y, Y243F, W284D;

[0163] f.W140Y, N195F, V206Y, Y243F, E260G, G477E;

[0164] g.G109A, W140Y, N195F, V206Y, Y243F, E260G;

[0165] h.T51I, S52Q, N54K, G109A, W140Y, N195F, V206Y, Y243F, E260G, G476E;

[0166] i.W140Y, N195F, V206Y, Y243F, E260G, W284R, G477K;

[0167] j.W140Y, N195F, V206Y, Y243F, E260G, W284F, G477R; and

[0168] k. H1*, G7A, G109A, W140Y, D183*, G184*, N195F, V206Y, Y243F, E260G, N280S, G304R, E391A, G476K, wherein each position corresponds to a position in SEQ ID NO:5;

[0169] h) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:6, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:6, which comprises two amino acid deletions in the sequence region R181, G182, D183, G184 compared to SEQ ID NO:6, wherein each position corresponds to a position in SEQ ID NO:6;

[0170] i) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:6, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:6, said amylase comprising one set of alterations compared to SEQ ID NO:6 selected from the group consisting of:

[0171] I.R118K, D183*, G184*, N195F, R320K, R458K;

[0172] II.M9l, D183*, G184*, R118K, N195F, M202L, R320K, M323T, R458K;

[0173] III.M9L, G149A, R118K, G182T, D183*, G184*, G186A, N195F, M202L, T257I, Y295F, N299Y, M323T, A339S, E345R, R458K;

[0174] IV. M9L, G149A, R118K, G182T, D183*, G184*, G186A, N195F, T246V, T257I, Y295F, N299Y, M323T, A339S, E345R, R458K; and

[0175] V. M9L, G149A, G182T, D183*, G184*, G186A, M202L, T257I, Y295F, N299Y, M323T, A339S, E345R, N471E, wherein each position corresponds to a position in SEQ ID NO: 6;

[0176] j) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:7, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:7, said amylase comprising two amino acid deletions in the sequence region R181, G182, D183, G184 compared to SEQ ID NO:7, wherein each position corresponds to a position in SEQ ID NO:7;

[0177] k) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:7, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:7, said amylase comprising one set of changes selected from the group consisting of:

[0178] a.D183*, G184*, N195F, V206Y, R320K, R458K;

[0179] b.D183*, G184*, N195F, M202L, V206L, R320K, R458K;

[0180] c.G149A, G182T, D183*, G184*, N195F, M202L, V206L, T257I, Y295F, Q299Y, A339S, Q345R, R458K;

[0181] d.G149A, G182T, D183*, G184*, N195F, V206L, M246V, T257I, Y295F, Q299Y, A339S, Q345R, R458K;

[0182] e. G149A, G182T, D183*, G184*, M202L, V206L, T257I, Y295F, Q299Y, A339S, Q345R, H471E; and

[0183] f. H1A, N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182*, D183*, G184T, N195F, V206L, K391A, F473R, G476K, wherein each position corresponds to a position in SEQ ID NO:7;

[0184] l) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:8, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:8, said amylase comprising two amino acid deletions in the sequence region R181, G182, H183, G184 compared to SEQ ID NO:8, wherein each position corresponds to a position in SEQ ID NO:8;

[0185] m) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:8, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:8, said amylase comprising one set of changes selected from the group consisting of:

[0186] a.H183*, G184*, I405L, A421H, A422P, A428T;

[0187] b.R118K, H183*, G184*, N195F, R320K, R458K;

[0188] c.M9l, H183*, G184*, R118K, N195F, M202L, R320K, S323T, R458K;

[0189] d.M9L, G149A, R118K, G182T, H183*, G184*, N195F, M202L, T257I, Y295F, N299Y, A339S, E345R, R458K;

[0190] e.M9L, G149A, R118K, G182T, H183*, G184*, N195F, T246V, T257I, Y295F, N299Y, A339S, E345R, R458K; and

[0191] f. M9L, G149A, G182T, H183*, G184*, M202L, T257I, Y295F, N299Y, S323T, A339S, E345R, wherein each position corresponds to a position in SEQ ID NO: 8;

[0192] n) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:9, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:9, said amylase comprising two amino acid deletions in the sequence region R181, G182, G183, D183 compared to SEQ ID NO:9, wherein each position corresponds to a position in SEQ ID NO:9; and

[0193] o) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:9, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:9, the amylase comprising one set of changes compared to SEQ ID NO:9 selected from the group consisting of:

[0194] a.H1*, D183*, G184*, N195F, V206Y;

[0195] b.H1*, D183*, G184*, N195F, M202L, V206L, R320K, R458K;

[0196] c.G149A, G182T, D183*, G184*, N195F, M202L, V206L, T257I, Y295F, Q299Y, A339S, Q345R, R458K;

[0197] d.G149A, G182T, D183*, G184*, N195F, V206L, M246V, T257I, Y295F, Q299Y, A339S, Q345R, R458K;

[0198] e.G149A, G182T, D183*, G184*, M202L, V206L, T257I, Y295F, Q299Y, A339S, Q345R,

[0199] f.H1*、N54S、V56T、G109A、Q169E、Q172K、A174*、G182*、D183*、N195F、V206L、K391A、G476K;

[0200] g.G182*、D183*、N195F、W140Y、N260G、S304R、R320A、G476K、V410I、V429l、F451W、C474V;

[0201] h.H1*、N54S、V56T、K72R、G109A、F113Q、R116Q、W167F、Q172G、A174S、G182*、D183*、G184T、N195F、V206L、K391A、P473R、G476K;

[0202] i.H1*、N54S、V56T、G109A、Q169E、Q172K、A174*、G182*、D183*、N195F、V206L、K391A、G476K;

[0203] j.H1*、N54S、V56T、G109A、R116H、A174S、G182*、D183*、N195F、V206L、K391A、G476K;

[0204] k.H1*、N54S、V56T、K72R、G109A、F113Q、R116Q、W167F、Q172G、A174S、G182*、D183*、G184T、N195F、V206L、K391A、P473R、G476K;

[0205] l.H1*、N54S、V56T、G109A、F113Q、R116Q、Q172N、A174S、G182*、D183*、N195F、V206L、A265G、K391A、P473R、G476K;

[0206] m.H1*、N54S、V56T、K72R、G109A、F113Q、W167F、Q172R、A174S、G182*、D183*、N195F、V206L、K391A、G476K;

[0207] n.H1*、N54S、V56T、K72R、G109A、R116H、T134E、W167F、Q172G、L173V、A174S、G182*、D183*、N195F、V206L、G255A、K391A、G476K;

[0208] o.H1*, N54S, V56T, K72R, G109A, R116H, T134E, W167F, Q172G, L173V, A174 S, G182*, D183*, N195F, V206L, G255A, K391A, Q395P, T444Q, P473R, G476K;

[0209] p.H1*, N54S, V56T, G109A, T134E, A174S, G182*, D183*, N195F, V206L, K391A, G476K;

[0210] q.H1*, N54S, V56T, K72R, G109A, A174S, G182*, D183*, N195F, V206L, G255A, K391A, G476K;

[0211] r.H1*, N54S, V56T, G109A, W167F, Q172E, L173P, A174K, G182*, D183*, N195F, V206L, K391A, G476K;

[0212] s.H1*, N54S, V56T, G109A, R116Q, V120L, Q172G, L173V, A174S, G182*, D183*, G184T, N195F, V206L, A422P; and

[0213] t.H1*, N54S, V56T, G109A, F113Q, R116Q, W167F, Q172G, l173V, A174S, G182*, D183*, G184T, N195F, V206L, A422P, wherein each position corresponds to a position in SEQ ID NO:9.

[0214] Cellulase

[0215] A preferred enzyme to be combined with a deoxyribonuclease is a cellulase, particularly an enzyme that exhibits endo-β-1,4-glucanase activity. Cellulose is a polymer of glucose linked by β-1,4-glycosidic bonds. Cellulose chains form many intramolecular and intermolecular hydrogen bonds, which lead to the formation of insoluble cellulose microfibrils. Microbial hydrolysis of cellulose with glucose involves three main classes of cellulases: (i) endoglucanases (EC 3.2.1.4), which randomly cleave β-1,4-glycosidic bonds throughout the cellulose molecule, also known as endo-β-1,4-glucanases; (ii) cellobiohydrolases (EC 3.2.1.91), which digest cellulose from the non-reducing ends, releasing cellobiose; and (iii) β-glucosidases (EC3.2.1.21), which hydrolyze cellobiose and low molecular weight cellodextrins to release glucose. The cellulase that can be used in the composition of the present invention is preferably an endoglucanase (EC 3.2.1.4). β-1,4-glycosidic bonds are also β-glucans from plants such as barley and oats. In some cases, endoglucanases also provide hydrolysis of such non-cellulose polymers. Cellulase is placed in glycosyl hydrolases of different families; fungal and bacterial glycosyl hydrolases have been classified into 35 families (Henrissat, B.: A classification of glycosyl hydrolases based on amino acid sequences similarities. Biochem. J. 280 (1991), 309-316. Henrissat, B., and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequences similarities. Biochem. J. 293 (1993), 781-788.). Most cellulases include or consist of a cellulose binding domain (CBD) and a catalytic domain (CAD), which is separated by a joint that may be rich in proline and hydroxy amino acid residues. Another classification of cellulases based on the similarity of their CBDs was established (Gilkes et al. (1991)), providing five families of glycosyl hydrolases (IV). Cellulases are synthesized by a large number of microorganisms, including fungi, actinomycetes, slime molds and eubacteria, but also by plants. In particular, several specific endo-β-1,4-glucanases have been identified.Many bacterial endoglucanases have been described (Gilbert, HJ and Hazlewood, GP (1993) J. Gen. Microbiol. 139: 187-194. Henrissat, B., and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293 (1993), 781-788.). A preferred cellulase comprises an endo-β-1,4-glucanase activity (EC 3.2.1.4), preferably obtained from Bacillus species AA349 (DSM12648), as described in WO2002 / 099091. Other cellulases that are endo-β-1,4-glucanases include the cellulase shown in SEQ ID NO: 10. Other preferred cellulases include those described in WO1996 / 029397, which discloses Family 45 endoglucanases, e.g., cellulases from Thielavia, particularly Thielavia inparticular astrain of Thielavia terrestris, and cellulases described in WO1991 / 017243, which discloses endoglucanases from, e.g., Humicola, such as Humicola insolens.

[0216] Suitable cellulases include those from Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include those from Humicola insolens (US 4,435,307) or from Trichoderma, such as T. reesei or T. viride. Other suitable cellulases are from the genus Thielavia, for example Thielavia terrestris described in WO 96 / 29397, or fungal cellulases produced by Myceliophthorathermophila and Fusarium oxysporum disclosed in US 5,648,263, US 5,691,178, US 5,776,757, WO 89 / 09259 and WO 91 / 17244. Also relevant are cellulases from Bacillus, as described in WO 02 / 099091 and JP 2000210081. Suitable cellulases are alkaline or neutral cellulases having conditioning benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307.

[0217] Cellulases include Family 44 xyloglucanases, which are xyloglucanases, such as the xyloglucanase set forth in SEQ ID NO:31.

[0218] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a DNase, a cellulase, and a cleaning aid, preferably a surfactant, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the cellulase belongs to (EC 3.2.1.4), (EC 3.2.1.91) or (EC 3.2.1.21).

[0219] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a DNase, a cellulase, and a cleaning aid, preferably a surfactant, wherein the DNase has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the cellulase is obtained from Thielavia, Humicola, Paenibacillus or Melanocarpus, preferably Thielavia terrestris, Humicola insolens, Paenibacillus polymyxa or Thermotrichum thermophilum.

[0220] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a DNase, a cellulase, and a cleaning aid, preferably a surfactant, wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the cellulase is selected from the group consisting of:

[0221] a) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 10;

[0222] b) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 11;

[0223] c) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 12

[0224] d) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 13,

[0225] e) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 31, and

[0226] f) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:32.

[0227] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a cellulase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:10 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Bacillus.

[0228] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, preferably a cellulase, and a cleaning aid, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:11 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Humicola, such as Humicola insolens.

[0229] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a cellulase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:12 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Humicola, such as Humicola insolens.

[0230] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a cellulase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:13 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Thielavia, such as Thielavia terrestris.

[0231] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a cellulase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:31 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Paenibacillus, such as Paenibacillus polymyxa.

[0232] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a cellulase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the cellulase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:32 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Melanocarp, such as Thermowhitethread.

[0233] Lipase

[0234] A preferred enzyme to combine with the deoxyribonuclease is a lipase. Lipases are enzymes that catalyze the hydrolysis of fats (lipids). Lipases are used in detergents to remove greasy stains. Lipases EC 3.1.1. are a subclass of esterase EC 3.1. Examples include esterases from the genus Thermomyces, such as T. lanuginosus (previously named Humicola lanuginosus) described in EP258068 and EP305216. lanuginosa); lipases from Humicola such as H. insolens (WO96 / 13580); cutinases from strains of Pseudomonas (some of these are now renamed Burkholderia) such as Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP218272), Pseudomonas cepacia (P. (EP331376), Pseudomonas strain (P.sp.strain) SD705 (WO95 / 06720 & WO96 / 27002), Wisconsin Pseudomonas (P.wisconsinensis) (WO96 / 12012); GDSL-type Streptomyces lipase (WO10 / 065455); cutinase from Magnaporthe grisea (WO10 / 107560); Pseudomonas mendocinae (Pseudomonas mendocina) (US Pat. No. 5,389,536); lipase from Thermobifida fusca (WO 11 / 084412); Geobacillus stearothermophilus lipase (WO 11 / 084417), lipase from Bacillus subtilis (WO 11 / 084599); and lipases from Streptomyces griseus (WO 11 / 150157) and S. pristinaespiralis (WO 12 / 137147).

[0235] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a lipase and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the amino acid sequence shown in SEQ ID NO: 1, wherein the lipase belongs to EC 3.1.1.

[0236] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a lipase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the lipase is obtained from Thermomyces spp., such as from Thermomyces lanuginosus; Pseudomonas, such as Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes, Pseudomonas cepacia, Pseudomonas strain SD705, Pseudomonas wisconsinensis, Pseudomonas mendocina; Streptomyces; Magnaporthe, such as Magnaporthe grisea; Thermobifida, such as Thermobifida; Geobacillus, such as Bacillus stearothermophilus; Bacillus, such as Bacillus subtilis; Streptomyces, such as Streptomyces griseus or Streptomyces viridiflorus.

[0237] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a lipase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the lipase is a lipase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or 100% sequence identity to SEQ ID NO: 14, or a lipase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or 100% sequence identity to SEQ ID NO: 15. NO:14 has a lipase with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity, which comprises one or more substitutions selected from the group consisting of D27R, G38A, G91A / Q, D96E, G163K, T231R, N233R, D254S and P256T compared to SEQ ID NO:14, wherein each position corresponds to a position in SEQ ID NO:14.

[0238] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a lipase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, and wherein the lipase is NO:14 has a lipase with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity, wherein the lipase comprises one or two substitutions T231R and / or N233R, wherein the positions correspond to the positions of SEQ ID NO:14.

[0239] The lipase is preferably a "first cycle lipase", for example sold under the trade name and The ones that are sold.

[0240] Mannanase

[0241] Preferably, the composition comprises a mannanase. Mannanases are enzymes that catalyze the hydrolysis of 1,4-β-D-mannosidic bonds of mannans, galactomannans, glucomannans and galactoglucomannans. Mannan is a hemicellulose that constitutes up to 25% of the dry weight of wood in softwoods, but is also present in other plant materials, especially various seeds. Mannans are polysaccharides with a backbone of β-1,4-linked D-mannosyl residues, which may contain galactose or acetyl substitutions and may have glucose residues in the backbone. The main enzyme type involved in the degradation of mannans is endo-1,4-β-mannanase (EC 3.2.1.78), which hydrolyzes internal glycosidic bonds in the mannan backbone. The present invention provides a cleaning composition, the cleaning composition comprising a deoxyribonuclease and a mannanase, the mannanase comprising a polypeptide having mannan endo-1,4-β-mannosidase activity (EC3.2.1.78), which catalyzes the hydrolysis of 1,4-3-D-mannosidic bonds in mannan, galactomannan and / or glucomannan. According to CAZy (www.cazy.org), endo-1,4-β-mannanase can be found in glycoside hydrolase families 5, 26 and 113. Couturier et al. (2013), "Structuraland Biochemical Analyses of Glycoside Hydrolase Families 5 and 26-(1,4)-Mannanases from Podospora anserina Reveal Differences upon Manno-oligosaccharide Catalysis", J. Biol. Chem., 288(20): 14624-14635, have reported a GH26 mannanase from Podospora anserina with 56.1% and 76.4% identity to SEQ ID NOs: 3 and 6, respectively. Preferred mannanases include GH5 mannanases obtained from Bacillus bogoria described in WO1999 / 064619 or any GH26 mannanase, mannanases from Acanthopanax WO 2017 / 021515 (SEQ ID NO: 2), mannanases from Pseudomonas syringae WO 2017 / 021516 (SEQ ID NO: 2), mannanases from Pseudomonas aeruginosa WO 2017 / 021517 (SEQ ID NO: 2), mannanases from Chaetomium brasiliensis WO 2017 / 021518 (SEQ ID NO: 2), mannanases from Pseudomonas aeruginosa, or mannanases from Chaetomium viridis SEQ ID NOs: 3 and 6 of WO2015 / 040159.

[0242] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the mannanase belongs to EC 3.2.1.78.

[0243] One embodiment relates to an enzyme composition, e.g., a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the mannanase comprises a GH5 and / or GH26 mannanase, preferably a GH5 mannanase.

[0244] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease is identical to SEQ ID The amino acid sequence shown in NO:1 has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity, wherein the mannanase is obtained from Bacillus, such as Bacillus bogoria or Bacillus hemicellulolyticus; Paenibacillus, such as Paenibacillus piniporus or Paenibacillus ilinorum; Spirillum species; Light black shell genus, such as competitive light black shell; Yunnan mold genus, such as Yunnan mold; Myrophyte genus, such as Myrophyte dew wet; Chaetomium genus, such as Chaetomium brasiliensis; Fecal disc fungus, such as Fecal disc fungus; or Chaetomium, such as green Chaetomium.

[0245] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the mannanase is selected from the group consisting of:

[0246] a) a mannanase, wherein the mannanase preferably belongs to glycoside hydrolase family 5 mannanase;

[0247] i. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 15;

[0248] b) a mannanase, wherein the mannanase preferably belongs to glycoside hydrolase family 26 mannanase;

[0249] i. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 16;

[0250] ii. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 17;

[0251] iii. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 18;

[0252] iv. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 19;

[0253] v. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 20;

[0254] vi. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 21;

[0255] vii. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 22;

[0256] viii. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 23;

[0257] ix. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 24;

[0258] x. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 33; and

[0259] xi. a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO:34.

[0260] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:15 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Bacillus, such as Bacillus bogoria.

[0261] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase is identical to the amino acid sequence shown in SEQ ID NO: 37. NO:16 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Bacillus sp., such as Bacillus spp.

[0262] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:17 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Paenibacillus, such as Paenibacillus illinois.

[0263] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO: 18 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from a Spirillum species.

[0264] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase is identical to the amino acid sequence shown in SEQ ID NO: 37. NO:19 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from the genus Melanocystis, such as the competitive Melanocystis.

[0265] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:20 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Yunnan mold, such as Yunnan mold.

[0266] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:21 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Myrocera solani, such as Myrocera solani.

[0267] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase is identical to the amino acid sequence shown in SEQ ID NO: 37. NO:22 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Chaetomium, such as Chaetomium brasiliensis.

[0268] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:23 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from a faecalis fungus, such as a faecalis fungus.

[0269] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:24 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Chaetomium, such as Chaetomium viridis.

[0270] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:33 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Paenibacillus.

[0271] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a mannanase, and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, with the proviso that the deoxyribonuclease is not the deoxyribonuclease shown in SEQ ID NO: 36 and wherein the mannanase has at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1 NO:34 has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity and is preferably obtained from Bacillus, such as Bacillus hemicellulolyticus.

[0272] Protease

[0273] A preferred enzyme in combination with a deoxyribonuclease is a protease. Proteases are enzymes that hydrolyze peptide bonds. The most commonly used proteases for home care fragments are serine proteases (or serine endopeptidases), EC3.4.21, which are enzymes that cleave peptide bonds in proteins, wherein serine is used as a nucleophilic amino acid at the active site. Suitable proteases include those of bacterial, fungal, plant, viral or animal origin, such as plant or microbial origin. Preferred microbial origin. Preferably, the protease is a subtilisin, and even more preferably, the protease belongs to the subtilisin subgroup of subtilisin. Most of the proteases currently used in the cleaning industry are obtained from Bacillus, such as Bacillus lentus and Bacillus amyloliquefaciens. One embodiment of the present invention relates to an enzyme composition, such as a cleaning composition, comprising a DNase, a protease and preferably at least one cleaning adjunct, wherein the protease is obtained from Bacillus, preferably from Bacillus lentus, Bacillus amyloliquefaciens, Bacillus gibsonii, Bacillus licheniformis, Bacillus pumilus, Bacillus halodurans or Bacillus subtilis.

[0274] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a protease and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the amino acid sequence shown in SEQ ID NO: 1, wherein the protease belongs to EC 3.4.21.

[0275] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a deoxyribonuclease, a protease and a cleaning aid, preferably a surfactant, wherein the deoxyribonuclease has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, wherein the protease is obtained from Bacillus, preferably from Bacillus lentus, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus brevis, Bacillus halodurans or Bacillus subtilis.

[0276] One embodiment relates to an enzyme composition, such as a cleaning composition, comprising a DNase, a protease, and a cleaning aid, preferably a surfactant, wherein the DNase has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 1, and wherein the protease is selected from the group consisting of:

[0277] a) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 25, preferably obtained from Bacillus lentus;

[0278] b) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 26; preferably obtained from Bacillus amyloliquefaciens;

[0279] c) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 27, preferably obtained from Bacillus sp.;

[0280] d) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 28, preferably obtained from Bacillus gibsonii;

[0281] e) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 29, preferably obtained from Bacillus lentus;

[0282] f) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:30, preferably obtained from Bacillus licheniformis;

[0283] g) or a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises the substitution T22R or T22A compared to SEQ ID NO: 25, wherein the position corresponds to the position of SEQ ID NO: 25;

[0284] h) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of S3T, V4I, A188P and V199I compared to SEQ ID NO: 25, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0285] i) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of N114L, T207A, A226V and E265F compared to SEQ ID NO: 25, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0286] j) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of S97D, S101A, V102I and G157S compared to SEQ ID NO: 25, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0287] k) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of S85N, G116V, S126L, P127Q and S128A compared to SEQ ID NO: 25, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0288] l) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of Y161A, R164S and A188P compared to SEQ ID NO:25, wherein the positions correspond to the positions of SEQ ID NO:25;

[0289] m) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of S3T, R19L and A188P, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0290] n) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises one or more, preferably all, substitutions selected from the group consisting of S9R, R19L and N60D, wherein the positions correspond to the positions of SEQ ID NO: 25;

[0291] o) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:25, wherein the protease comprises the amino acid arginine (R) at the position corresponding to the position selected from the group consisting of 9, 42 and 239 of SEQ ID NO:25;

[0292] p) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:25, wherein the protease comprises the amino acid glutamic acid (E) or aspartic acid (D) at the position corresponding to the position selected from the group consisting of 9, 42, 60, 61, 74, 157, 176, 179, 182, 212, 250, 253 and 256 of SEQ ID NO:25;

[0293] q) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises an insertion of the amino acid Aspartic Acid (D) or Glutamic Acid (E) at the position corresponding to position 97 of SEQ ID NO: 25;

[0294] r) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:25, wherein the protease comprises an amino acid selected from the group consisting of glutamic acid (E), aspartic acid (D), glycine (G), arginine (R), and methionine (M) at the position corresponding to position 99 of SEQ ID NO:25;

[0295] s) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 25, wherein the protease comprises an amino acid selected from the group consisting of glutamic acid (E), aspartic acid (D), and glutamine (Q) at the position corresponding to position 211 of SEQ ID NO: 25;

[0296] t) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:26, wherein the protease comprises an amino acid selected from the group consisting of glutamic acid (E), aspartic acid (D), and glutamine (Q) at the position corresponding to position 217 of SEQ ID NO:26; and

[0297] u) a protease having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO:26, wherein the protease comprises one or more substitutions selected from the group consisting of S24G / R, S53G, S78N, S101N, G128A / S and Y217Q / L compared to SEQ ID NO:26, wherein the positions correspond to the positions of SEQ ID NO:26.

[0298] As mentioned above, particularly preferred compositions according to the invention comprise a DNase and the additional enzymes include a mannanase and an amylase.

[0299] Cleaning aids

[0300] In addition to the DNase and additional enzymes, the cleaning composition also comprises a cleaning aid / detergent aid, preferably a surfactant. The expression cleaning aid herein generally includes a combination of more than one cleaning aid. Typically, the cleaning aid will be present in the composition in an amount of 0.0001 wt % to 99.9999 wt %, preferably 10 wt % to 99.999 wt %, preferably at least 30 wt % or 40 wt % or 50 wt % of the cleaning aid. Suitable cleaning adjuncts include surfactants, builders, bleaches, bleach catalysts, colorants, bleach boosters, chelating agents, dye transfer agents, deposition aids, dispersants, other additional enzymes and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, fluorescent brighteners, photoactivators, fluorescent agents, fabric hueing agents, fabric conditioners, preformed peracids, polymeric dispersants, clay soil removal / anti-redeposition agents, filler salts, hydrotropes, brighteners, foam suppressants, structure elasticizers, fabric softeners, hydrolyzable surfactants, preservatives, antioxidants, anti-shrinkage agents, bactericides, fungicides, anti-staining agents, anti-corrosion agents, alkalinity sources, solubilizers, carriers, processing aids, pigments, dyes, fragrances and pH control agents, encapsulates, polymers and mixtures thereof.For example, these cleaning adjuncts may include: bleaching ingredients such as imine bleach boosters; hydrogen peroxide sources such as percarbonates and / or perborates, particularly percarbonates coated with materials such as carbonates and / or sulfates, silicates, borosilicates, and any mixtures thereof; preformed peracids, including preformed peracids in encapsulated form; transition metal catalysts; suds suppressors or suds suppressors, such as silicone-based suds suppressors and / or fatty acid-based suds suppressors; fabric softeners such as clays, silicones and / or quaternary ammonium compounds; flocculants such as polyethylene oxide; dye transfer inhibitors such as polyvinyl pyrrolidone, poly 4-vinyl pyridine N-oxide and / or copolymers of vinyl pyrrolidone and vinyl imidazole; fabric integrity components, for example oligomers formed by condensation of imidazole and epichlorohydrin; soil dispersants and soil anti-redeposition aids such as alkoxylated polyamines and ethoxylated ethyleneimine polymers; anti-redeposition components such as polyesters; carboxylate polymers such as maleic acid polymers or copolymers of maleic acid and acrylic acid; fragrances such as fragrance microcapsules, starch encapsulated blends, fragrance sprays; soap rings; aesthetic particles; dyes; fillers such as sodium sulfate and / or citrus fiber, but the composition may preferably be substantially free of fillers; silicates such as sodium silicate (including 1.6R and 2.0R sodium silicate) or sodium metasilicate; copolyesters of dicarboxylic acids and glycols; cellulosic polymers such as methylcellulose, carboxymethylcellulose, hydroxyethoxycellulose, or other alkyl or alkyl alkoxycelluloses; solvents such as 1,2-propylene glycol, monoethanolamine; diethylene glycol, ethanol, and any mixtures thereof; hydrotropes such as sodium cumene sulfonate, sodium xylene sulfonate, sodium toluene sulfonate, and any mixtures thereof; organic acids such as citric acid; and any combination thereof. Preferably, the composition comprises a cleaning adjuvant comprising a surfactant and an additional enzyme. Preferably, the composition comprises one or more adjuvants selected from the group consisting of: (i) perfume microcapsules; (ii) fabric hueing agents; (iii) proteases; (iv) amphiphilic cleaning polymers; (v) ribonucleases, (viii) xanthan lyases; (ix) hexosaminidase; or (viii) mixtures thereof.

[0301] Preferably, the composition comprises a surfactant, preferably comprising 0.1 wt % to 60 wt %, or 0.5 wt % to 50 wt %, or 1 wt % to 40 wt % of the composition. The surfactant preferably comprises a surfactant system comprising a mixture of more than one surfactant, the surfactant may include, for example, anionic surfactants, nonionic surfactants, including semi-polar, cationic, zwitterionic and / or amphoteric surfactants and mixtures thereof. Preferably, the composition comprises an amine oxide.

[0302] Preferably, the composition comprises anionic surfactants. Preferred anionic surfactants are sulfonate and sulfate surfactants, preferably alkylbenzene sulfonates and / or (optionally alkoxylated) alkyl sulfates. Particularly preferred anionic surfactants include linear alkylbenzene sulfonates (LAS). Preferred alkyl sulfates include alkyl ether sulfates, particularly C-9-15 alcohol ether sulfates (particularly those with an average ethoxylation degree of 0.5 to 7, preferably 1 to 5), C8-C16 ester sulfates and C10-C14 ester sulfates (such as monododecyl ester sulfates). In preferred compositions according to the present invention, the surfactant includes anionic surfactants, preferably alkylbenzene sulfonates and / or optionally ethoxylated alkyl sulfates, preferably with an ethoxylation degree of 0 to 7, more preferably 0.5 to 3. Isomers of LAS, branched alkylbenzene sulfonates (BABS), phenylalkanesulfonates, α-olefin sulfonates (AOS), polyolefin sulfonates, monoolefin sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkylsulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkyl sulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerides, α-sulfo fatty acid methyl esters (α-SFMe or SES) including methyl ester sulfonate (MES), alkyl succinic acid or alkenyl succinic acid, dodecyl / tetradecyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or salts of fatty acids (soaps), and combinations thereof are also suitable anionic surfactants. In a preferred embodiment, the surfactant comprises an anionic surfactant, preferably comprising an alkylbenzene sulfonate and / or optionally an ethoxylated alkyl sulfate, preferably having a degree of ethoxylation of from 0 to 7, more preferably from 0.5 to 3.

[0303] Anionic surfactants are preferably added to the cleaning composition in salt form. Preferred cations are alkali metal ions, such as sodium and potassium. However, the salt form of anionic surfactants can be formed in situ by neutralizing the acid form of the surfactant using a base (such as sodium hydroxide or an amine such as monoethanolamine, diethanolamine or triethanolamine). Preferably, the surfactant includes a nonionic surfactant. Preferably, the surfactant includes anionic surfactants and nonionic surfactants, and the weight ratio of the anionic surfactant to the nonionic surfactant is 50:1 or 30:1 to 1:2 or 1:1, preferably 20:1 to 2:3 or 1:1.

[0304] Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and / or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamide, GA or fatty acid glucamide, FAGA), and products available under the trade names SPAN and TWEEN, and combinations thereof. Particularly preferred are alcohol ethoxylates, preferably having a C9-18 alkyl chain, preferably a C12-15 alkyl chain, and preferably having an average degree of ethoxylation of 3 to 9, more preferably 3 to 7. Commercially available nonionic surfactants include Plurafac from BASF TM , lutensol TM and pluronic TM , Dehypon from Cognis TM series, and Cognis and genapol from Clariant TM series.

[0305] The cleaning composition preferably comprises from about 1% to about 40% of an anionic surfactant. The cleaning composition preferably comprises from 0.2% to about 40% of a nonionic surfactant, such as alcohol ethoxylates, ethoxylated nonylphenols, alkyl polyglycosides, alkyl dimethylamine oxides, ethoxylated fatty acid monoethanolamides, fatty acid monoethanolamides, polyhydroxy alkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine ("glucamides").

[0306] The cleaning compositions preferably comprise one or more additional additional enzymes. Thus, preferred compositions comprise (a) a deoxyribonuclease as defined herein, and (b) one or more additional enzymes selected from the group consisting of amylases, cellulases, lipases, mannanases, proteases and mixtures thereof; and one or more further additional enzymes, preferably selected from the group consisting of carboxypeptidases, catalases, chitinases, cyclodextrin glycosyltransferases, deoxyribonucleases, α-galactosidases, β-galactosidases, haloperoxidases, haloperoxidases, hexosaminidase, invertases, laccases, lichenidases, mannosidases, oxidases, pectinases, pectin lyases, pectinolytic enzymes, peptidoglutaminases, peroxidases, phytases, polyphenol oxidases, peroxidases, ribonucleases, phytases, polyphenol oxidases, peroxidases, ribonucleases, transglutaminases, xylanases, xanthan gum, xanthan gum lyases, xyloglucanase and mixtures thereof. Preferably, the composition comprises further additional enzymes selected from xanthan lyase, xanthanase and mixtures thereof. Also particularly preferred are xanthan lyase and xanthanase and mixtures thereof.Further additional enzymes may be produced, for example, by microorganisms belonging to the genus Aspergillus, such as Aspergillus aculeatus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger or Aspergillus oryzae; by microorganisms belonging to the genus Fusarium, such as Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum. or produced by a microorganism belonging to the genus Humicola, such as Humicola insolens or Humicola lanuginosa; or produced by a microorganism belonging to the genus Trichoderma, such as Trichoderma harzianum, Trichoderma koningii, or Trichoderma sambucinum. koningii), Trichoderma longibrachiatum, Trichoderma reesei, or Trichoderma viride.

[0307] Preferably, the composition comprises one or more of the following: a CGTase, a pectinase, a pectate lyase and / or a laccase or a mixture of more than one thereof.

[0308] In general, the properties of the selected enzyme will generally be compatible with the selected detergent (i.e., optimum pH, compatibility with other enzymes or non-enzyme ingredients, etc.), and the enzyme should be present in an effective amount. Preferably, the compositions of the present invention comprise at least 0.01 mg, preferably from about 0.05 mg to about 10 mg, more preferably from about 0.1 mg to about 6 mg, especially from about 0.2 mg to about 5 mg of additional active enzyme / g composition.

[0309] Peroxidase / oxidase: Suitable peroxidase / oxidase include those derived from plants, bacteria or fungi. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus (e.g., from C. cinereus) and variants thereof, such as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257.

[0310] Commercially available peroxidases include (Novozymes A / S).

[0311] Pectate lyase: Other preferred enzymes include those sold under the trade names Pectate lyase sold by HYDRAZYME® (from Novozymes A / S, Bagsvaerd, Denmark).

[0312] Enzymes can be added to the cleaning composition by adding a single additive (premix) comprising one or more enzymes or by adding a mixed additive (premix) comprising all of these enzymes. The detergent additive of the present invention (i.e., a single additive or a mixed additive) can be formulated, for example, as a granule, a liquid, a slurry, etc. Preferred detergent additive formulations are granules, particularly non-dusting granules, liquids, particularly stable liquids, or suspensions.

[0313] Dust-free granules can be produced and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) having an average molar weight of 1000 to 20000; ethoxylated p-nonylphenol having 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 fatty acid monoglycerides, diglycerides and triglycerides. Film-forming coating materials can be applied, for example, by fluidized bed technology. For example, liquid enzyme preparations can be stabilized by adding polyols such as propylene glycol, sugars or sugar alcohols, lactic acid or boric acid according to established methods.

[0314] The cleaning composition may include a fabric hueing agent (sometimes referred to as an opacifier, bluing agent or whitening agent). Hueing agents typically provide a blue or purple hue to the fabric. Hueing agents can be used alone or in combination to produce a specific hueing shade and / or to hue different fabric types. This can be provided, for example, by mixing a red and a cyan dye to produce a blue or purple hue. The toner may be selected from dyes of any known chemical class, including but not limited to acridine, anthraquinone (including polycyclic quinones), azine, azo (e.g., monoazo, disazo, triazo, tetrazo, polyazo), including premetallated azo, benzodifuran and benzodifuranone, carotenoids, coumarins, cyanines, diaza hemicyanines, diphenylmethanes, formazans, hemicyanines, indigos, methanes, naphthylimides, naphthoquinones, nitro and nitroso, oxazines, phthalocyanines, pyrazoles, stilbenes, styryls, triarylmethanes, triphenylmethanes, xanthenes, and mixtures thereof, with preferred dyes being azo, particularly disazo, anthraquinone, azine and triarylmethane dyes. Azo dyes are particularly preferred.

[0315] Suitable fabric hueing agents include dyes, dye-clay conjugates, and organic and inorganic pigments. Suitable dyes include small molecule dyes and polymeric dyes; polymeric dyes are preferred. Suitable small molecule dyes include those selected from direct, basic, reactive, or hydrolyzed reactive, solvent or disperse dyes belonging to the Colour Index (CI) classification (e.g., classified as blue, violet, red, green or black) and providing the desired hue, either alone or in combination. In another aspect, suitable small molecule dyes include small molecule dyes selected from the group consisting of: direct violet dyes such as 9, 35, 48, 51, 66 and 99, direct blue dyes such as 1, 71, 80 and 279, acid red dyes such as 17, 73, 52, 88 and 150, acid violet dyes such as 15, 17, 24, 43, 49 and 50, acid blue dyes such as 15, 17, 25, 29, 40, 45, 75, 80, 83, 90 and 113, acid black dyes such as 1, basic violet dyes such as 1, 3, 4, 10 and 35, basic blue dyes such as 3, 16, 22, 47, 66, 75 and 159, disperse dyes or solvent dyes such as those described in EP1794275 or EP1794276, or as described in US Pat. 7,208,459 B2, and mixtures thereof. In another aspect, suitable small molecule dyes include small molecule dyes selected from the group consisting of: Acid Violet 17, Direct Blue 71, Direct Violet 51, Direct Blue 1, Acid Red 88, Acid Red 150, Acid Blue 29, Acid Blue 113, or mixtures thereof of Color Index Numbers.

[0316] Suitable polymeric dyes include polymeric dyes selected from the group consisting of: polymers containing covalently bound (sometimes referred to as conjugated) chromogens (dye-polymer conjugates) (e.g., polymers having chromogens copolymerized into the polymer backbone) and mixtures thereof. Polymeric dyes include those described in WO2011 / 98355, WO2011 / 47987, US2012 / 090102, WO2010 / 145887, WO2006 / 055787, and WO2010 / 142503.

[0317] On the other hand, suitable polymeric dyes include polymeric dyes selected from the group consisting of: (Milliken, Spartanburg, South Carolina, USA), a dye-polymer conjugate formed from at least one reactive dye and a polymer selected from the group consisting of polymers comprising a moiety selected from the group consisting of a hydroxyl moiety, a primary amine moiety, a secondary amine moiety, a thiol moiety, and mixtures thereof. On the other hand, suitable polymeric dyes include polymeric dyes selected from the group consisting of: Violet CT, carboxymethyl cellulose (CMC) covalently bonded to a reactive blue, reactive violet or reactive red dye, such as CMC conjugated to CI Reactive Blue 19, sold by Megazyme, Wicklow, Ireland under the product name AZO-CM-CELLULOSE, product code S-ACMC, alkoxylated triphenyl-methane polymeric colorants, alkoxylated thiophene polymeric colorants, and mixtures thereof.

[0318] Preferred hueing dyes include, for example, the alkoxylated thiophene azo brighteners described in US2008 / 0177090, which may optionally be anionic, such as those selected from Examples 1 to 42 in Table 5 of WO2011 / 011799. Other preferred dyes are disclosed in US8138222.

[0319] Suitable pigments include pigments selected from the group consisting of flavanthrone, blue anthrone, chlorinated blue anthrone containing 1 to 4 chlorine atoms, pyranthrone, dichloropyranthrone, monobromodichloropyranthrone, dibromodichloropyranthrone, tetrabromopyranthrone, perylene-3,4,9,10-tetracarboxylic acid diimide, wherein the imide group may be unsubstituted or substituted by a C1 to C3 alkyl group or a phenyl group or a heterocyclic group, and wherein the phenyl and heterocyclic groups may additionally carry substituents which do not provide solubility in water, anthrapyrimidinecarboxylic acid amides, anthrone violet, isoanthrone violet, dioxazine pigments, copper phthalocyanines which may contain up to 2 chlorine atoms per molecule, polychlorinated copper phthalocyanines or polybrominated chlorinated copper phthalocyanines containing up to 14 bromine atoms per molecule, ultramarine blue (CI Pigment Blue 29), ultramarine violet (CI Pigment Violet 15), and mixtures thereof.

[0320] Builder - The cleaning composition may also contain a builder, such as a carbonate, bicarbonate or silicate based builder, which may be a zeolite, such as zeolite A, zeolite MAP (high aluminum type P). Zeolites useful for laundry washing preferably have the formula Na 12 (AlO2) 12 (SiO2) 12·27H2O and the particle size of zeolite A is typically between 1 μm and 10 μm, the particle size of zeolite MAP is typically between 0.7 μm and 2 μm. Other builders are sodium metasilicate (Na2SiO3·nH2O or Na2Si2O5·nH2O) strong bases and are preferably used for dishwashing. In a preferred embodiment, the amount of detergent builder may be higher than 5%, higher than 10%, higher than 20%, higher than 30%, higher than 40% or higher than 50%, and may be lower than 80%, 65%. In dishwashing detergents, the builder content is typically 40% to 65%, especially 50% to 65% or even 75% to 90%.

[0321] Encapsulates - The composition may comprise an encapsulate. In one aspect, the encapsulate comprises a core, a shell having an inner surface and an outer surface, the shell encapsulating the core.

[0322] In one aspect of the encapsulate, the core may comprise a material selected from the group consisting of: fragrances; whiteners; dyes; insect repellents; silicones; waxes; flavors; vitamins; fabric softeners; skin care agents, in one aspect paraffin; enzymes; antimicrobial agents; bleaches; sensates; and mixtures thereof; and the shell may comprise a material selected from the group consisting of: polyethylene; polyamides; polystyrenes; polyisoprenes; polycarbonates; polyesters; polyacrylates; aminoplasts, in one aspect the aminoplasts may comprise polyureas, polyurethanes, and / or polyureaurethanes, in one aspect the polyureas may comprise polyformaldehyde ureas and / or melamine formaldehyde resins; polyolefins; polysaccharides, in one aspect the polysaccharides may comprise alginates and / or deacetylated chitosan; gelatin; shellac; epoxy resins; vinyl polymers; water-insoluble inorganics; silicones; and mixtures thereof.

[0323] In one aspect of the encapsulate, the core may comprise a fragrance. Such encapsulates are fragrance microcapsules. Suitable encapsulating shells may comprise melamine formaldehyde and / or cross-linked melamine formaldehyde, and / or polyacrylates.

[0324] In one aspect, at least 75%, 85% or even 90% of the encapsulates may have a particle size of about 1 micron to about 80 microns, about 5 microns to 60 microns, about 10 microns to about 50 microns, or even about 15 microns to about 40 microns.

[0325] In one aspect, at least 75%, 85%, or even 90% of the encapsulates may have a particle wall thickness of from about 30 nm to about 250 nm, from about 80 nm to about 180 nm, or even from about 100 nm to about 160 nm.

[0326] In one aspect, the core material of the encapsulate may comprise a material selected from the group consisting of: a fragrance raw material and / or optionally selected from the following materials: a vegetable oil (including pure vegetable oil and / or blended vegetable oil), including castor oil, coconut oil, cottonseed oil, grape oil, rapeseed oil, soybean oil, corn oil, palm oil, linseed oil, safflower oil, olive oil, peanut oil, coconut oil, palm kernel oil, castor oil, lemon oil, and mixtures thereof; esters of vegetable oils, esters including dibutyl adipate, dibutyl phthalate , benzyl butyl adipate, octyl benzyl adipate, tricresyl phosphate, trioctyl phosphate, and mixtures thereof; straight or branched chain hydrocarbons, including those having a boiling point greater than about 80°C; partially hydrogenated terphenyls, phthalates, alkyl biphenyls (including monoisopropyl biphenyl), alkylated naphthalenes (including dipropyl naphthalene), white spirits (including kerosene), mineral oils, and mixtures thereof; aromatic solvents, including benzene, toluene, and mixtures thereof; silicone oils; and mixtures thereof.

[0327] In one aspect, the wall material of the encapsulate can comprise a suitable resin comprising the reaction product of an aldehyde and an amine, and suitable aldehydes include formaldehyde. Suitable amines include melamine, urea, benzoguanamine, glycoluril and mixtures thereof. Suitable melamines include methylol melamine, methylated methylol melamine, imino melamine and mixtures thereof. Suitable ureas include dimethylol urea, methylated dimethylol urea, urea-resorcinol and mixtures thereof.

[0328] In one aspect, suitable formaldehyde scavengers can be used with the encapsulate, for example, in a capsule slurry, and / or added to a consumer product before, during, or after the encapsulate is added to such consumer product.

[0329] Suitable capsules are commercially available from Appleton Papers Inc. (Appleton, Wisconsin USA).

[0330] In addition, the materials used to prepare the above-mentioned encapsulates can be obtained from Solutia Inc. (St Louis, Missouri U.S.A.), Cytec Industries (West Paterson, New Jersey USA), Sigma-Aldrich (St. Louis, Missouri USA), CP Kelco Corp. (San Diego, California, USA); BASF AG (Ludwigshafen, Germany); Rhodia Corp. (Cranbury, New Jersey, USA); Hercules Corp. (Wilmington, Delaware, USA); Agrium Inc. (Calgary, Alberta, Canada), ISP (New Jersey U.S.A.), Akzo Nobel (Chicago, IL, USA); Stroever Shellac Bremen (Bremen, Germany); Dow Chemical Company (Midland, MI, USA); Bayer AG (Leverkusen, Germany); Sigma-Aldrich Corp. (St. Louis, Missouri, USA).

[0331] The composition may comprise a structurant selected from the group consisting of di- and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose-based materials, microfiber cellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof.

[0332] polymer

[0333] The cleaning composition may comprise one or more polymers. Examples are carboxymethylcellulose, poly(vinyl pyrrolidone), poly(ethylene glycol), poly(vinyl alcohol), poly(vinyl pyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic acid / acrylic acid copolymers and lauryl methacrylate / acrylic acid copolymers and amphiphilic polymers.

[0334] Amphiphilic cleaning polymers

[0335] Preferably, the amphiphilic cleaning polymer is a compound having the following general structure: bis((C2H5O)(C2H4O)n)(CH3)-N + -C x H 2x -N +-(CH3)-bis((C2H5O)(C2H4O)n), wherein n=20 to 30, and x=3 to 8, or sulfated or sulfonated versions thereof.

[0336] The amphiphilic alkoxylated grease cleaning polymers of the present invention refer to any alkoxylated polymers having balanced hydrophilic and hydrophobic properties, enabling them to remove grease particles from fabrics and surfaces. Specific embodiments of the amphiphilic alkoxylated grease cleaning polymers of the present invention comprise a core structure and a plurality of alkoxylate groups attached to the core structure. These may include alkoxylated polyalkyleneimines, preferably having inner polyethylene oxide blocks and outer polypropylene oxide blocks.

[0337] The core structure may comprise a polyalkyleneimine structure comprising repeating units of formula (I), (II), (III) and (IV) in condensed form:

[0338]

[0339] wherein # represents in each case two adjacent nitrogen atoms and a radical A of a repeating unit of the formula (I), (II), (III) or (IV) 1 In each case, * represents one-half of the bonds to one of the alkoxylate groups; and A 1 independently selected from linear or branched C2-C6-alkylene; wherein the polyalkyleneimine structure consists of 1 repeating unit of formula (I), x repeating units of formula (II), y repeating units of formula (III) and y+1 repeating units of formula (IV), wherein in each case, x and y have a value in the range of 0 to about 150; wherein the average weight average molecular weight Mw of the polyalkyleneimine core structure is a value in the range of about 60 g / mol to about 10,000 g / mol.

[0340] The core structure may alternatively comprise a polyalkanolamine structure of at least one condensation product of a compound selected from the group consisting of N-(hydroxyalkyl)amines of formula (Ia) and / or (Ib),

[0341]

[0342] wherein A is independently selected from C1-C6-alkylene; R 1 , R 1 *、R 2 , R 2 *、R 3 , R 3 *、R 4 , R 4 *、R 5 and R 5* is independently selected from hydrogen, alkyl, cycloalkyl or aryl, wherein the last three mentioned groups may be optionally substituted; and R 6 is selected from hydrogen, alkyl, cycloalkyl or aryl, wherein the last three mentioned radicals may be optionally substituted.

[0343] The plurality of alkyleneoxy groups attached to the core structure are independently selected from alkyleneoxy units of formula (V)

[0344]

[0345] wherein in each case * represents one half of the bonds to the nitrogen atom of the repeating unit of formula (I), (II) or (IV); in each case A 2 A is independently selected from 1,2-propylene, 1,2-butene and 1,2-isobutylene; 3 is 1,2-propylene; at each occurrence, R is independently selected from hydrogen and C1-C4-alkyl; m has an average value in the range of 0 to about 2; n has an average value in the range of about 20 to about 50; and p has an average value in the range of about 10 to about 50.

[0346] Specific embodiments of the amphiphilic alkoxylated grease cleaning polymer can be selected from alkoxylated polyalkyleneimines having inner polyethylene oxide blocks and outer polypropylene oxide blocks, having a degree of ethoxylation and a degree of propoxylation not higher or lower than specific limits. The alkoxylated polyalkyleneimines preferably have a minimum ratio of polyethylene blocks to polypropylene blocks (n / p) of about 0.6 and a ratio of about 1.5 (x+2y+1) 1 / 2 The maximum ratio of n / p has been found to be about 0.8 to about 1.2 (x+2y+1) 1 / 2 The alkoxylated polyalkyleneimines have particularly advantageous properties. The alkoxylated polyalkyleneimines may have a main chain consisting of primary, secondary and tertiary amino nitrogen atoms, which are connected to each other by alkylene groups A and are randomly arranged. The primary amino moieties of the main chain and side chains of the polyalkyleneimine main chain that start or terminate and whose remaining hydrogen atoms are subsequently replaced by alkyleneoxy units are referred to as repeating units of formula (I) or (IV), respectively. The secondary amino moieties of the remaining hydrogen atoms that are subsequently replaced by alkyleneoxy units are referred to as repeating units of formula (II). The tertiary amino moieties that branch the main chain and side chains are referred to as repeating units of formula (III).

[0347] The polyalkyleneimine backbone consisting of nitrogen atoms and groups A preferably has an average molecular weight Mw of about 60 g / mol to about 10,000 g / mol, preferably about 100 g / mol to about 8,000 g / mol, and more preferably about 500 g / mol to about 6,000 g / mol.

[0348] The sum of (x+2y+1) corresponds to the total number of alkyleneimine units present in one single polyalkyleneimine backbone and is thus directly related to the molecular weight of the polyalkyleneimine backbone. However, the values ​​given in the specification relate to the quantitative mean of all polyalkyleneimines present in the mixture. The sum of (x+2y+2) corresponds to the total number of amino groups present in one single polyalkyleneimine backbone.

[0349] The group A attached to the amino nitrogen atom may be identical or different, linear or branched C2-C6-alkylene groups, such as 1,2-ethylene, 1,2-propylene, 1,2-butylene, 1,2-isobutylene, 1,2-pentylene, 1,2-hexylene or hexamethylene. Preferred branched alkylene groups are 1,2-propylene. Preferred linear alkylene groups are ethylene and hexanediol. More preferred alkylene groups are 1,2-ethylene.

[0350] The hydrogen atoms of the primary and secondary amino groups in the main chain of the polyalkyleneimine are substituted by alkyleneoxy units of the formula (V).

[0351]

[0352] In the formula, the variables preferably have one of the meanings given below:

[0353] In each case, A 2 is selected from 1,2-propylene, 1,2-butene and 1,2-isobutene; preferably, A 2 A is 1,2-propylene. 3 is 1,2-propylene; R is in each case selected from hydrogen and C1-C4-alkyl, such as methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl and tert-butyl; preferably, R is hydrogen. In each case, the index m has a value of 0 to about 2; preferably, m is 0 or about 1; more preferably, m is 0. The index n has an average value in the range of about 20 to about 50, preferably in the range of about 22 to about 40, and more preferably in the range of about 24 to about 30. The index p has an average value in the range of about 10 to about 50, preferably in the range of about 11 to about 40, and more preferably in the range of about 12 to about 30. Preferably, the alkyleneoxy units of formula (V) are non-random sequences of alkoxylate blocks. A non-random sequence refers to the addition of [-A 2 -O-] m (i.e. the bond closest to the nitrogen atom of the repeating unit of formula (I), (II) or (III)), followed by the addition of [-CH2-CH2-O-] n , and the third time added [-A 3 -O-] pThis orientation provides an alkoxylated polyalkylene imine having an inner polyethylene oxide block and an outer polypropylene oxide block. The major part of these alkyleneoxy units of formula (V) consists of oxyethylene units -[CH2-CH2-O)] n - and oxypropylene units -[CH2-CH2(CH3)-O] p -formed. The alkyleneoxy units may also additionally have a small proportion of oxypropylene or oxybutylene units -[A 2 -O] m -, that is, the hydrogen atom-saturated polyalkyleneimine backbone may initially react (i.e., incipient alkoxylation) with up to about 2 mol, especially about 0.5 mol to about 1.5 mol, specifically about 0.8 mol to about 1.2 mol, of propylene oxide or butylene oxide per mole of NH- ​​moieties contained.

[0354] The amphiphilic alkoxylated grease cleaning polymer is preferably present in the cleaning composition of the present invention at a level ranging from about 0.05% to 10% by weight based on the weight of the fabric and home care product. Embodiments of fabric and home care products may contain from about 0.1% to about 5% by weight. More specifically, these embodiments may contain from about 0.25% to about 2.5% of the grease cleaning polymer.

[0355] Carboxylate polymers - The cleaning compositions of the present invention may also include one or more carboxylate polymers, such as maleate / acrylate random copolymers or polyacrylate homopolymers. In one aspect, the carboxylate polymer is a polyacrylate homopolymer having a molecular weight of 4,000Da to 9,000Da, or 6,000Da to 9,000Da.

[0356] Detergent Polymers - The cleaning compositions of the present invention may also contain one or more detergent polymers having a structure defined by one of the following structures (I), (II), or (III):

[0357] (I)-[(OCHR 1 -CHR 2 ) a -O-OC-Ar-CO-] d

[0358] (II)-[(OCHR 3 -CHR 4 ) b -O-OC-sAr-CO-] e

[0359] (III)-[(OCHR 5 -CHR 6 ) c -OR7 ] f

[0360] in:

[0361] a, b and c are 1 to 200;

[0362] d, e and f are 1 to 50;

[0363] Ar is 1,4-substituted phenylene;

[0364] sAr is 1,3-substituted phenylene substituted at position 5 with SO3Me;

[0365] Me is Li, K, Mg / 2, Ca / 2, Al / 3, ammonium, monoalkylammonium, dialkylammonium, trialkylammonium or tetraalkylammonium, wherein the alkyl group is C1-C 18 Alkyl or C2-C 10 Hydroxyalkyl or mixtures thereof;

[0366] R 1 , R 2 , R 3 , R 4 , R 5 and R 6 Independently selected from H or C1-C 18 n-alkyl or C1-C 18 isoalkyl; and

[0367] R 7 A straight or branched C1-C 18 Alkyl, or straight or branched C2-C 30 alkenyl, or a cycloalkyl group having 5 to 9 carbon atoms, or a C8-C 30 Aryl group, or C6-C 30 Arylalkyl group.

[0368] Suitable soil release polymers are polyester soil release polymers such as Repel-o-tex polymers, including Repel-o-tex SF, SF-2 and SRP6 supplied by Rhodia. Other suitable soil release polymers include Texcare polymers, including Texcare SRA100, SRA300, SRN100, SRN170, SRN240, SRN300 and SRN325 supplied by Clariant. Other suitable soil release polymers are Marloquest polymers, such as Marloquest SL supplied by Sasol.

[0369] Cellulosic polymers - The cleaning compositions of the present invention may also include one or more cellulosic polymers, including those selected from the group consisting of alkyl celluloses, alkyl alkoxyalkyl celluloses, carboxyalkyl celluloses, alkyl carboxyalkyl celluloses. In one aspect, the cellulosic polymer is selected from the group consisting of carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixtures thereof. In one aspect, the carboxymethyl cellulose has a degree of carboxymethyl substitution of 0.5 to 0.9 and a molecular weight of 100,000 Da to 300,000 Da.

[0370] The detergent may comprise a bleaching system which may comprise a H2O2 source such as a perborate or a percarbonate which may be mixed with a peracid-forming bleach activator such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate. Alternatively, the bleaching system may comprise a peroxyacid such as an amide, imide, or sulfone peroxyacid. Generally speaking, when a bleaching agent is used, the compositions of the present invention may comprise from about 0.1% to about 50% or even from about 0.1% to about 25% of a bleaching agent by weight of the subject cleaning composition.

[0371] Chelating agent - The cleaning compositions herein may contain a chelating agent. Suitable chelating agents include copper, iron and / or manganese chelating agents, and mixtures thereof. When a chelating agent is used, the subject cleaning composition may contain from about 0.005% to about 15%, or even from about 3.0% to about 10%, by weight of the subject cleaning composition. Suitable chelating agents include DTPA (diethylenetriaminepentaacetic acid), HEDP (hydroxyethanediphosphonate), DTPMP (cyclobutanetriaminepenta(methylenephosphonic acid)), 1,2-dihydroxybenzene-3,5-disulfonic acid disodium salt hydrate, ethylenediamine, cyclobutanetriamine, ethylenediaminedisuccinic acid (EDDS), N-hydroxyethylethylenediaminetriacetic acid (HEDTA), triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (EDTP) and derivatives thereof.

[0372] The enzyme variants of the present invention can be stabilized using conventional stabilizers and / or protease inhibitors such as polyols (such as propylene glycol or glycerol, sugars or sugar alcohols), salts (such as sodium chloride and potassium chloride), lactic acid, formic acid, boric acid or boric acid derivatives (such as aromatic boric acid esters, or phenylboronic acid derivatives such as 4-formylphenylboronic acid), or peptide aldehydes (such as dipeptide aldehydes, tripeptide aldehydes or tetrapeptide aldehydes or aldehyde analogs) (any of the B1-BO-R form, wherein R is H, CH3, CX3, CHX2 or CH2X (X = halogen)). ), B0 is a single amino acid residue (preferably with optionally substituted aliphatic or aromatic side chains); and B1 consists of one or more amino acid residues (preferably one, two or three amino acid residues), optionally comprising an N-terminal protecting group, or as described in WO09118375, WO98 / 13459), or a proteinaceous type protease inhibitor such as RASI, BASI, WASI (bifunctional α-amylase / subtilisin inhibitor of rice, barley and wheat) or CI2 or SSI. In some embodiments, the enzyme used herein is stabilized by a water-soluble zinc (II), calcium (II) and / or magnesium (II) ion and other metal ions (e.g. barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II) and vanadium (IV)) source present in the finished composition that can provide the enzyme.

[0373] The composition may comprise an enzyme stabilizer selected from the group consisting of: (a) an inorganic salt selected from the group consisting of calcium salts, magnesium salts and mixtures thereof; (b) a carbohydrate selected from the group consisting of oligosaccharides, polysaccharides and mixtures thereof; (c) a highly effective reversible protease inhibitor selected from the group consisting of phenylboronic acid and its derivatives; and (d) a mixture thereof.

[0374] The composition may include: (1) a reversible protease inhibitor, such as a boron-containing compound; (2) 1-2 propanediol; (3) calcium formate and / or sodium formate; and (4) any combination thereof.

[0375] The cleaning composition may also contain other conventional detergent ingredients (as cleaning adjuvants), such as fabric conditioners, including clays, foam boosters, foam suppressants, corrosion inhibitors, soil suspension agents, anti-soil redeposition agents, dyes, bactericides, fluorescent whitening agents, hydrotropes, discoloration inhibitors, organic solvents (such as ethanol) or perfumes. In addition, the cleaning detergent may contain pre-drip agents or synergists, which are added to the wash to enhance the general cleaning level, and some of these additives may also be used as pre-treatment agents applied to the textile before the washing step.

[0376] It is currently contemplated that in the cleaning composition, any enzyme (particularly the enzymes essential to the present invention) may be added in an amount corresponding to 0.001 mg to 100 mg of enzyme protein per liter of wash liquid, preferably 0.005 mg to 5 mg of enzyme protein per liter of wash liquid, more preferably 0.01 mg to 1 mg of enzyme protein per liter of wash liquid, and particularly 0.1 mg to 1 mg of enzyme protein per liter of wash liquid. However, the composition of the present invention comprises at least 0.0001% to about 0.1% by weight of pure enzyme protein, such as about 0.0001% to about 0.01%, about 0.001% to about 0.01% or about 0.001% to about 0.01%. However, when formulated enzymes are used, the cleaning composition comprises from about 0.02 wt % to about 20 wt % of the formulated enzymes, for example, or from about 0.05 wt % to about 15 wt %, or from about 0.05 wt % to about 20 wt %, or from about 0.05 wt % to about 5 wt %, or from about 0.05 wt % to about 3 wt %.

[0377] How to use

[0378] The present invention includes methods for cleaning and / or treating surfaces (preferably fabrics). In one aspect, such methods include the steps of optionally washing and / or rinsing the surface, contacting the surface with an aqueous wash liquor comprising a cleaning composition as described herein, and then optionally washing and / or rinsing the surface.

[0379] The aqueous wash liquor preferably has a pH of from about 4 or about 7 or 8 to about 12, preferably to about 10.5. The composition is preferably used at a concentration of from about 500 ppm to about 15,000 ppm in solution. The water temperature is typically in the range of from about 5°C to about 90°C. The water to fabric ratio is typically from about 1:1 to about 30:1.

[0380] The present invention also provides the use of a cleaning composition of the present invention in detergent applications, such as dishwashing or laundry washing at low temperatures to provide improved cleaning performance.

[0381] In another aspect, the present invention relates to a method for removing stains from a surface, the method comprising contacting the surface with a hybrid polypeptide or amylase variant as described herein and a cleaning adjunct, wherein the cleaning adjunct comprises a surfactant and optionally one or more cleaning aids, the cleaning adjunct being selected from the list comprising: hydrotropes, builders and co-builders, bleaching systems, polymers, fabric hueing agents and adjunct materials, or any mixture thereof in detergent compositions and in detergent applications. Another aspect is a method for removing stains from a surface, the method comprising contacting the surface with a cleaning composition as described herein.

[0382] The present invention is further described by the following examples, which should not be construed as limiting the scope of the invention.

[0383] Example

[0384] Determination

[0385] Assay I: DNase activity test

[0386] Deoxyribonuclease activity was measured on a DNase test agar (BD, Franklin Lakes, NJ, USA) with methyl green prepared according to the supplier's manual. In short, 21 g of agar was dissolved in 500 ml of water and then autoclaved at 121 ° C for 15 minutes. The autoclaved agar was warmed to 48 ° C in a water bath, and 20 ml of agar was poured into a culture dish and solidified by incubation overnight at room temperature. On the solidified agar plate, 5 μl of enzyme solution was added, and the DNase activity was observed as a colorless area around the spot enzyme solution.

[0387] Assay II: DNase activity test

[0388] Deoxyribonuclease activity was determined using the DNaseAlert™ kit (11-02-01-04, IDT Intergrated DNA Technologies) according to the supplier's manual. Briefly, 95 μl of the deoxyribonuclease sample was mixed with 5 μl of substrate in a microtiter plate and fluorescence was immediately measured using a Clariostar microtiter reader from BMG Labtech (536 nm excitation, 556 nm emission).

[0389] Assay III: α-amylase activity test

[0390] The alpha-amylase activity can be determined by a method using a G7-pNP substrate. G7-pNP is the abbreviation of 4,6-ethylene (G7)-p-nitrophenyl (G1)-α, D-maltoheptaglycoside, a capped oligosaccharide that can be cleaved by an endoamylase such as an alpha-amylase. After cleavage, the alpha-glucosidase contained in the kit digests the hydrolyzed substrate, further releasing the free PNP molecules in yellow, and can therefore be measured by visible light spectrophotometry at λ=405nm (400nm-420nm). The kit containing the G7-pNP substrate and alpha-glucosidase is manufactured by Roche / Hitachi (Catalog No. 11876473). The G7-pNP substrate from the kit contains 22mM 4,6-ethylene-G7-pNP and 52.4mM HEPES (2-[4-(2-hydroxyethyl)-1-piperazinyl]-ethanesulfonic acid), pH 7.0. α-Glucosidase reagent contains 52.4 mM HEPES, 87 mM NaCl, 12.6 mM MgCl2, 0.075 mM CaCl2, ≥ 4 kU / L α-glucosidase. Prepare substrate working solution by mixing 1 mL of α-glucosidase reagent with 0.2 mL of G7-pNP substrate. Prepare this substrate working solution immediately before use. Dilution buffer: 50 mM MOPS, 0.05% (w / v) Triton X100 (polyethylene glycol p-(1,1,3,3-tetramethylbutyl)-phenyl ether (C 14 H 22 O(C2H4O) n (n=9-10))), 1 mM CaCl2, pH 8.0. The amylase sample to be analyzed is diluted in dilution buffer to ensure a pH of 7 in the diluted sample. The assay is performed by transferring 20 μl of the diluted enzyme sample to a 96-well microtiter plate and adding 80 μl of substrate working solution. The solution is mixed and pre-incubated at room temperature for 1 minute and the absorption is measured every 20 seconds for 5 minutes at OD 405nm. The slope of the time-dependent absorption curve (absorbance / minute) is proportional to the specific activity (activity per mg of enzyme) of the α-amylase in question under the given conditions. The amylase sample should be diluted to a level where the slope is below 0.4 absorbance units / minute.

[0391] Assay IV: Cellulase activity test

[0392] The AZCL-He-cellulose (azapurine dye covalently cross-linked cellulose) assay is used to detect cellulase (endoglucanase) activity. AZCL-He-cellulose (75 mg) is suspended in 15 mL of detergent (e.g., Type A detergent). 100 μL of enzyme (0.09 mg enzyme protein / mL) is added to 1 mL of this solution in an Eppendorf tube and incubated at 40° C. for 15 minutes while shaking at 1250 rpm in a preheated thermomixer and rotating at 13200 rpm for 2 minutes. 250 μL of the solution is transferred to a microtiter plate and the sample absorbance is measured at 590 nm.

[0393] Assay V: Lipase activity test

[0394] The lipase was diluted to the specified concentration with buffer (10 mM succinic acid + 2 mM CaCl2 + 0.02% Brij 35, adjusted to pH 6.5). 10 μL of 100 ppm lipase solution was added to 90 μL of detergent composition, stirred for 5 minutes and sealed. The samples were stored in detergent D002 at 4°C (unstressed) and in detergent D002 at 47°C (stressed). The storage time was 335.5 hours. After storage, possible condensed liquid was collected by centrifugation. 235 μL of buffer (0.1 M Tris-HCl, 9 mM CaCl2, 0.0225% Brij-30, pH 8.0 + 0.85% 4-FBPA (31.5 g / l)) was added to 100 μL of stressed or unstressed samples, corresponding to a 3.35-fold dilution. After stirring for 10 minutes, a 5 μL sample aliquot was further diluted 60 times with the same buffer. Then a part of this lipase dilution was mixed with four parts of 0.5mM pNP-palmitate, 1mM calcium chloride, 100mM Tris (pH8.0), 6.5mM deoxycholate, 1.4g / L AOS, and the 30 minutes release of the pNP chromophore was measured by spectrophotometry. This is used for measuring activity via the initial linear slope of the reaction. The residual activity was calculated as the ratio of the measurement speed of the stressed and unstressed sample. The median of the residual activity was calculated based on four replicates, and was normalized by using each experimental group as a lipase variant reference run.

[0395] Assay VI: Mannanase activity test

[0396] Mannanase activity can be tested according to standard test procedures known in the art, for example by applying the solution to be tested to wells of 4 mm diameter punched out in an agar plate containing 0.2% AZCL galactomannan (carob bean gum), i.e. the substrate for the determination of endo-1,4-β-D-mannanase, which can be purchased from the company Megazyme under the trade name Cat No. I-AZGMA (website of Megazyme: http: / / www.megazyme.com / Purchase / index.html).

[0397] Assay VII: Protease activity test

[0398] Proteolytic activity can be measured by a method using Suc-AAPF-PNA as a substrate. Suc-AAPF-PNA is an abbreviation for N-succinyl-alanine-alanine-proline-phenylalanine-p-nitroaniline, and is a closed peptide that can be cleaved by an endoprotease. After cleavage, free PNA molecules in yellow are released, and therefore can be measured at a wavelength of 405nm by visible light spectrophotometry. Suc-AAPF-PNA substrates are manufactured by Bachem (Catalog No. L1400, dissolved in DMSO). The protease sample to be analyzed is diluted in a residual activity buffer (100mM Tris pH 8.6). The enzyme sample is transferred to a 96-well microtiter plate and 70μl of substrate working solution (0.72mg / ml in 100mM Tris pH8.6) is added for determination. The solution is mixed at room temperature, and at OD 405nm, absorption is measured every 20 seconds within 5 minutes. The slope of the time-dependent absorbance curve (absorbance / minute) is directly proportional to the activity of the protease in question under the given conditions. The protease sample is diluted to a level at which the slope is linear.

[0399] Cleaning Composition Examples

[0400] Example 1 to Example 6

[0401] Granular laundry detergent compositions designed for use in hand or top loading washing machines.

[0402]

[0403]

[0404] *Amylase amounts are each indicated as mg of active enzyme per 100 g of detergent.

[0405] ** DNase (according to one of the examples described in claim 11; mg of active enzyme per 100 g of detergent.)

[0406] Example 7 to Example 12

[0407] A granular laundry detergent composition designed for use in a front-loading automatic washing machine.

[0408]

[0409]

[0410] *Amylase amounts are each indicated as mg of active enzyme per 100 g of detergent.

[0411] ** DNase (according to one of the examples described in claim 11; mg of active enzyme per 100 g of detergent.)

[0412] Example 13 to Example 18 Heavy-duty liquid laundry detergent compositions

[0413]

[0414]

[0415] 1 The random graft copolymer is a polyethylene oxide copolymer grafted with polyvinyl acetate, which has a polyethylene oxide main chain and a plurality of polyvinyl acetate side chains. The molecular weight of the polyethylene oxide main chain is about 6000, and the weight ratio of polyethylene oxide to polyvinyl acetate is about 40 to 60, and there is no more than 1 grafting point per 50 ethylene oxide units.

[0416] 2 Polyethyleneimine (MW=600) with 20 ethoxylated groups per -NH.

[0417] 3 The amphiphilic alkoxylated grease cleaning polymer is polyethyleneimine (MW=600) with 24 ethoxylated groups per -NH and 16 propoxylated groups per -NH

[0418] *Amylase and DNase (one of the DNases from claim 11) amounts are indicated as mg of active enzyme per 100 g of detergent.

[0419] Example 19 to Example 21 Heavy-duty liquid laundry detergent compositions

[0420]

[0421]

[0422] *Amylases are shown as milligrams of active enzyme per 100 g of detergent.

[0423] **Not to exceed 7% water by weight of the total cleaning and / or treatment composition.

[0424] Raw Materials and Instructions for Cleaning Composition Examples 1 to 21

[0425] With C 11 -C 18 Average aliphatic carbon chain length linear alkylbenzene sulfonate

[0426] C 12-18 Dimethyl Hydroxyethyl Ammonium Chloride

[0427] AE3S is C 12-15 Alkyl ethoxy (3) sulfate

[0428] AE7 is C 12-15 Alcohol ethoxylate, average degree of ethoxylation 7

[0429] AE9 is C 12-16 Alcohol ethoxylate, average degree of ethoxylation 9

[0430] HSAS is a middle branched primary alkyl sulfate having a carbon chain length of about 16-17 as disclosed in US 6,020,303 and US 6,060,443

[0431] Polyacrylate MW 4500 was supplied by BASF. Carboxymethyl cellulose was supplied by CP Kelco (Arnhem, Netherlands). V

[0432] CHEC is a cationically modified hydroxyethyl cellulose polymer.

[0433] Phosphonate chelating agents are, for example, diethylenetetraaminepentaacetic acid (DTPA) hydroxyethane diphosphate (HEDP)

[0434] Celluclean TM , and All are products of Novozymes (Bagsvaerd, Denmark).

[0435] Purafect It is a product of Genencor International (Palo Alto, California, USA)

[0436] Fluorescent brightener 1 is AMS, fluorescent brightener 2 is CBS-X, Direct Purple 9 is Violet BN-Z NOBS is sodium nonanoyloxybenzene sulfonate

[0437] TAED is tetraacetylethylenediamine

[0438] S-ACMC is carboxymethyl cellulose conjugated with CI Reactive Blue 19 product name AZO-CM-CELLULOSE

[0439] Detergent is PF

[0440] The molecular weight of the acrylic acid / maleic acid copolymer is 70,000 and the ratio of acrylate to maleate is 70:30

[0441] EDDS is the sodium salt of ethylenediamine-N,N'-disuccinic acid. (S,S) isomer antifoam agglomerates are provided by Dow Corning, Midland, Michigan, USA. HSAS is a mid-branched alkyl sulfate.

[0442] Violet CT provided by Milliken, Spartanburg, South Carolina, USA

[0443] 1 The random graft copolymer is a polyethylene oxide copolymer grafted with polyvinyl acetate, which has a polyethylene oxide main chain and a plurality of polyvinyl acetate side chains. The molecular weight of the polyethylene oxide main chain is about 6000, and the weight ratio of polyethylene oxide to polyvinyl acetate is about 40 to 60, and there is no more than 1 grafting point per 50 ethylene oxide units.

[0444] 2 Polyethyleneimine (MW=600) with 20 ethoxylated groups per -NH.

[0445] 3 The amphiphilic alkoxylated polymer was polyethyleneimine (MW 600) prepared from a polymer derivatized to contain 24 ethoxylate groups per -NH and 16 propoxylate groups per -NH.

[0446] Amylase 4 Any one of a) to k) herein (mg active protein).

[0447] Example 22 to Example 26 Unit dose laundry detergent composition Such unit dose formulations may comprise one or more compartments.

[0448]

[0449]

[0450] *Amylases of the present invention are expressed as milligrams of active enzyme per 100 g of detergent.

[0451] 1 Polyethyleneimine (MW=600) with 20 ethoxylated groups per -NH.

[0452] Embodiment 27 Multi-compartment unit dose composition

[0453] The multi-compartment unit dose laundry detergent formulations of the present invention are provided below. In these examples, the unit dose has three compartments, but similar compositions can be made with two, four or five compartments. The film used to encapsulate the compartments is polyvinyl alcohol.

[0454]

[0455] Multi-compartment formula

[0456]

[0457]

[0458] * The deoxyribonucleases of the present invention are shown in all examples as milligrams of active enzyme per 100 g of detergent unless otherwise stated for a specific example.

[0459] The dimensions and values ​​disclosed herein are not to be understood as being strictly limited to the exact numerical values ​​cited. Instead, unless otherwise indicated, each such dimension is intended to represent the stated value and a functionally equivalent range around that value. For example, a dimension disclosed as "40 mm" is intended to mean "about 40 mm".

[0460] The scope of the present invention as described herein and protected by the claims is not limited by the specific aspects disclosed herein, as these aspects are intended to illustrate several aspects of the present invention. Any equivalent aspects are intended to be included within the scope of the present invention. In fact, various modifications of the present invention will become apparent to those skilled in the art from the foregoing description, in addition to those shown and described herein. Such modifications are also intended to fall within the scope of the appended claims. In the event of a conflict, the present disclosure and the definitions included therein will prevail.

Claims

1. A cleaning composition comprising: (i) a deoxyribonuclease as shown in SEQ ID NO: 1; (ii) at least one additional enzyme, wherein the at least one additional enzyme is selected from the group consisting of: mannanase, amylase, cellulase, lipase, protease and mixtures thereof, wherein the at least one additional enzyme comprises the mannanase of SEQ ID NO: 15; and (iii) a cleaning aid, wherein the cleaning aid comprises a surfactant.

2. The composition of claim 1, wherein the at least one additional enzyme further comprises A mannanase belonging to the glycoside hydrolase family 26 mannanase selected from the group consisting of; i. the mannanase shown in SEQ ID NO: 16; ii. mannanase shown in SEQ ID NO: 17; iii. mannanase shown in SEQ ID NO: 18; iv. mannanase shown in SEQ ID NO: 19; v. Mannanase shown in SEQ ID NO: 20; vi. mannanase shown in SEQ ID NO: 21; vii. Mannanase shown in SEQ ID NO: 22; viii. mannanase shown in SEQ ID NO: 23; ix. mannanase shown in SEQ ID NO: 24; x. the mannanase shown in SEQ ID NO: 33; and xi. mannanase shown in SEQ ID NO: 34; and mixtures thereof.

3. A cleaning composition according to claim 1 or claim 2, wherein the amount of deoxyribonuclease in the composition is from 0.01 ppm to 1000 ppm and the amount of the or each additional enzyme is from 0.01 ppm to 1000 ppm.

4. The cleaning composition of claim 1, wherein the additional enzyme comprises an amylase, and the amylase is selected from the group consisting of: a) an amylase shown in SEQ ID NO: 2 or SEQ ID NO: 35; b) an amylase shown in SEQ ID NO: 3; c) an amylase represented by SEQ ID NO: 4; d) an amylase represented by SEQ ID NO: 5; e) an amylase represented by SEQ ID NO: 6; f) an amylase represented by SEQ ID NO: 7; g) an amylase represented by SEQ ID NO: 8; h) an amylase represented by SEQ ID NO: 9; and i) mixtures thereof.

5. The composition of claim 1, wherein the additional enzyme comprises a cellulase, and wherein the cellulase is selected from the group consisting of: a) the cellulase shown in SEQ ID NO: 10; b) a cellulase represented by SEQ ID NO: 11; c) Cellulase shown in SEQ ID NO: 12 d) a cellulase represented by SEQ ID NO: 13, e) a cellulase as shown in SEQ ID NO: 31, and f) a cellulase as shown in SEQ ID NO: 32; and g) mixtures thereof.

6. The composition of claim 1, wherein the additional enzyme comprises a lipase, wherein the lipase is the lipase set forth in SEQ ID NO:

14.

7. The composition of claim 1, wherein the additional enzyme comprises a protease, and wherein the protease is selected from the group consisting of: a) the protease represented by SEQ ID NO: 25, obtained from Bacillus lentus; b) the protease shown in SEQ ID NO: 26; obtained from Bacillus amyloliquefaciens; c) the protease represented by SEQ ID NO: 27, obtained from Bacillus sp.; d) the protease represented by SEQ ID NO: 28, obtained from Bacillus gibsonii; e) the protease represented by SEQ ID NO: 29, obtained from Bacillus lentus; f) the protease represented by SEQ ID NO: 30, obtained from Bacillus licheniformis; and g) mixtures thereof. 8 . The cleaning composition according to claim 1 , comprising an anionic surfactant and a nonionic surfactant, wherein the weight ratio of the anionic surfactant to the nonionic surfactant is 50:1 to 1:

2. 9 . The cleaning composition according to claim 8 , wherein the weight ratio of the anionic surfactant to the nonionic surfactant is 30:1 to 1:

1.

10. The cleaning composition of claim 1, wherein the cleaning adjunct further comprises an additional enzyme selected from the group consisting of pectinase, xanthanase, hexosaminidase, laccase, and catalase, or any mixture thereof.

11. The cleaning composition of claim 10, wherein the pectinase is a pectin lyase.

12. The cleaning composition of claim 10, wherein the xanthanase is a xanthan lyase.

13. The cleaning composition of claim 1, wherein the cleaning composition is in the form of a liquid composition.

14. The cleaning composition of claim 1, wherein the cleaning composition is in the form of a laundry cleaning composition.

15. The cleaning composition of claim 1, wherein the cleaning composition is in the form of a hard surface cleaning composition.

16. A method of treating a surface, the method comprising: (1) forming an aqueous washing liquid, wherein the aqueous washing liquid comprises: (i) a deoxyribonuclease as shown in SEQ ID NO: 1; (ii) at least one additional enzyme selected from the group consisting of amylases, cellulases, lipases, mannanases, proteases, and mixtures thereof, wherein the at least one additional enzyme comprises the mannanase of SEQ ID NO: 15; and a cleaning aid, wherein the cleaning aid comprises a surfactant; and water, (2) treating the surface with the aqueous washing liquid at a temperature of 10° C. to 40° C.; as well as (3) Rinse the surface.

17. The method of claim 16, wherein the surface is a fabric.

18. The method of claim 16, wherein the surface is treated with the aqueous washing liquid at a temperature of at most 35°C.

19. The method of claim 16, wherein the surface is treated with the aqueous washing liquid at a temperature of 30°C or less.

20. The method of claim 16, wherein the surface is treated with the aqueous washing liquid at a temperature of 20°C or less.

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