Use of cellulase for improvement of sustainability of detergents

Abstract

To provide detergent compositions with improved sustainability where the level of antiredeposition polymer is reduced by use of cellulase, optionally in combination with a DNase.SOLUTION: Use of a cellulase for improving a sustainability profile of a detergent composition is provided, where the cellulase, optionally in combination with at least one additional enzyme, improves the sustainability profile of the detergent composition, where the sustainability profile of the detergent composition is improved when one or more antiredeposition polymers of the detergent composition is replaced partly or fully by a biodegradable ingredient.SELECTED DRAWING: None

Description

[Technical Field]

[0001] Array list reference This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference.

[0002] The present invention relates to detergent compositions with improved sustainability in which the level of anti-redeposition polymers is reduced through the use of cellulase, optionally in combination with DNase. [Background technology]

[0003] The ability of a detergent to keep soil suspended is of great importance to its efficiency. Particulate soil that is not kept suspended by the detergent will redeposit on the fabric. Redeposited soil is known to be often more difficult to remove than the original soil, partly because of its smaller particle size. Since the ability of surfactants in detergents to keep soil suspended is often insufficient, anti-redeposition polymers are added to detergents. Avoiding redeposition by adding polymers helps prevent graying, dinginess, and yellowing of clothing, which are obviously of concern from the consumer's perspective. Summary of the Invention [Problem to be solved by the invention]

[0004] However, polymers have faced scrutiny due to environmental concerns because they are often derived from petrochemical resources, especially non-renewable sources, and are therefore unsustainable, poorly biodegradable, or even persistent in the environment. It would be desirable to provide alternatives with improved sustainability profiles while maintaining compatibility with other detergent ingredients. Additionally, customer benefits and performance effects must be maintained. [Means for solving the problem]

[0005] The petrochemical-derived polymers present in detergents are unsustainable because they are derived from non-renewable sources, and are poorly biodegradable or even persist in the environment. The inventors of the present invention have surprisingly found that by adding cellulase to partially or completely replace the polymers in detergents while maintaining the detergent's cleaning performance, it is possible to achieve a more sustainable detergent composition, i.e., a detergent composition with an improved sustainability profile. In contrast to polymers, which are produced from renewable agricultural sources, cellulase is naturally found in the environment and is easily biodegradable.

[0006] Replacing polymers with cellulases addresses the United Nations Sustainable Development Goals, particularly Goal 12, "Responsible Consumption and Production." Replacing polymers with cellulases allows detergent manufacturers, and ultimately end users, to transition from fossil feedstocks to renewable feedstocks and reduce the amount of persistent chemicals released into the environment. Therefore, the present invention discloses how polymers that reduce or remove soil redeposition from items during the wash cycle can be partially or completely replaced with cellulases to improve the sustainability profile of detergents. When the anti-redeposition polymer in detergents is reduced from 4% to 0.5% (by weight) through cellulase replacement, the amount of persistent fossil-based polymers that can be avoided in production, transportation, and environmental loss is estimated to be 490,000 tons per year.

[0007] definition Anti-redeposition polymers: In the context of the present invention, polymers include, but are not limited to, polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, methylcellulose, and / or combinations thereof.

[0008] Bacterial: In relation to a polypeptide (e.g., an enzyme such as cellulase), the term "bacterial" refers to a polypeptide that is encoded by, and therefore directly derivable from, the genome of a bacterium, provided that the bacterium has not been genetically modified to encode the polypeptide, such as by introducing a coding sequence into its genome by recombinant DNA technology. Thus, in the context of the present invention, the terms "bacterial cellulase" or "polypeptide having cellulase activity obtained from a bacterial source" or "polypeptide of bacterial origin" refer to a cellulase that is encoded by, and therefore directly derivable from, the genome of a bacterial species, provided that the bacterial species has not been genetically modified to introduce recombinant DNA encoding the cellulase. Thus, a nucleotide sequence encoding a bacterial polypeptide with cellulase activity is, by definition, a sequence in the genetic background of a bacterial species. A sequence encoding a bacterial polypeptide with cellulase activity may also be referred to as a wild-type cellulase (or parent cellulase). A bacterial polypeptide with cellulase activity includes a recombinantly produced wild-type. In a further aspect, the present invention provides a polypeptide with cellulase activity, provided that the polypeptide is substantially homologous to a bacterial cellulase. In the context of the present invention, the term "substantially homologous" refers to a polypeptide having cellulase activity that is at least 80%, preferably at least 85%, more preferably at least 90%, more preferably at least 95%, even more preferably at least 96%, 97%, 98%, and most preferably at least 99% identical to the amino acid sequence of a selected bacterial cellulase.

[0009] Cellulase: The term "cellulase" refers to one or more (e.g., several) enzymes that hydrolyze cellulosic materials. The two terms "polypeptide having cellulase activity" and "cellulase" are used interchangeably. The cellulase may be selected from the group consisting of cellulases belonging to GH5, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21, EC 3.2.1.91, and EC 3.2.1.172. Such enzymes include endoglucanases (e.g., EC 3.2.1.4), cellobiohydrolases, β-glucosidases, or combinations thereof.

[0010] Suitable cellulases include single and mixtures of enzymes of bacterial or fungal origin. Chemically or protein-modified mutants are also contemplated. The cellulase may be, for example, a single or mixture of single-component endo-1,4-β-glucanases, also called endoglucanases.

[0011] Suitable cellulases include those derived from the genera Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include fungal cellulases derived from Humicola insolens (U.S. Pat. No. 4,435,307) or from Trichoderma, e.g., T. reesei or T. viride. Other suitable cellulases are those from the genus Thielavia, such as Thielavia terrestris, as described in WO 96 / 29397, or fungal cellulases produced by Myceliophthora thermophila and Fusarium oxysporum, as disclosed in U.S. Patent Nos. 5,648,263, 5,691,178, 5,776,757, WO 89 / 09259, and WO 91 / 17244. Also suitable are cellulases from the genus Bacillus, as described in WO 02 / 099091 and JP 2000-210081. Suitable cellulases are alkaline or neutral cellulases with care benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940.Other examples are cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, U.S. Pat. No. 5,457,046, U.S. Pat. No. 5,686,593, U.S. Pat. No. 5,763,254, WO 95 / 24471, WO 98 / 12307.

[0012] Other cellulases are endo-β-1,4-glucanase enzymes having a sequence that is at least 97% identical to the amino acid sequence from position 1 to position 773 of SEQ ID NO:2 in WO 2002 / 099091, or family 44 xyloglucanases, which are xyloglucanase enzymes having a sequence that is at least 60% identical to positions 40 to 559 of SEQ ID NO:2 in WO 2001 / 062903.

[0013] Commercially available cellulases include Carezyme®, Carezyme® Premium, Celluzyme®, Celluclean®, Celluclast®, Endolase®, Renozyme®, Whitezyme®, Celluclean® Classic, Cellusoft® (Novozymes A / S), Puradax®, Puradax HA, and Puradax EG, Revitalenz 1000, Revitalenz 200, Revitalenz 2000 (Dupont Industrial Biosciences), KAC-500(B)™ (Kao Corporation), Biotouch DCL, and Biotouch FLX1 (AB enzymes).

[0014] Two basic approaches to measuring cellulolytic enzyme activity, reviewed in Zhang et al. (2006) Biotechnology Advances 24:452-481, include (1) measuring total cellulolytic enzyme activity and (2) measuring individual cellulolytic enzyme activities (endoglucanases, cellobiohydrolases, and β-glucosidases). Total cellulolytic enzyme activity can be measured using insoluble substrates such as Whatman No. 1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, and pretreated lignocellulose. The most common total cellulolytic activity assay is the filter paper assay, which uses Whatman No. 1 filter paper as the substrate. The assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987) Pure Appl. Chem. 59:257-68.

[0015] Color difference (L value): The Lab color space is an opponent color space with dimension L, which means lightness. * L * = 0 indicates the darkest black, and L * = 100 indicates the brightest white. In the context of the present invention, the L value is also called color difference.

[0016] Detergent Adjunct Ingredients: Detergent adjunct ingredients are distinct from the cellulase of the present invention. The exact nature of these additional adjunct ingredients, as well as their inclusion levels, can vary depending on the physical form of the composition and the type of application for which it is intended. Suitable adjunct ingredients include, but are not limited to, those described below, such as surfactants, builders, flocculating aids, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, brighteners, suds suppressors, dyes, fragrances, structural elastomers, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, defoamers, dispersants, processing aids, solvents, and / or pigments.

[0017] Detergent Composition: The term "detergent composition" refers to a composition useful for removing unwanted compounds from items to be cleaned, such as fabrics. Detergent compositions can be used in both domestic and institutional cleaning applications, for example, to clean fabrics. The term encompasses any materials / compounds selected for a particular type of desired cleaning composition and product form (e.g., liquid, gel, powder, granule, paste, bar, or spray composition), including, but not limited to, detergent compositions (e.g., liquid and / or solid laundry detergents and delicate detergents, fabric fresheners, fabric softeners, laundry boosters, and fabric and laundry pre-spotters / pre-treats). In addition to containing the enzymes of the present invention, the detergent formulations may contain one or more additional enzymes (e.g., proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, and mannanases, or mixtures of any of these), and / or detergent adjunct ingredients such as surfactants, builders, chelants or chelating agents, bleach systems or components, polymers (as defined herein), fabric conditioners, suds boosters, suds suppressors, dyes, fragrances, colorfastness inhibitors, optical brighteners, bactericides, mildewcides, soil suspending agents, corrosion inhibitors, enzyme inhibitors or stabilizers, enzyme activators, bluing and fluorescent dyes, antioxidants, and dissolving agents.

[0018] Enzyme Detergency Benefits: As used herein, the term "enzyme detergency benefit" is defined as the beneficial effect that an enzyme can add to a detergent compared to the same detergent without the enzyme. Important detergency benefits that enzymes can provide are stain removal with no or little visible soil after washing and / or cleaning (an effect also known as anti-redeposition), prevention or reduction of redeposition of soil liberated in the washing process (an effect also known as whitening), and complete or partial restoration of whiteness to fabrics that were originally white but have acquired a grayish or yellowish appearance after repeated use and washing. Also included is whiteness maintenance, e.g., prevention of graying or dullness. Textile care benefits not directly related to catalytic stain removal or soil redeposition prevention are also important to enzyme detergency benefits. Examples of such fabric treatment benefits are preventing or reducing dye transfer from one fabric to another or to other parts of the same fabric (an effect also known as dye transfer or back-soiling prevention); removing protruding or broken fibers from the fabric surface to reduce pilling or removing existing pilling or fuzz (an effect also known as anti-pilling); improving fabric softness; clarifying the color of the fabric; and removing particulate soils trapped in the fibers of the fabric or garment. Enzyme bleaching is a further enzyme detergency benefit, where catalytic activity is generally used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.

[0019] Fragment: The term "fragment" refers to a polypeptide having one or more (several) amino acids deleted from the amino and / or carboxyl terminus of a mature polypeptide or domain; wherein the fragment contains cellulase activity.

[0020] Fungal: In the context of the present invention, the term "fungal" with respect to a polypeptide (such as an enzyme, e.g., cellulase) refers to a polypeptide that is encoded by, and thus directly derivable from, the genome of a fungus, and such fungus has not been genetically modified to encode said polypeptide, for example, by introducing a coding sequence into its genome by recombinant DNA technology. Thus, in the context of the present invention, the term "fungal cellulase" or "polypeptide having cellulase activity obtained from a fungal source" refers to a cellulase that is encoded by, and thus directly derivable from, the genome of a fungal species, and such fungal species has not been subjected to genetic modification to introduce recombinant DNA encoding said cellulase. Thus, a nucleotide sequence encoding a fungal polypeptide having cellulase activity is a sequence that naturally occurs in the genetic background of a fungal species. A fungal polypeptide having cellulase activity encoded by such a sequence may also be referred to as a wild-type cellulase (or parent cellulase). In another aspect, the present invention provides a polypeptide having cellulase activity, wherein said polypeptide is substantially homologous to a fungal cellulase. In the context of the present invention, the term "substantially homologous" refers to a polypeptide having cellulase activity that is at least 80%, preferably at least 85%, more preferably at least 90%, more preferably at least 95%, even more preferably at least 96%, 97%, 98%, and most preferably at least 99% identical to the amino acid sequence of a selected fungal cellulase. Polypeptides that are substantially homologous to fungal cellulases may be included in detergents and / or used in methods of the present invention.

[0021] Host cell: The term "host cell" refers to any cell type that is susceptible to transformation, transfection, transduction, etc., with a nucleic acid construct or expression vector comprising a polynucleotide of the invention. The term "host cell" encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.

[0022] Improved cleaning performance: The term "improved cleaning performance" is defined herein as an enzyme that exhibits an increase in the cleaning performance of a detergent composition, for example, by increased soil removal or reduced redeposition, relative to the cleaning performance of the same detergent composition without the enzyme. The term "improved cleaning performance" encompasses cleaning performance in the laundry.

[0023] Isolated: The term "isolated" refers to a substance in a form or setting that does not occur in nature. Non-limiting examples of isolated substances include: (1) any non-naturally occurring substance; (2) any substance, including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide, or cofactor that is at least partially removed from one, more, or all of the natural components with which it is associated in nature; (3) any substance that has been artificially modified relative to the substance found in nature; or (4) any substance that has been modified by increasing the amount of the substance relative to other components with which it is associated in nature (e.g., recombinant production in a host cell; multiple copies of the gene encoding the substance; and use of a stronger promoter than that naturally associated with the gene encoding the substance). An isolated substance may be present in a fermentation broth sample; for example, the host cells may be genetically modified to express a polypeptide of the invention. The fermentation broth from the host cells may contain the isolated polypeptide.

[0024] Laundry: The term "laundering," in both domestic and commercial laundering, refers to the process of treating fabrics with a solution containing the cleaning or detergent composition of the present invention. The laundering process can be carried out, for example, using a domestic or commercial washing machine, or by hand.

[0025] Malodor: The term "malodor" refers to an undesirable odor on a clean item. A washed item should smell fresh and clean, without any malodor adhering to the item. One example of a malodor is a compound with an unpleasant odor that may be produced by a microorganism. Another example is an unpleasant odor that may be sweat or body odor adhering to an item that has been in contact with a human or animal. Another example of a malodor may be the odor from spices adhering to the item, such as curry or other foreign spices with a strong odor. One way to measure the extent to which an item has acquired a malodor is by using Assay II disclosed herein.

[0026] Mature Polypeptide: 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.

[0027] Mature polypeptide coding sequence: The term "mature polypeptide coding sequence" refers to a polynucleotide that encodes a mature polypeptide having cellulase activity.

[0028] Nucleic Acid Construct: The term "nucleic acid construct" refers to a nucleic acid molecule, either single-stranded or double-stranded, which is isolated from a naturally occurring gene or which has been modified to contain segments of nucleic acid in a manner not otherwise found in nature, or which is synthetic, and which includes one or more regulatory sequences.

[0029] Operably linked: The term "operably linked" refers to a construct in which control sequences are positioned in appropriate relation to a coding sequence of a polynucleotide so that the control sequences direct the expression of the coding sequence.

[0030] Sequence identity: The relatedness between two amino acid sequences or two nucleotide sequences is expressed by the parameter "sequence identity." For the purposes of the present invention, the degree of sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453), preferably as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16:276-277), version 5.0.0 or later. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output labeled "longest identity" (obtained using the -nobrief option) of Needle is used as the percentage identity, calculated as follows: (equivalent residues × 100) / (length of alignment − total number of gaps in the alignment)

[0031] For the purposes of the present invention, the degree of sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra), preferably as implemented in the Needle program of the EMBOSS package (EM-BOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), version 5.0.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version in NCBI NUC4.4) substitution matrix. The output of the Needle labelled "longest identity" (obtained using the -nobrief option) is used as the percentage identity, calculated as follows: (equivalent deoxyribonucleotides × 100) / (length of alignment − total number of gaps in alignment)

[0032] Sustainability: Sustainability and sustainable means the use of renewable resources that cause little or no damage to the environment and are biodegradable.

[0033] Sustainability Profile: In the context of the present invention, the term sustainability profile is used to compare the sustainability of ingredients (e.g., in a detergent composition) when one or more ingredients are able to replace other, less sustainable ingredients while maintaining the performance of the system (e.g., the performance of the detergent composition when washing items).

[0034] Fabric: The term "fabric" refers to any textile material, such as yarns, yarn intermediates, fibers, nonwoven materials, natural materials, synthetic materials, and any other textile material, fabrics made from these materials, and products (e.g., garments and other articles) made from textiles. Fabrics or textiles may be in the form of knits, wovens, denim, nonwovens, felts, yarns, and toweling. Fabrics may be natural cellulosic materials, including cotton, flax / linen, jute, ramie, sisal, or coir, or man-made cellulosic materials (e.g., derived from wood pulp), including viscose / rayon, cellulose acetate fibers (tricellular), lyocell, or blends thereof. Fabrics or textiles may also be non-cellulosic materials, such as natural polyamides, such as wool, camel, cashmere, mohair, rabbit, and silk, or synthetic polymers, such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulosic and non-cellulosic fibers. Examples of blends are blends of cotton and / or rayon / viscose with one or more companion 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, ramie, flax / linen, jute, cellulose acetate fibers, lyocell). The fabric may be, for example, a conventional washable laundry, such as a soiled domestic laundry. When the terms fabric or garment are used, the broader term textile is also included. In the context of the present invention, the term "textile" also encompasses textiles. In the context of the present invention, the term "textile" is used interchangeably with textile and cloth.

[0035] Used or Worn: As used herein with respect to fabrics, the term "used or worn" means fabrics that have been used or worn by a customer or that have come into contact with human skin during manufacture, retail, etc. A customer may be a purchaser of fabrics, for example, a person purchasing fabrics (e.g., new cloths or bed linens) in a store, or a business purchasing fabrics (e.g., bed linens, dish towels, or tablecloths) for use in a business, for example, a hotel, restaurant, professional kitchen, institution, hospital, etc. In some situations, such used or worn fabrics may have regular stains that have not been adequately washed away, as well as forming a gluing base that attracts and accumulates more airborne particulate matter.

[0036] Variant: The term "variant" refers to a polypeptide that has the same activity as a parent enzyme but contains modifications (i.e., substitutions, insertions, and / or deletions) at one or more (e.g., several) positions. A substitution refers to the replacement of an amino acid at a position with a different amino acid; a deletion refers to the removal of an amino acid at a position; and an insertion refers to the addition of an amino acid adjacent to and immediately following the amino acid at a position. In the context of the present invention, the identified cellulase variants retain the enzymatic activity of the parent, i.e., the ability to catalyze the hydrolytic cleavage of phosphodiester bonds in the DNA backbone (deoxyribonuclease activity). In one embodiment, the deoxyribonuclease activity of the variant is increased relative to the mature polypeptide of the parent cellulase, e.g., SEQ ID NO: 2.

[0037] Wash Cycle: The term "wash cycle" is defined herein as a washing operation in which fabrics are immersed in wash liquor, some mechanical action is applied to the fabric to release soil and promote the inflow and outflow of wash liquor into the fabric, and finally excess wash liquor is removed. After one or more wash cycles, the fabrics are typically rinsed and dried.

[0038] Washing Solution: The term "washing solution" is defined herein as a solution or mixture of water and detergent ingredients (optionally containing an enzyme of the present invention).

[0039] Washing Performance: The term "washing performance" is used as the ability of a detergent composition, enzyme, or polymer to remove stains present on the object being cleaned or to maintain the color and whiteness of the fabric during washing. The improvement in washing performance can be quantified by calculating the so-called Delta REM, which is described in the experimental section.

[0040] Weight percentage: abbreviated as w / w%, weight %, or w%. The abbreviations are used interchangeably.

[0041] Whiteness: The term "whiteness" is defined herein as a broad term that has different meanings in different fields and for different customers. Whiteness may refer to white fabrics or can be used interchangeably as brightness for colored fabrics. Loss of whiteness or brightness can be due, for example, to graying, yellowing, or removal of optical brighteners / hues. Graying and yellowing can be due to soil redeposition, spot redeposition, dust / mud redeposition, soil particles, body soils, staining by iron or copper ions, etc., or dye transfer. Loss of whiteness can include one or more items from the following list: colorant or dye action; incomplete stain removal (e.g., body soils, sebum, etc.); redeposition (graying, yellowing, or other discoloration of an object) (reattachment of removed soil to another part of the fabric, soiled or unsoiled); chemical changes in the fabric upon application; and color clarity or whitening.

[0042] Array Overview SEQ ID NO: 1 is a DNase obtained from Aspergillus oryzae. SEQ ID NO: 2 is a DNase obtained from Bacillus licheniformis. SEQ ID NO: 3 is a DNase obtained from Bacillus subtilis. SEQ ID NO: 4 is a DNase obtained from Serratia marcescens. SEQ ID NO: 5 is a DNase obtained from Bacillus idriensis. SEQ ID NO: 6 is a DNase isolated from Bacillus cibi. SEQ ID NO: 7 is a DNase obtained from Bacillus horikoshii. SEQ ID NO: 8 is a DNase obtained from a Bacillus species. SEQ ID NO: 9 is a DNase obtained from a Bacillus species. SEQ ID NO: 10 is a cellulase obtained from Humicola insolens. SEQ ID NO: 11 is a cellulase obtained from Bacillus akibai. SEQ ID NO: 12 is a cellulase obtained from Paenibacillus polymyxa. SEQ ID NO: 13 is a cellulase obtained from Melanocarpus albomyces. SEQ ID NO: 14 is a DNase obtained from Aspergillus oryzae. DETAILED DESCRIPTION OF THE INVENTION

[0043] The inventors of the present invention have surprisingly found that by partially or even completely replacing anti-redeposition polymers in detergents with cellulase while maintaining the detergent's cleaning performance, it is possible to achieve a more sustainable detergent composition, i.e., a detergent composition with an improved sustainability profile. In contrast to polymers other than those produced from renewable agricultural sources, cellulase is naturally found in the environment and is readily biodegradable. In particular, cellulase can replace anti-redeposition polymers found in liquid and powder detergent systems, while still preventing particles from adhering to clothes during washing, even in the absence of typical anti-redeposition polymers.

[0044] As demonstrated in the Examples section, anti-redeposition polymers provide benefits to fabrics during washing, while cellulases can provide competing benefits, thereby improving the sustainability profile.

[0045] Therefore, in one embodiment, the present invention relates to the use of polypeptides with cellulase activity for improving the sustainability profile of detergent compositions by reducing the level of anti-redeposition polymers, in particular anti-redeposition polymers selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, methylcellulose, and / or combinations thereof, while maintaining or improving the cleaning performance of the detergent.

[0046] In one embodiment, the present invention relates to the use of polypeptides with cellulase activity to prevent, reduce or remove redeposition of soils on fabrics during a wash cycle while improving the sustainability profile of detergent compositions by reducing the level of anti-redeposition polymers, particularly polymers selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof. When soils do not adhere to items, fabrics appear cleaner.

[0047] In one embodiment, the present invention relates to a detergent composition with an improved sustainability profile comprising a polypeptide having cellulase activity and at least one detergent adjunct ingredient, wherein the composition comprises less than 1 wt.%, e.g., less than 0.8 wt.%, less than 0.7 wt.%, less than 0.6 wt.%, less than 0.5 wt.%, less than 0.4 wt.%, less than 0.3 wt.%, less than 0.2 wt.%, less than 0.1 wt.%, less than 0.05 wt.%, less than 0.025 wt.% of an anti-redeposition polymer, in particular an anti-redeposition polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof.

[0048] The present invention relates to a detergent composition with an improved sustainability profile comprising a polypeptide having cellulase activity, an anti-redeposition polymer and at least one detergent adjunct ingredient, wherein the ratio of anti-redeposition polymer to the incorporated cellulase (w / w) is in the range of 0.5 to 20, such as 0.5 to 10, such as 0.5 to 5, such as 0.5 to 2.5, such as 0.5 to 1, and wherein the particular polymer is selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof.

[0049] In yet another embodiment, the present invention relates to a detergent composition having an improved sustainability profile comprising a polypeptide having cellulase activity, an anti-redeposition polymer in the range of 0-0.5% (w / w), and at least one adjunct detergent ingredient, wherein the compounded cellulase is added in an amount of 0.15-0.5% (w / w), 0.2-0.5% (w / w), 0.3-0.5% (w / w), or 0.4-0.5% (w / w), and the anti-redeposition polymer is selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, or combinations thereof.

[0050] In yet another embodiment, the present invention relates to a detergent composition with an improved sustainability profile comprising a polypeptide having cellulase activity, an anti-redeposition polymer, and at least one detergent adjunct ingredient, wherein the ratio of anti-redeposition polymer to polypeptide having cellulase activity (active enzyme protein) is in the range of 0-20, such as 2-20, 5-20, 5-15, 5-10, such as 5, 6, 7, 8, 9, or 10.

[0051] The present invention further provides a method of laundering an item, comprising: a) exposing the items to a wash liquor containing a polypeptide having cellulase activity or to a detergent composition containing this polypeptide and a reduced level of an anti-redeposition polymer, particularly a polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof; b) completing at least one cleaning cycle; c) optionally adding additional soiling material; and d) optionally rinsing the item (where the item is a fabric); The present invention relates to a method comprising:

[0052] In one embodiment, a laundry method with a polypeptide having cellulase activity provides the same or better whiteness of items compared to a laundry method performed with a detergent composition that does not include cellulase and includes a higher amount of an anti-redeposition polymer, such as a polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof.

[0053] The pH of the liquid solution at 25°C is in the range of 1 to 11, such as in the range of 5.5 to 11, in the range of 7 to 9, in the range of 7 to 8, or in the range of 7 to 8.5. The pH of the powder detergent may be measured as 1 g / L in demineralised water and is preferably in the range of 1 to 12, such as 5.5 to 11.5, such as 7.5 to 11.5, such as 8 to 11.

[0054] The cleaning solution may have a temperature in the range of 5° C. to 95° C., or in the range of 10° C. to 80° C., or in the range of 10° C. to 70° C., or in the range of 10° C. to 60° C., or in the range of 10° C. to 50° C., or in the range of 15° C. to 40° C., or in the range of 20° C. to 40° C. In one embodiment, the temperature of the cleaning solution is 30° C.

[0055] In one embodiment of the present invention, the method of washing items further comprises draining the wash solution or a portion of the wash solution after the wash cycle is completed. The wash solution can then be reused in a subsequent wash cycle or a subsequent rinse cycle. The items may be exposed to the wash solution during the first wash cycle and, optionally, the second or third wash cycle. In one embodiment, after exposing the items to the wash solution, they are rinsed. The items may be rinsed with water or water containing a conditioner.

[0056] Cellulases suitable for use as described in this application are preferably microbial cellulases, such as Bacillus or fungal cellulases.

[0057] In one embodiment, the cellulase is obtained from the genus Humicola, particularly Humicola insolens. In one embodiment, the cellulase comprises the amino acid sequence of SEQ ID NO: 10 or comprises an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 10. In one aspect, the polypeptide differs from the polypeptide comprising SEQ ID NO: 10 by 10 or fewer amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids.

[0058] In one embodiment, the cellulase is obtained from the genus Bacillus, particularly Bacillus akibai. In one embodiment, the cellulase comprises the amino acid sequence of SEQ ID NO: 11 or comprises an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 11. In one aspect, the polypeptide differs from the polypeptide comprising SEQ ID NO: 11 by 10 or fewer amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids.

[0059] In one embodiment, the cellulase is obtained from the genus Paenibacillus, particularly Paenibacillus polymyxa. In one embodiment, the cellulase comprises the amino acid sequence of SEQ ID NO: 12 or comprises an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 12. In one aspect, the polypeptide differs from the polypeptide comprising SEQ ID NO: 12 by 10 or fewer amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids.

[0060] In one embodiment, the cellulase is obtained from the genus Melanocarpus, particularly Melanocarpus albomyces. In one embodiment, the cellulase comprises the amino acid sequence of SEQ ID NO: 13 or comprises an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 13. In one aspect, the polypeptide differs from the polypeptide comprising SEQ ID NO: 13 by 10 or fewer amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids.

[0061] Cellulases and even DNases useful according to the present invention may be present in detergent compositions in an amount corresponding to at least 0.00002% active enzyme protein as a weight percent of the detergent composition, preferably at least 0.000005%, 0.000001%, 0.00005%, 0.00001%, 0.0005%, 0.0001%, 0.005%, 0.001%, 0.002%, 0.003%, 0.004%, 0.005%, 0.006%, 0.008%, 0.01%, 0.02%, 0.03%, 0.05%, 0.1%, 0.2%, 0.3%, 0.4%, 0.6%, 0.7%, 0.8%, 0.9%, or 1.0% active cellulase protein as a weight percent of the detergent composition.

[0062] Cellulases and / or DNases useful in the present invention can be added as a blend enzyme in an amount of 0.05% to 10% by weight of the detergent composition, such as 0.05% to 5%, e.g., 0.05% to 3%, e.g., 0.05%, 0.075%, 0.1%, 0.15%, 0.2%, 0.25%, 0.3%, 0.35%, 0.4%, 0.45%, 0.5%, 0.6%, 0.7%, 0.8%, 0.9%, 1%, 1.5%, 2%, 2.5%, 3%, 3.5%, 4%, 4.5%, 5%, 5.5%, 6%, 6.5%, 7%, 7.5%, 8%, 8.5%, 9%, or 9.5%, or even 10% by weight of the detergent composition.

[0063] In one embodiment, the cellulase of SEQ ID NO: 10 or the cellulase of SEQ ID NO: 11, SEQ ID NO: 12, or SEQ ID NO: 13 comprises substitutions, deletions, and / or insertions at one or more (e.g., several) positions. In one embodiment, the number of amino acid substitutions, deletions, and / or insertions introduced into the polypeptide SEQ ID NO: 10 or the cellulase of SEQ ID NO: 11, SEQ ID NO: 12, or SEQ ID NO: 13 is 10 or less, e.g., 1, 2, 3, 4, 5, 6, 7, 8, or 9. The amino acid mutations may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect protein folding and / or activity; small deletions, typically 1-30 amino acids; small amino- or carboxyl-terminal extensions such as an amino-terminal methionine residue; small linker peptides of 20-25 residues or less; or small extensions that facilitate purification by altering net charge or other function, such as a polyhistidine sequence, antigenic epitope, or binding domain.

[0064] Examples of conservative substitutions are included in the following groups: basic amino acids (arginine, lysine, and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, and valine), aromatic amino acids (phenylalanine, tryptophan, and tyrosine), and low molecular weight amino acids (glycine, alanine, serine, threonine, and methionine). Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, in H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly.

[0065] Alternatively, the amino acid mutations may be of such a nature that they alter the physicochemical properties of the polypeptide, for example, improving the thermostability of the polypeptide, altering its substrate specificity, or changing its optimum pH.

[0066] Essential amino acids in a polypeptide can be identified according to techniques known in the art, such as site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, 1989, Science 244:1081-1085). In the latter technique, single alanine mutations are introduced at every residue in a molecule, and the resulting mutant molecules are tested for enzymatic activity to identify amino acid residues important for the molecule's activity. See also Hilton et al., 1996, J. Biol. Chem. 271:4699-4708. Enzyme active sites or other biological interactions can also be determined by physical analysis of the structure, as determined by techniques such as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, combined with mutation of putative contact site amino acids. See, e.g., de Vos et al., 1992, Science 255:306-312; Smith et al., 1992, J. Mol. Biol. 224:899-904; Wlodaver et al., 1992, FEBS Lett. 309:59-64. The identities of essential amino acids can also be inferred from alignments with related polypeptides.

[0067] Single or multiple amino acid substitutions, deletions, and / or insertions can be made and tested using known mutagenesis, recombination, and / or shuffling methods, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241:53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86:2152-2156; WO 95 / 17413; or WO 95 / 22625, followed by associated screening methods. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30:10832-10837; U.S. Pat. No. 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46:145; Ner et al., 1988, DNA 7:127).

[0068] Mutagenesis / shuffling methods can be combined with high-throughput automated screening methods to detect the activity of cloned mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17:893-896). Mutagenized DNA molecules encoding active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide.

[0069] The polypeptide may be a hybrid polypeptide in which a region of one polypeptide is fused at the N-terminus or C-terminus of a region of another polypeptide.

[0070] The polypeptide may be a fusion polypeptide or a cleavable fusion polypeptide in which another polypeptide is fused at the N-terminus or C-terminus of the polypeptide of the present invention. Fusion polypeptides are produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention. Techniques for producing fusion polypeptides are known in the art and involve ligating coding sequences encoding the polypeptides so that they are in frame and expression of the fusion polypeptide is under the control of the same promoter and terminator. Fusion polypeptides may also be constructed using intein technology, which results in the formation of a fusion polypeptide after translation (Cooper et al., 1993, EMBO J. 12:2575-2583; Dawson et al., 1994, Science 266:776-779).

[0071] The fusion polypeptide may further comprise a cleavage site between the two polypeptides that is cleaved to release the two polypeptides when the fusion protein is secreted. Examples of cleavage sites include, but are not limited to, those described in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3:568-576; Svetina et al., 2000, J. Biotechnol. 76:245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63:3488-3493; Ward et al., 1995, Biotechnology 13:498-503; and Contreras et al., 1991, Biotechnology 9:378-381; Eaton et al., 1986, Biochemistry 25:505-512; Collins-Racie et al., 1995, Biotechnology 13:982-987; Carter et al. al., 1989, Proteins: Structure, Function, and Genetics 6:240-248; and Stevens, 2003, Drug Discovery World 4:35-48.

[0072] General methods such as PCR, cloning, and nucleotide ligation are well known to those skilled in the art and can be found, for example, in the following literature: "Molecular cloning: A laboratory manual", Sambrook et al. (1989), Cold Spring Harbor lab., Cold Spring Harbor, NY, Ausubel, FM et al. (eds.); "Current protocols in Molecular Biology", John Wiley and Sons, (1995), Harwood, CR, and Cutting, SM (eds.); "DNA Cloning: A Practical Approach, Volumes I and II", DN Glover ed. (1985); "Oligonucleotide Synthesis", MJ Gait ed. (1984); "Nucleic Acid Hybridization", B.D. Hames & S.J. Higgins eds. (1985); "A Practical Guide To Molecular Cloning", B. Perbal, (1984).

[0073] The concentration of enzymes (cellulase, DNase and other enzymes present) in the detergent solution is typically in the range of 0.00004 to 100 ppm enzyme protein, for example, in the range of 0.00008 to 100, in the range of 0.0001 to 100, in the range of 0.0002 to 100, in the range of 0.0004 to 100, in the range of 0.0008 to 100, in the range of 0.001 to 100 ppm enzyme protein, in the range of 0.01 to 100 ppm enzyme protein, preferably in the range of 0.05 to 50 ppm enzyme protein, more preferably in the range of 0.1 to 50 ppm enzyme protein, more preferably in the range of 0.1 to 30 ppm enzyme protein, more preferably in the range of 0.5 to 20 ppm enzyme protein, and most preferably in the range of 0.5 to 10 ppm enzyme protein.

[0074] The enzymes (cellulase, DNase and other enzymes present) of the detergent compositions of the invention may be stabilized using conventional stabilizers, for example polyols such as propylene glycol or glycerol, sugars or sugar alcohols, lactic acid, boric acid or boric acid derivatives, for example aromatic boric acid esters, or phenylboronic acid derivatives such as 4-formylphenylboronic acid, and the compositions may be formulated, for example, as described in WO 92 / 19709 and WO 92 / 19708.

[0075] Polypeptides of the present invention may also be incorporated into detergent formulations as disclosed in WO 72 / 07202, incorporated herein by reference.

[0076] liquid enzyme formulation Enzymes (cellulase, DNase, and other enzymes present) are typically formulated as liquid enzyme formulations that are pourable compositions, but also have a high viscosity. The physical appearance and properties of liquid enzyme formulations can vary considerably. For example, they can have different viscosities (gel to watery), be colored or uncolored, clear or cloudy, and even contain solid particles, such as slurries or suspensions. The minimum ingredients are the enzymes (cellulase, DNase, and other enzymes present) and a solvent system to make them liquid.

[0077] The solvent system may include water, a polyol (e.g., glycerol, (mono-, di-, or tri-)propylene glycol, (mono-, di-, or tri-)ethylene glycol, a sugar alcohol (e.g., sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol, or adonitol), polypropylene glycol, and / or polyethylene glycol), ethanol, a sugar, and a salt. Typically, the solvent system also includes a preservative and / or other stabilizer.

[0078] Liquid enzyme formulations can be prepared by mixing a solvent system with an enzyme concentrate (or enzyme particles to obtain a slurry / suspension) having the desired purity.

[0079] In one embodiment, the liquid enzyme composition comprises: (a) at least 0.01% w / w active enzyme protein; (b) at least 0.5% w / w polyol; (c) water, and (d) optionally a preservative Includes:

[0080] The enzymes (cellulase, DNase, and other enzymes present) in the liquid compositions of the present invention can be stabilized using conventional stabilizers. Examples of stabilizers include, but are not limited to, sugars such as glucose, fructose, sucrose, and trehalose, polyols such as glycerol and propylene glycol, the addition of salts to increase ionic strength, and divalent cations (e.g., Ca). 2+ or Mg 2+ ), and enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP). Selecting the optimal pH for the formulation may be crucial to enzyme stability. The optimal pH depends on the specific enzyme, but is typically in the pH 4-9 range. In some cases, surfactants such as nonionic surfactants (e.g., alcohol ethoxylates) can improve the physical stability of enzyme formulations.

[0081] One embodiment of the present invention is a composition comprising cellulase, wherein the composition comprises: (i) a polyol, preferably selected from glycerol, (mono-, di-, or tri-)propylene glycol, (mono-, di-, or tri-)ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, dulcitol, inositol, xylitol, and adonitol; (ii) optionally an additional enzyme, preferably selected from a protease, amylase, or lipase, DNAse, mannanase; (iii) optionally a surfactant, preferably selected from anionic and nonionic surfactants; (iv) optionally a salt, a divalent cation, a polymer, or an enzyme inhibitor; (v) optionally having a pH in the range of pH 4 to 9; and (vi) Water The present invention relates to a composition further comprising:

[0082] Enzyme slurries or dispersions are typically prepared by dispersing small particles of enzyme (e.g., spray-dried particles) in a liquid medium in which the enzyme is sparingly soluble, such as a liquid nonionic surfactant or liquid polyethylene glycol. Powders can also be added to aqueous systems in amounts that do not dissolve completely (above the solubility limit). Another form is a crystal suspension, which can also be an aqueous liquid (see, for example, WO 2019 / 002356). Another way to prepare such dispersions is by preparing a water-in-oil emulsion in which the enzyme is in the aqueous phase and allowing water to evaporate from the droplets. Such slurries / suspensions can be physically stabilized (to reduce or avoid settling), typically by the addition of rheology modifiers such as fumed silica or xanthan gum to obtain a shear-thinning rheology.

[0083] Granular enzyme formulation Enzymes (cellulase, DNase, and other enzymes present) can also be formulated as solid / granular enzyme formulations. Non-dusting granules can be produced, for example, as disclosed in U.S. Pat. Nos. 4,106,991 and 4,661,452, and optionally coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycols, PEGs) having an average molecular weight of 1,000 to 20,000, ethoxylated nonylphenols having 16 to 50 ethylene oxide units, ethoxylated fatty alcohols in which the alcohol contains 2 to 20 carbon atoms and 15 to 80 ethylene oxide units are present, fatty alcohols, fatty acids, and mono-, di-, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed technology are described in GB 1,483,591.

[0084] Cellulases can be formulated as granules, for example, composite granules combining one or more enzymes or benefit agents (e.g., MnTACN or other bleaching ingredients). Examples of such additional enzymes include lipase, xyloglucanase, perhydrolase, peroxidase, lipoxygenase, laccase, hemicellulase, protease, keratinase, cellulase, cellobiose dehydrogenase, xylanase, phospholipase, esterase, cutinase, pectinase, mannanase, pectate lyase, keratinase, reductase, oxidase, phenoloxidase, ligninase, pullulanase, tannase, pentosanase, lichenase, glucanase, arabinosidase, hyaluronidase, chondroitinase, amylase, DNAse, and mixtures thereof. In this case, more granules of each enzyme will be present to ensure a more uniform distribution of the enzyme throughout the detergent. This also reduces physical segregation of the different enzymes due to different particle sizes. A method for producing multi-enzyme composite granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0085] One embodiment of the present invention relates to an enzyme granule / particle containing cellulase. The granule consists of a core and, optionally, one or more coatings (outer layers) surrounding the core. Typically, the granule / particle size, measured as the equivalent spherical diameter of the granule (mean particle size by volume), is 20 to 2000 μm, particularly 50 to 1500 μm, 100 to 1500 μm, or 250 to 1200 μm.

[0086] The core may contain additional materials such as fillers, fibrous materials (cellulose or synthetic fibers), stabilizers, solubilizers, suspending agents, viscosity modifiers, light spheres, plasticizers, salts, lubricants, and flavorings. The core may contain binders such as synthetic polymers, waxes, fats, and carbohydrates. The core may contain, typically as a homogeneous blend, salts of polyvalent cations, reducing agents, antioxidants, peroxide decomposition catalysts, and / or acid buffer components. The core may consist of inert particles imbibed with enzymes or having enzymes applied to their surfaces, such as by fluidized bed coating. The core may have a diameter of 20 to 2000 μm, particularly 50 to 1500 μm, 100 to 1500 μm, or 250 to 1200 μm. The cores can be prepared by granulating a blend of ingredients, for example, by methods including granulation techniques such as crystallization, precipitation, pan coating, fluidized-bed coating, fluidized-bed agglomeration, rotary atomization, extrusion, prilling, spheronization, size reduction, drum granulation, and / or high-shear granulation. Methods for preparing the cores can be found in Handbook of Powder Technology; Particle size enlargement by CECapes; Volume 1; 1980; Elsevier. These methods are well known in the art and are also described in International Patent Application WO 2015 / 028567, pages 3-5, which are incorporated by reference.

[0087] The core of the enzyme granule / particle may be surrounded by at least one coating, for example, to improve storage stability, reduce dust formation during handling, or to color the granules. The optional coating may include a salt coating or other suitable coating materials, such as polyethylene glycol (PEG), methylhydroxypropylcellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with multi-layer coatings are shown in WO 93 / 07263 and WO 97 / 23606.

[0088] Such coatings are well known in the art and have been previously described, for example, in WO 00 / 01793, WO 2001 / 025412 and WO 2015 / 028567, which are incorporated by reference.

[0089] In one aspect, the present invention provides a method for producing a pharmaceutical composition comprising: (a) a core comprising the cellulase of the present invention, and (b) optionally, a (salt) coating consisting of one or more layers surrounding the core; The present invention provides granules comprising:

[0090] Another aspect of the present invention is a method for producing a composition comprising: (a) (non-enzymatic) core, (b) a coating surrounding the core, wherein the coating comprises cellulase; and (c) optionally a (salt) coating consisting of one or more layers surrounding the enzyme-containing coating; The present invention relates to a layered granule comprising:

[0091] Encapsulated enzyme formulation The enzymes (cellulase, DNase, and other enzymes present) can also be formulated as encapsulated enzyme formulations ("encapsulates"), which are particularly useful for separating the enzymes from other ingredients when the enzymes are added to (liquid) cleaning compositions, such as the detergent compositions described below.

[0092] Physical separation can be used to resolve incompatibilities between enzymes and other components. Incompatibility can arise either when the other component is reactive with the enzyme or when the other component is a substrate for the enzyme. The other enzyme may be a substrate for the protease.

[0093] The enzymes can be encapsulated in a matrix, preferably a water-soluble or water-dispersible matrix (e.g., water-soluble polymer particles), as described, for example, in WO 2016 / 023685. An example of a water-soluble polymer matrix is ​​a matrix composition comprising polyvinyl alcohol. Such compositions are also used to encapsulate detergent compositions in unit dose form.

[0094] Enzymes can also be encapsulated in core-shell microcapsules, for example, as described in WO 2015 / 144784 or in IP.com disclosure IPCOM000239419D.

[0095] Such core-shell capsules can be prepared using several techniques known in the art, for example, by interfacial polymerization using either water-in-oil or oil-in-water emulsions, where the polymer is crosslinked at the surface of the droplets in the emulsion (at the water-oil interface), thus forming a wall / membrane around each droplet / capsule.

[0096] Complex granular enzyme blend The enzymes (cellulase, DNase, and other enzymes present) can be formulated as granules, for example, as composite granules combining one or more enzymes, where each enzyme will be present in more granules to ensure a more uniform distribution of the enzymes in the detergent. This also reduces physical segregation of the different enzymes due to different particle sizes. A method for producing multi-enzyme composite granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0097] Another example of an enzyme formulation using composite granules is disclosed in WO 2013 / 188331, which relates to a detergent composition comprising: (a) a multi-enzyme composite granule; (b) less than 10 wt. % of a zeolite (on an anhydrous basis); and (c) less than 10 wt. % of a phosphate (on an anhydrous basis), wherein the enzyme composite granule comprises 10 wt. % to 98 wt. % of a moisture sink component, and the composition additionally comprises 20 wt. % to 80 wt. % of a detergent moisture sink component.

[0098] WO 2013 / 188331 also relates to a method of treating and / or cleaning a surface, preferably a fabric surface, comprising the steps of: (i) contacting said surface with the detergent composition described herein as claimed in an aqueous wash liquor; and (ii) rinsing and / or drying the surface.

[0099] The multi-enzyme complex granules may contain cellulase and one or more enzymes selected from the group consisting of (a) lipase, xyloglucanase, perhydrolase, peroxidase, lipoxygenase, laccase, and mixtures thereof, and (b) hemicellulase, protease, keratinase, cellulase, cellobiose dehydrogenase, xylanase, phospholipase, esterase, cutinase, pectinase, mannanase, pectate lyase, keratinase, reductase, oxidase, phenoloxidase, ligninase, pullulanase, tannase, pentosanase, lichenase, glucanase, arabinosidase, hyaluronidase, chondroitinase, amylase, DNAse, and mixtures thereof.

[0100] Purity of the enzyme in the formulation The enzymes used in the above enzyme blends (cellulase, DNase, and other enzymes present) can be purified to any desired degree of purity, including high levels of purification achieved, for example, using crystallization methods, as well as no purification or low levels of purification achieved, for example, using crude fermentation broth as described in WO 2001 / 025411 or WO 2009 / 152176.

[0101] microorganisms The enzyme formulations, as well as the detergent formulations described below, may contain one or more microorganisms or microbes. Generally, any microorganism may be used in the enzyme / detergent formulation in any suitable amount / concentration. The microorganism may be used as the sole biologically active ingredient, or may be used in combination with one or more of the enzymes described above.

[0102] The purpose of adding microorganisms may be, for example, to reduce malodors as described in WO 2012 / 112718. Other purposes may include the in-situ production of desirable biological compounds or the inoculation / habitation of microorganisms at a microbial location to competitively prevent other undesirable microorganisms from inhabiting the same location (competitive exclusion).

[0103] The term "microorganism" generally refers to a small organism that can be seen through a microscope. Microorganisms often exist as single cells or as colonies of cells. Some microorganisms may be multicellular. Microorganisms include prokaryotic (e.g., bacteria and archaea) and eukaryotic (e.g., some fungi, algae, protozoa) organisms. Examples of bacteria may be gram-positive or gram-negative bacteria. Examples of bacterial forms include vegetative cells and endospores. Examples of fungi may be yeast, mold, and mushrooms. Examples of fungal forms include hyphae and spores. As used herein, viruses may be considered microorganisms.

[0104] The microorganisms may be recombinant or non-recombinant. In some instances, the microorganisms may produce various substances (e.g., enzymes) that are useful for inclusion in detergent compositions. Extracts from the microorganisms or fractions from the extracts may be used in detergents. The medium in which the microorganisms are cultured or fractions or extracts from the medium may also be used in detergents. In some instances, substances produced by the microorganisms that are unique to the microorganisms, their extracts, medium, and fractions may be specifically excluded from the detergent. In some instances, the microorganisms or substances produced by or extracted from the microorganisms may activate, enhance, preserve, extend, etc., detergent activity or ingredients contained in the detergent.

[0105] Generally, microorganisms may be cultured using methods known in the art. The microorganisms may then be treated or formulated in a variety of ways. In some instances, the microorganisms may be dried (e.g., freeze-dried). In some instances, the microorganisms may be encapsulated (e.g., spray-dried). Many other treatments or formulations are possible. These treatments or preparations may promote retention of microbial viability over time and / or in the presence of detergent ingredients. However, in some instances, the microorganisms in the detergent may not be viable. The treated / formulated microorganisms may be added to the detergent before or at the time of use.

[0106] In one embodiment, the microorganism is a Bacillus species, such as at least one Bacillus species selected from the group consisting of Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus atrophaeus, Bacillus pumilus, Bacillus megaterium, or a combination thereof. In a preferred embodiment, the Bacillus species is in the endospore form, which significantly improves storage stability.

[0107] Detergent Composition In one embodiment, the present invention relates to a detergent composition comprising a cellulase in combination with one or more additional cleaning composition components. In one embodiment, the detergent composition comprises a polypeptide having cellulase activity and an amino acid sequence having at least 60% identity, e.g., 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, or even 100% identity, to the amino acid sequence set forth in SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, or SEQ ID NO:13. The detergent composition may also comprise an additional enzyme, e.g., a DNase having an amino acid sequence having at least 60% identity, e.g., 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, or even 100% identity, to the amino acid sequence set forth in SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, or SEQ ID NO:14. In one embodiment, the detergent composition is in solid form. In another embodiment, the detergent composition is in liquid or gel form. In another embodiment, the detergent composition is in bar form. In one embodiment, the detergent may be wrapped in a water-soluble PVOH film. The selection of additional ingredients is within the skill of one in the art and includes conventional ingredients such as the non-limiting example ingredients set forth below.

[0108] Liquid detergent composition Liquid detergent compositions may comprise the microcapsules of the present invention and may therefore form part of any detergent composition in any form, including liquid and powder detergents, as well as soaps and detergent bars.

[0109] In one embodiment, the present invention relates to a liquid detergent composition comprising the microcapsules described above in combination with one or more additional cleaning composition ingredients.

[0110] As mentioned above, the microcapsules may be added to the liquid detergent composition in an amount corresponding to 0.0001% to 5% (w / w) active enzyme protein (AEP); preferably 0.001% to 5%, more preferably 0.005% to 5%, more preferably 0.005% to 4%, more preferably 0.005% to 3%, more preferably 0.005% to 2%, even more preferably 0.01% to 2%, and most preferably 0.01% to 1% (w / w) active enzyme protein.

[0111] A liquid detergent composition has a physical form that is not a solid (or gas). It may be a pourable liquid, a paste, a pourable gel, or a non-pourable gel. It may be isotropic or structured, preferably isotropic. It may be a formulation useful for automatic or hand washing. It may also be a personal care product such as shampoo, toothpaste, or hand soap.

[0112] Liquid detergent compositions may be aqueous, typically containing at least 20% by weight and no more than 95% water, e.g., no more than 70% water, no more than 50% water, no more than 40% water, no more than 30% water, or no more than 20% water. Other types of liquids, such as, but not limited to, alkanols, amines, diols, ethers, and polyols, may also be included in aqueous liquid detergents. Aqueous liquid detergents may contain 0-30% organic solvents. Liquid detergents may also be non-aqueous, in which case the water content is less than 10%, preferably less than 5%.

[0113] The detergent ingredients can be physically separated from one another by compartments in the water-soluble pouch, which avoids negative storage interactions between the ingredients, and the different dissolution profiles of each compartment can delay dissolution of selected ingredients in the wash solution.

[0114] The detergent composition may be in the form of a unit dose product. A unit dose product is a single-dose package in a non-reusable container. This is increasingly used in laundry detergents. A single-dose detergent product is a package (e.g., in a pouch made from a water-soluble film) of the amount of detergent used for one wash.

[0115] The pouch may be of any form, shape, and material suitable for retaining the composition without allowing it to leak from the pouch, for example, prior to contact with water. The pouch is fabricated from a water-soluble film that contains an internal volume. This internal volume can be divided into multiple compartments of the pouch. Preferred films are polymeric materials, preferably polymers that can be formed into films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected from polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, with polyvinyl alcohol copolymers and hydroxymethylcellulose (HPMC) being most preferred. Preferably, the level of polymer in the film, e.g., PVA, is at least about 60%. Preferred average molecular weights will typically be from about 20,000 to about 150,000. The film may also be a blend composition comprising a hydrolyzable and water-soluble polymer blend such as polylactide and polyvinyl alcohol (known under product reference number M8630, sold by Chris Craft in. Prod. Of Gary, Ind., US) and a plasticizer such as glycerol, ethylene glycerol, propylene glycol, sorbitol, and mixtures thereof. The pouch may contain a solid laundry cleaning composition or some of its components and / or a liquid cleaning composition or some of its components, separated by a water-soluble film. The liquid component compartment may be different in composition from the solid-containing compartment (see, e.g., US Patent Application Publication No. 2009 / 0011970).

[0116] The selection of detergent ingredients, for fabric care, may include consideration of the type of fabric to be cleaned, the type and / or degree of soiling, the temperature at which cleaning will be performed, and the detergent product formulation. The ingredients set forth below are grouped under general headings according to specific functionality, but this should not be construed as limiting, as one skilled in the art will appreciate that one ingredient may contain additional functionality.

[0117] The selection of additional ingredients is within the skill of one of ordinary skill in the art and includes conventional ingredients such as the non-limiting example ingredients set forth below.

[0118] surfactants The cleaning composition may contain one or more surfactants, which may be anionic and / or cationic and / or nonionic and / or semi-polar and / or zwitterionic, or mixtures thereof. In certain embodiments, the detergent composition contains a surfactant system (comprising two or more surfactants), such as a mixture of one or more nonionic surfactants and one or more anionic surfactants. In one embodiment, the detergent contains at least one anionic surfactant and at least one nonionic surfactant, and the weight ratio of the anionic surfactant to the nonionic surfactant may be from 20:1 to 1:20. In one embodiment, the amount of anionic surfactant is greater than the amount of nonionic surfactant, for example, the weight ratio of the anionic surfactant to the nonionic surfactant may be from 10:1 to 1.1:1 or from 5:1 to 1.5:1. The amounts of the anionic surfactant and the nonionic surfactant may also be equal, or may be in a weight ratio of 1:1. In one embodiment, the amount of nonionic surfactant is greater than the amount of anionic surfactant, and the weight ratio may be 1:10 to 1:1.1. Preferably, the weight ratio of anionic surfactant to nonionic surfactant is 10:1 to 1:10, e.g., 5:1 to 1:5 or 5:1 to 1:1.2. Preferably, the weight ratio of nonionic surfactant to anionic surfactant is 0 to 0.5 or 0 to 0.2, so that nonionic surfactant can be present or absent when the weight ratio is 0. However, when nonionic surfactant is present, the weight ratio of nonionic surfactant is preferably at most 50% or at most 20% of the total weight of anionic surfactant and nonionic surfactant. Light-duty detergents typically contain more nonionic surfactant than anionic surfactant, and the ratio of nonionic surfactant to anionic surfactant is preferably 0.5 to 0.9. The total weight of surfactant is typically present at a level of from about 0.1% to about 60% by weight, e.g., from about 1% to about 40% by weight, or from about 3% to about 20% by weight, or from about 3% to about 10% by weight. The surfactant is selected based on the desired cleaning application and may include any conventional surfactant known in the art.When included, detergents will typically contain from about 1% to about 40% by weight of anionic surfactant, e.g., from about 5% to about 30%, e.g., from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25%. Non-limiting examples of anionic surfactants include sulfates and sulfonates, typically available as sodium or potassium salts or salts of monoethanolamine (MEA, 2-aminoethan-1-ol) or triethanolamine (TEA, 2,2',2''-nitrilotriethan-1-ol), particularly linear alkylbenzene sulfonates (LAS), isomers of LAS, e.g., branched alkylbenzene sulfonates (BABS) and phenylalkane sulfonates, olefin sulfonates, particularly α-olefin sulfonates (AOS), alkyl sulfates (AS), particularly fatty alcohol sulfates (FAS), i.e., primary alcohol sulfates. Examples of surfactants include: sulfates (PAS), such as dodecyl sulfate (SLS), alcohol ether sulfates (AES, also known as AEOS or FES, alcohol ethoxy sulfates or fatty alcohol ether sulfates), paraffin sulfonates (PS), such as alkane-1-sulfonates and secondary alkane sulfonates (SAS), ester sulfonates, such as sulfonated fatty acid glycerol esters and α-sulfofatty acid methyl esters (α-SFMe, SES, or MES), alkyl or alkenyl succinic acids, such as dodecenyl / tetradecenyl succinic acid (DTSA), diesters and monoesters of sulfosuccinic acid, and fatty acid derivatives of amino acids. Anionic surfactants can be added as acids, salts, or ethanolamine derivatives.

[0119] When included, detergents will typically contain from about 1% to about 40% by weight of anionic surfactant, e.g., from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25%, including from about 5% to about 30% anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, particularly linear alkylbenzene sulfonates (LAS), isomers of LAS, branched alkylbenzene sulfonates (BABS), phenylalkane sulfonates, α-olefin sulfonates (AOS), olefin sulfonates, alkenesulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkane sulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (alcohol sulfates), and the like. Examples of suitable sulfonates include ethanol esters, sulfonated fatty acid glycerol esters, α-sulfofatty acid methyl esters (α-SFMe or SES) including sulfonate methyl esters (MES), alkyl- or alkenyl succinic acids, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or salts of fatty acids (soaps), and combinations thereof.

[0120] When included, the detergent typically contains about 1% to about 40% by weight of cationic surfactant, for example, about 0.5% to about 30%, particularly about 1% to about 20%, about 3% to about 10%, for example, about 3% to about 5%, about 8% to about 12%, or about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), such as the AEO series, for example AEO-7, alcohol propoxylates, in particular propoxylated fatty alcohols (PFAs), ethoxylated and propoxylated alcohols, alkoxylated fatty acid alkyl esters, such as ethoxylated and / or propoxylated fatty acid alkyl esters (in particular methyl ester ethoxylates, MEE), alkyl polyglycosides (APGs), alkoxylated amines, fatty acid monoethanolamides (FAMs), fatty acid diethanolamides (FADAs), ethoxylated fatty acid monoethanolamides (EFAMs), propoxylated fatty acid monoethanolamides (PFAMs), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamide GA or fatty acid glucamide FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.

[0121] When included, detergents will typically contain from about 0.01 to about 10% by weight of semi-polar surfactants. Non-limiting examples of semi-polar surfactants include amine oxides (AOs), such as alkyl dimethyl amine oxides, particularly N-(cocoalkyl)-N,N-dimethyl amine oxide and N-(tallow-alkyl)-N,N-bis(2-hydroxyethyl) amine oxide, and combinations thereof.

[0122] If included, detergents will typically contain from about 0.01% to about 10% by weight of zwitterionic surfactants. Non-limiting examples of zwitterionic surfactants include betaines, such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.

[0123] Additional biosurfactants may be used, for example, where the surfactant is a sugar-based nonionic surfactant which may be hexyl-β-D-maltopyranoside, thiomaltopyranoside, or cyclic maltopyranoside, as described, for example, in EP 2516606 B1. Other biosurfactants may include rhamnolipids and sophorolipids.

[0124] Hydrotrope Hydrotropes are compounds that solubilize hydrophobic compounds in aqueous solutions (or, conversely, polar substances in non-polar environments). Typically, hydrotropes possess both hydrophilic and hydrophobic properties (the so-called amphiphilic properties known from surfactants); however, the molecular structure of hydrotropes generally does not favor spontaneous self-aggregation; see, for example, the review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12:121-128. Hydrotropes do not exhibit a critical concentration above which self-aggregation occurs, as is found for surfactants and lipids that form micellar, lamellar, or other well-defined mesophases. Instead, many hydrotropes exhibit a continuous-type aggregation process in which aggregate size increases with increasing concentration. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing polar and non-polar substances, including mixtures of water, fats, surfactants, and polymers. Hydrotropes are traditionally used in industries ranging from pharmaceutical, personal care, and food to technical applications. Their use in detergent compositions allows, for example, more concentrated formulations of surfactants (as in the process of compacting liquid detergents by excluding water) without inducing undesirable phenomena such as phase separation or high viscosity.

[0125] The detergent may contain 0 to 10% by weight of a hydrotrope, e.g., 0 to 5% by weight, such as about 0.5 to about 5% or about 3% to about 5%. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluenesulfonate (STS), sodium xylenesulfonate (SXS), sodium cumenesulfonate (SCS), sodium cymenesulfonate, amine oxides, alcohols and polyglycol ethers, sodium hydroxynaphthalene, sodium hydroxynaphthalenesulfonate, sodium ethylhexyl sulfate, and combinations thereof.

[0126] Builders and co-builders The detergent composition may contain from about 0 to 65% by weight, such as from about 5% to about 50%, of a detergent builder or co-builder, or mixtures thereof. The builder and / or co-builder may be, in particular, a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and / or co-builder known in the art for use in detergents may be used.

[0127] Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Clariant), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2′-iminodiethanol-1-ol), triethanolamine (TEA, also known as 2,2′,2″-nitrilotriethanol-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

[0128] The detergent composition may also contain about 0 to 50% by weight, e.g., about 5% to about 30%, of a detergent co-builder. The detergent composition may contain the co-builder alone or in combination with a builder, such as a zeolite builder. Non-limiting examples of co-builders include poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA), or copolymers thereof. In accordance with the present invention, these ingredients may be included at lower levels than in currently available detergent compositions. Further non-limiting examples include citrates, chelating agents, such as aminocarboxylates, aminopolycarboxylates, and phosphonates, and alkyl or alkenyl succinic acids.Additional specific examples include 2,2',2"nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycine diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid (HEDP)), ethylenediaminetetramethylenetetrakis(phosphonic acid) ( EDTMPA), diethylenetriaminepentamethylenepentakis(phosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS ), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA), sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)ethylenediamine-N,N',N"-triacetic acid (HEDTA), diethanolglycine (DEG), aminotrimethylenetris(phosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and / or co-builders are described, for example, in WO 09 / 102854 and U.S. Pat. No. 5,977,053.

[0129] bleaching type The cleaning composition may contain 0 to 50% by weight of a bleaching system, such as 1 to 40%, such as 1 to 30%, such as about 1% to about 20%. Any oxygen-based bleaching system containing components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include a hydrogen peroxide source, a peracid and a peracid source (bleach activator), and a bleach catalyst or booster.

[0130] Hydrogen peroxide source: Suitable sources of hydrogen peroxide are inorganic persalts, such as alkali metal salts such as sodium percarbonate and sodium perborate (usually the mono- or tetrahydrate), and hydrogen peroxide-urea (1 / 1).

[0131] Peracid source: The peracids can be (a) directly incorporated as preformed peracids, or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis), or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.

[0132] a) Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-α-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, ε-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid] (PAP), and o-carboxybenzamidoperoxycaproic acid, aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic acid, isophthalic acid, and terephthalic acid, perimidic acid, peroxymonosulfuric acid, peroxydisulfuric acid, peroxyphosphoric acid, peroxysilicic acid, and mixtures of the foregoing. It will be understood that the peracids mentioned may in some cases best be added as a suitable salt, for example an alkali metal salt (eg Oxone®) or an alkaline earth metal salt.

[0133] b) Suitable bleach activators include those belonging to the classes of esters, amides, imides, nitriles, or anhydrides, and, where applicable, their salts. Suitable examples include tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), sodium 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO 98 / 17767. A specific family of bleach activators of interest is disclosed in EP 624154, and a particularly preferred member of that family is acetyl triethyl citrate (ATC). ATC or short-chain triglycerides such as triacetin have the advantage of being environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin have good hydrolytic stability in the product during storage and are efficient bleach activators. Finally, ATC is multifunctional because the citrate released in the perhydrolysis reaction can function as a builder.

[0134] Bleach Catalysts and Boosters The bleaching system may also include a bleach catalyst or booster.

[0135] Some non-limiting examples of bleaching catalysts that can be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese collagen, cobalt-amine catalysts, and manganese triazacyclononane (MnTACN) catalysts; particularly advantageous are manganese complexes with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Me4-TACN), especially Me3-TACN, such as the binuclear manganese complexes [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2 and [2,2',2"-nitrilotris(ethane-1,2-diylazanylylidene-κN-methanylylidene)triphenolato-κ3O]manganese(III). The bleaching catalyst may also be a compound of another metal, such as an iron or cobalt complex.

[0136] In some embodiments, when a peracid source is included, it may be selected from the group consisting of: [ka] (iii) and mixtures thereof (wherein each R1 is independently a branched alkyl group containing 9 to 24 carbon atoms or a linear alkyl group containing 11 to 24 carbon atoms, preferably each R1 is independently a branched alkyl group containing 9 to 18 carbon atoms or a linear alkyl group containing 11 to 18 carbon atoms, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl, and isopentadecyl). An organic bleach catalyst or bleach booster having one of the following may be used.

[0137] Other exemplary bleaching systems are described, for example, in WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259, EP 1 867 708 (vitamin K), and WO 2007 / 087242. Suitable photobleaches may be, for example, sulfonated zinc or aluminum phthalocyanine.

[0138] Polymers and Dispersants Generally, detergent compositions may contain 0-10% by weight of polymer, e.g., 0.5-5%, 2-5%, 0.5-2%, or 0.2-1%. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as described above, or may provide anti-redeposition, fabric protection, soil release, dye transfer prevention, grease cleaning, and / or anti-foam properties. Some polymers may have two or more of the above properties and / or two or more of the motifs listed below. Exemplary polymers include poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethylene glycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and silicone, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO), and polyvinylpyrrolidone vinylimidazole (PVPVI). Further exemplary polymers include polyethylene oxide and polypropylene oxide (PEO-PPO), diquaternium ethoxysulfate, styrene / acrylic copolymers, and fragrance capsules. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the above polymers are also contemplated.

[0139] The detergent compositions of the present invention can also contain dispersants. In particular, powder detergents can contain dispersants. Suitable water-soluble organic materials include homo- or copolymeric acids or salts thereof, and polycarboxylic acids containing at least two carboxyl groups separated from each other by no more than two carbon atoms. Suitable dispersants are described, for example, in Powdered Detergents, Surfactant Science Series Volume 71, Marcel Dekker, Inc.

[0140] However, in accordance with the present invention, some of the above polymers, i.e., polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose, and / or combinations thereof, may be included at lower levels than in currently available detergent compositions, or even, more preferably, may be eliminated altogether.

[0141] Fabric color toning agent The detergent compositions of the present invention may also contain fabric hueing agents, such as dyes or pigments, which, when incorporated into the detergent composition, adhere to fabrics when the fabrics are contacted with a wash liquor containing the detergent composition, thereby changing the color of the fabrics through the absorption / reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents change the color of a surface by absorbing at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay complexes, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include those selected from the group consisting of dyes belonging to the Dye Index (CI) classification of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet, and Basic Red, or mixtures thereof, as described in, for example, WO 2005 / 03274, WO 2005 / 03275, WO 2005 / 03276, and EP 1876226 (incorporated herein by reference). The detergent composition preferably comprises from about 0.00003% to about 0.2%, from about 0.00008% to about 0.05%, or even from about 0.0001% to about 0.04% by weight of the fabric hueing agent. The composition may comprise from 0.0001% to 0.2% by weight of the fabric hueing agent, which may be particularly preferred when the composition is in the form of a unit-dose pouch. Suitable hueing agents are also disclosed, for example, in WO 2007 / 087257 and WO 2007 / 087243.

[0142] Additional enzymes The detergent additives, as well as detergent compositions, may contain one or more additional enzymes, such as proteases, lipases, cutinases, amylases, carbohydrases, DNases, pectinases, mannanases, arabinases, galactanases, xylanases, oxidases, e.g., laccases, and / or peroxidases.

[0143] In general, the properties of the selected enzyme should be compatible with the selected detergent (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic components, etc.), and the enzyme should be present in an effective amount.

[0144] DNase (deoxyribonuclease) The term "DNase" refers to a polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, thereby degrading DNA. For purposes of the present invention, DNase activity is determined according to the procedure described in Assay I.

[0145] Preferably, the DNase is a polypeptide comprising an amino acid sequence having at least 60% identity, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or even 100% sequence identity to any of the polypeptides of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, or SEQ ID NO:14.

[0146] Mannanase Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are also included. The mannanase may be an alkaline mannanase of family 5 or 26. It may be a wild-type mannanase from the genus Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999 / 064619. A commercially available mannanase is Mannaway (Novozymes A / S).

[0147] Proteases Suitable proteases may be of any origin, preferably bacterial or fungal, and optionally in the form of protein-modified or chemically modified mutants. The protease may be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease may be, for example, from the S1 family, such as trypsin, or the S8 family, such as subtilisin. The metalloprotease may be, for example, thermolysin, for example, from the M4 family, or other metalloproteases, for example, from the M5, M7, or M8 families.

[0148] The term "subtilase" refers to a subgroup of serine proteases as described by Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with the substrate. Subtilases can be classified into six subdivisions: the subtilisin family, thermitase family, proteinase K family, lantibiotic peptidase family, kexin family, and pyrrolysin family.

[0149] Although proteases suitable for detergent use can be obtained from a variety of organisms, including fungi such as Aspergillus, detergent proteases are generally obtained from bacteria, particularly Bacillus. Examples of Bacillus species from which subtilases are derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus, and Bacillus gibsonii. Specific subtilisins include subtilisin lentus, subtilisin novo, subtilisin Carlsberg, subtilisin BPN', subtilisin 309, subtilisin 147, and subtilisin 168, as well as, for example, protease PD138 (described in WO 93 / 18140). Other useful proteases are, for example, those described in WO 01 / 16285 and WO 02 / 16547.

[0150] Examples of trypsin-like proteases include the Fusarium proteases described in WO 94 / 25583 and WO 2005 / 040372, and the chymotrypsin proteases from Cellumonas described in WO 2005 / 052161 and WO 2005 / 052146.

[0151] Examples of metalloproteases include, for example, the neutral metalloproteases described in WO 2007 / 044993, such as those derived from Bacillus amyloliquefaciens, as well as the metalloproteases described in WO 2015 / 158723 and WO 2016 / 075078.

[0152] Examples of useful proteases are those described in WO 89 / 06279, WO 92 / 19729, WO 96 / 34946, WO 98 / 20115, WO 98 / 20116, WO 99 / 11768, WO 01 / 44452, WO 03 / 006602, WO 04 / 006603, WO 05 / 006604, WO 06 / 006606, WO 07 / 006608, WO 08 / 006609, WO 09 / 006610, WO 10 / 006611, WO 11 / 006612, WO 12 / 006613, WO 13 / 006614, WO 14 / 006615, WO 15 / 006616, WO 16 / 006617, WO 17 / 006618, WO 18 / 006619, WO 19 ... and protease variants described in WO 2004 / 003186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2014 / 207227, WO 2016 / 087617, and WO 2016 / 174234. Preferred protease variants include, for example, the following: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S126L, P127Q, S128A, S154 D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Q200L, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256D, T268A, and R269H. wherein the position numbers correspond to the positions of the Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016 / 001449.Protease variants having one or more of these mutations are preferably variants of Bacillus lentus protease (also known as Savinase® subtilisin 309) set forth in SEQ ID NO: 1 of WO 2016 / 001449, or variants of Bacillus amyloliquefaciens protease (BPN') set forth in SEQ ID NO: 2 of WO 2016 / 001449. Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016 / 001449.

[0153] Other proteases of interest are, for example, the alkaline protease from Bacillus lentus DSM 5483 described in WO 91 / 02792 and variants thereof described in WO 92 / 21760, WO 95 / 23221, EP 1921147, EP 1921148, and WO 2016 / 096711.

[0154] The protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004 / 067737, for example a variant comprising substitutions at one or more positions corresponding to positions 27, 109, 111, 171, 173, 174, 175, 180, 182, 184, 198, 199, and 297 of SEQ ID NO: 1 of WO 2004 / 067737, provided that the protease variant has at least 75% but less than 100% sequence identity to SEQ ID NO: 1 of WO 2004 / 067737. TY145 variants of interest are described, for example, in WO 2015 / 014790, WO 2015 / 014803, WO 2015 / 014804, WO 2016 / 097350, WO 2016 / 097352, WO 2016 / 097357, and WO 2016 / 097354.

[0155] Examples of preferred proteases include: (a) a variant of SEQ ID NO: 1 of WO 2016 / 001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D, and L262E, such as a variant having the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261W, and L262E, or a variant having the substitutions S9E, N43R, N76D, N185E, S188E, Q191N, A194P, Q206L, Y209W, S259D, and L262E, wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449; (b) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the mutation S99SE (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (c) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the mutation S99AD (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (d) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions Y167A+R170S+A194P (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (e) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+V68A+N218D+Q245R (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (f) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (g) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S99D+S101R / E+S103A+V104I+G160S, for example a variant of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S3T+V4I+S99D+S101E+S103A+V104I+G160S+V205I (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (h) a variant of the polypeptide of SEQ ID NO: 2 of WO 2016 / 001449 having the substitutions S24G+S53G+S78N+S101N+G128A / S+Y217Q (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (i) the polypeptide disclosed in GENESEQP under accession number BER84782, which corresponds to SEQ ID NO: 302 of WO 2017 / 210295; (j) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S99D+S101E+S103A+V104I+S156D+G160S+L262E (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (k) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions S9R+A15T+G61E+V68A+N76D+S99G+N218D+Q245R (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449); (l) a variant of the polypeptide of SEQ ID NO: 1 of WO 2016 / 001449 having the substitutions V68A+S106A (wherein the position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016 / 001449), and (m) A variant of the polypeptide of SEQ ID NO: 1 of WO 2004 / 067737 having the substitutions S27K+N109K+S111E+S171E+S173P+G174K+S175P+F180Y+G182A+L184F+Q198E+N199+T297P (wherein the position numbers are based on the numbering of SEQ ID NO: 1 of WO 2004 / 067737).

[0156] Suitable commercially available protease enzymes include Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase™, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In, and Progress® Excel (available from Novozymes). A / S), Maxatase™, Maxacal™, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2™, FN3™, FN4 ex(trade name), Excellase®, Excellenz® P1000, Excellenz® P1250, Eraser®, Preferenz® P100, Purafect Prime, Preferenz P110®, Effectenz P1000®, Purafect®, Effectenz P1050®, Purafect® Ox, Effectenz® P2000, Purafast®, Properase®, Opticlean®, and Optimase® (Danisco / DuPont), BLAP (sequence shown in Figure 29 of U.S. Pat. No. 5,352,604) and variants thereof (Henkel AG), and those sold under the trade name KAP (Bacillus alkalophilus subtilisin) manufactured by Kao.

[0157] Lipase and cutinase Suitable lipases and cutinases include those of bacterial or fungal origin. These include chemically modified or protein-modified mutant enzymes. Examples include those derived from Thermomyces, such as T. lanuginosus (formerly Humicola lanuginosa), as described in EP 258068 and EP 305216. lipases from Humicola species, such as H. insolens (WO 96 / 13580), such as P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331376), Pseudomonas sp. SD705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (P.Lipases from Pseudomonas strains (some of which have now been renamed Burkholderia) such as Pseudomonas wisconsinensis (WO 96 / 12012); GDSL-type Streptomyces lipases (WO 10 / 065455), Magnaporthe grisea (WO 10 / 107560), cutinase from Pseudomonas mendocina (U.S. Pat. No. 5,389,536), lipase from Thermobifida fusca (WO 11 / 084412), Geobacillus stearothermophilus Examples of lipases that can be used include lipases from Bacillus stearothermophilus (WO 11 / 084417), Bacillus subtilis (WO 11 / 084599), and lipases from Streptomyces griseus (WO 11 / 150157) and Streptomyces pristinaespiralis (WO 12 / 137147).

[0158] Other examples are lipase variants such as those described in EP 407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO 97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 07 / 87508 and WO 09 / 109500.

[0159] Preferred commercially available lipase enzymes include Lipolase™, Lipex™; Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (DuPont) and Lipomax (Gist-Brocades).

[0160] Further examples are lipases, sometimes called acyltransferases or perhydrolases, such as acyltransferases homologous to Candida antarctica lipase A (WO 10 / 111143), acyltransferases from Mycobacterium smegmatis (WO 05 / 56782), perhydrolases from the CE 7 family (WO 09 / 67279), and mutants of M. smegmatis perhydrolase, in particular the S54V mutant used in the product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 10 / 100028).

[0161] amylase Suitable amylases include α-amylases or glucoamylases, and may be of bacterial or fungal origin, including chemically modified or protein-engineered mutants. Amylases include α-amylases obtained from Bacillus species, such as specialized strains of Bacillus licheniformis, which are described in more detail in GB Patent No. 1,296,839.

[0162] Suitable amylases include the amylase having SEQ ID NO: 2 in WO 95 / 10603, or a variant thereof having 90% sequence identity to SEQ ID NO: 3. Preferred variants are those set forth in SEQ ID NO: 4 of WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and WO 99 / 019467, such as variants with substitutions at one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

[0163] Another suitable amylase is the amylase having SEQ ID NO: 6 described in WO 02 / 010355, or a variant having 90% sequence identity to SEQ ID NO: 6. A preferred variant of SEQ ID NO: 6 has deletions at positions 181 and 182 and a substitution at position 193.

[0164] Another suitable amylase is a hybrid α-amylase comprising residues 1-33 of the α-amylase from B. amyloliquefaciens (SEQ ID NO: 6) in WO 2006 / 066594 and residues 36-483 of the B. licheniformis α-amylase (SEQ ID NO: 4) in WO 2006 / 066594, or a variant thereof with 90% sequence identity. Preferred variants of this hybrid α-amylase include those with substitutions, deletions, or insertions at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209, and Q264. The most preferred variants of the hybrid α-amylase comprising residues 1-33 of the α-amylase obtained from B. amyloliquefaciens as set forth in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 have the following substitutions: M197T; H156Y+A181T+N190F+A209V+Q264S; or G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

[0165] Yet another suitable amylase is the amylase having SEQ ID NO: 6 described in WO 99 / 019467, or a variant thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those with substitutions, deletions or insertions at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those with deletions at positions R181 and G182, or H183 and G184.

[0166] Further amylases that can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96 / 023873, or variants having 90% sequence identity to SEQ ID NO: 1, SEQ ID NO: 3 or SEQ ID NO: 7 in WO 96 / 023873. The aforementioned preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are variants with substitutions, deletions or insertions at one or more of the following positions, using SEQ ID NO: 2 of WO 96 / 023873 for numbering: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476. More preferred variants are those with deletions at two positions selected from 181, 182, 183 and 184, for example, 181 and 182, 182 and 183. The most preferred variants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those which have a deletion at positions 183 and 184 and a substitution at one or more of positions 140, 195, 206, 243, 260, 304 and 476.

[0167] Other amylases that can be used are amylases having SEQ ID NO: 2 of WO 08 / 153815, SEQ ID NO: 10 of WO 01 / 66712, or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08 / 153815, or variants having 90% sequence identity to SEQ ID NO: 10 of WO 01 / 66712. Preferred variants of SEQ ID NO: 10 of WO 01 / 66712 are those with substitutions, deletions or insertions at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264.

[0168] Yet another suitable amylase is the amylase having SEQ ID NO: 2 of WO 09 / 061380 or a variant thereof having 90% sequence identity to SEQ ID NO: 2. Preferred variants of SEQ ID NO: 2 are C-terminal truncations and / or variants with substitutions, deletions or insertions at one or more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those with substitutions at one or more of the following positions: Q87E,R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K, and / or deletions at the following positions: R180 and / or S181 or T182 and / or G183. Most preferred amylase variants of SEQ ID NO: 2 are those with the following substitutions: N128C+K178L+T182G+Y305R+G475K; N128C+K178L+T182G+F202Y+Y305R+D319T+G475K; S125A+N128C+K178L+T182G+Y305R+G475K; or S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K wherein the variant is C-terminally truncated and optionally further comprises a substitution at position 243 and / or a deletion at positions 180 and / or 181.

[0169] A further suitable amylase is the amylase having SEQ ID NO: 1 of WO 13184577 or a variant thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 are those having substitutions, deletions, or insertions at one or more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, 1203, S241, R458, T459, D460, G476, and G477. More preferred variants of SEQ ID NO: 1 are those with substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K and / or deletions at positions R178 and / or S179 or T180 and / or G181. Most preferred amylase variants of SEQ ID NO: 1 are those with the following substitutions: E187P+I203Y+G476K E187P+I203Y+R458N+T459S+D460T+G476K and optionally the variant further comprises a substitution at position 241 and / or a deletion at position 178 and / or position 179.

[0170] Further suitable amylases are those having SEQ ID NO: 1 of WO 10104675 or variants thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 have substitutions, deletions, or insertions at one or more of the following positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477, and G478. More preferred variants of SEQ ID NO: 1 have substitutions at one or more of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K, and G478K and / or deletions at positions R179 and / or S180 or I181 and / or G182. The most preferred amylase variants of SEQ ID NO: 1 have the following substitutions: N21D+D97N+V128I and optionally the variant further comprises a substitution at position 200 and / or a deletion at position 180 and / or position 181.

[0171] Other suitable amylases are α-amylases having SEQ ID NO: 12 as described in WO 01 / 66712 or variants having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those with substitutions, deletions or insertions at one or more of the following positions of SEQ ID NO: 12 as described in WO 01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases are variants having a deletion of D183 and G184 and the following substitutions: R118K, N195F, R320K and R458K, and variants further having substitutions at one or more positions selected from the group consisting of M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, with variants further having substitutions at these positions being most preferred.

[0172] Other examples are amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078 and WO 2013 / 001087.

[0173] Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X, and BAN™ Amplify, Amplify Prime (manufactured by Novozymes A / S), as well as Rapidase™, Purastar™ / Effectenz™, Powerase, Preferenz S1000, Preferenz S100, and Preferenz S110 (manufactured by Genencor International Inc. / DuPont).

[0174] Peroxidase / Oxidase Suitable peroxidases / oxidases include those of plant, bacterial, or fungal origin. Chemically or protein-modified mutants are also included. Examples of useful peroxidases include peroxidases from the genus Coprinus, e.g., C. cinereus, and variants thereof, such as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercially available peroxidases include Guardzyme™ (Novozymes A / S).

[0175] Suitable peroxidases are preferably peroxidase enzymes included in the enzyme classification EC 1.11.1.7 as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragments derived therefrom which exhibit peroxidase activity.

[0176] Suitable peroxidases also include haloperoxidase enzymes, such as chloroperoxidase, bromoperoxidase, and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidase (EC 1.11.1.10) catalyzes the formation of hypochlorite from chloride ions. The haloperoxidase may be a chloroperoxidase. Preferably, the haloperoxidase is a vanadium peroxidase, i.e., a vanadate-containing haloperoxidase. In a preferred method, the vanadate-containing haloperoxidase is combined with a chloride ion source.

[0177] Haloperoxidases have been isolated from a variety of fungi, particularly from the fungal group of dematiaceous hyphomycetes, e.g., Caldariomyces such as C. fumago, Alternaria, Curvularia such as C. verruculosa and C. inaequalis, Drechslera, Ulocladium, and Botrytis.

[0178] Haloperoxidases have also been isolated from bacteria such as Pseudomonas, eg, P. pyrrocinia, and Streptomyces, eg, S. aureofaciens.

[0179] The haloperoxidase may be derived from Curvularia sp., in particular Curvularia verruculosa and Curvularia inaequalis, e.g., C. inaequalis CBS102.42 as described in WO 95 / 27046; or C. verruculosa CBS147.63 or C. verruculosa CBS444.70 as described in WO 97 / 04102; or Drechslera hartlebii as described in WO 01 / 79459, Dendryphiella salina as described in WO 01 / 79458, or Drechslera hartlebii as described in WO 01 / 79459, or Drechslera salina as described in WO 01 / 79458, or Drechslera salina CBS147.63 or Drechslera salina CBS444.70 ... salina), Phaeotrichoconis crotalarie, as described in WO 01 / 79461, or Geniculosporium sp., as described in WO 01 / 79460.

[0180] Suitable oxidases include, in particular, any laccase enzyme included in the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting similar activity, such as catechol oxidase (EC 1.10.3.1), o-aminophenol oxidase (EC 1.10.3.4), or bilirubin oxidase (EC 1.3.3.5).

[0181] Preferred laccase enzymes are those of microbial origin: the enzymes can be obtained from plants, bacteria or fungi (including filamentous fungi and yeasts).

[0182] Suitable examples of fungal origin include strains of the following genera: Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes versicolor, ametes, for example, T. villosa and T. versicolor, Rhizoctonia, for example, R. solani, Coprinopsis, for example, C. cinerea, C. comatus, C. friesii, and C. Examples of laccases that can be used include laccases obtained from the genus Psathyrella, such as P. condoleana, the genus Panaeolus, such as P. papilionaceus, the genus Myceliophthora, such as M. thermophila, the genus Schytalidium, such as S. thermophilum, the genus Polyporus, such as P. pinsitus, the genus Phlebia, such as P. radiata (WO 92 / 01046), or the genus Coriolus, such as C. hirsutus (JP 2238885).

[0183] A suitable example of bacterial origin is laccase obtained from a strain of the genus Bacillus.

[0184] Laccases derived from the genus Coprinopsis or Myceliophthora are preferred; in particular, laccases obtained from Coprinopsis cinerea, as disclosed in WO 97 / 08325; or Myceliophthora thermophila, as disclosed in WO 95 / 33836.

[0185] Other materials Any detergent ingredient known in the art for use in detergents may also be utilized. Other optional detergent ingredients include, alone or in combination, anti-corrosion agents, anti-shrinkage agents, anti-resoiling agents, anti-wrinkle agents, bactericides, binders, corrosion inhibitors, disintegrants / decomposers, dyes, enzyme stabilizers (including boric acid, borates, and / or polyols such as propylene glycol), fabric conditioners including clay, fillers / processing aids, fluorescent whitening agents / optical brighteners, foam boosters, foam (soap suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, colorfastness inhibitors, and wicking agents. Any formulation ingredient known in the art for use in detergents may be utilized. The selection of such formulation ingredients is well within the skill of one of ordinary skill in the art.

[0186] Dye Transfer Inhibitors—The detergent compositions of the present invention may also include one or more dye transfer inhibitors. Suitable polymeric dye transfer inhibitors include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidone and polyvinylimidazole, or mixtures thereof. When present in the subject compositions, the dye transfer inhibitors may be present at levels of from about 0.0001% to about 10%, from about 0.01% to about 5%, or even from about 0.1% to about 3% by weight of the composition.

[0187] Fluorescent Whitening Agents—The detergent compositions of the present invention will also preferably contain additional ingredients capable of altering the color shade of the items being cleaned, such as fluorescent whitening agents or optical brighteners. When present, the whitening agent is preferably present at a level of about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in laundry detergent compositions may be used in the compositions of the present invention. The most commonly used fluorescent whitening agents belong to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives, and bisphenyl-distyryl derivatives. Examples of fluorescent whitening agents of the diaminostilbene-sulfonic acid derivative type include: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(2-anilino-4(N-methyl-N-2- Examples of suitable fluorescent whitening agents include (hydroxy-ethylamino)-s-triazin-6-ylamino)stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1,2,3-triazol-2-yl)stilbene-2,2'-disulfonate, and the sodium salt of sodium 5-(2H-naphtho[1,2-d][1,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS, commercially available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino)stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate. Another preferred fluorescent whitening agent is Parawhite KX, available from Paramount Minerals and Chemicals, Mumbai, India. Tinopal CBS-X is 4,4'-bis-(sulfostyryl)-biphenyl disodium salt, also known as disodium distyrylbiphenyl disulfonate.Other fluorescent agents suitable for use in the present invention include 1-3-diarylpyrazolines and 7-alkylaminocoumarins.

[0188] Suitable fluorescent brightener levels include lower levels of about 0.01, 0.05, about 0.1, or even about 0.2% by weight, to upper levels of 0.5 or even 0.75% by weight.

[0189] Soil-releasing polymer—The detergent compositions of the present invention may also contain one or more soil-releasing polymers that aid in the removal of soil from fabrics, such as cotton and polyester-based fabrics, particularly hydrophobic soils from polyester-based fabrics. Soil-releasing polymers can be, for example, nonionic or anionic terephthalate-based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, or polyester polyamides (see, for example, Chapter 7, Powdered Detergents, Surfactant Science Series, Volume 71, Marcel Dekker, Inc.). Another type of soil-releasing polymer is an amphiphilic alkoxylated grease-cleaning polymer that includes a core structure and multiple alkoxylate groups attached to the core structure. The core structure may include a polyalkyleneimine structure or a polyalkanolamine structure, as detailed in WO 2009 / 087523 (incorporated herein by reference). Additionally, random graft copolymers are suitable soil-releasing polymers. Suitable graft copolymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856 and WO 2006 / 113314, which are incorporated herein by reference.

[0190] Anti-resoiling agents—The detergent compositions of the present invention may also include one or more anti-resoiling agents, such as carboxymethyl cellulose (CMC), polyvinyl alcohol (PVA), polyoxyethylene and / or polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, etc. The cellulosic polymers described above as soil-releasing polymers may also function as anti-resoiling agents.

[0191] However, in accordance with the present invention, some of the above polymers, i.e., polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, methyl cellulose, and / or combinations thereof, may be included at lower levels than in currently available detergent compositions or may be eliminated altogether to improve the sustainability profile of the detergent composition.

[0192] Rheology Modifiers The detergent compositions of the present invention may also contain one or more rheology modifiers, structurants, or thickeners different from the viscosity reducing agent. The viscosity reducing agent is selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, and polymeric rheology modifiers that impart shear thinning properties to the aqueous liquid matrix of the liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example, as shown in EP 2169040.

[0193] Other suitable adjuncts include, but are not limited to, anti-shrinkage agents, anti-wrinkle agents, disinfectants, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, fragrances, pigments, suds suppressors, solvents, liquid detergent structurants, and / or structural elasticizers.

[0194] Detergent Product Formulation The detergent compositions of the present invention may be in any convenient form, such as, for example, a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compressed powder, granules, a paste, a gel, or a regular, compressed or concentrated liquid.

[0195] The pouch can be configured as a single or multiple compartments. It can be of any form, shape, and material suitable for holding the composition, preventing leakage of the composition, e.g., leakage of the composition from the pouch prior to contact with water. The pouch is made of a water-soluble film having an internal volume. The internal volume can be separated into the pouch compartments. Preferred films are polymeric materials, preferably polymers, that are formed into films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected from polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer in the film is at least about 60%, e.g., PVA. Preferred average molecular weights will typically be from about 20,000 to about 150,000. The film may also be comprised of a blend composition including a blend of hydrolytically degradable, water-soluble polymers, such as polylactide and polyvinyl alcohol (known under the trade name M8630, available from MonoSol LLC, Indiana, USA), and a plasticizer, such as glycerol, ethylene glycerol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain solid laundry cleaning compositions or components and / or liquid cleaning compositions or components separated by a water-soluble film. The compartment for the liquid components can be different in composition from the compartment containing the solids; see U.S. Patent Application Publication No. 2009 / 0011970 A1.

[0196] The detergent formulation ingredients can be physically separated from each other by compartments in a water-soluble pouch or in different layers of a tablet, which can prevent negative storage interactions between the ingredients. The different dissolution profiles of each compartment can also delay the dissolution of selected ingredients in the wash solution.

[0197] Liquid or gel detergents that are not unit doses may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, or up to about 35% water. Other types of liquids may be included in the aqueous liquid or gel, including, but not limited to, alkanols, amines, diols, ethers, and polyols. Aqueous liquid or gel detergents may contain 0-30% organic solvents. Liquid or gel detergents may also be non-aqueous.

[0198] Solid laundry soap The cellulase of the present invention can be added to a laundry bar and used for hand washing laundry, fabrics, and / or textiles. The term "laundry bar" includes laundry soap, bar soap, complex toilet soap, synthetic toilet soap, and detergent soap. Bar soap types generally differ in the type of surfactant they contain, and the term laundry bar encompasses those containing fatty acid-derived soap and / or synthetic soap. A laundry bar is in a solid physical form at room temperature and is not a liquid, gel, or powder. The term "solid" is defined as a physical form that does not change significantly over time. That is, when a bar (e.g., a laundry bar) is placed in a container, the bar does not change to fill the container in which it is placed. Laundry bar soaps are typically bar-shaped, but may also be in other shapes, such as round or oval.

[0199] The laundry bar may contain one or more enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adducts or hemiacetal adducts), boric acid, borate salts, borax and / or phenylboronic acid derivatives, e.g., 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerin, fatty acids, pH-regulating compounds such as citric acid, acetic acid and / or formic acid, and / or salts of monovalent cations and organic anions, where the monovalent cations are, for example, Na + , K. + or NH4 + and the organic anion may be, for example, formate, acetate, citrate or lactate, and thus the salt of the monovalent cation and the organic anion may be, for example, sodium formate.

[0200] The laundry bar may also contain complexing agents such as EDTA and HEDP, perfumes and / or other types of fillers, surfactants, e.g., anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelating agents, stabilizers, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, suds suppressors, structurants, binders, leaching agents, bleach activators, mud stain removers, anti-redeposition agents, polymeric dispersants, whitening agents, fabric softeners, perfumes and / or other compounds known in the art.

[0201] The laundry soap bar may be processed in conventional laundry soap bar manufacturing equipment, including, but not limited to, mixers, plodders (e.g., two-stage vacuum plodders), extruders, cutters, logo stampers, cooling tunnels, and wrapping devices. The present invention is not limited to producing laundry soap bars by any single method. The premix of the present invention may be added to the soap at various stages of the process. For example, after preparing a premix containing soap, cellulase, optionally one or more additional enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion, the mixture is plodded. The cellulase and optional additional enzymes may be added simultaneously with the protease inhibitor, for example, in liquid form. In addition to the mixing and plodding steps, the method may further include steps of grinding, extruding, cutting, stamping, cooling, and / or wrapping.

[0202] Embodiments of the present invention The present invention is further summarized in the following embodiments, which are designated as E1, E2, etc.

[0203] E1. Use of cellulase to improve the sustainability profile of a detergent composition, cellulase, optionally in combination with at least one additional enzyme, improves the sustainability profile of the detergent composition; A use wherein the sustainability profile of a detergent composition is improved when one or more anti-redeposition polymers of the detergent composition are partially or completely replaced by biodegradable ingredients.

[0204] E2. The use described in E1, wherein the cellulase is selected from the group consisting of cellulases belonging to GH5, GH7, GH12, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21, EC 3.2.1.91, and EC 3.2.1.172.

[0205] E3. The use of E1 or E2, wherein the cellulase is selected from the group consisting of GH5, GH7, GH12, GH44, GH45, and cellulases belonging to EC 3.2.1.4.

[0206] E4. The use of any of E1-E3, wherein the cellulase is obtained from a fungal source, preferably Humicola insolens or Thielavia terrestris, or a bacterial source, preferably Bacillus akibai or Paenibacillus polymyxa.

[0207] E5. The use of any of the preceding embodiments, wherein the cellulase has an amino acid sequence selected from the group consisting of SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:13, or a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity thereto.

[0208] E6. The use of any of the preceding embodiments, wherein the cellulase is in combination with at least one additional enzyme, and the at least one additional enzyme is selected from the group consisting of proteases, amylases, deoxyribonucleases, lipases, xyloglucanases, cutinases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, and mannanases.

[0209] E7. The use of any of the preceding embodiments, wherein the additional enzyme is a deoxyribonuclease.

[0210] E8. The use described in E7, wherein the additional enzyme is a deoxyribonuclease obtained from a fungal source, preferably an Aspergillus species, e.g., A. oryzae, or from a bacterial source, preferably a Bacillus species, e.g., B. cibi.

[0211] E9. The use of E7, wherein the deoxyribonuclease has an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, and SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, and SEQ ID NO:14, or a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity thereto.

[0212] E10. The use of any of the preceding embodiments, wherein the cellulase is present in the detergent composition in an amount corresponding to 0.0001% to 5% (w / w) active enzyme protein.

[0213] E11. The use of any of E6 to E10, wherein the optional one or more additional enzymes are present in the detergent composition in an amount corresponding to 0.0001% to 5% (w / w) active enzyme protein.

[0214] E12. The use according to any one of claims 1 to 10, wherein the one or more replaced anti-redeposition polymers are selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or a combination of two or more of said polymers.

[0215] E13. The use of any of the preceding embodiments, wherein the use provides improved laundry performance compared to use in the presence of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or combinations thereof.

[0216] E14. The use of any of the preceding embodiments, wherein the whiteness of the item is at least maintained, and optionally improved, after at least one full-scale cleaning cycle.

[0217] E15. A detergent composition comprising cellulase and optionally at least one additional enzyme and detergent adjunct ingredients, wherein the composition comprises less than 2%, preferably less than 1% by weight, preferably 0.5% by weight or less of an anti-redeposition polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or a combination of two or more of said polymers.

[0218] E16. The detergent composition according to E15, wherein the cellulase is obtained from a fungal source, preferably Humicola insolens or Thielavia terrestris, or a bacterial source, preferably Bacillus akibai or Paenibacillus polymyxa.

[0219] E17. The detergent composition as described in E15, further comprising a deoxyribonuclease obtained from a fungal source, preferably from the genus Aspergillus, e.g., A. oryzae, or from a bacterial source, preferably from the genus Bacillus, e.g., B. cibi.

[0220] E18. The detergent composition of any of E15-E17, wherein the cellulase has an amino acid sequence selected from the group consisting of SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:13, or a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity thereto.

[0221] E20. The detergent composition described in E17, wherein the deoxyribonuclease has an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3 and SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, and SEQ ID NO:14, or a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity thereto.

[0222] E21. A method of laundering an item, comprising: a) exposing the item to a wash liquor comprising cellulase and optionally at least one additional enzyme or a detergent composition comprising cellulase and optionally at least one additional enzyme in the absence of an anti-redeposition polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, methylcellulose, or combinations thereof; b) completing at least one cleaning cycle; c) optionally adding additional soiling material; and d) optionally rinsing the item (provided the item is fabric); A method comprising:

[0223] E22. The method of E21, wherein the cellulase provides the same or better cleaning performance of items compared to a laundry method performed with a detergent composition comprising polyacrylic acid, modified polyacrylic acid polymer, modified polyacrylic acid copolymer, maleic acid-acrylic acid copolymer, carboxymethylcellulose, cellulose gum, methylcellulose, and / or combinations thereof.

[0224] E23. The method of any of E21 and E22, wherein the cellulase is obtained from a fungal source, preferably Humicola insolens or Thielavia terrestris, or a bacterial source, preferably Bacillus akibai or Paenibacillus polymyxa.

[0225] E24. The method of any of E21-E23, wherein the cellulase has an amino acid sequence selected from the group consisting of SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:13, or a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity thereto.

[0226] E25. The method of any of E21 to E24, wherein the anti-redeposition polymer is selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethyl cellulose, cellulose gum, and methyl cellulose, or combinations thereof, providing improved laundry performance compared to methods in the presence of an anti-redeposition polymer.

[0227] E26. The method of E21, further comprising a polypeptide having DNase activity.

[0228] E27. The method of E26, wherein the polypeptide having DNase activity has an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3 and SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9 and SEQ ID NO:14, or a polypeptide having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity thereto.

[0229] Detergent Composition The following ranges of detergent ingredients are generally useful in conjunction with the low polymer detergent compositions of the present invention.

[0230] [Table 1]

[0231] [Table 2]

[0232] [Table 3]

[0233] [Table 4]

[0234] [Table 5]

[0235] [Table 6]

[0236] The surfactant components are available from BASF, Ludwigshafen, Germany (Lutensol®); Shell Chemicals, London, UK; Stepan, Northfield, Ill., USA; Huntsman, Salt Lake City, Utah, USA; Clariant, Sulzbach, Germany (Praepagen®).

[0237] Sodium tripolyphosphate is available from Rhodia, Paris, France. Zeolite is available from Industrial Zeolite (UK) Ltd, Grays, Essex, UK. Citric acid and sodium citrate are available from Jungbunzlauer, Basel, Switzerland. NOBS is sodium nonanoyloxybenzenesulfonate supplied by Eastman, Batesville, Ark., USA.

[0238] TAED is tetraacetylethylenediamine supplied by Clariant GmbH, Sulzbach, Germany under the trade name Peractive®.

[0239] Sodium carbonate and sodium bicarbonate are available from Solvay, Brussels, Belgium.

[0240] Polyacrylate, polyacrylate / maleate copolymers are available from BASF, Ludwigshafen, Germany.

[0241] Repel-O-Tex® is available from Rhodia, Paris, France.

[0242] Texcare® is available from Clariant, Sulzbach, Germany. Sodium percarbonate and sodium carbonate are available from Solvay, Houston, Tex., USA.

[0243] Ethylenediamine-N,N'-disuccinic acid sodium salt, (S,S) isomer (EDDS) was supplied by Octel, Ellesmere Port, UK.

[0244] Hydroxyethanediphosphate (HEDP) was supplied by Dow Chemical, Midland, Mich., USA.

[0245] Enzymes: Savinase®, Savinase® Ultra, Stainzyme® Plus, Lipex®, Lipolex®, Lipoclean®, Celluclean®, Carezyme®, Natalase®, Stainzyme®, Stainzyme® Plus, Termamyl®, Termamyl® ultra, and Mannaway® are available from Novozymes, Bagsvaerd, Denmark.

[0246] Enzymes: Purafect®, FN3, FN4 and Optisize are available from Genencor International Inc., Palo Alto, California, US.

[0247] Direct violet 9 and 99 are available from BASF DE, Ludwigshafen, Germany. Solvent violet 13 is available from Ningbo Lixing Chemical Co., Ltd. Ningbo, Zhejiang, China. Whitening agents are available from Ciba Specialty Chemicals, Basel, Switzerland.

[0248] All percentages are calculated by weight unless otherwise stated. All percentages and ratios are calculated based on the active level of the total composition unless otherwise stated.

[0249] It should be understood that every maximum numerical limit given throughout this specification will include every lower numerical limit, as if such lower numerical limit were expressly written. Every minimum numerical limit given throughout this specification will include every higher numerical limit, as if such higher numerical limit were expressly written. Every numerical range given throughout this specification will include every narrower numerical range that is subsumed within such broader numerical range, as if such narrower numerical ranges were expressly written herein.

[0250] experiment material Powder detergent

[0251] [Table 7]

[0252] [Table 8]

[0253] contaminants W-SBL 2004 Soil Ballast Load Fabric was purchased from CFT (Center for Test Materials BV). Red clay garden soil was purchased from a Chinese horticultural market and filtered through a 50-mesh sieve before use.

[0254] [Table 9]

[0255] To summarize the results, the tracers were classified into three categories: Natural fabrics: W-10A, W-12A, W-80, A, CN-11, CN-42; T-266, pre-aged T-266 Semi-synthetic fabric: P-CN-01, W-20A Synthetic fabrics: T-720, PN-01, W-30A, W-40A, T-340 nylon / lycra 81 / 19;

[0256] Actual item Actual items refer to cloths or fabrics used / worn by the volunteers and not washed prior to FSW testing.

[0257] [Table 10]

[0258] Test Method Test #1: Full-scale washing (FSW) assay for whiteness evaluation FSW is used to evaluate the cleaning performance of a washer under scientifically designed conditions.

[0259] [Table 11]

[0260] The following cleaning procedure instructions were followed. a. Prepare ballast, test swatches, and hard water with Ca / Mg based on desired water hardness. b. Dissolve the detergent in 1L of hard water and stir for 30 minutes. c. Add red clay powder to 1 L of detergent solution and stir for 10 min. Note that the red clay powder must be sieved through a 50-mesh sieve. d. Add the test stain, soil ballast, and ballast into the washer drum. e. Wash parameters: Select program, water level, and temperature. f. Press the start button on the machine to start filling with water. The water consumption will be automatically registered at this point. g. Add the detergent-red clay mixture through the detergent tank. Rinse the beaker with hard water and add the rinse water into the washer until all the clay powder is added into the machine drum. h. After washing is complete, remove the test swatch from the towel and place on a tray to dry. i. Repeat the above steps several times to mimic greying / yellowing in real-life conditions.

[0261] Test #2: Full-Scale Wash (FSW) Assay of Whiteness on Actual (Used) Items FSW is used to evaluate the cleaning performance of a washer under scientifically designed conditions.

[0262] Washing conditions: Standard EU washing conditions are listed below.

[0263] [Table 12]

[0264] The following cleaning procedure instructions were followed. a. Prepare ballast, test swatches, and hard water with Ca / Mg based on desired water hardness. Select a core of the actual item and cut it into 2 or 4 uniform pieces. Note that stains, yellowing, and graying should be uniformly distributed on each piece. b. Add the ballast and cut pieces of the actual item to the washer. Each piece from one actual item is randomly added to each test condition. c. Dissolve the detergent in 1L of hard water and stir for 30 minutes. d. Wash parameters: Select program, water level, and temperature. e. Press the start button on the machine to start filling with water. Water consumption will be automatically registered at this point. j. Add detergent solution via detergent tank, rinse beaker with hard water and add rinse water to machine to ensure all detergent is added to machine drum. f. After the wash is complete, remove the ballast and leave the actual item pieces in the washer. g. Add 7.5 g of detergent B and 7.5 g of pigmented soil to 1 L of hard water (14 dH as this is the main wash) and stir for 10 minutes. h. Parameters for soil rinse: select program and water level. i. After the water is automatically drawn in, add the Model O-Pigment Soil Solution via the detergent tank. Rinse the beaker several times with hard water and add the rinse water to the washer. j. After washing is complete, remove the test swatch from the towel and place on a tray to dry.

[0265] Terg-O-tometer (TOM) washing assay The Terg-O-Meter (TOM) is a mid-scale model washing system that can be adapted to simultaneously test up to 16 different washing conditions. The TOM is essentially a large, temperature-controlled water bath with up to 16 open metal beakers immersed within it. Each beaker constitutes a small, top-loading washing machine, and during the experiment, each contains a solution of a specific detergent / enzyme / polymer system and soiled and unsoiled fabrics whose performance is to be tested. Mechanical stress is achieved by a rotating stirring arm, which agitates the liquid in each beaker.

[0266] The TOM model wash system is primarily used for medium-scale testing of detergents, enzymes, and polymers under EU or AP wash conditions. In TOM experiments, factors such as the ratio of ballast to soil and the ratio of fabric to wash liquor can be varied. In this way, TOM serves as a bridge between small-scale experiments and more time-consuming full-scale experiments.

[0267] Equipment: A water bath with 16 steel beakers and one rotating arm per beaker with a detergent solution capacity of 1 L. The temperature range is 5°C to 80°C. The water bath must be filled with deionized water. The rotation speed can be set to 70-120 rpm / min.

[0268] Set the temperature of the Terg-O-Tometer and start the rotation in the water bath. Wait for the temperature to adjust (to a tolerance of + / - 0.5°C). All beakers should be clean and free from traces of previous test material.

[0269] Prepare a cleaning solution in a bucket with the desired amount of detergent, temperature, and water hardness. Dissolve the detergent during 10 minutes of magnetic stirring. The cleaning solution should be used within 30-60 minutes of preparation.

[0270] 1 L of cleaning solution is added to a TOM beaker. The cleaning solution is stirred at 120 rpm, and then, optionally, one or more enzymes or polymers are added to the beaker. The rags are introduced into the beaker, followed by a ballast load. A time measurement begins when the rags and ballast are added to the beaker. The rags are washed for 20 or 30 minutes, after which the stirring is stopped.

[0271] The wash load is then transferred from the TOM beaker to a sieve and rinsed with room temperature tap water. The soiled rags are separated from the ballast load. The soiled rags are transferred to a 5 L beaker containing room temperature tap water under running water for 5 minutes. The ballast load is kept separate for subsequent inactivation. The rags are gently squeezed by hand to drain and placed on a paper-covered tray. The rags are allowed to dry overnight before being subjected to analysis, including delta REM measurement.

[0272] Actual item whiteness panel The panel test is based on visual whiteness ratings by eight panelists. To increase panel differentiation, the actual item is cut into two equal pieces and washed in two conditions that are compared pairwise.

[0273] Panelists are asked to assign these priorities based on the cleaning appearance of each actual item after paired washing and then assign these panel scores based on the following criteria:

[0274] [Table 13]

[0275] When comparing the test conditions to the benchmark, a positive score means that the test conditions appear better / brighter / cleaner than the benchmark, and a negative score suggests that the test conditions appear worse / darker / dirtier than the benchmark. The benchmark will be determined at the time of trial and will be indicated in the results presentation.

[0276] % Preference is the percentage of panelists who prefer the test condition (in this trial, calculated as the number of panelists who prefer the test condition over the benchmark divided by the total of 8 panelists in %). Mean reliability = Σ(panel score for each item).

[0277] Optical reflectance measurement (Delta REM) After washing and rinsing, the swatches were laid out flat and allowed to air dry overnight at room temperature. All washes are evaluated the day after washing. Brightness can also be expressed as re-emission (R), which is a measure of the light reflected or emitted from the test material when illuminated with white light. The re-emission (R) of fabrics is measured at 460 nm using a Macbeth Color Eye 7000 reflectance spectrophotometer equipped with a very small aperture. Measurements were made without including UV in the incident light, and the reflectance at 460 nm was extracted. Measurements are performed according to the manufacturer's protocol.

[0278] Enzyme assay Assay I: Test for DNase activity DNase activity was determined using DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), which was prepared according to the supplier's instructions. Briefly, 21 g of agar was dissolved in 500 ml of water and then autoclaved at 121°C for 15 min. The autoclaved agar was then thermostated at 48°C in a water bath, after which 20 ml of the agar was poured into a Petri dish and allowed to solidify by incubation at room temperature overnight. Five μl of enzyme solution was added to the solidified agar plate, and DNase activity was observed as a colorless area surrounding the spotted enzyme solution.

[0279] Assay II: Test for cellulase activity Cellulase activity is determined as the ability of an enzyme to catalyze the hydrolysis of 1,4-β-D-glucosidic bonds in β-1,4-glucan (cellulose). For purposes of the present invention, cellulase activity is determined using AZCL-HE-Cellulose (Megazyme) as the reaction substrate. [Example]

[0280] Example 1 Anti-redeposition performance by clay assay Example 1a: Detergent A, as added on top, below, performance tested as described in "Test #1."

[0281] [Table 14]

[0282] Example 1b: Detergent A added on top of

[0283] [Table 15]

[0284] It is clear from Tables E7 and E8 that the loss of performance that occurs when polycarboxylate polymers are removed can be fully regained or even surpassed in part with cellulase, as exemplified by SEQ ID 11 and SEQ ID 12.

[0285] Example 2: Evaluation of stain prevention on actual items For dinginess prevention on real items (used items), real item pieces were cleaned (Test #2) according to the protocol described above in the "Full Scale Cleaning (FSW)" assay and measured by reflectance at 460 nm. Delta REM is relative to REF.

[0286] [Table 16]

[0287] For prevention of dinginess on real items (used items), real item pieces were washed (Test #2) according to the protocol described above in the Full Scale Wash (FSW) assay and measured by panel scores.

[0288] [Table 17]

[0289] [Table 18]

[0290] It is clear from the panel results that high polymer is more beneficial than no polymer (condition 2 is less preferable than condition 1), and that DNAse or DNAse plus cellulase are each preferable to high polymer on T-shirts and some socks (conditions 3 or 4 are preferable to condition 1). When no polymer is present, both DNAse and DNAse plus cellulase are beneficial on most items (conditions 3 or 4 are preferable to condition 2). Similar conclusions cannot be reached from "Delta REM" or "Reliability Average."

[0291] Example 3 Powder detergent Detergent compositions C-K below are non-limiting examples of powder detergents. Detergents C, F, and I are reference detergents, while detergents D, E, G, H, J, K, and L have reduced levels of anti-redeposition polymer and increased levels of cellulase and / or DNase.

[0292] [Table 19]

[0293] [Table 20]

[0294] Example 4: Projected sustainability improvements through polymer reduction When the anti-redeposition polymer was reduced from 4% to 0.5% (wt%) by replacement with cellulase, the amount of persistent fossil polymer that could be avoided in production, transportation, and environmental loss was calculated based on publicly available data as follows:

[0295] [Table 21]

Claims

1. 1. Use of cellulase for improving the sustainability profile of a detergent composition, comprising: the cellulase, optionally in combination with at least one additional enzyme, improves the sustainability profile of the detergent composition; A use wherein the sustainability profile of said detergent composition is improved when one or more anti-redeposition polymers of said detergent composition are partially or completely replaced by biodegradable ingredients.

2. The use according to claim 1, wherein the cellulase is selected from the group consisting of cellulases belonging to GH5, GH7, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21, EC 3.2.1.91, and EC 3.2.1.

172.

3. 3. Use according to claim 1 or 2, wherein the cellulase is obtained from a fungal source, preferably Humicola insolens or Thielavia terrestris, or a bacterial source, preferably Bacillus akibai or Paenibacillus polymyxa.

4. The use described in claim 1 or 2, wherein the cellulase has an amino acid sequence selected from the group consisting of SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, and SEQ ID NO: 13, or an amino acid sequence 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 96%, at least 97%, at least 98%, or even 99% sequence identity to any of SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, and SEQ ID NO:

13.

5. 5. The use according to any one of claims 1 to 4, wherein the cellulase is in combination with at least one additional enzyme, and the at least one additional enzyme is selected from the group consisting of proteases, amylases, deoxyribonucleases, lipases, xyloglucanases, cutinases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, and mannanases.

6. 6. The use according to claim 1 or 5, wherein the additional enzyme is a deoxyribonuclease.

7. 7. The use according to claim 6, wherein the deoxyribonuclease is obtained from a fungal source, preferably from the genus Aspergillus, e.g., A. oryzae, or from a bacterial source, preferably from the genus Bacillus, e.g., B. cibi.

8. 8. The use of claim 7, wherein the deoxyribonuclease has an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, and SEQ ID NO:14, or a deoxyribonuclease having an amino acid sequence 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%, or even at least 99% sequence identity to any of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, and SEQ ID NO:

14.

9. The use according to any one of claims 1 to 8, wherein the cellulase is present in the detergent composition in an amount corresponding to from 0.0001% to 5% (w / w) active enzyme protein.

10. 9. Use according to any one of claims 5 to 8, wherein the one or more optional additional enzymes are present in the detergent composition in an amount corresponding to from 0.0001% to 5% (w / w) active enzyme protein.

11. 11. The use according to any one of claims 1 to 10, wherein the one or more replaced anti-redeposition polymers are selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or a combination of two or more of said polymers.

12. 12. The use according to any one of claims 1 to 11, wherein the cleaning performance of the item as measured by delta REM is at least maintained, and optionally improved, after at least one full-scale cleaning cycle.

13. 1. A detergent composition comprising a cellulase and optionally at least one additional enzyme and detergent adjunct ingredients, said composition comprising less than 1% by weight, preferably 0.5% by weight or less, of an anti-redeposition polymer selected from the group consisting of polyacrylic acid, modified polyacrylic acid polymers, modified polyacrylic acid copolymers, maleic acid-acrylic acid copolymers, carboxymethylcellulose, cellulose gum, and methylcellulose, or a combination of two or more of said polymers.

14. 14. The detergent composition of claim 13, wherein the cellulase is obtained from a fungal source, preferably Humicola insolens or Thielavia terrestris, or a bacterial source, preferably alkaliphilic Bacillus akibai or Paenibacillus polymyxa.

15. 14. The detergent composition of claim 13, further comprising a deoxyribonuclease obtained from a fungal source, preferably from the genus Aspergillus, e.g., A. oryzae, or from a bacterial source, preferably from the genus Bacillus, e.g., B. cibi.

16. 15. The detergent composition of claim 13 or 14, wherein the cellulase has an amino acid sequence selected from the group consisting of SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:13, or a cellulase having an amino acid sequence 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 96%, at least 97%, at least 98%, or even 99% sequence identity to any of SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:

13.

17. 16. The detergent composition of claim 15, wherein the deoxyribonuclease has an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, and SEQ ID NO:14, or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or even 99% sequence identity thereto.

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