Detergent composition containing catalase and amylase

Abstract

The present invention relates to detergent compositions comprising catalase and amylase. The present invention also relates to methods of using the detergent compositions.

Description

[Technical Field]

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

[0002] The present invention relates to novel compositions comprising catalase and α-amylase. The compositions of the present invention are suitable as cleaning or detergent compositions, such as laundry detergent compositions and dishwashing compositions, including automatic dishwashing compositions and hand dishwashing compositions. [Background technology]

[0003] In the detergent industry, enzymes have been used for decades as part of cleaning formulations. α-Amylase is one of the most suitable enzymes in such formulations from a commercial standpoint, but other enzymes, including proteases, lipases, additional amylases, cellulases, hemicellulases, or mixtures of enzymes, are often used. To improve the cost and / or performance of enzymes, enzymes are often modified to increase activity at low temperatures, for example, to increase stability in the presence of chelating agents, to increase specific activity at a given pH, or to enhance Ca 2+ The search for enzymes with altered properties, such as altered dependency and increased stability in the presence of other detergent ingredients (e.g., bleach, surfactants, etc.), is ongoing. For example, α-amylases have typically been derived from Bacillus licheniformis, also known as Termamyl. Other α-amylases may also be used.

[0004] Catalases [hydrogen peroxide:hydrogen peroxide oxidoreductase (EC 1.11.1.6)] are enzymes that catalyze the conversion of hydrogen peroxide (HO) to oxygen (O) and water (HO). These widespread enzymes have been purified from a variety of animal tissues, plants, and microorganisms (see Chance and Maehly, 1955, Methods Enzymol. 2; 764-791).

[0005] Catalase preparations are used commercially for diagnostic enzyme kits, the enzymatic production of sodium gluconate from glucose, the neutralization of H2O2 waste, and the removal of H2O2 and / or the production of O2 in foods and beverages. Summary of the Invention [Problem to be solved by the invention]

[0006] The present invention provides a detergent composition comprising catalase and α-amylase, wherein the enzymes maintain activity and stability in the detergent composition in the presence of detergent ingredients such as chemicals, bleaching systems, or chelating agents. [Means for solving the problem]

[0007] The present invention relates to detergent compositions comprising (i) a polypeptide having catalase activity and having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 1, 2, 3, 4 or 5, and (ii) a polypeptide having alpha amylase activity.

[0008] The present invention also relates to the use of the detergent composition according to any one of the embodiments described herein in laundry, hand dishwashing, or automatic dishwashing.

[0009] The present invention also relates to a method of laundering fabrics, comprising laundering a fabric with the detergent composition according to any one of the embodiments described herein.

[0010] The present invention also relates to a method of washing dishes in an automatic dishwashing machine using the detergent composition according to any one of the embodiments described herein, comprising the steps of adding the detergent composition to a detergent composition compartment in the automatic dishwashing machine and discharging the detergent composition during a main wash cycle. DETAILED DESCRIPTION OF THE INVENTION

[0011] Array Overview SEQ ID NO: 1 is the amino acid sequence of catalase (Scytalidium thermophilum). SEQ ID NO: 2 is the amino acid sequence of catalase (Malbranchea cinnamomea). SEQ ID NO: 3 is the amino acid sequence of catalase (Rhizomucor pusillus). SEQ ID NO: 4 is the amino acid sequence of catalase (Rhizomucor pusillus). SEQ ID NO: 5 is the amino acid sequence of catalase (Penicillium emersonii). SEQ ID NO: 6 is the amino acid sequence of α-amylase (AAI10). SEQ ID NO: 7 is the amino acid sequence of α-amylase (AA560). SEQ ID NO: 8 is the amino acid sequence of α-amylase (SP722). SEQ ID NO: 9 is the amino acid sequence of α-amylase (TS23). SEQ ID NO: 10 is the amino acid sequence of alpha-amylase (Cytophaga sp.). SEQ ID NO: 11 is the amino acid sequence of α-amylase (SP707). SEQ ID NO: 12 is the amino acid sequence of the fusion alpha-amylase (LASB0000). SEQ ID NO: 13 is the amino acid sequence of α-amylase (SP.7-7). SEQ ID NO: 14 is the amino acid sequence of α-amylase (Termamyl). SEQ ID NO: 15 is the amino acid sequence of the fusion α-amylase. SEQ ID NO: 16 is the amino acid sequence of the fusion alpha-amylase (LABM). SEQ ID NO: 17 is the amino acid sequence of α-amylase (KSM-AP1378). SEQ ID NO: 18 is the amino acid sequence of α-amylase (KSM-K36 / -K38). SEQ ID NO: 19 is the amino acid sequence of α-amylase (BSG). SEQ ID NO: 20 is the amino acid sequence of alpha-amylase (BAN). SEQ ID NO: 21 is the amino acid sequence of the synthetic construct. SEQ ID NO: 22 is the amino acid sequence of the synthetic construct. SEQ ID NO: 23 is the amino acid sequence of the synthetic construct. SEQ ID NO: 24 is the amino acid sequence of the synthetic construct. SEQ ID NO: 25 is the amino acid sequence of the synthetic construct. SEQ ID NO: 26 is the amino acid sequence of the synthetic construct. SEQ ID NO: 27 is the amino acid sequence of the synthetic construct. SEQ ID NO: 28 is the amino acid sequence of the synthetic construct. SEQ ID NO: 29 is the amino acid sequence of the synthetic construct. SEQ ID NO: 30 is the amino acid sequence of the synthetic construct. SEQ ID NO: 31 is the amino acid sequence of the synthetic construct. SEQ ID NO: 32 is the amino acid sequence of the synthetic construct. SEQ ID NO: 33 is the amino acid sequence of the synthetic construct.

[0012] definition In accordance with this detailed description, the following definitions apply: Note that the singular forms "a," "an," and "the" include plural references unless the context clearly indicates otherwise.

[0013] Reference herein to "about" a value or parameter includes aspects related to this value or parameter itself. For example, a description that refers to "about X" includes the aspect "X."

[0014] Unless otherwise defined or clearly indicated by context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs.

[0015] The term "α-amylase" is synonymous with "polypeptide having α-amylase activity." α-1,4-glucan-4-glucanohydrolases (EC 3.2.1.1) comprise a group of enzymes that catalyze the hydrolysis of starch and other linear and branched 1,4-glucoside oligosaccharides and polysaccharides. Thus, as used herein, the term "α-amylase" refers to an enzyme with α-amylase activity (enzyme classification: EC 3.2.1.1) that hydrolyzes the α-linkages of large α-linked polysaccharides, such as starch and glycogen, to yield glucose and maltose. The terms "α-amylase" and "amylase" may be used interchangeably and have the same meaning and purpose herein. For purposes of the present invention, α-amylase activity is determined according to the procedure described under the subheading "Methods" below. In one aspect, the α-amylase of the invention has at least 20%, e.g., at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 100% of the α-amylase activity of one or more of the polypeptides of SEQ ID NOs: 6-20.

[0016] The term "catalase activity" as used herein refers to hydrogen peroxide oxidoreductase activity (EC 1.11.1.6) that catalyzes the conversion of 2H2O2 to hydrogen peroxide:O2 + 2H2O. For purposes of the present invention, catalase activity is determined according to U.S. Pat. No. 5,646,025. One unit of catalase activity is equal to the amount of enzyme that catalyzes the oxidation of 1 μmole of hydrogen peroxide under assay conditions.

[0017] As used herein, the term "amino acid" refers to the 20 standard genetically encoded amino acids and their corresponding "d" stereoisomers (as compared to the naturally occurring "I" form), omega-amino acids, other naturally occurring amino acid sequences, non-standard amino acids (e.g., α,α-disubstituted amino acids, N-alkyl amino acids, etc.), and chemically derivatized amino acids. Chemical derivatives of one or more amino acids can be obtained by reaction with a functional side group. Such derivatized molecules include, for example, molecules in which a free amino group is derivatized to form an amine hydrochloride, p-toluenesulfonyl, carboxybenzoxy, t-butyloxycarbonyl, chloroacetyl, or formyl groups. Free carboxyl groups can be derivatized to form salts, methyl and ethyl esters or other types of esters, and hydrazides. Free hydroxyl groups can be derivatized to form O-acyl or O-alkyl derivatives. Also included as chemical derivatives are peptides containing naturally occurring amino acid derivatives of the 20 standard amino acids. For example, proline may be substituted with 4-hydroxyproline, lysine with 5-hydroxylysine, histidine with 3-methylhistidine, serine with homoserine, and lysine with ornithine. Derivatives also include peptides containing one or more additions or deletions, so long as the requisite activity is maintained. Other included modifications are amidation, amino-terminal acylation (e.g., acetylation or thioglycolic acid amidation), terminal carboxylation (e.g., ammonia or methylamine), and similar terminal modifications.

[0018] When an amino acid is specifically listed, such as with terms like "alanine" or "Ala" or "A," the term refers to both l-alanine and d-alanine unless expressly stated otherwise. Other non-conventional amino acids may also be suitable components of the polypeptides of the invention, so long as the desired functional properties are retained by the polypeptide. For the peptides shown, each encoded amino acid residue is represented, where appropriate, by the single-letter designation corresponding to the trivial name of the conventional amino acid. In one embodiment, the polypeptides of the invention comprise or consist of l-amino acids.

[0019] The term "catalytic domain" refers to the region of an enzyme that contains the enzyme's catalytic machinery.

[0020] The term "cDNA" refers to a DNA molecule that can be prepared by reverse transcription from a mature, spliced ​​mRNA molecule obtained from a eukaryotic cell. cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before the mature, spliced ​​mRNA appears.

[0021] The term "coding sequence" refers to a polynucleotide that directly specifies the amino acid sequence of its polypeptide product. The boundaries of the coding sequence are generally determined by an open reading frame, which usually begins with the ATG start codon or alternative start codons such as GTG and TTG and ends with a stop codon such as TAA, TAG, and TGA. A coding sequence can be a DNA, cDNA, synthetic, or recombinant polynucleotide.

[0022] The term "control sequences" refers to all components necessary for expression of a polynucleotide encoding a variant of the present invention. Each control sequence may be native or foreign to the polynucleotide encoding the variant, or native or foreign to each other. Such control sequences include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, control sequences include a promoter and transcriptional and translational stop signals. Control sequences may be provided with linkers to introduce specific restriction sites facilitating ligation of the control sequences with the coding region of the polynucleotide encoding the variant.

[0023] As used herein, the term "corresponding to" refers to a method of determining a particular amino acid of a sequence, with reference to a particular amino acid sequence. For example, for purposes of the present invention, when a particular amino acid position is referenced, one of skill in the art can determine which particular amino acid may be associated in another amino acid sequence by aligning the other amino acid sequence with the referenced amino acid sequence. Alignment of another amino acid sequence with, for example, the sequence set forth in SEQ ID NO: 5, or any other sequence listed herein, is described elsewhere herein. Alternative alignment methods may be used and are known to those of skill in the art.

[0024] As used herein, the term "dishwashing composition" refers to any type of composition for cleaning hard surfaces. The present invention is not limited to any particular type of dishwashing composition or any particular detergent. Thus, in one embodiment, the dishwashing composition is a liquid dishwashing composition, a powder dishwashing composition, and the composition may optionally be in the form of a unit dose.

[0025] The term "enzyme detergency benefits" as used herein refers to the beneficial effects that enzymes can impart to a detergent compared to the same detergent without enzymes. Important detergency benefits that enzymes can provide are stain removal of soils that are not or only slightly visible after washing and / or cleaning, preventing or reducing the redeposition of soils that are released during the laundering process (an effect also known as anti-redeposition), and fully or partially restoring the whiteness of fabrics that were originally white but that have become grayish or yellowish in appearance after repeated use and washing (an effect also known as whitening). Fabric care benefits are also important to enzyme detergency benefits, even though they are not directly related to catalytic soil removal or prevention of soil redeposition. Examples of such fabric care benefits are the prevention or reduction of dye transfer from one fabric to another or to another part of the same fabric (an effect also referred to as dye transfer prevention or back-soiling prevention), the removal of protruding or broken fibers from the fabric surface to reduce pilling tendency or to remove existing pilling or fluff (an effect also referred to as anti-pilling); improved fabric softness, clarification of fabric color, and the removal of particulate soils trapped in the fibers of fabrics or garments. Enzymatic bleaching is a further enzyme detergency benefit, where catalytic activity is commonly used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.

[0026] The term "expression" as used herein refers to any step involved in the production of a variant, including but not limited to transcription, post-transcriptional modification, translation, post-translational modification, and secretion.

[0027] As used herein, the term "expression vector" refers to a linear or circular DNA molecule that contains a polynucleotide encoding a variant and is operably linked to a control sequence that allows for its expression.

[0028] The term "fragment" refers to a polypeptide having one or more (several) amino acids deleted from the amino and / or carboxyl terminus of the mature polypeptide, wherein the fragment has α-amylase activity.

[0029] The term "high stringency conditions" refers to 12-24 hours of prehybridization and hybridization for probes at least 100 nucleotides long, following standard Southern blotting procedures: 5x SSPE, 0.3% SDS, 200 micrograms / mL sheared denatured salmon sperm DNA, and 50% formamide at 42°C. Finally, the carrier material is washed three times with 2x SSC, 0.2% SDS for 15 minutes each at 65°C.

[0030] The term "hard surface cleaning" as used herein refers to cleaning of hard surfaces, which may include surfaces of hard articles such as floors, tables, walls, etc., as well as cars (auto-washing) and dishes (dishwashing). Dishwashing includes, but is not limited to, cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, and forks, serving utensils, ceramics, plastics, metals, china, glass, and acrylic.

[0031] The term "improved property" is defined herein as a characteristic associated with a variant that is improved relative to the parent α-amylase. Such improved properties include, but are not limited to, increased amylolytic activity, improved catalytic efficiency, improved catalytic rate, improved chemical stability, improved oxidative stability, improved pH activity, improved pH stability, increased relative specific activity, increased specific activity, increased substrate binding, increased substrate cleavage, increased substrate specificity, improved substrate stability, improved surface properties, increased thermal activity, improved heat resistance, improved soil removal performance, e.g., performance on starch-containing soils, improved cleaning performance, such as stain removal and graying prevention, stability, e.g., thermal stability, pH stability, or stability in the presence of builders, including chelating agents, stability in powder, liquid, or gel detergent formulations or dishwashing compositions, temperature-dependent performance and activity profile, pH activity, substrate specificity, product specificity, and chemical stability. The improved property can be any of the properties defined and described herein, such as cleaning performance.

[0032] As used herein, the term "isolated" refers to a substance that exists in a form or environment 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, from which one or more or all of the naturally occurring components with which it is naturally associated have been at least partially removed; (3) any substance that has been modified by the hand of man 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 naturally associated (e.g., multiple copies of the gene encoding the substance, 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.

[0033] The term "isolated polynucleotide" refers to a polynucleotide that has been artificially modified. In one aspect, an isolated polynucleotide is at least 1% pure, e.g., at least 5% pure, at least 10% pure, at least 20% pure, at least 40% pure, at least 60% pure, at least 80% pure, at least 90% pure, and at least 95% pure, as measured by agarose gel electrophoresis. The polynucleotide can be of genomic, cDNA, RNA, semisynthetic, synthetic origin, or any combination thereof.

[0034] As used herein, the term "mature polypeptide" refers to a polypeptide in its final form after translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc. It is known in the art that a host cell can produce a mixture of two or more different mature polypeptides (i.e., with different C- and / or N-terminal amino acids) expressed by the same polynucleotide.

[0035] As used herein, the term "mature polypeptide coding sequence" refers to a polynucleotide that encodes a mature polypeptide having α-amylase activity.

[0036] The term "modified," in the context of a polypeptide of the invention, means that one or more amino acids in a reference amino acid sequence have been altered by substitution with a different amino acid, by insertion of an amino acid, or by deletion, preferably by at least two deletions. The terms "modified," "altered," and "mutated" may be used interchangeably and have the same meaning and purpose.

[0037] The term "moderate stringency conditions" refers to 12-24 hours of prehybridization and hybridization for probes at least 100 nucleotides long, following standard Southern blotting procedures: 5x SSPE, 0.3% SDS, 200 micrograms / mL sheared denatured salmon sperm DNA, and 35% formamide at 42°C. Finally, the carrier material is washed three times with 2x SSC, 0.2% SDS for 15 minutes each at 55°C.

[0038] The term "medium-to-high stringency conditions" refers to 12-24 hours of prehybridization and hybridization for probes at least 100 nucleotides long, following standard Southern blotting procedures, in 5x SSPE, 0.3% SDS, 200 micrograms / mL sheared denatured salmon sperm DNA, and 35% formamide at 42°C. Finally, the carrier material is washed three times with 2x SSC, 0.2% SDS for 15 minutes each at 60°C.

[0039] The term "mutant" refers to a polynucleotide that encodes a variant.

[0040] The term "nucleic acid construct" refers to a nucleic acid molecule, having a single or double helix, that is isolated from a naturally occurring gene, or that has been modified to contain segments of nucleic acid in a manner not otherwise found in nature, or that is synthetic. The term nucleic acid construct is synonymous with the term "expression cassette" when the nucleic acid construct contains the control sequences required for expression of a coding sequence of the present invention.

[0041] The term "operably linked" refers to a configuration in which a control sequence is positioned in relation to a coding sequence of a polynucleotide so that the control sequence directs the expression of the coding sequence.

[0042] The terms "parent" or "parent α-amylase" refer to an α-amylase that has been modified to produce an enzyme variant of the invention. The parent may be a naturally occurring (wild-type) polypeptide or a variant thereof.

[0043] As used herein, the term "sequence identity" refers to the relatedness between two amino acid sequences or between two nucleotide sequences, which is described by the parameter "sequence identity."

[0044] The term "variant" refers to a polypeptide having enzymatic activity that contains alterations, 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 occupying a position with a different amino acid, a deletion refers to the removal of an amino acid occupying a position, and an insertion refers to the addition of an amino acid adjacent to and immediately following the amino acid occupying a position.

[0045] As used herein, the term "subsequence" refers to a polynucleotide lacking one or more (e.g., multiple) nucleotides at the 5' and / or 3' end of a mature polypeptide coding sequence, wherein the subsequence encodes a fragment that has α-amylase activity.

[0046] The term "textile" refers to staple fibers and filaments suitable for conversion into or use as fabrics, yarns, woven, knitted, and nonwoven fabrics. The term encompasses yarns made from natural and synthetic (e.g., man-made) fibers. The term "textile material" is a general term for fibers, yarn intermediates, yarns, fabrics, and products (e.g., clothing and other products) made from fabrics.

[0047] The term "fabric care benefits," as used herein, is defined as those not directly related to catalytic stain removal or prevention of soil redeposition, but which are also important to enzyme cleaning benefits. Examples of such fabric care benefits are prevention or reduction of dye transfer from one fabric to another or to other parts of the same fabric (an effect also known as dye transfer prevention or backstain prevention), removal of protruding or broken fibers from the fabric surface to reduce pilling tendency, or removal of pre-existing pills or fluff (an effect also known as pill prevention); improved fabric softness, fabric color clarification, and removal of particulate soils trapped in fabric fibers. Enzyme bleaching is yet another enzyme cleaning benefit, in which catalytic activity is typically used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides or other bleaching species.

[0048] The term "high stringency conditions" refers to 12-24 hours of prehybridization and hybridization for probes at least 100 nucleotides long, following standard Southern blotting procedures: 5x SSPE, 0.3% SDS, 200 micrograms / mL sheared denatured salmon sperm DNA, and 50% formamide at 42°C. Finally, the carrier material is washed three times with 2x SSC, 0.2% SDS for 15 minutes each at 70°C.

[0049] The term "very low stringency conditions" refers to 12-24 hours of prehybridization and hybridization following standard Southern blotting procedures for probes at least 100 nucleotides long in 5x SSPE, 0.3% SDS, 200 micrograms / mL sheared denatured salmon sperm DNA, and 25% formamide at 42°C. Finally, the carrier material is washed three times with 2x SSC, 0.2% SDS for 15 minutes each at 45°C.

[0050] The term "washing performance" is defined herein to refer to the change in washing performance of an amylase of the invention relative to the washing performance of a parent amylase. Improved washing performance may be measured by comparing so-called intensity values.

[0051] As used herein, the term "wild-type α-amylase" refers to an α-amylase expressed by a naturally occurring microorganism, such as a naturally occurring bacterium, yeast, or filamentous fungus.

[0052] The term "wash cycle" is defined herein in relation to dishwashing as a washing operation in which dishware are exposed to washing liquid for a specified period of time by circulating washing liquid to clean the dishes, spraying the washing liquid onto the dishes, and finally removing the excess washing liquid. The wash cycle may be repeated 1, 2, 3, 4, 5, or even 6 times at the same or different temperatures. The dishes are then typically rinsed and dried. One of the wash cycles may be a soak step, in which the dishes are left submerged in the washing liquid for a specified period of time.

[0053] The term dishware is intended to mean any form of kitchen utensil, dinnerware or tableware, such as, but not limited to, pans, plates, cups, knives, forks, spoons, china, etc.

[0054] As used herein, the term "grease" or "greasy" refers to a material that comprises, at least in part (i.e., at least 0.5% by weight of the grease), saturated and unsaturated fats and oils, preferably oils and fats derived from animal sources such as bovine, porcine and / or chicken.

[0055] The term "dishwashing" refers to all forms of washing dishes, for example, by manual (MDW) or automatic dishwashing (ADW). Washing dishware includes, but is not limited to, cleaning all forms of ceramics, such as plates, cups, glasses, bowls, etc., all forms of cutlery, such as spoons, knives, forks, and serving utensils, as well as ceramics, plastics, metals, china, glass, and acrylic.

[0056] The term "dishwashing composition" refers to a composition for cleaning tableware such as plates, cups, glassware, and bowls, cutlery such as spoons, knives, and forks, kitchen utensils, ceramics, plastics, metals, pottery, glass, and acrylic products in a dishwasher. The term encompasses any material / compound selected for household or commercial cleaning applications, and the product may be in the form of a liquid, powder, or granule. In addition to enzymes, automatic dishwashing compositions contain detergent ingredients such as polymers, bleaching systems, bleach activators, bleach catalysts, silicates, dyes, and metal care agents. Dishwashing compositions can be used in manual dishwashing (MDW) or automatic dishwashing (ADW).

[0057] Thus, in one embodiment, the dishwashing composition is a liquid dishwashing composition, a powdered dishwashing composition, which composition may optionally be in unit dose form.

[0058] The term "washing solution" is defined herein as a solution or mixture of water and detergent ingredients.

[0059] The term "wash time" in relation to automatic dishwashing is defined herein as the time taken for the entire washing process, ie the combined wash and rinse cycles.

[0060] The term "detergent composition" includes, unless otherwise indicated, granular or powdered all-purpose or heavy-duty detergents, especially cleaning detergents; liquid, gel, or paste all-purpose detergents, especially so-called heavy-duty liquid (HDL) types; liquid detergents for delicate fabrics; hand dishwashing detergents or light-duty dishwashing detergents, especially high-foaming types; dishwashing detergents, including various tablet, granular, liquid, and rinse aid types for household and industrial use; liquid cleaning and disinfecting agents, including antibacterial hand washing types, cleaning bars, soap bars, mouthwashes, denture cleaners, car or carpet shampoos, and bathroom cleaners; hair shampoos and hair rinses; shower gels, foam baths; metal cleaners; and cleaning aids such as bleaching additives and "stain sticks" or pre-treatment types. The terms "detergent composition" and "detergent formulation" are used in reference to mixtures intended for use in a washing medium for cleaning soiled objects. In some embodiments, the terms are used in reference to the washing of fabrics and / or clothes (e.g., "laundry detergents"). In another embodiment, the term refers to other detergents, such as those used to clean dishes, cutlery, etc. (eg, "dishwashing detergents").

[0061] The term "automatic dishwashing detergent composition" refers to a composition containing detergent ingredients intended for cleaning tableware such as plates, cups, glasses, bowls, spoons, knives, forks, kitchen utensils, cutlery such as ceramics, plastics, metals, porcelain, glass, and acrylic in a dishwasher. It is not intended that the present invention be limited to any particular detergent formulation or composition.

[0062] The term "detergent composition" is not intended to be limited to compositions containing surfactants. It is contemplated that in addition to the enzymes described herein, the detergent composition may include one or more additional ingredients selected from, for example, stabilizers, surfactants, hydrotropes, builders, co-builders, chelating agents, bleaching systems, bleach activators, bleach catalysts, polymers, metal care agents, glass care agents, crystal growth inhibitors, and fabric hueing agents.

[0063] The term "non-fabric detergent compositions" includes surface detergent compositions other than fabrics, including, but not limited to, hard surface cleaning compositions such as dishwashing detergent compositions, mouthwash compositions, denture cleaner compositions, and personal cleansing compositions.

[0064] The term "effective amount of enzyme" refers to the amount of enzyme necessary to achieve the enzymatic activity required for a particular application, e.g., a defined detergent composition. Such an effective amount is readily ascertained by one of ordinary skill in the art and is based on a variety of factors, such as, for example, the particular enzyme used, the cleaning application, the specific composition of the detergent composition, and whether a liquid or dry (e.g., granular, bar) composition is desired. The term "effective amount" of enzyme refers to the amount of enzyme, as described above herein, that achieves a desired level of enzymatic activity, e.g., in a defined detergent composition. In one embodiment, the effective amount of protease is the same as the effective amount of α-amylase. In another embodiment, the effective amount of protease is different from the effective amount of α-amylase; e.g., the effective amount of protease may be greater than or less than the effective amount of α-amylase.

[0065] As used herein, the term "water hardness" or "hardness" or "dH" or "°dH" refers to the German hardness scale, where one degree is defined as 10 milligrams of calcium oxide per liter of water.

[0066] The term "relevant washing conditions" is used herein to refer to the conditions actually used in homes in the detergent market segment, in particular washing temperature, time, washing machine, detergent concentration, detergent type and water hardness.

[0067] The term "additive substance" refers to any liquid, solid, or gaseous material selected for a particular type of detergent composition and product form (e.g., liquid, granular, powder, bar, paste, spray, tablet, gel, or foam composition), which material is preferably also compatible with the enzymes used in the composition. In some embodiments, granular compositions are in "compacted" form, while in other embodiments, liquid compositions are in "concentrated" form.

[0068] The term "stain removal enzyme" as used herein refers to an enzyme that aids in the removal of soil or contaminants from fabrics or hard surfaces. Stain removal enzymes act on specific substrates, for example, proteases act on proteins, amylases act on starches, lipases and cutinases act on lipids (fats and oils), pectinases act on pectins, and hemicellulases act on hemicelluloses. Soils are often deposits of complex mixtures of various components, which can lead to localized discoloration of the material itself or leave a sticky surface on the item that can attract soil dissolved in the wash liquor, thereby causing discoloration of the soiled area. When an enzyme acts on the specific substrate present in the soil, it breaks down or partially breaks down the substrate, thereby aiding in the removal of soil and soil components bound to the substrate during the washing process. For example, when a protease acts on grass soil, it can break down the protein components of the grass and release a green / brown color during the wash.

[0069] The term "reduced amount" in this context means that the amount of a component is less than the amount that would be used in a reference process under otherwise the same conditions. In preferred embodiments, the amount is reduced, e.g., by at least 5%, e.g., by at least 10%, at least 15%, at least 20%, or otherwise as described herein.

[0070] The term "low detergent concentration" system includes detergents in which less than about 800 ppm of detergent ingredients are present in the wash water. Asian, e.g., Japanese, detergents are typically considered low detergent concentration systems.

[0071] The term "mid detergent concentration" system includes detergents having from about 800 ppm to about 2000 ppm of detergent components present in the wash water. North American detergents are generally considered to be mid detergent concentration systems.

[0072] The term "high detergent concentration" systems includes detergents in which more than about 2000 ppm of detergent ingredients are present in the wash water. European detergents are generally considered to be high detergent concentration systems.

[0073] As used herein, the term "liquid laundry detergent composition" refers to a detergent composition that is in a stabilized liquid form and is used in a method of laundering fabrics. Thus, the detergent composition is formulated to be in liquid form.

[0074] As used herein, the term "powder laundry detergent composition" refers to a detergent composition in solid form, such as a granulate, non-dusting granulate, which is used in a method of laundering fabrics.

[0075] As used herein, the term "liquid dishwashing detergent composition" refers to a detergent composition that is in a stabilized liquid form and is used for dishwashing. Dishwashing may be any type of dishwashing, such as, for example, hand dishwashing and automatic dishwashing (ADW).

[0076] As used herein, the term "powder dishwashing detergent composition" refers to a detergent composition in solid form, such as a granule, powder, or compressed unit, that is used for dishwashing. Powder dishwashing detergent compositions are typically used in automatic dishwashing, but the use is not limited to such ADW, and may also be intended for use in any other type of dishwashing, such as manual dishwashing.

[0077] The term "delta strength" or "delta strength value" as used herein refers to a test material, such as a melamine tile stained with Starch 277 (Center For Test materials BV, PO Box 120, 3133 KT Vlaardingen, the Netherlands) or hard surface. Delta strength is the strength value of the test material washed with amylase minus the strength value of the test material washed without amylase.

[0078] As used herein, the term "numbering according to" refers to the method by which each of the amino acid residues in the polypeptides of the present invention is numbered. That is, one skilled in the art would know that, for example, when position 202 is numbered according to SEQ ID NO: 5, the corresponding amino acid residue in any other polypeptide can be determined by aligning SEQ ID NO: 5 with any other polypeptide. Alignment of two or more amino acid sequences is described elsewhere herein.

[0079] The term "laundry process" refers to the process of treating fabrics with a solution containing cleaning ingredients or compositions, e.g., laundry detergent compositions, in both domestic and industrial laundering. The laundering process may be carried out, for example, using a domestic or industrial washing machine, or may be carried out manually. In the present invention, the laundering process may include a wash cycle and a rinse cycle.

[0080] The term "rinse cycle" is defined herein as a rinsing operation in which the fabric is exposed to water for a period of time by circulating the water, optionally mechanically treating the fabric to rinse the fabric, and finally removing excess water. The rinse cycle is usually of short duration compared to the wash cycle and may be repeated 1, 2, 3, 4, 5, or even 6 times at the same or different temperatures.

[0081] For purposes of the present invention, sequence identity between two amino acid sequences is preferably determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453) as implemented in the Needle program in the EMBOSS package 5.0.0 or later (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16:276-277). The parameters used may be a gap opening penalty of 10, a gap extension penalty of 0.5, and an EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "Longest Identity" (obtained using the -nobrief option) is used as the percent identity, calculated as follows: (Identical residues × 100) / (length of alignment − total number of gaps in the alignment)

[0082] Alternatively, the parameters used can be a gap open penalty of 10, a gap extension penalty of 0.5, and an EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The Needle output labeled "Longest Identity" (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: (identical deoxyribonucleotides × 100) / (length of alignment−total number of gaps in the alignment).

[0083] Rules for naming variants For purposes of the present invention, the polypeptide disclosed in SEQ ID NO: 6 is used to determine the corresponding amino acid residue in another α-amylase. The amino acid sequence of the other α-amylase is aligned with the polypeptide disclosed in SEQ ID NO: 5, and based on this alignment, the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in SEQ ID NO: 6 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453), preferably as implemented in the Needle program in the EMBOSS package, version 3.0.0 or later (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16:276-277).

[0084] The identification of corresponding amino acid residues in other α-amylases can be confirmed by alignment of multiple polypeptide sequences using "ClustalW" (Larkin et al., 2007, Bioinformatics 23:2947-2948).

[0085] Other pairwise sequence comparison algorithms can be used when other enzymes diverge from the polypeptide of SEQ ID NO:6, such that traditional sequence-based comparisons do not detect their relationship (Lindahl and Elofsson, 2000, J. Mol. Biol. 295:613-615). Greater sensitivity in sequence-based searches can be achieved using search programs that utilize probabilistic representations of polypeptide families (profiles) to search databases. For example, the PSI-BLAST program generates profiles through an iterative database search process to detect distant homologs (Atschul et al., 1997, Nucleic Acids Res. 25:3389-3402). Even greater sensitivity can be achieved if a polypeptide family or superfamily has more than one representative in a protein structure database. Programs such as GenTHREADER (Jones, 1999, J. Mol. Biol. 287:797-815; McGuffin and Jones, 2003, Bioinformatics 19:874-881) utilize information from a variety of sources (PSI-BLAST, secondary structure prediction, structural alignment profiles, and solvation potential) as input to a neural network that predicts the structural fold for a query sequence. Similarly, the method of Gough et al., 2000, J. Mol. Biol. 313:903-919 can be used to align sequences of unknown structure with superfamily models present in the SCOP database. These alignments can then be used to generate homology models for the polypeptide, and such models can be evaluated for accuracy using a variety of tools developed for this purpose.

[0086] Several tools and resources are available for searching and generating structural alignments for proteins with known structures. For example, the SCOP superfamily of proteins has been structurally aligned, and these alignments are accessible and downloadable. Two or more protein structures can be aligned using various algorithms, such as distance alignment matrices (Holm and Sander, 1998, Proteins 33:88-96) or combinatorial extension (Shindyalov and Bourne, 1998, Protein Engineering 11:739-747), and implementations of these algorithms can also be used to search structural databases with structures of interest to find possible structural homologs (e.g., Holm and Park, 2000, Bioinformatics 16:566-567).

[0087] In describing the variants of the present invention, the nomenclature described below is adapted for ease of reference: Recognized IUPAC single-letter or three-letter amino acid abbreviations are employed.

[0088] Substitutions: For amino acid substitutions, the following nomenclature is used: original amino acid, position, substituted amino acid. Thus, a substitution of threonine with alanine at position 226 is designated "Thr226Ala" or "T226A." Multiple mutations are separated by a symbol ("+"), e.g., "Gly205Arg+Ser411Phe" or "G205R+S411F" represent a substitution of glycine (G) with arginine (R) and serine (S) with phenylalanine (F) at positions 205 and 411, respectively.

[0089] Deletions: For amino acid deletions, the following nomenclature is used: use the original amino acid, the position, and an *. Thus, a deletion of glycine at position 195 is designated "Gly195*" or "G195*". Multiple deletions are separated by adding a symbol ("+"), e.g., "Gly195*+Ser411*" or "G195*+S411*".

[0090] Insertions. For amino acid substitutions, the following nomenclature is used: original amino acid, position, original amino acid, inserted amino acid. Thus, an insertion of lysine after glycine at position 195 is designated as "Gly195GlyLys" or "G195GK." An insertion of multiple amino acids is designated as [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2, etc.]. For example, an insertion of lysine and alanine after glycine at position 195 is designated as "Gly195GlyLysAla" or "G195GKA."

[0091] In such cases, the inserted amino acid residue is numbered by adding a lower case letter to the position number of the amino acid residue preceding the inserted amino acid residue. In the above example, the sequence would therefore be:

[0092] [Table 1]

[0093] Multiple Modification: Multiple Alterations. Variants containing multiple alterations are separated by a symbol ("+"), for example, "Arg170Tyr+Gly195Glu" or "R170Y+G195E" represent substitutions of arginine and glycine with tyrosine and glutamic acid at positions 170 and 195, respectively.

[0094] Various modifications: When different alterations can be introduced at a position, the different changes are separated by a comma, for example, "Arg170Tyr,Glu" represents the substitution of arginine with tyrosine or glutamic acid at position 170. Thus, "Tyr167Gly,Ala+Arg170Gly,Ala" names the following variant: "Tyr167Gly+Arg170Gly", "Tyr167Gly+Arg170Ala", "Tyr167Ala+Arg170Gly" and "Tyr167Ala+Arg170Ala".

[0095] composition In one aspect, the present invention provides a method for producing a pharmaceutical composition comprising: (i) a polypeptide having catalase activity and having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 1, 2, 3, 4 or 5; and (ii) a polypeptide having α-amylase activity The present invention relates to a detergent composition comprising:

[0096] Alpha-amylase variants of the detergent compositions of the invention containing one or more substitutions at defined positions, using SEQ ID NO: 6 for numbering, were generated and tested for stability and performance in model detergents as described in Materials and Methods. Additionally, the inventors have identified substitutions at positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313, 314, 315, 316, 317, 318, 319, 320, 321, 322, 323, 324, 325, 326, 327, 328, 329, 330, 331, 332, 333, 334, 335, 336, 337, 338, 339, 340, 341, 342, 343, 344, 345, 346, 347, 348, 349, 350, 351, 352, 353, 354, 355, 356, 357, 358, 359, 360, 361, 362, 363, 364 It has been demonstrated that one or more substitutions of one or more amino acids at positions corresponding to 47, 391, 395, 439, 469, 444, 473, 476, and 477 improve detergent stability and / or performance, for example, compared to α-amylases having the amino acid sequences of SEQ ID NOs: 6 and 16 but without substitutions at one or more of these specific positions, or compared to an α-amylase having SEQ ID NO: 6. As can be seen from the examples, the combination of an α-amylase variant with catalase has a synergistic effect, i.e., improved performance, on stain removal. One of the examples described herein also shows that the combination of an α-amylase variant with catalase has at least the same stability as the variant tested alone.

[0097] Thus, the present invention relates to a detergent composition, wherein at least one α-amylase is selected from the group consisting of α-amylases at positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391, 395, 439, 469, 444, 445, 450, 451, 452, 453, 454, 455, 456, 457, 458, 459, 460, 461, 462, 463, 464, 465, 466, 467, 468, 470, 471, 472, 473, 474, 475, 476, 477, 478, 479, 480, 481, 482, 483, 484, 485, 486, 487, 488, 489, 490, 500, 501, 502, 503, 504, 505, 506, 507, 508, 509, 510, 511, 512, 513, 514, 515, 516, 517 and the α-amylase variant comprises one or more amino acid modifications at positions corresponding to positions 73, 476 or 477, and the α-amylase variant has at least 60% sequence identity to the parent α-amylase of SEQ ID NO: 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20, e.g., at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, but less than 100%, sequence identity, and catalase activity and at least 60%, for example at least 65%, to SEQ ID NO: 1, 2, 3, 4 or 5. , having a polypeptide having at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity.

[0098] In the context of the present invention, "α-amylase variant" or "α-amylase variant" should be understood to mean "at least one α-amylase variant", unless the context indicates otherwise, e.g., "one α-amylase mutant". Thus, in all embodiments, the detergent composition according to the present invention comprises at least one α-amylase variant. This applies equally to proteases or lipases or variants of either of these. In particular embodiments, the at least one α-amylase variant comprises a protease or lipase at positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 208, 210, 212, 214, 216, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 228, 229, 230, 231, 232, 233, 234, 235, 236, 237, 238, 239, 240, 241, 242, 243, 244, 245, 246, 247, 248, 249, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 264, 265, 26 The modifications include modifications at positions 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or 13, corresponding to positions 255, 260, 262, 265, 284, 289, 304, 305, 347, 391, 395, 439, 469, 444, 473, 476 or 477, where the numbering is according to SEQ ID NO: 6.

[0099] In one embodiment, the at least one α-amylase variant is selected from the group consisting of X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E ,X172K,X172G,X172N,X173P,X174*,X174S,X181*,X182*,X183*,X184*,X184T,X189 Y, X189F, X189H, X189E, X189D, X189Q, X189N, X194D, X194N, X194S, X195F, X206L, 6F, X206Y, X255A, X260G, X260P, X260A, X260G, X260P, X260A, 89H, X304K, X304R, X304Q, X304E, X305K, X305R, X305Q, X305E, X347Y, X347F, 391A, X395P, X439N, X439Q, X439T, X444Q, X469T, X469N, X473R, X476R, X476Q, X476E, X476K, X477K, X477R, X477Q and X477E, wherein the positions correspond to those of SEQ ID NO: 6.

[0100] In certain embodiments, the at least one α-amylase variant comprises any of the following modifications: X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E, X172K, X172G, X172N, X173P, X174*, X174S, X181*, X182*, X183*, X184*, X184T, X189Y, X189F, X189H, X18 ... 189E, X189D, X189Q, X189N, X194D, X194N, X194S, X195F, X206L, X206F, X206Y, X255A, X260G, X260P, X260A, X260G, X260P, X260A, X265G, X284G ,X284H,X289H,X304K,X304R,X304Q,X304E,X305K,X305R,X305Q,X305 E, X347Y, X347F, X347H, X391A, X395P, X439N, X439Q, X439T, X444Q, X469 and wherein the α-amylase variant comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 of T, X469N, X473R, X476R, X476Q, X476E, X476K, X477K, X477R, X477Q or X477E, wherein the numbering of positions is according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110% or at least 111% of SEQ ID NO: 6 or 16. Also, the α-amylase variants may have 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0101] In a preferred embodiment, at least one α-amylase variant comprises deletions and / or substitutions at two or more positions corresponding to positions 181, 182, 183 or 184 of SEQ ID NO: 6, and the α-amylase variant has at least 60%, such as at least 61%, at least 62%, at least 63%, at least 64%, 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%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6 but less than 100% sequence identity to SEQ ID NO: 6.

[0102] Thus, in one embodiment, the at least one α-amylase variant comprises a deletion at positions corresponding to 181+182, 181+183, 181+184, 182+183, 182+184 or 183+184 of SEQ ID NO:6.

[0103] In certain embodiments, the at least one α-amylase variant comprises any of the following modifications: X1*, X1A, X54S, X56T, X72R, X109A, X113Q, X116Q, X116H, X134E, X140Y, X140F, X140H, X159Y, X159F, X159H, X167Y, X167H, X167F, X169E, X172K, X172G, X172N, X173P, X174*, X174S, X181*, X182*, X183*, X184*, X184T, X189Y, X189F, X189H, X189E, X189D, X189E, X189F, X189H, X189E, X189D, X189F, X189F, X189H, X189F, X189F, X189H, X189F, X189D, X189F ... 189Q, X189N, X194D, X194N, X194S, X195F, X206L, X206F, X206Y, X255A, X26 0G, X260P, X260A, X260G, X260P, X260A, X265G, X284G, X284H, X289H, X304K ,X304R,X304Q,X304E,X305K,X305R,X305Q,X305E,X347Y,X347F,X347H,X 391A, X395P, X439N, X439Q, X439T, X444Q, X469T, X469N, X473R, X476R, X476 and one or more of X181*+X182*, X181*+X183*, X181*+X184*, X182*+X183*, X182*+X184* or X183*+X184* pairwise deletions, numbering according to SEQ ID NO: 6, wherein the α-amylase variant comprises at least 60%, at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, for example at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99% relative to SEQ ID NO: 6 or 16. At least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%,The α-amylase variant has at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0104] In one embodiment, the α-amylase variant in (i) is H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K; H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S +G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K; H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K and H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, wherein said α-amylase variant is selected from the group consisting of: H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, and ... %, such as at least 65%, for example at least 70%, for example at least 80%, such as at least 85%, for example at least 90%, such as at least 93%, for example at least 94%, such as at least 95%, for example at least 96%, such as at least 97%, for example at least 98%, but less than 100% sequence identity, and said α-amylase variant has α-amylase activity.

[0105] In one embodiment, the α-amylase variant in (i) has the following modification: H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K; H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S +G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K; H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K and H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, wherein said alpha-amylase variant shares at least 60%, such as at least 65%, for example at least 70%, such as at least 80%, for example at least 85%, such as at least 90%, for example at least 93%, such as at least 94%, for example at least 95%, such as at least 96%, for example at least 97%, such as at least 98%, but less than 100%, sequence identity with the polypeptide of SEQ ID NO: 6 or SEQ ID NO: 16, and wherein said alpha-amylase variant has alpha-amylase activity.

[0106] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 117%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 12 The α-amylase variant is an α-amylase variant having at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0107] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16 by at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least The α-amylase variant has 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0108] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16, at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 117%, at least 118%, at least 119%, at least 120%, at least 121%, at least The α-amylase variant has 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0109] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16 by at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least In some embodiments, the α-amylase variant has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0110] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16, at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least The α-amylase variant has 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0111] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16, at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 117%, at least 118%, at least 119%, at least 120%, at least 121%, at least The α-amylase variant has 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0112] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16, at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 117%, at least 118%, at least 11 The α-amylase variant has 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0113] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16 by at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least The α-amylase variant has 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0114] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 117%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128 The α-amylase variant is an α-amylase variant having at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0115] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence similar to SEQ ID NO: 6 or 16, at least 60%, at least 65%, at least 70%, such as at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, such as at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, or at least 81%. , at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to a parent α-amylase.

[0116] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0117] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0118] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:3, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0119] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:4, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0120] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0121] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, The α-amylase variant of the parent α-amylase has at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0122] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, The α-amylase variant of the parent α-amylase has at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0123] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:3 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0124] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:4 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0125] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0126] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:1, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0127] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:2 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0128] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:3 and having catalase activity and a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0129] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:4 and having catalase activity and a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0130] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0131] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:1, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0132] In certain embodiments, at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140%, at least 141%, at least 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:2 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0133] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:3, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0134] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:4, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0135] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0136] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity, and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0137] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, or 100% sequence identity to SEQ ID NO:2 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0138] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, or 100% sequence identity to SEQ ID NO:3 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0139] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, or 100% sequence identity to SEQ ID NO:4 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0140] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 130%, at at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0141] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:1, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0142] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:2 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0143] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:3 and having catalase activity and a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0144] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:4 and having catalase activity and a polypeptide having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0145] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a sequence identity at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 87%, at least 89%, at least 90%, at least 95%, at least 97%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 129%, at least 130%, at least 131%, at least 132%, at least 133%, at least 134%, at least 135%, at least 136%, at least 137%, at least 138%, at least 139%, at least 140 1%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0146] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95 ... at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity to SEQ ID NO: 1, and have at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least The α-amylase variant is an α-amylase variant having a polypeptide with at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to a parent α-amylase.

[0147] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95 ... at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, and have at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity to SEQ ID NO:2, and have at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least The α-amylase variant is an α-amylase variant having a polypeptide with at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to a parent α-amylase.

[0148] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95 ... at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity to SEQ ID NO:3, and have at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least The α-amylase variant is an α-amylase variant having a polypeptide with at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to a parent α-amylase.

[0149] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95 ... at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, and having at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity to SEQ ID NO:4, and at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least The α-amylase variant is an α-amylase variant having a polypeptide with at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to a parent α-amylase.

[0150] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95 ... at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity to SEQ ID NO:5, and have at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least The α-amylase variant is an α-amylase variant having a polypeptide with at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to a parent α-amylase.

[0151] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, The α-amylase variant of the parent α-amylase has at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0152] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, The α-amylase variant of the parent α-amylase has at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity and catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0153] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:3 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0154] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:4 and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0155] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence that is at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least 128%, at least 129%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or 100% sequence identity to SEQ ID NO:5, and having catalase activity and a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0156] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0157] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0158] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:3, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0159] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:4, and having catalase activity and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0160] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 119%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 127%, at least at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity, and catalase activity, and having a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0161] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 130%, at least 131%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:1, and has catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:1.

[0162] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 130%, at least 131%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:2, and has catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:2.

[0163] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 130%, at least 131%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:3, and has catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:3.

[0164] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 130%, at least 131%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:4, and has catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:4.

[0165] In certain embodiments, the at least one α-amylase variant comprises the modifications H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, numbering according to SEQ ID NO: 6, and the α-amylase variant has a nucleotide sequence at least 60%, at least 65%, at least 70%, at least 71%, at least 72%, at least 74%, at least 76%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 100%, at least 101%, at least 102%, at least 103%, at least 104%, at least 105%, at least 106%, at least 107%, at least 108%, at least 109%, at least 110%, at least 111%, at least 112%, at least 113%, at least 114%, at least 115%, at least 116%, at least 118%, at least 119%, at least 120%, at least 121%, at least 122%, at least 123%, at least 124%, at least 125%, at least 126%, at least 128%, at least 129%, at least 130%, at least 131%, at least 73%, at least 74%, at least 75%, for example, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least In some embodiments, the α-amylase variant has at least 96%, at least 97%, at least 98%, at least 99%, e.g., at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6, or 100% sequence identity to SEQ ID NO:5, and has catalase activity and has a polypeptide with at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO:5.

[0166] Preferably, the composition is enriched in such variants. The term "enriched" means that the α-amylase activity of the composition is increased (e.g., by an enrichment factor of 1.1).

[0167] In one embodiment, the present invention relates to a composition comprising a variant of the present invention in combination with one or more additional ingredients, the selection of which is within the skill of one in the art and includes conventional ingredients such as the exemplary, non-limiting ingredients described below.

[0168] In one embodiment, the present invention relates to a composition comprising one or more additional ingredients selected from the group consisting of one or more enzymes, oxidizing agents, bleach activators, bleach catalysts, chelating agents, extenders, builders, buffers, structurants, sequestrants, optical brighteners, defoamers, enzymes, fragrances, anti-resoiling agents, skin conditioning agents, emollients, emulsifiers, crystal growth inhibitors, metal care agents, glass care agents, and colorants.

[0169] In one embodiment, the present invention relates to a composition comprising a surfactant.

[0170] In one embodiment, the present invention relates to a composition wherein the surfactant is one or more surfactants selected from the group consisting of anionic surfactants, cationic surfactants, nonionic surfactants, zwitterionic surfactants, and amphoteric surfactants, or any mixture thereof.

[0171] In one embodiment, the present invention relates to a composition, wherein the composition is a detergent composition.

[0172] In one embodiment, the composition is a liquid laundry or liquid dishwashing composition, such as an automatic dishwashing (ADW) liquid detergent composition, or a powder laundry, such as a soap bar, or a powder dishwashing composition, such as an ADW unit dose detergent composition, such as a hand dishwashing (HDW) detergent composition.

[0173] In one embodiment, the present invention relates to a composition, wherein the composition comprises one or more additional enzymes.

[0174] The composition may comprise a variant of the primary enzyme component, e.g., a single-component composition. Alternatively, the composition may comprise multiple enzyme activities, e.g., protease, amylase, phospholipase, esterase, lipase, cutinase, cellulase, endoglucanase, xyloglucanase, xylanase, pectinase, hemicellulase, pectin lyase, xanthanase, peroxidase, keratinase, haloperoxygenase, catalase, mannanase, rekinase, RNase, DNAse, reductase, oxidase, phenoloxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malanase, β-glucanase, arabinosidase, hyaluronidase, chondroitinase, and laccase, or any mixture thereof.

[0175] The additional enzyme may be derived from, for example, a Bacillus species, such as, for example, Bacillus licheniformis and Bacillus subtilis, or from an Aspergillus species, such as, for example, Aspergillus aculeatus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, or Aspergillus oryzae;For example, Fusarium bacterioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcocroum. Fusarium species, such as Fusarium sarcochroum, Fusarium sulphureum, Fusarium toruloseum, Fusarium trichothecioides or Fusarium venenatum; Humicola species, such as Humicola insolens or Humicola lanuginosa; or species of Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei or Trichoderma viride. It can be produced, for example, by a microorganism belonging to the genus Trichoderma, such as Trichoderma viride, or any other host cell described herein;

[0176] The compositions may be prepared according to methods known in the art and may be in the form of a liquid or dry composition. For example, the compositions may be in the form of granules or microgranules. The variants may be stabilized according to methods known in the art.

[0177] Such compositions comprise a cleaning / detergent ingredient, preferably a mixture of ingredients. Typically, the cleaning ingredient is present in the composition in an amount of from 0.001 to 99.9% by weight, more typically from 0.01 to 80% by weight.

[0178] In another preferred embodiment, the composition comprises one or more surfactants, which may be nonionic, including semi-polar, and / or anionic and / or cationic and / or zwitterionic and / or amphoteric and / or semi-polar nonionic and / or mixtures thereof. The surfactants are typically present at a level of from 0.1% to 60%, or from 0.5 to 50%, or from 1 to 40% by weight of the composition.

[0179] In one embodiment of the invention, the variant of the invention may be added to a detergent composition in an amount corresponding to 0.001 to 100 mg of protein per liter of wash liquor, for example 0.01 to 100 mg of protein, preferably 0.005 to 50 mg of protein, more preferably 0.01 to 25 mg of protein, even more preferably 0.05 to 10 mg of protein, most preferably 0.05 to 5 mg of protein, and even most preferably 0.01 to 1 mg of protein. In this context, the term "protein" should be understood to include the variant of the invention.

[0180] A composition for use in automatic dishwashing (ADW) may contain, for example, from 0.0001% to 50% by weight of the composition of enzyme protein, such as from 0.001% to 20% by weight, for example, from 0.01% to 10% by weight, for example, from 0.05 to 5% by weight.

[0181] A composition for use in hand dishwashing (HDW) may contain, for example, from 0.0001% to 50% by weight of the composition of enzyme protein, such as from 0.001% to 20% by weight, for example, from 0.01% to 10% by weight, for example, from 0.05 to 5% by weight.

[0182] Compositions for use in granular laundry detergents may contain, for example, from 0.0001% to 50% by weight of the composition of enzyme protein, such as from 0.001% to 20% by weight, for example, from 0.01% to 10% by weight, for example, from 0.05% to 5% by weight.

[0183] Compositions for use in liquid laundry detergents may, for example, contain from 0.0001% to 10%, such as from 0.001 to 7%, for example from 0.1% to 5% enzyme protein by weight of the composition.

[0184] The variants of the invention and further active ingredients (e.g. additional enzymes) can be stabilized by the use of conventional stabilizers (e.g. polyols such as propylene glycol or glycerol, sugars or sugar alcohols, lactic acid, boric acid or boric acid derivatives, e.g. aromatic boric acid esters, or phenylboronic acid derivatives such as 4-formylphenylboronic acid), and the compositions can be formulated as described, for example, in WO 92 / 19709 and WO 92 / 19708.

[0185] In certain markets, different washing conditions and therefore different types of detergents are used, as disclosed for example in EP 1 025 240. For example, in Asia (Japan), low detergent concentration systems are used, while in the United States, medium detergent concentration systems are used and in Europe, high detergent concentration systems are used.

[0186] Low detergent concentration systems include detergents with less than about 800 ppm of detergent components present in the wash water. Japanese detergents are typically considered low detergent concentration systems, with about 667 ppm of detergent components present in the wash water.

[0187] Medium detergent concentrations include detergents with approximately 800 ppm to 2000 ppm of detergent components in the wash water. North American detergents have approximately 975 ppm of detergent components in the wash water, so they are generally considered to be medium detergent concentrations.

[0188] High detergent concentration systems include detergents with greater than about 2000 ppm of detergent components present in the wash water. European detergents are generally considered high detergent concentration systems because they have about 4500-5000 ppm of detergent components in the wash water.

[0189] Latin American detergents are generally high foaming phosphate builder detergents, and the variety of detergents used in Latin America ranges from 1500 ppm to 6000 ppm of detergent ingredients in the wash water, and thus can be included in medium and high detergent concentrations. Such detergent compositions are all embodiments of the present invention.

[0190] Variants of the present invention may also be incorporated into detergent formulations as disclosed in WO 97 / 07202, which is incorporated by reference.

[0191] Examples of preferred uses of the compositions of the present invention are described herein. The dosage of the compositions and other conditions under which the compositions are used can be determined based on methods known in the art.

[0192] In particular, the compositions of the present invention further comprise a chelating agent.

[0193] The term "chelating agent" as used herein refers to a chemical substance that forms a molecule with certain metal ions, inactivating those ions so that they cannot react with other elements. Therefore, a chelating agent can be defined as a binding agent that inhibits chemical activity by forming a chelate. Chelation is the formation or presence of two or more separate bonds between a ligand and a single central atom. The ligand may be any organic compound, silicate, or phosphate. For the purposes of the present invention, the term "chelating agent" includes a chelant, chelating agent, multiple chelating agents, complexing agent, or sequestering agent that forms water-soluble complexes with metal ions, such as calcium and magnesium. The chelating effect refers to the increased affinity of a chelating ligand for a metal ion compared to the affinity of a population of similar non-chelating ligands for the same metal. Chelators are commonly used in detergents and compositions for cleaning, such as laundry or dishwashing, due to their ability to bind metal ions, particularly calcium (Ca2+) ions. However, chelating agents themselves have been shown to inhibit enzyme activity. The term chelating agent is used interchangeably herein with "complexing agent" or "chelating agent" or "chelant."

[0194] Because most α-amylases are calcium-sensitive, the presence of these chelating agents can impair enzyme activity. The calcium sensitivity of an α-amylase can be determined by incubating a given α-amylase in the presence of a strong chelating agent and analyzing the effect of this incubation on the activity of the α-amylase of interest. Calcium-sensitive α-amylases lose most or all of their activity during incubation. The chelating agent can be present in the composition in an amount of 0.0001% to 20% by weight, preferably 0.01 to 10% by weight, and more preferably 0.1 to 5% by weight.

[0195] Non-limiting examples of chelating agents are EDTA, DTMPA, HEDP and citrate. Thus, in one embodiment, a composition comprises a variant according to the invention and a chelating agent, such as EDTA, DTMPA, HEDP or citrate.

[0196] As used herein, the term "EDTA" refers to ethylene-diamine-tetra-acetic acid, which falls within the definition of a "strong chelating agent."

[0197] As used herein, the term "DTMPA" refers to diethylenetriaminepenta(methylene phosphate). DTMPA can inhibit carbonate, sulfate, and phosphate scale formation.

[0198] As used herein, the term "HEDP" refers to hydroxy-ethanediphosphonic acid, which falls within the definition of a "strong chelating agent."

[0199] Chelating effect or chelating effectiveness refers to the increased affinity of a chelating ligand for a metal ion compared to the affinity of a population of similar non-chelating ligands for the same metal. However, the strength of this chelating effect can be determined by various assays or measurement methods, allowing chelators to be differentiated or ranked according to their chelating effectiveness (or strength).

[0200] In one assay, a chelating agent can be characterized by its ability to reduce the concentration of free calcium ion (Ca2+) from 2.0 mM to below 0.10 mM at pH 8.0, using a test based on the method described, for example, by M.K. Nagarajan et al., JAOCS, Vol. 61, no. 9 (September 1984), pp. 1475-1478.

[0201] As a reference, a chelator that has the same ability to reduce the concentration of free calcium ions (Ca2+) at pH 2.0 mM to 0.10 mM as EDTA at an equivalent chelator concentration can be said to be a strong chelator.

[0202] The compositions of the present invention may be in any convenient form, such as, for example, a bar, a homogenous tablet, a tablet with two or more layers, a pouch with one or more compartments, a regular or compressed powder, a granule, a paste, a gel, or a regular compressed or concentrated liquid. There are several detergent formulation forms, such as layers (same or different phases), pouches, and forms for mechanical dosing units.

[0203] The pouch may be configured as a single or multiple compartments. For example, it may be of any form, shape, and material suitable for retaining the composition without releasing it from the pouch prior to contact with water. The pouch is fabricated from a water-soluble film that encloses an internal volume. The internal volume may be divided into pouch compartments. Preferred films are polymeric materials, preferably polymers that can be formed into films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected 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, e.g., PVA, in the film is at least about 60%. Preferred average molecular weights are typically from about 20,000 to about 150,000. The film can also be a hydrolytically degradable and water-soluble polymer blend, such as a blend composition including polylactide and polyvinyl alcohol (known under trade reference M8630 as sold by Chris Craft In, Prod. Of Gary, Ind., US) plus a plasticizer such as glycerol, ethylene glycerol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain a solid laundry cleaning composition or component and / or a liquid cleaning composition or component separated by a water-soluble film. The compartment for the liquid component can be different in composition from the compartment containing the solid. Reference: (U.S. Patent Application Publication No. 2009 / 0011970 A1).

[0204] The detergent ingredients may be physically separated from each other by compartments in a water-soluble pouch or in different layers of a tablet. This can prevent negative storage interactions between the ingredients. The different dissolution profiles of each of the compartments can also cause delayed dissolution of selected ingredients in the cleaning solution.

[0205] Non-unit-dose liquid or gel detergents typically contain at least 20% by weight and up to 95% water, e.g., 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, and may be aqueous. Other types of liquids, including but not limited to alkanols, amines, diols, ethers, and polyols, may be included in aqueous liquids or gels. Water-soluble liquid or gel detergents may contain 0-30% organic solvents. Liquid or gel detergents may also be non-aqueous.

[0206] Another form of the composition is a soap bar, such as a laundry soap bar, which can be used on hand-washed laundry, fabrics, and / or materials. As used herein, the term "soap bar" is meant to include laundry bars, soap bars, combo bars, synthetic detergent bars, and detergent bars. Bar types typically differ in the type of surfactant they contain, and the term laundry soap bar includes those containing fatty acid-derived soap and / or synthetic soap. Laundry soap bars have a physical form that is solid at room temperature and is not a liquid, gel, or powder. As used herein, the term "solid" refers to a physical form that does not change significantly over time, i.e., when a solid item (e.g., a laundry soap bar) is placed inside a container, the solid item does not change to fill the container in which it is placed.

[0207] The soap bars may also contain complexing agents such as EDTA and HEDP, perfumes and / or various fillers, surfactants, such as 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, clay soil removers, anti-redeposition agents, polymeric dispersants, color brighteners, fabric softeners, perfumes and / or other compounds known in the art.

[0208] The soap bars may be processed using 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 wrappers. The present invention is not limited to preparing 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, enzymes, optionally one or more additional enzymes, protease inhibitors, and salts of monovalent cations and organic anions, the mixture may be plodded. The enzymes and any additional enzymes may be added simultaneously with enzyme inhibitors, such as protease inhibitors, in liquid form, for example. In addition to the mixing and plodding steps, the process may further include steps of grinding, extruding, cutting, stamping, cooling, and / or packaging.

[0209] surfactants The compositions of the present invention preferably contain at least one surfactant selected from nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof. The surfactant may be present in an amount of from about 1% to about 50%, preferably from about 5% to about 40%, more preferably from 5% to about 30%, e.g., from about 10% to about 20% by weight of the liquid detergent composition. In one embodiment, an effective yet mild surfactant system may comprise from about 4% to about 40%, preferably from 6% to about 32%, more preferably from about 11% to about 25%, and most preferably from about 11% to about 18% by weight of the total composition of anionic surfactant, and optionally, up to about 15%, preferably up to about 10%, more preferably up to about 5% by weight of the total composition of a sulfonate surfactant.

[0210] Suitable anionic surfactants for use in the compositions and methods of the present invention include sulfates, sulfosuccinates, sulfonates and / or alkyl ethoxy sulfates, more preferably combinations of alkyl sulfates and / or alkyl ethoxy sulfates having a combined degree of ethoxylation of less than about 5, preferably less than about 3, more preferably less than about 2.

[0211] In alternative embodiments, the surfactant system may be based on high levels of nonionic surfactant (e.g., from about 10% to about 45% by weight of the total composition, preferably from about 15% to about 40% by weight, more preferably from about 20% to about 35% by weight), preferably in combination with an amphoteric surfactant, more preferably in combination with low levels of anionic surfactant (e.g., less than about 20% by weight of the total composition, preferably less than 10% by weight, more preferably less than about 5% by weight).

[0212] Sulfate surfactants Suitable sulfate surfactants for use in the compositions herein include C 10 -C 14 Water-soluble salts or acids of alkyl or hydroxyalkyl sulfates and / or ether sulfates are included. Suitable counterions include hydrogen, alkali metal cations or ammonium or substituted ammonium, preferably sodium.

[0213] If the hydrocarbyl chain is branched, it is preferably C 14 The average branching percentage of the sulfate surfactants preferably is greater than 30%, more preferably 35% to 80%, most preferably 40% to 60% of the total hydrocarbyl chains.

[0214] Sulfate surfactants are C8-C 20 Primary branched and random alkyl sulfates (AS), C 10 -C 18 Secondary (2,3) alkyl sulfate, C 10 -C 18Alkylalkoxy sulfates (AExS), where x is preferably 1 to 30; 10 -C 18 Alkyl alkoxy sulfates (AExS), preferably containing 1 to 5 ethoxy units, C 10 -C 18 It may be selected from alkyl alkoxy carboxylates, mid-chain branched alkyl sulfates as described in U.S. Pat. Nos. 6,020,303 and 6,060,443, and mid-chain branched alkyl alkoxy sulfates as described in U.S. Pat. Nos. 6,008,181 and 6,020,303.

[0215] Alkyl sulfosuccinate-sulfoacetate Other suitable anionic surfactants are alkyl, preferably dialkyl, sulfosuccinates and / or sulfoacetates. Dialkyl sulfosuccinates are C 6-15 It may be a linear or branched dialkyl sulfosuccinate. The alkyl moieties may be symmetrical (i.e., the same alkyl moieties) or asymmetrical (i.e., different alkyl moieties). Preferably, the alkyl moieties are symmetrical.

[0216] Sulfonate Surfactants The compositions of the present invention preferably contain no more than 15% by weight of the total composition of sulfonate surfactants, preferably no more than 10% by weight, and even more preferably no more than 5% by weight. 10- C 14 Water-soluble salts or acids of alkyl or hydroxyalkyl sulfonic acids; C as described in WO 99 / 05243, WO 99 / 05242, WO 99 / 05244, WO 99 / 05082, WO 99 / 05084, WO 99 / 05241, WO 99 / 07656, WO 00 / 23549 and WO 00 / 23548 11 -C 18These include alkyl benzene sulfonates (LAS), modified alkyl benzene sulfonates (MLAS), methyl ester sulfonates (MES), and alpha-olefin sulfonates (AOS). These include paraffin sulfonates, which may be monosulfonates and / or disulfonates obtained by sulfonating paraffins of 10 to 20 carbon atoms. Sulfonate surfactants also include alkyl glyceryl sulfonate surfactants.

[0217] Amphoteric and Zwitterionic Surfactants Amphoteric and zwitterionic surfactants may be included in the composition at levels of from 0.01% to 20% by weight, preferably from 0.2% to 15% by weight, more preferably from 0.5% to 12% by weight. Suitable amphoteric and zwitterionic surfactants are amine oxides and betaines.

[0218] Amine oxides are most preferred, especially cocodimethylamine oxide or cocoamidopropyldimethylamine oxide. The amine oxides can have straight chain or mid-chain branched alkyl moieties. Exemplary straight chain amine oxides include those of formula R 1 -N(R 2 )(R 3 )→O, wherein R 1 is C 8-18 is an alkyl moiety, and R 2 and R 3 is C 1-3 Alkyl groups and C 1-3 The linear amine oxide surfactants are independently selected from the group consisting of hydroxyalkyl groups, preferably methyl, ethyl, propyl, isopropyl, 2-hydroxyethyl, 2-hydroxypropyl, and 3-hydroxypropyl. 10 -C 18 Alkyl dimethyl amine oxide and linear C8-C 12Alkoxyethyl dihydroxyethyl amine oxides may be mentioned. Preferred amine oxides include linear C 10 , linear C 10 -C 12 and linear C 12 -C 14 Examples include alkyl dimethyl amine oxides. As used herein, "mid-branched" means that the amine oxide has one alkyl moiety having n1 carbon atoms with one alkyl branch on the alkyl moiety having n2 carbon atoms. The alkyl branch is located on the alpha carbon from the nitrogen on the alkyl moiety. This type of branching of amine oxides is also known in the art as internal amine oxides. The sum of n1 and n2 is 10 to 24 carbon atoms, preferably 12 to 20 carbon atoms, and more preferably 10 to 16 carbon atoms. The number of carbon atoms in one alkyl moiety (n1) should be approximately the same as the number of carbon atoms in one alkyl branch (n2) so that one alkyl moiety and one alkyl branch are symmetrical. As used herein, "symmetrical" means that n1-n2 is 5 or less, preferably 4 or less, and most preferably 0 to 4 carbon atoms in at least 50% by weight, more preferably at least 75% to 100% by weight, of the mid-branched amine oxides used herein.

[0219] Amine oxides are C 1-3 Alkyl, C 1-3 The copolymer further comprises two moieties independently selected from a hydroxyalkyl group or a polyethylene oxide group containing an average of about 1 to about 3 ethylene oxide groups. Preferably, the two moieties are C 1-3 alkyl, more preferably both are selected as C1 alkyl. Other suitable surfactants include betaines such as alkylbetaines, alkylamidobetaines, amidoazolinium betaines, sulfobetaines (INCI: sultaines), as well as phosphobetaines.

[0220] One preferred surfactant system is a mixture of an anionic surfactant and an amphoteric or zwitterionic surfactant in a ratio ranging from 1:1 to 5:1, preferably from 1:1 to 3.5:1.

[0221] For more information regarding amphoteric and zwitterionic surfactants, see WO 2012 / 015852.

[0222] Nonionic surfactants When present as a co-surfactant, the nonionic surfactant may be present in a typical amount of 0.1% to 20%, preferably 0.5% to 15%, more preferably 0.5% to 10% by weight of the liquid detergent composition. When present as a primary surfactant, it may be present in a typical amount of 0.1% to 45%, preferably 15% to 40%, more preferably 20% to 35% by weight of the total composition. Suitable nonionic surfactants include the condensation products of fatty alcohols with 1 to 25 moles of ethylene oxide. The alkyl chain of the fatty alcohol can be linear or branched, primary or secondary, and generally contains 8 to 22 carbon atoms. Particularly preferred are the condensation products of 2 to 18 moles, 2 to 15 moles, more preferably 5 to 12 moles of ethylene oxide per mole of alcohol with an alcohol having an alkyl group containing 10 to 18 carbon atoms, preferably 10 to 15 carbon atoms. Also suitable are alkyl polyglycosides, alkyl glycerol ethers and sorbitan esters, as well as fatty acid amide surfactants, for example as described in WO 2012 / 015852.

[0223] Cationic surfactants When present in the composition, the cationic surfactant is present in an effective amount, for example, from 0.1% to 20% by weight of the liquid detergent composition. Suitable cationic surfactants are quaternary ammonium surfactants. Suitable quaternary ammonium surfactants include mono C6-C 16 , preferably C6-C 10The cationic surfactant is selected from the group consisting of N-alkyl or alkenyl ammonium surfactants, wherein the remaining N-positions are substituted by methyl, hydroxyethyl, or hydroxypropyl groups. Another preferred cationic surfactant is a C6-C quaternary ammonium alcohol surfactant, such as a quaternary chlorine ester. 18 It is an alkyl or alkenyl ester.

[0224] cationic polymer In one embodiment, the detergent compositions herein may include at least one cationic polymer to further enhance skin benefits. The cationic polymer may be present in an amount of 0.001% to 10%, preferably 0.01% to 5%, more preferably 0.05% to 1% by weight of the total composition. Suitable cationic polymers contain cationic nitrogen-containing moieties, such as quaternary ammonium or cationic protonated amino moieties, and may have an average molecular weight of about 5,000 to about 10,000,000, preferably at least about 100,000, more preferably at least about 200,000, but preferably no more than about 3,000,000. For more information regarding the use of cationic polymers in liquid dishwashing compositions, see, for example, WO 2012 / 015852.

[0225] Wetting agent The detergent composition may further comprise one or more wetting agents. Alternatively, the composition may be free of wetting agents. When present, wetting agents may be used in an amount of 0.1% to 50% by weight of the total composition, preferably 1% to 20% by weight, more preferably 1% to 10% by weight, even more preferably 1% to 6% by weight, and most preferably 2% to 5% by weight.

[0226] Suitable humectants include substances that have an affinity for water and help increase water absorption into the substrate, preferably the skin. Specific, non-limiting examples of particularly suitable humectants include glycerol, diglycerol, polyethylene glycol (4), propylene glycol, hexylene glycol, butylene glycol, (di)propylene glycol, glyceryl triacetate, polyalkylene glycols, and mixtures thereof. Others may be polyethylene glycol ethers of methyl glucose, pyrrolidone carboxylic acid (PCA) and its salts, pidolic acid and salts, such as sodium pidolic acid, polyols such as sorbitol, xylitol, and maltitol, or polymer polyols, such as polydextrose or natural extracts, or lactic acid or urea. Alkyl polyglycosides, polybetaine polysiloxanes, and mixtures thereof are also included. Further suitable humectants are polymeric moisturizers from the family of water-soluble and / or swellable polysaccharides, such as hyaluronic acid, chitosan and / or fructose-rich polysaccharides, available, for example, as Fucogel® 1000 by SOLABIA S (CAS number 178463-23-5).

[0227] Humectants containing oxygen atoms are preferred over those containing nitrogen or sulfur atoms. More preferred humectants are polyols or carboxyl-containing such as glycerol, diglycerol, sorbitol, propylene glycol, polyethylene glycol, butylene glycol, and / or humectants selected from the group consisting of pidoric acid and its salts, most preferably glycerol, sorbitol, sodium lactate, and urea, or mixtures thereof.

[0228] Cleaning Polymer The detergent compositions herein may optionally further comprise an alkoxylated polyethyleneimine polymer, as described in WO 2007 / 135645, in an amount of from 0.01% to 10%, preferably from 0.01% to 2%, more preferably from 0.1% to 1.5%, and even more preferably from 0.2% to 1.5% by weight of the total composition. The alkoxylated polyethyleneimine polymer may have a polyethyleneimine backbone having a weight average molecular weight of 400 to 10,000, preferably a weight average molecular weight of 400 to 7000, alternatively a weight average molecular weight of 3000 to 7000.

[0229] The alkoxylation of the polyethyleneimine backbone may comprise: (1) one or two alkoxylation modifications per nitrogen atom in the polyethyleneimine backbone, depending on whether the modification occurs at an internal or terminal nitrogen atom, wherein the alkoxylation modification consists of the replacement of a hydrogen atom with a polyalkoxylene chain, having an average of about 1 to 40 alkoxyl moieties per modification, and wherein the terminal alkoxy moieties of the alkoxylation modification are capped with hydrogen, C1-C4 alkyl, or a mixture thereof; and (2) one or two alkoxylation modifications per nitrogen atom in the polyethyleneimine backbone. and (3) combinations thereof, including substitution of one C1-C4 alkyl or benzyl moiety and one or two alkoxylated modifications per nitrogen atom, depending on whether the modification occurs at an internal or terminal nitrogen atom, wherein the alkoxylated modification consists of the replacement of a hydrogen atom with a polyalkoxylene chain, having an average of about 1-40 alkoxy moieties per modification, and wherein the terminal alkoxy moiety of the alkoxylated modification is capped with hydrogen, C1-C4 alkyl, or a mixture thereof.

[0230] The composition may further comprise an amphiphilic graft polymer (A) based on a water-soluble polyalkylene oxide as graft base and side chains (B) formed by polymerization of vinyl ester components, said polymer having on average not more than one grafting site per 50 alkylene oxide units and an average molar mass Mw of 3,000 to 100,000, as described in WO 2007 / 138053.

[0231] Magnesium ions The optional presence of magnesium ions may be utilized in detergent compositions when the compositions are used in softened water containing little to no divalent ions. When utilized, magnesium ions are preferably added to the compositions of the present invention as hydroxide, chloride, acetate, sulfate, formate, oxide, or nitrate. When included, magnesium ions are present at an active level of 0.01% to 1.5%, preferably 0.015% to 1%, more preferably 0.025% to 0.5% by weight of the detergent composition.

[0232] solvent The detergent composition may optionally contain a solvent. Suitable solvents include C 4- C 14 Ethers and diethers, glycols, alkoxylated glycols, C6-C 16 Glycol ethers, alkoxylated aromatic alcohols, aromatic alcohols, branched aliphatic alcohols, alkoxylated branched aliphatic alcohols, alkoxylated linear C1-C5 alcohols, linear C1-C5 alcohols, amines, C8-C 14 Examples of solvents include alkyl and cycloalkyl hydrocarbons and halohydrocarbons, and mixtures thereof. When present, the liquid detergent composition contains from 0.01% to 20%, preferably from 0.5% to 20%, more preferably from 1% to 10% by weight of the liquid detergent composition. These solvents may be used in conjunction with an aqueous liquid carrier such as water, or in the absence of any aqueous liquid carrier.

[0233] Hydrotrope The detergent compositions of the present invention may optionally contain an effective amount of a hydrotrope to ensure that the liquid detergent composition is properly compatible in water. Hydrotropes suitable for use herein include anionic hydrotropes, particularly sodium, potassium, and ammonium xylene sulfonate, and sodium, potassium, and ammonium toluene sulfonate, sodium, potassium, and ammonium cumene sulfonate, and mixtures thereof, and related compounds. The liquid detergent compositions of the present invention may contain from 0% to 15% by weight of the total liquid detergent composition of a hydrotrope or mixtures thereof, preferably from 1% to 10% by weight, and most preferably from 3% to 10% by weight of the liquid hand dishwashing composition.

[0234] Polymer Foam Stabilizer The detergent compositions of the present invention may optionally contain polymeric suds stabilizers. These polymeric suds stabilizers increase the suds volume and suds duration of the liquid detergent compositions. These polymeric suds stabilizers can be selected from homopolymers of (N,N-dialkylamino) alkyl esters and (N,N-dialkylamino) alkyl acrylate esters.

[0235] The weight average molecular weight of the polymeric suds booster, as measured by conventional gel permeation chromatography, is from 1,000 to 2,000,000, preferably from 5,000 to 1,000,000, more preferably from 10,000 to 750,000, more preferably from 20,000 to 500,000, and even more preferably from 35,000 to 200,000. The polymeric suds stabilizer can optionally be present in the form of a salt, either an inorganic salt or an organic salt.

[0236] One preferred polymeric suds stabilizer is (N,N-dimethylamino) alkyl acrylate ester. Another preferred suds booster polymer is hydroxypropyl acrylate / dimethylaminoethyl methacrylate copolymer (HPA / DMAM copolymer).

[0237] When present in the composition, the polymeric suds booster / stabilizer may be present at from 0.01% to 15%, preferably from 0.05% to 10%, more preferably from 0.1% to 5% by weight of the liquid detergent composition.

[0238] Another preferred class of polymeric suds booster polymers are hydrophobically modified cellulosic polymers having a number average molecular weight (Mw) of less than 45,000, preferably 10,000 to 40,000, more preferably 13,000 to 25,000. Hydrophobically modified cellulosic polymers include water-soluble cellulose ether derivatives, such as nonionic and cationic cellulose derivatives. Preferred cellulose derivatives include methyl cellulose, hydroxypropyl methyl cellulose, hydroxyethyl methyl cellulose, and mixtures thereof.

[0239] Diamine Another optional component of the detergent compositions of the present invention is a diamine. Because liquid detergent compositions exhibit considerable variation, the compositions may contain from 0% to 15%, preferably from 0.1% to 15%, preferably from 0.2% to 10%, more preferably from 0.25% to 6%, more preferably from 0.5% to 1.5%, by weight of the composition, of at least one diamine.

[0240] Preferred organic diamines have pK1 and pK2 values ​​in the range of 8.0 to 11.5, preferably 8.4 to 11, and even more preferably 8.6 to 10.75. Preferred materials include 1,3-bis(methylamine)-cyclohexane (pK = 10-10.5), 1,3-propanediamine (pK = 10.5; pK = 8.8), 1,6-hexanediamine (pK = 11; pK = 10), 1,3-pentanediamine (DYTEK A®) (pK = 10.5; pK = 8.9), and 2-methyl-1,5-pentanediamine (DYTEK A®) (pK = 11.2; pK = 10.0). Other preferred materials include primary / primary diamines with alkylene spacers in the C4-C5 range.

[0241] Carboxylic Acid The detergent compositions of the present invention may contain linear or cyclic carboxylic acids or their salts to improve the rinsing feel of the compositions. The presence of anionic surfactants, especially when present in higher amounts in the range of 15-35% by weight of the composition, can impart a slippery feel to the user's hands and dishes. This slippery feel is reduced when using carboxylic acids as defined herein.

[0242] Carboxylic acids useful herein include C 1-6 Examples include linear or cyclic acids containing at least 3 carbon atoms. The linear or cyclic carbon-containing chain of the carboxylic acid or salt thereof may be substituted with a substituent selected from the group consisting of hydroxy, ester, ether, aliphatic groups having 1 to 6, more preferably 1 to 4, carbon atoms, and mixtures thereof.

[0243] Preferred carboxylic acids are those selected from the group consisting of salicylic acid, maleic acid, acetylsalicylic acid, 3-methylsalicylic acid, 4-hydroxyisophthalic acid, dihydroxyfumaric acid, 1,2,4-benzenetricarboxylic acid, pentanoic acid, and salts thereof, and mixtures thereof. When the carboxylic acid is in the form of a salt, the cation of the salt is preferably selected from alkali metals, alkaline earth metals, monoethanolamine, diethanolamine, or triethanolamine, and mixtures thereof.

[0244] When present, the carboxylic acid or salt thereof is preferably present at a level of from 0.1% to 5%, more preferably from 0.2% to 1%, most preferably from 0.25% to 0.5% by weight of the total composition.

[0245] Bleaching type The detergent composition may contain 0 to 50% by weight of a bleaching system, such as 1 to 40%, for example 1 to 30%, for example about 1% to about 20%. Any oxygen-based bleaching system containing ingredients known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include a hydrogen peroxide source; a peracid and a peracid source (bleach activator); and a bleach catalyst or accelerator.

[0246] Hydrogen peroxide source: Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborate (usually the monohydrate or tetrahydrate), and hydrogen peroxide-urea (1 / 1).

[0247] Sources of peracid: 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, such as an ester.

[0248] 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, diperoxyisophthalic acid, and diperoxyterephthalic acid; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of the foregoing compounds. It will be appreciated that the above-listed peracids may in some cases best be added as a suitable salt, such as an alkali metal salt (eg, Oxone®) or an alkaline earth metal salt.

[0249] b) Suitable bleach activators include those belonging to the classes of esters, amides, imides, nitriles, or anhydrides, as well as their salts, if appropriate. Suitable examples include tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), sodium 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO 98 / 17767. A particular family of bleach activators of interest is disclosed in EP 624154, and within that family, acetyltriethyl citrate (ATC) is particularly preferred. ATC or the short-chain triglyceride-like triacetin has the advantage of being environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin are effective bleach activators with good hydrolytic stability of the products during storage. Finally, ATC is multifunctional because the citrate released during the perhydrolysis reaction can function as a builder.

[0250] Bleaching catalysts and accelerators The bleaching system may also include a bleaching catalyst or accelerator.

[0251] 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; complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Me4-TACN), particularly Me3-TACN, such as the dinuclear 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), are particularly preferred. The bleaching catalyst may also be other metal compounds, such as iron or cobalt complexes.

[0252] In some embodiments that include a source of peracid, the source may be selected from the group consisting of: [ka] and In the formula, 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.

[0253] 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.

[0254] Suitable photobleaches may be, for example, sulfonated zinc or aluminum phthalocyanine.

[0255] Builders and co-builders The detergent composition may contain about 0 to 65% by weight of a detergent builder or co-builder, or a mixture thereof, such as about 5% to about 50%, 20 to 60%, etc. For dishwashing detergents, the builder level is typically 40 to 65%, particularly 50 to 65%. The builder and / or co-builder may be, in particular, a chelating agent that forms a water-soluble complex with Ca and Mg. Any builder and / or co-builder known in the art for use in cleaning detergents may be utilized.

[0256] 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′-iminodiethane-1-ol), triethanolamine (TEA, also known as 2,2′,2″-nitrilotriethane-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

[0257] The detergent composition may also contain 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, e.g., a zeolite builder. Non-limiting examples of co-builders include polyacrylate homopolymers or copolymers thereof, e.g., poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA). Further non-limiting examples include citrates, chelating agents, e.g., aminocarboxylates, aminopolycarboxylates, and phosphonates, and alkyl or alkenyl succinic acids.Further specific examples include 2,2',2''-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycine diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid) (HEDP), and 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 (SEA S), 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 Examples of suitable builders and / or co-builders include acetic acid (TUDA) and 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.

[0258] Other ingredients The detergent compositions herein may further comprise a variety of other optional ingredients suitable for use in liquid detergent compositions, such as perfumes, dyes, opacifiers, other enzymes, chelating agents, pH buffering means and rheology modifiers, including those of the polyacrylate, polysaccharide or polysaccharide derivative type, and / or combinations of solvents and polycarboxylate polymers.

[0259] Thickness The detergent compositions herein are typically thickened, preferably having a viscosity of 50 to 5000 centipoise (50-5000 mPa*s), more preferably 100 to 4000 centipoise (100-4000 mPa*s), even more preferably 500 to 3500 centipoise (500-3500 mPa*s). s-1 and 800-3000 centipoise (800-3000 mPa*s) at 20°C. Viscosity can be determined by conventional methods known in the art, for example, using a TA Instruments AR 550 rheometer using a 40 mm diameter plate steel spindle and a 500 μm gap size. s-1 High shear viscosity at 0.05 s-1 The low shear viscosity at 20°C for 3 minutes is 0.1 s-1 ~25 s-1 The preferred rheology can be achieved using internal intrinsic structuring with detergent ingredients, or by using external rheology modifiers and / or crystalline structurants that provide the composition with a pseudoplastic or shear thinning rheological profile and time-dependent recovery of viscosity after shear (thixotropy).

[0260] Crystalline structurants The detergent compositions of the present invention may further comprise one or more crystalline structurants, which are materials that form a thread-like structuring system and / or an insoluble particle network throughout the matrix of the composition. The crystalline structurant may be crystallized in situ within the aqueous liquid matrix of the composition or within a premix used to form the aqueous liquid matrix, etc. It has been found that the network created by the crystalline wax structurant prevents the hydrophobic emollient droplets from agglomerating and phase separating in the product, thereby providing superior stability for the hand dishwashing liquid composition.

[0261] When present, the crystalline structurant is typically included at a level of from 0.02% to 5%, preferably from 0.025% to 3%, more preferably from 0.05% to 2%, and most preferably from 0.1% to 1.5% by weight of the total composition. Preferred crystalline structurants are hydroxy-containing crystalline structurants such as hydroxy-containing fatty acids, fatty esters, or fatty soap waxy materials, such as those described in U.S. Patent No. 6,080,707.

[0262] Other suitable crystalline structurants include C 10-22 Ethylene glycol fatty acid esters are examples. 10-22 Ethylene glycol fatty acid esters can be used alone or in combination with another crystalline structurant, such as hydrogenated castor oil. Typical examples are the mono- and / or diesters of fatty acids containing from about 6 to about 22, preferably from about 12 to about 18, carbon atoms, such as caproic acid, caprylic acid, 2-ethylhexanoic acid, capric acid, lauric acid, isotridecanoic acid, myristic acid, palmitic acid, palmitoleic acid, stearic acid, isostearic acid, oleic acid, elaidic acid, petroselinic acid, linoleic acid, linolenic acid, arachidic acid, gadoleic acid, behenic acid, erucic acid, and mixtures thereof, with ethylene glycol, propylene glycol, diethylene glycol, dipropylene glycol, triethylene glycol, or tetraethylene glycol.

[0263] For further information regarding suitable crystalline structurants, see WO 2012 / 015852.

[0264] polymer The detergent composition may contain 0.005 to 10% by weight of polymer, e.g., 0.5 to 5%, 2 to 5%, 0.5 to 2%, or 0.2 to 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 inhibition, grease cleaning, and / or defoaming properties. Some polymers may have two or more of the above properties. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(ethylene glycol) (PEG) or poly(ethylene oxide) (PEO), ethoxylated polyethyleneimine, (carboxymethyl) inulin (CMI), carboxylate polymers and polycarboxylates such as polyacrylates, maleic acid / acrylic acid copolymers, acrylate / styrene copolymers, poly(aspartic acid) and lauryl methacrylate / acrylic acid copolymers, hydrophobically modified CMC (HM-CMC) silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), poly(vinylpyrrolidone) (PVP), poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO), and copoly(vinylimidazole / vinylpyrrolidone) (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S-403E, and Chromabond S-100 manufactured by Ashland Aqualon, and Sokalan® HP 165, Sokalan® HP 50 (dispersant), Sokalan® HP 53 (dispersant), Sokalan® HP 59 (dispersant), Sokalan® HP 56 (dye transfer inhibitor), and Sokalan® HP 66 K (dye transfer inhibitor) manufactured by BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternium ethoxy sulfate.A particularly preferred polymer is the ethoxylated homopolymer Sokalan® HP 20 manufactured by BASF, which helps prevent redeposition of soil in the wash liquor. Additional exemplary polymers include sulfonated polycarboxylates, ethylene oxide-propylene oxide copolymers (PEO-PPO), copolymers of PEG with vinyl acetate, and diquaternium ethoxy sulfate or quaternized sulfated ethoxylated hexamethylenediamine. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the aforementioned polymers are also contemplated.

[0265] microorganisms The detergent composition may also include one or more microorganisms, such as one or more fungi, yeasts, or bacteria.

[0266] In one embodiment, the one or more microorganisms are dehydrated (eg, by freeze-drying) bacteria or yeast, such as strains of Lactobacillus.

[0267] In another embodiment, the microorganism is one or more microbial spores (as opposed to vegetative cells), such as bacterial spores; or fungal spores, conidia, or hyphae. Preferably, the one or more spores are Bacillus endospores; more preferably, the one or more spores are endospores of Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus megaterium.

[0268] Microorganisms can be included in detergent compositions or additives in the same way as enzymes (see below).

[0269] 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, can be deposited on fabrics when the fabrics come into contact with a wash liquor containing the detergent composition, thereby changing the color of the fabric by absorbing / reflecting visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents absorb at least a portion of the visible light spectrum, thereby changing the color of the surface. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling within the Color Index (CI) classifications 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, for example, in WO 2005 / 03274, WO 2005 / 03275, WO 2005 / 03276, and EP 1 876 226 (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 a fabric hueing agent. The composition may comprise from 0.0001% to about 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.

[0270] Additive substance Any detergent ingredient known in the art for use in laundry, ADW, or hard surface cleaning detergents can also be used. Other optional detergent ingredients include, alone or in combination, anti-corrosion agents, anti-shrinkage agents, soil redeposition inhibitors, anti-wrinkle agents, bactericides, binders, corrosion inhibitors, disintegrants / disintegration agents, dyes, enzyme stabilizers (including boric acid, borates, CMC, and / or polyols such as propylene glycol), fabric softeners including clay, fillers / processing aids, optical brighteners / optical brighteners, foam boosters, foam (soap suds) regulators, perfumes, soil suspending agents, softeners, foam suppressors, tan inhibitors, and wicking agents. Any formulation ingredient known in the art for use in laundry, ADW, or hard surface cleaning detergents can also be used. The selection of such ingredients is well within the skill of those skilled in the art.

[0271] Dispersants The detergent compositions of the present invention may also contain dispersants. In particular, powder detergents may contain dispersants. Suitable water-soluble organic materials include homo- or copolymeric acids or salts thereof, where the polycarboxylic acid contains 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.

[0272] Dye transfer inhibitor The detergent compositions of the present invention may also contain 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.

[0273] Optical brighteners The detergent compositions of the present invention will preferably also contain additional ingredients that can alter the color shade of the washed items, such as fluorescent or optical brighteners. When present, the brightener is preferably at a level of about 0.01% to about 0.5%. Any fluorescent brightener suitable for use in laundry detergent compositions can be used in the compositions of the present invention. The most commonly used fluorescent brighteners belong to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives, and bisphenyl-distyryl derivatives. Examples of diaminostilbene-sulfonic acid derivative type fluorescent brighteners 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-hydrogen)-2-hydroxybenzoates, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydrobenzoates), ... Examples of suitable fluorescent whitening agents include 4,4'-bis-(2-morpholino-4-anilino-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, 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. A preferred optical brightener is also commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals (Mumbai, India). Other optical brighteners suitable for use in the present invention include 1-3-diarylpyrazolines and 7-alkylaminocoumarins.

[0274] Suitable fluorescent brightener levels include lower levels of about 0.01, 0.05, about 0.1, or about 0.2% by weight, to upper levels of 0.5 or 0.75% by weight.

[0275] Soil Release Polymer The detergent compositions of the present invention may also contain one or more soil release polymers that aid in the removal of soil from fabrics such as cotton and polyester-based fabrics, particularly hydrophobic soil removal from polyester-based fabrics. The soil release polymer may be, for example, a nonionic or anionic terephthalate-based polymer, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, or polyester polyamides, as described, for example, in Chapter 7 of Powdered Detergents, Surfactant Science Series, Volume 71, Marcel Dekker, Inc. Another type of soil release 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 described in detail in International Publication No. 2009 / 087523 (incorporated herein by reference). Furthermore, random graft copolymers are suitable soil release polymers. Suitable graft copolymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856, and WO 2006 / 113314 (incorporated herein by reference). Other soil-release polymers are substituted polysaccharide structures, particularly substituted cellulosic structures, such as modified cellulose derivatives such as those described in EP 1867808 or WO 2003 / 040279 (both incorporated herein by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides, and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxymethyl cellulose, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, ester carboxymethyl cellulose, and mixtures thereof.

[0276] Anti-redeposition agent The detergent compositions of the present invention may also include one or more anti-redeposition agents, such as carboxymethyl cellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and / or polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimine. The cellulosic polymers described above under soil release polymers may also function as anti-redeposition agents.

[0277] 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 rheology modifiers are 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.

[0278] Other suitable additives include, but are not limited to, anti-shrinkage agents, anti-wrinkle agents, disinfectants, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, suds suppressors, solvents, and liquid detergent structurants and / or structural elasticizers.

[0279] microorganisms The detergent compositions described above may contain one or more microorganisms or microorganisms. Generally, any microorganism can be used in any suitable amount / concentration in the enzyme / detergent formulation. Microorganisms can be used as the sole biologically active ingredient, but they can also be used in combination with one or more of the enzymes described above.

[0280] 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 a microorganism at a microorganism location to competitively prevent other undesirable microorganisms from inhabiting the same location (competitive exclusion).

[0281] The term "microorganism" generally refers to a small organism visible through a microscope. Microorganisms often exist as single cells or colonies of cells. Some microorganisms may be multicellular. Microorganisms include prokaryotes (e.g., bacteria and archaea) and eukaryotes (e.g., some fungi, algae, protozoa). Examples of bacteria may be gram-positive or gram-negative bacteria. Example forms of bacteria include vegetative cells and endospores. Examples of fungi may be yeast, mold, and mushrooms. Example forms of fungi include hyphae and spores. As used herein, viruses may be considered microorganisms.

[0282] The microorganisms can be recombinant or non-recombinant. In some instances, the microorganisms can produce various substances (e.g., enzymes) that are useful for inclusion in detergent compositions. Extracts from the microorganisms or fractions from the extracts can be used in detergents. Extracts or fractions from the medium in which the microorganisms are cultured or the medium can also be used in detergents. In some instances, substances produced by the microorganism, its extracts, medium, and fractions that are unique to the microorganism can be specifically excluded from the detergent. In some instances, the microorganisms or substances produced by or extracted from the microorganisms can activate, enhance, preserve, extend, etc., detergent activity or ingredients contained in the detergent.

[0283] 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 facilitate 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.

[0284] In one embodiment, the microorganism is a Bacillus species, e.g., 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.

[0285] Detergent product formulation The detergent compositions of the present invention may be in any convenient form, such as a bar, a homogeneous tablet, a tablet with two or more layers, a pouch with one or more compartments, a regular or compact powder, granules, a paste, a gel, or a regular, compact or concentrated liquid.

[0286] The pouches can be configured as single or multiple compartments. They can be of any form, shape, and material suitable for holding the composition, e.g., preventing release of the composition from the pouch prior to contact with water. The pouches are made from a water-soluble film that encloses an internal volume. The internal volume can be divided into pouch compartments. Preferred films are polymeric materials, preferably polymers that can be formed into films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected 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, e.g., PVA, in the film is at least about 60%. Preferred average molecular weights are typically from about 20,000 to about 150,000. The film can also be a blended composition comprising a hydrolytically degradable, water-soluble polymer blend, such as polylactide and polyvinyl alcohol (known under the trade name M8630 sold by MonoSol LLC, Indiana, USA), and a plasticizer such as glycerol, ethylene glycerol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain a solid laundry cleaning composition or component and / or a liquid cleaning composition or component separated by a water-soluble film. The compartment for the liquid component can be different in composition from the compartment containing the solid; see U.S. Patent Application Publication No. 2009 / 0011970 A1.

[0287] The detergent ingredients can be physically separated from each other by compartments in different layers of the water-soluble pouch or tablet. This can avoid undesirable storage interactions between the ingredients. The different dissolution profiles of each of the compartments can also cause delayed dissolution of selected ingredients in the wash solution.

[0288] Non-unit-dose liquid or gel detergents may typically be aqueous, containing at least 20% by weight and up to 95% water, e.g., 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 aqueous liquids or gels, including, but not limited to, alkanols, amines, diols, ethers, and polyols. Water-soluble liquid or gel detergents may contain 0-30% organic solvents.

[0289] The liquid or gel detergent may be non-aqueous.

[0290] Soap bar The α-amylase of the present invention can be added to a soap bar and used for laundry, dishwashing, and hand-washing surfaces, fabrics, and / or fabrics. The term laundry soap bar is meant to include laundry bars, soap bars, combo bars, synthetic detergent bars, and detergent bars. Bar types typically differ in the type of surfactant they contain, and the term laundry soap bars includes those containing fatty acid-derived soaps and / or synthetic soaps. Laundry soap bars have a physical form that is solid 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; i.e., when a solid object (e.g., a laundry soap bar) is placed in a container, the solid object does not change and fill the container in which it is placed. Bars are typically rod-shaped solids, but can also be other solid shapes, such as round or oval.

[0291] The laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adducts or hemiacetal adducts), boric acid, borate salts, borax and / or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerin, fatty acids, pH adjusting 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 can be, for example, a formate, acetate, citrate, or lactate anion, so that the salt of the monovalent cation and the organic anion can be, for example, sodium formate.

[0292] The laundry soap bars may also contain complexing agents such as EDTA and HEDP, perfumes and / or various fillers, surfactants, such as 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, clay soil removers, anti-redeposition agents, polymeric dispersants, color brighteners, fabric softeners, perfumes and / or other compounds known in the art.

[0293] The laundry soap bars may be processed using 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 wrappers. The present invention is not limited to preparing 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, α-amylase, 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 α-amylase and any additional enzymes may be added simultaneously with the protease inhibitor, for example, in liquid form. In addition to the mixing and plodding steps, the process may further include grinding, extruding, cutting, stamping, cooling, and / or packaging steps.

[0294] Granular detergent formulations Granular detergents may be formulated as described in WO 09 / 092699, EP 1705241, EP 1382668, WO 07 / 001262, U.S. Pat. No. 6,472,364, WO 04 / 074419 or WO 09 / 102854.Other useful detergent formulations are those described in WO 09 / 124162, WO 09 / 124163, WO 09 / 117340, WO 09 / 117341, WO 09 / 117342, WO 09 / 072069, WO 09 / 063355, WO 09 / 132870, WO 09 / 121757, WO 09 / 122069, WO 09 / 123356 ...3356, WO 09 / 124163, WO 09 / 124164, WO 09 / 124165, WO 09 / 124166, WO 09 / 124167, WO 09 / 124168, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 124169, WO 09 / 12 Pamphlet No. 09 / 112296, Pamphlet No. 09 / 112298, Pamphlet No. 09 / 103822, Pamphlet No. 09 / 087033, Pamphlet No. 09 / 050026, Pamphlet No. 09 / 047125, Pamphlet No. 09 / 047126, Pamphlet No. 09 / 047127, Pamphlet No. 09 / 047128, Pamphlet No. 09 / 021784 WO 09 / 010375, WO 09 / 000605, WO 09 / 122125, WO 09 / 095645, WO 09 / 040544, WO 09 / 040545, WO 09 / 024780, WO 09 / 004295, WO 09 / 004294, WO 09 / 121725 No. 2009 / 015951, WO 09 / 115391, WO 09 / 115392, WO 09 / 074398, WO 09 / 074403, WO 09 / 068501, WO 09 / 065770, WO 09 / 021813, WO 09 / 030632 and WO 09 / 015951.

[0295] International Publication No. 2011025615, International Publication No. 2011016958, International Publication No. 2011005803, International Publication No. 2011005623, International Publication No. 2011005730, International Publication No. 2011005844, International Publication No. 2011005904, International Publication No. 2011005630, International Publication No. 201100 5830 pamphlet, International Publication No. 2011005912 pamphlet, International Publication No. 2011005905 pamphlet, International Publication No. 2011005910 pamphlet, International Publication No. 2011005813 pamphlet, International Publication No. 2010135238 pamphlet, International Publication No. 2010120863 pamphlet, International Publication No. 2010108002 pamphlet, International Publication No. 2010111365 pamphlet, International Publication No. 2010108000, International Publication No. 2010107635, International Publication No. 2010090915, International Publication No. 2010033976, International Publication No. 2010033746, International Publication No. 2010033747, International Publication No. 2010033897, International Publication No. 2010033979, International Publication No. 201003 0540 pamphlet, International Publication No. 2010030541 pamphlet, International Publication No. 2010030539 pamphlet, International Publication No. 2010024467 pamphlet, International Publication No. 2010024469 pamphlet, International Publication No. 2010024470 pamphlet, International Publication No. 2010025161 pamphlet, International Publication No. 2010014395 pamphlet, International Publication No. 2010044905 pamphlet,

[0296] International Publication No. 2010145887, International Publication No. 2010142503, International Publication No. 2010122051, International Publication No. 2010102861, International Publication No. 2010099997, International Publication No. 2010084039, International Publication No. 2010076292, International Publication No. 2010069742, International Publication No. 2010069718, International Publication No. 2010069957, International Publication No. 2010057784, International Publication No. 2010054986, International Publication No. 2010018043, International Publication No. 2010003783, International Publication No. 2010003792,

[0297] International Publication No. 2011023716, International Publication No. 2010142539, International Publication No. 2010118959, International Publication No. 2010115813, International Publication No. 2010105942, International Publication No. 2010105961, International Publication No. 2010105962, International Publication No. 2010094356, International Publication No. 2010084203, International Publication No. 2010078979, International Publication No. 2010072456, International Publication No. 2010069905, International Publication No. 2010076165, International Publication No. 2010072603, International Publication No. 2010066486, International Publication No. 2010066631, International Publication No. 2010066632, International Publication No. 2010063689, International Publication No. 2010060821, International Publication No. 2010049187, International Publication No. 2010031607, International Publication No. 2010000636.

[0298] Formulation of enzymes in co-granules The enzymes of the present invention can be formulated as granules, for example, co-granules that combine one or more enzymes, where each enzyme is present in more granules, ensuring a more uniform distribution of the enzymes within the detergent. This also reduces the physical segregation of the various enzymes due to their varying particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0299] Another example of incorporating enzymes through the use of 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 weight percent of a zeolite (on an anhydrous basis); and (c) less than 10 weight percent of a phosphate (on an anhydrous basis), wherein the enzyme composite granule comprises 10 to 98 weight percent of a moisture sink component, and the composition further comprises 20 to 80 weight percent of a detergent moisture sink component. WO 2013 / 188331 relates to a method of treating and / or cleaning a surface, preferably a fabric surface, comprising the steps of: (i) contacting the surface with a detergent composition as claimed and described herein in an aqueous wash liquor; and (ii) rinsing and / or drying the surface.

[0300] The multi-enzyme complex granules may contain the enzyme of the present invention and one or more enzymes selected from the group consisting of (a) first-wash lipase, cleaning cellulase, xyloglucanase, perhydrolase, peroxidase, lipoxygenase, laccase, and mixtures thereof; and (b) hemicellulase, protease, keratinase, cellobiose dehydratase, xylanase, phospholipase, esterase, cutinase, pectinase, mannanase, pectate lyase, keratinase, reductase, oxidase, phenoloxidase, ligninase, pullulanase, tannase, pentosanase, lichenase, glucanase, arabinosidase, hyaluronidase, chondroitinase, amylase, and mixtures thereof.

[0301] liquid enzyme formulation Enzymes may be formulated as liquid enzyme formulations, which are generally injectable compositions but may have a high viscosity. The physical appearance and properties of liquid enzyme formulations can vary greatly. For example, they can have various viscosities (from gel to watery), be colored or uncolored, clear or opaque, and even have solid particles, such as slurries and suspensions. The minimum components are the enzyme and a solvent system that makes it liquid. In addition to the enzyme, liquid enzyme formulations may also contain other enzyme activities, such as protease, amylase, lipase, cellulase, and / or nuclease (e.g., DNase, RNase) activity.

[0302] 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.

[0303] Liquid enzyme formulations can be prepared by mixing a solvent system with an enzyme concentrate (or enzyme particles to obtain a slurry / suspension) of the desired purity.

[0304] In one embodiment, the liquid enzyme composition comprises: (a) at least 0.01% by weight of active enzyme protein; (b) at least 0.5 wt. % of a polyol; (c) water; (d) optionally a preservative; Includes.

[0305] The enzymes in the liquid compositions of the present invention may be stabilized using conventional stabilizers, such as sugars such as glucose, fructose, sucrose, and trehalose, the addition of salts to increase ionic strength, and divalent cations (e.g., Ca). 2+or Mg 2+ These include, but are not limited to, enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP). Selecting the optimal pH for the formulation can be crucial for enzyme stability. The optimal pH depends on the specific enzyme, but is typically in the range of pH 4 to 9. In some cases, surfactants such as nonionic surfactants (e.g., alcohol ethoxylates) can improve the physical stability of enzyme formulations.

[0306] One embodiment of the present invention is a composition comprising an enzyme, the composition comprising: (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; (iii) optionally a surfactant, preferably a surfactant selected from anionic and nonionic surfactants; (iv) optionally a divalent cation, a polymer, or an enzyme inhibitor; (v) optionally having a pH in the range of pH 4 to 9; (vi) Water and The present invention relates to a composition further comprising:

[0307] Enzyme slurries or dispersions are typically prepared by dispersing small particles (e.g., spray-dried particles) of the enzyme in a liquid medium in which the enzyme is sparingly soluble, such as a liquid nonionic surfactant or liquid polyethylene glycol. Powders can be added to aqueous systems in amounts that do not dissolve completely (above the solubility limit). Another form is a crystalline suspension, which can also be an aqueous liquid (see, for example, WO 2019 / 002356). Another method for preparing such dispersions is by preparing a water-in-oil emulsion in which the enzyme is in the aqueous phase and evaporating water from the droplets. Such slurries / suspensions can typically be physically stabilized (to reduce or avoid settling) by the addition of rheology modifiers such as fumed silica or xanthan gum to obtain a shear-thinning rheology.

[0308] Granular enzyme formulation Enzymes can also be formulated as solid / granular enzyme preparations. 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 wax 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 12 to 20 carbon atoms and in which 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 shown in GB 1,483,591.

[0309] Enzymes may be formulated as granules, for example, as composite granules that combine one or more enzymes or beneficial agents (e.g., MnTACN or other bleaching ingredients). Examples of such additional enzymes include proteases, amylases, lipases, cellulases, and / or nucleases (e.g., DNase, RNase). Each enzyme is then present in more granules, ensuring a more uniform distribution of the enzymes within the detergent. This also reduces the physical segregation of the various enzymes due to their varying particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0310] One embodiment of the present invention relates to enzyme granules / particles comprising an enzyme. The granules consist of a core and, optionally, one or more coatings (outer layers) surrounding the core. Typically, the granules have a particle size, measured as the equivalent spherical diameter (average particle size by volume), of 20 to 2000 μm, in particular 50 to 1500 μm, 100 to 1500 μm, or 250 to 1200 μm.

[0311] 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 fragrances. The core may contain binders such as synthetic polymers, waxes, fats, or carbohydrates. The core may contain salts of polyvalent cations, reducing agents, antioxidants, peroxide decomposition catalysts, and / or acidic buffer components, typically as a homogeneous blend. The core may consist of inert particles imbibed with enzymes or onto which enzymes are applied, for example, 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 CE Capes, Handbook of Powder Technology; Particle size enlargement Volume 1; 1980; Elsevier. These methods are known in the art and are also described in International Patent Application WO 2015 / 028567, pages 3-5, which are incorporated by reference.

[0312] 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 granule. Optional coatings may include salt coatings or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxypropyl cellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with multi-layer coatings are shown in WO 93 / 07263 and WO 97 / 23606.

[0313] Such coatings are known in the art and have already been described, for example, in WO 00 / 01793, WO 2001 / 025412 and WO 2015 / 028567, which are incorporated by reference.

[0314] In one aspect, the present invention provides a method for producing a pharmaceutical composition comprising: (a) a core comprising an enzyme according to the invention, and (b) optionally, a (salt) coating consisting of one or more layers surrounding the core; The present invention provides granules comprising:

[0315] Another aspect of the present invention is a method for producing a semiconductor device comprising: (a) (non-enzymatic) core, (b) a coating surrounding the core, the coating comprising an enzyme; 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:

[0316] Encapsulated enzyme formulation The enzymes may also be formulated as encapsulated enzyme formulations ("capsules"), which are particularly useful for separating the enzymes from other ingredients when they are added to (liquid) cleaning compositions, such as the detergent compositions described below.

[0317] Physical separation can be used to resolve incompatibilities between enzymes and other components. The 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 can be a substrate for the amylase.

[0318] 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.

[0319] Enzymes can also be encapsulated in core-shell microcapsules, for example, as described in WO 2015 / 144784 or IP.com disclosure IPCOM000239419D.

[0320] 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.

[0321] enzyme The detergent composition may also include one or more additional enzymes such as a protease, lipase, cutinase, a second amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase such as a laccase, and / or a peroxidase.

[0322] Additional enzymes The detergent compositions of the present invention may further comprise one or more additional enzymes to provide cleaning and / or washing performance. Examples of suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, nucleases, hyaluronidases, chondroitinases, laccases, chlorophyllases, other amylases, or mixtures thereof. A typical combination is an enzyme cocktail, which may include, for example, α-amylase and protease in combination with mannanase. When present in the composition, the aforementioned additional enzymes may be present at a level of 0.00001 to 2%, 0.0001 to 1%, or 0.001 to 0.5% enzyme protein by weight of the active ingredient in the composition.

[0323] Generally, the properties of the selected enzyme should be compatible with the selected detergent (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme should be present in an effective amount.

[0324] cellulase In one aspect, preferred enzymes include cellulases. Suitable cellulases include single-component and mixtures of bacterial or fungal enzymes. Chemically modified or engineered mutants are also contemplated. Cellulases can be single-component or mixtures of single-component endo-1,4-beta-glucanases, also known as endoglucanases, for example.

[0325] Suitable cellulases include those from the genera Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include fungal cellulases 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 derived 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. Cellulases derived from the genus Bacillus are also important, as described in WO 02 / 099091 and JP 2000210081. Suitable cellulases include 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.

[0326] Other cellulases include endo-beta-1,4-glucanase enzymes having a sequence that is at least 97% identical to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091, or family 44 xyloglucanases, which have a sequence that is at least 60% identical to positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903.

[0327] 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 (available from Genencor International Inc.), and KAC-500(B). TM (Kao Corporation) is one example.

[0328] Mannanase In one embodiment, preferred enzymes include mannanases. 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 derived from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999 / 064619. Commercially available mannanases include Mannaway (Novozymes A / S).

[0329] Peroxidase / Oxidase In one embodiment, preferred enzymes include peroxidases. Suitable peroxidases are preferably peroxidase enzymes encompassed by the enzyme classification EC 1.11.1.7 as set forth by the Nomenclature Commission of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragments derived therefrom that exhibit peroxidase activity.

[0330] Suitable peroxidases include those of plant, bacterial, or fungal origin. They also include chemically modified or protein-engineered mutants. Examples of useful peroxidases include peroxidases from Coprinopsis species, such as C. cinerea (EP 179,486), and variants thereof, such as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257.

[0331] 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 haloperoxidase, i.e., a vanadate-containing haloperoxidase. In a preferred method, the vanadate-containing haloperoxidase is combined with a chloride ion source.

[0332] 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.

[0333] Haloperoxidases have also been isolated from bacteria such as Pseudomonas, eg, P. pyrrocinia, and Streptomyces, eg, S. aureofaciens.

[0334] The haloperoxidase may be derived from a Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, e.g., C. inaequalis CBS 102.42 as described in WO 95 / 27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97 / 04102; or Drechslera hartlebii as described in WO 01 / 79459, Dendrophiella salina as described in WO 01 / 79458, or from a Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, e.g., C. inaequalis ... inaequalis CBS 102.42 as described in WO 95 / 27046; or C. inaequalis CBS 102.42 as described in WO 95 / 27046; or C. inaequalis CBS 102.42 as described in WO 95 / 27046; or C. inaequalis CBS 102.4 salina, Phaeotrichoconis crotalarie as described in WO 01 / 79461, or Geniculosporium sp. as described in WO 01 / 79460.

[0335] Suitable oxidases include in particular any laccase enzyme included in the enzyme classification EC 1.10.3.2 or any fragment thereof 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).

[0336] Preferred laccase enzymes are those of bacterial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).

[0337] Suitable examples of fungal origin include Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, etc. s), for example, T. villosa and T. versicolor, Rhizoctonia, for example, R. solani, Coprinopsis, for example, C. cinerea, C. comatus, C. friesii, and C. pli catilis, Psathyrella such as P. condoleana, Panaeolus such as P. papilionaceus, Myceliophthora such as M. thermophila, Schytalidium such as S. thermophilum, Polyporus such as P. pinsitus, Phlebia such as P. radiata (WO 92 / 01046), or Coriolus such as C. hirsutus (Japanese Patent Publication No. 2238885).

[0338] A suitable example of bacterial origin is laccase obtained from a strain of the genus Bacillus.

[0339] Laccases obtained from the genus Coprinopsis or Myceliophthora are preferred; in particular, laccases obtained from Coprinopsis cinerea, as disclosed in WO 97 / 08325; or laccases obtained from Myceliophthora thermophila, as disclosed in WO 95 / 33836.

[0340] nuclease In one embodiment, preferred enzymes include nucleases. Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases), which are enzymes that catalyze the hydrolytic cleavage of phosphodiester bonds in the DNA or RNA backbone, respectively, thereby degrading DNA and RNA. There are two major classifications based on the site of activity: exonucleases digest nucleic acids from the ends; endonucleases act on the middle region of the target molecule. The nuclease is preferably a DNase, which can be obtained from a microorganism, preferably a fungus or bacterium. In particular, DNases obtainable from Bacillus species are preferred, especially those obtainable from Bacillus cibi, Bacillus subtilis, or Bacillus licheniformis. Examples of such DNases are described in WO 2011 / 098579, WO 2014 / 087011, and WO 2017 / 060475. Particularly preferred are DNases obtainable from Aspergillus species, particularly those obtainable from Aspergillus oryzae, such as the DNase described in WO 2015155350. Detergent enzymes can be included in detergent compositions by adding separate additives containing one or more enzymes, or by adding a combined additive containing all of these enzymes. The detergent additives of the present invention, either individually or in combination, can be formulated, for example, as granules, liquids, slurries, etc. Preferred detergent additive formulations are granules, particularly the non-shattering granules described above, and liquids, particularly stabilized liquids or slurries.

[0341] Proteases In one aspect, preferred enzymes include proteases. Suitable proteases can be of any origin, but are preferably of bacterial or fungal origin, and optionally in the form of protein-modified or chemically modified mutants. The protease can be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease can be, for example, from the S1 family, such as trypsin, or the S8 family, such as subtilisin. The metalloprotease can be, for example, thermolysin, for example, from the M4 family, or another metalloprotease, for example, from the M5, M7, or M8 family.

[0342] The term "subtilase" refers to a subclass of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997): 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with the substrate. Subtilases can be divided into six subdivisions: the subtilisin family, thermitase family, proteinase K family, lantibiotic peptidase family, kexin family, and pyrrolysin family.

[0343] 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. Particular 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 include, for example, those described in WO 01 / 16285 and WO 02 / 16547.

[0344] 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.

[0345] Examples of metalloproteases include 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.

[0346] Examples of useful proteases include 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, 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, S1 26L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Q200L, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256D The protease may comprise one or more mutations selected from the group consisting of T268A, T268B, and R269H, where the position numbers correspond to the positions in 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 the Bacillus lentus protease (also known as Savinase® subtilisin 309) set forth in SEQ ID NO: 1 of WO 2016 / 001449, or variants of the 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 SEQ ID NO: 2 of WO 2016 / 001449.

[0347] 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.

[0348] Alternatively, the protease may be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004 / 067737, for example a variant comprising 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, wherein the protease variant has at least 75% but less than 100% sequence identity to SEQ ID NO: 1 of WO 2004 / 067737. TY145 variants of interest are described, for example, in WO 2015 / 014790, WO 2015 / 014803, WO 2015 / 014804, WO 2016 / 097350, WO 2016 / 097352, WO 2016 / 097357, and WO 2016 / 097354.

[0349] 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, corresponding to SEQ ID NO: 302 in 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) Variants 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).

[0350] Suitable commercially available protease enzymes include Alcalase®, Duralase®, TM , Durazym TM , Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase TM, those sold under the trade names Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In, and Progress® Excel (Novozymes A / S), Maxatase TM , Maxacal TM , Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2 TM , FN3 TM , FN4 exTM , Excellase®, Excellenz TM P1000, Excellent TM P1250, Eraser TM , Preferenz® P100, Purafect Prime, Preferenz P110 TM , Effectenz P1000 TM , Purafect®, Effectenz P1050 TM , Purafect(R)Ox, Effectenz TM P2000, Purafast TM , Properase®, Opticlean TMand Optimase® (Danisco / DuPont), BLAP (sequence shown in Figure 29 of U.S. Pat. No. 5,352,604) and its variants (Henkel AG), and those sold under the tradename KAP (Bacillus alkalophilus subtilisin) manufactured by Kao.

[0351] Lipase and cutinase In one aspect, preferred enzymes include lipases and / or cutinases. Suitable lipases and cutinases include those of bacterial or fungal origin. These include chemically or protein-modified mutant enzymes. Examples include enzymes from the genus Thermomyces, such as T. lanuginosus (formerly Humicola lanuginosus), as described in EP 258068 and EP 305216. lanuginosa), for example cutinases from Humicola species such as H. insolens (WO 96 / 13580), for example P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331376), P. sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (P.Lipases from strains of Pseudomonas (some of which have now been renamed Burkholderia) such as Pseudomonas wisconsinensis (WO 96 / 12012), GDSL-type Streptomyces lipases (WO 10 / 065455), cutinases from Magnaporthe grisea (WO 10 / 107560), cutinases from Pseudomonas mendocina (U.S. Pat. No. 5,389,536), lipases from Thermobifida fusca (WO 11 / 084412), Geobacillus stearothermophilus (Geobacillus stearothermophilus), and the like. Examples of lipases that can be used include lipases from Bacillus stearothermophilus (WO 11 / 084417), lipases from Bacillus subtilis (WO 11 / 084599), and lipases from Streptomyces griseus (WO 11 / 150157) and S. pristinaespiralis (WO 12 / 137147).

[0352] 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.

[0353] A preferred commercially available lipase product is Lipolase TM , Lipex TM ;Lipolex TM , and Lipoclean TM (Novozymes A / S), Lumafast (originally manufactured by Genencor), and Lipomax (originally manufactured by Gist-Brocades).

[0354] Further examples are lipases, sometimes called acyltransferases or perhydrolases, such as acyltransferases with homology to Candida antarctica lipase A (WO 10 / 111143), acyltransferases from Mycobacterium smegmatis (WO 05 / 56782), perhydrolases from the CE 7 family (WO 09 / 67279), as well as variants of M. smegmatis perhydrolase, in particular the S54V variant used in the product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 10 / 100028).

[0355] amylase In one aspect, preferred enzymes include another (second) amylase. Suitable amylases that can be used with the compositions of the present invention may be α-amylases or glucoamylases and may be of bacterial or fungal origin, including chemically modified or engineered mutants. Amylases include, for example, α-amylases obtained from specialized strains of Bacillus, such as Bacillus licheniformis, which is described in more detail in GB Patent No. 1,296,839.

[0356] Suitable amylases include those having SEQ ID NO: 2 in WO 95 / 10603 or variants thereof having 90% sequence identity with SEQ ID NO: 3. Preferred variants are set out in SEQ ID NO: 4 of WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and WO 99 / 019467, such as variants having substitutions at one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408 and 444.

[0357] A different suitable amylase includes the amylase having SEQ ID NO: 6 in WO 02 / 010355 or a variant thereof having 90% sequence identity to SEQ ID NO: 6. A preferred variant of SEQ ID NO: 6 is one having deletions at positions 181 and 182 and a substitution at position 193.

[0358] Another suitable amylase is a hybrid α-amylase comprising residues 1-33 of the α-amylase from B. amyloliquefaciens as set forth in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of the α-amylase from B. licheniformis as set forth in SEQ ID NO: 4 of WO 2006 / 066594, or a variant thereof with 90% sequence identity. Preferred variants of this hybrid α-amylase are those with substitutions, deletions, or insertions at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, 1201, A209, and Q264. The most preferred variant of the hybrid α-amylase comprising residues 1-33 of the α-amylase from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 comprises the substitution: M197T; H156Y+A181T+N190F+A209V+Q264S; or It has G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

[0359] Further suitable amylases are those having SEQ ID NO: 6 in WO 99 / 019467, or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having substitutions, deletions, or insertions at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those having deletions at positions R181 and G182 or H183 and G184.

[0360] Additional amylases that can be used include those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2, or SEQ ID NO: 7 of WO 96 / 023873, or variants thereof having 90% sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 7 include those having 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 having deletions at two positions selected from 181, 182, 183, and 184, for example, positions 181 and 182, positions 182 and 183, or positions 183 and 184. The most preferred amylase variants of SEQ ID NO:1, SEQ ID NO:2, or SEQ ID NO:7 have deletions at positions 183 and 184 and substitutions at one or more of positions 140, 195, 206, 243, 260, 304, and 476.

[0361] Other amylases that can be used include amylases having SEQ ID NO: 2 in WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712, or variants thereof having 90% sequence identity to SEQ ID NO: 2 in WO 08 / 153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01 / 66712. Preferred variants of SEQ ID NO: 10 in WO 01 / 66712 are those that have substitutions, deletions, or insertions at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

[0362] Further suitable amylases include amylases having SEQ ID NO: 2 of WO 09 / 061380, or variants thereof having 90% sequence identity to SEQ ID NO: 2. Preferred variants of SEQ ID NO: 2 include those having C-terminal truncations and / or 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 positions R180 and / or S181 or T182 and / or G183. Most preferred amylase variants of SEQ ID NO:2 are those with 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, 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.

[0363] Further suitable amylases are those having SEQ ID NO: 1 of WO 13184577 or variants thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 include 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 include substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K, and / or deletions at positions R178 and / or S179 or T180 and / or G181. The most preferred amylase variants of SEQ ID NO: 1 include substitutions: E187P+I203Y+G476K E187P+I203Y+R458N+T459S+D460T+G476K T38N+N126Y+T129I+F153W+R178*+G179*+T180D+E187P+I203Y+G476K+G477E The variant optionally further comprises a substitution at position 241 and / or a deletion at positions 178 and / or 179.

[0364] 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 include those having substitutions, deletions, or insertions at one or more of the following positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477, and G478. More preferred variants of SEQ ID NO: 1 include those having substitutions at one or more of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K, and G478K, and / or deletions at positions R179 and / or S180 or I181 and / or G182. The most preferred amylase variant of SEQ ID NO: 1 has the substitution: N21D+D97N+V128I The variant optionally further comprises a substitution at position 200 and / or a deletion at positions 180 and / or 181.

[0365] Other suitable amylases include the α-amylase having SEQ ID NO: 12 in WO 01 / 66712, or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants include those having substitutions, deletions or insertions at one or more of the following positions of SEQ ID NO: 12 in WO 01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and substitutions R118K, N195F, R320K, and R458K, as well as variants that additionally have substitutions at one or more positions selected from the group of M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, with variants that additionally have substitutions at all of these positions being most preferred.

[0366] Other examples include amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078, and WO 2013 / 001087.

[0367] Commercially available amylase is Amplify Prime TM , Atlantic TM , Arctic TM , Everest TM , Duramyl TM , Termamyl TM , Fungamyl TM , Stainzyme TM , Stainzyme Plus TM , Natalase TM , Liquozyme X and BAN TM(Novozymes A / S), and Rapidase TM , Purastar TM / Effectenz TM , Powerase, Preferenz S1000, Preferenz S100, Preferenz S110 and Preferenz S210 (manufactured by Genencor International Inc. / DuPont).

[0368] Protease Stabilizers / Inhibitors Proteases can be stabilized using compounds (reversible inhibitors) that act by temporarily reducing proteolytic activity.

[0369] Thus, the compositions of the present invention may also include a protease inhibitor / stabilizer that is a reversible inhibitor of protease activity, e.g., serine protease activity. Preferably, the protease inhibitor is a (reversible) subtilisin protease inhibitor. In particular, the protease inhibitor may be a peptide aldehyde, boric acid, or boronic acid; or a derivative of any of these.

[0370] Boronic acids The protease inhibitor may be a boronic acid or derivative thereof, preferably a phenylboronic acid or derivative thereof. In one embodiment of the present invention, the phenylboronic acid derivative has the following formula: [ka] wherein R is selected from the group consisting of hydrogen, hydroxy, C1-C6 alkyl, substituted C1-C6 alkyl, C1-C6 alkenyl, and substituted C1-C6 alkenyl. Preferably, R is hydrogen, CH3, CH3CH2, or CH3CH2CH2.

[0371] In a preferred embodiment, the protease inhibitor (phenylboronic acid derivative) is 4-formyl-phenyl-boronic acid (4-FPBA).

[0372] In another particular embodiment, the protease inhibitor is thiophene-2-boronic acid, thiophene-3-boronic acid, acetamidophenylboronic acid, benzofuran-2-boronic acid, naphthalene-1-boronic acid, naphthalene-2-boronic acid, 2-FPBA, 3-FBPA, 4-FPBA, 1-thianthreneboronic acid, 4-dibenzofuranboronic acid, 5-methylthiophene-2-boronic acid, thionaphthreneboronic acid, furan-2-boronic acid, furan-3-boronic acid, 4,4-biphenyl-diboronic acid, 6-hydroxy-2-naphthalene, 4-(methylthio)phenylboronic acid, 4-(trimethyl-silyl)phenylboronic acid, 3-bromothiopheneboronic acid, 4-methylthiopheneboronic acid, 2-naphthylboronic acid, 5-bromothipheneboronic acid. acid), 5-chlorothiopheneboronic acid, dimethylthiopheneboronic acid, 2-bromophenylboronic acid, 3-chlorophenylboronic acid, 3-methoxy-2-thiophene, p-methyl-phenylethylboronic acid, 2-thianthreneboronic acid, dibenzothiopheneboronic acid, 4-carboxyphenylboronic acid, 9-anthrylboronic acid, 3,5-dichlorophenylboronic acid, diphenylboronic anhydride, o-chlorophenylboronic acid, p-chlorophenylboronic acid, m-bromophenylboronic acid, p-bromophenylboronic acid, p-fluorophenylboronic acid, p-tolylboronic acid, o-tolylboronic acid, octylboronic acid, 1,3,5-trimethylphenylboronic acid, 3-chloro-4-fluorophenylboronic acid, 3-aminophenylboronic acid, 3,5-bis-(trifluoromethyl)phenylboronic acid, 2,4-dichlorophenylboronic acid, and 4-methoxyphenylboronic acid.

[0373] Further boronic acid derivatives suitable as protease inhibitors in detergent compositions are described in U.S. Pat. No. 4,963,655, U.S. Pat. No. 5,159,060, WO 95 / 12655, WO 95 / 29223, WO 92 / 19707, WO 94 / 04653, WO 94 / 04654, U.S. Pat. No. 5,442,100, U.S. Pat. No. 5,488,157, and U.S. Pat. No. 5,472,628.

[0374] Peptide aldehyde or ketone The protease stabilizer has the formula: PALB-B0-R*: wherein R* is H (hydrogen), CH3, CX3, CHX2, or CH2X, where X is a halogen atom, in particular F (fluorine), preferably R*=H (the stabilizer is therefore a peptide aldehyde having the formula PALB-BO-H), L is absent or is a linker group of formula -C(=O)-, -C(=O)-C(=O)-, -C(=S)-, -C(=S)-C(=S)-, or -C(=S)-C(=O)-; A is absent if L is absent, or is one or two amino acid residues linked to L via the N-terminus, and thus A can represent A1 or A2-A1, where A2 and A1 each represent one amino acid residue; B can be one, two, or three amino acid residues, and thus B can represent B1, B2-B1, or B3-B2-B1 linked via the C-terminus to B0, where B3, B2, and B1 each represent one amino acid residue, and B0 is a single amino acid residue having the L- or D-configuration of the formula -NH-CH(R)-C(=O)-; R is independently optionally substituted with one or more identical or different substituents R′; 1~6 Alkyl, C 6~10 Aryl, or C 7~10 arylalkyl; R' is independently selected from the group consisting of halogen, -OH, -OR", -SH, -SR", -NH, -NHR, -NR, -COH, -CONH, -CONHR, -CONR, and -NHC(=N)NH; R'' is C 1~6 is an alkyl group, P is selected from the group consisting of hydrogen, or, if L is absent, an N-terminal protecting group.

[0375] B0 can be a single amino acid residue having an L- or D-configuration, linked to H through the C-terminus of the amino acid. B0 has the formula -NH-CH(R)-C(=O)-, where R is C 1-6 Alkyl, C 6-10 Aryl, or C 7-10 Arylalkyl side chains include, for example, methyl, ethyl, propyl, isopropyl, butyl, isobutyl, phenyl, or benzyl, and R may be optionally substituted with one or more identical or different substituents R'. Specific examples of B0 are the D- or L-forms of arginine (Arg), 3,4-dihydroxyphenylalanine, isoleucine (Ile), leucine (Leu), methionine (Met), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), m-tyrosine, p-tyrosine (Tyr), and valine (Val). Particular embodiments are those in which B0 is leucine, methionine, phenylalanine, p-tyrosine, or valine. Particularly preferred is p-tyrosine.

[0376] B1, which is linked to B0 via the C-terminus of the amino acid, can be an aliphatic amino acid, a hydrophobic amino acid, and / or a neutral amino acid. Examples of B1 include alanine (Ala), cysteine ​​(Cys), glycine (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), proline (Pro), serine (Ser), threonine (Thr), and valine (Val). Specific examples of B1 include alanine, glycine, isoleucine, leucine, and valine. A specific embodiment is when B1 is alanine, glycine, or valine.

[0377] When present, B2 is linked to B1 via the C-terminus of the amino acid and may be an aliphatic amino acid, a hydrophobic amino acid, a neutral amino acid, and / or a polar amino acid. Examples of B2 include alanine (Ala), arginine (Arg), capreomycin (Cpd), cysteine ​​(Cys), glycine (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), proline (Pro), serine (Ser), threonine (Thr), and valine (Val). Specific examples of B2 include alanine, arginine, capreomycin, glycine, isoleucine, leucine, phenylalanine, and valine. A specific embodiment is when B2 is arginine, glycine, leucine, phenylalanine, or valine.

[0378] If present, B3 is linked to B2 via the C-terminus of the amino acid and may be a large aliphatic amino acid, an aromatic amino acid, a hydrophobic amino acid, and / or a neutral amino acid. Examples of B3 are isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), phenylglycine, tyrosine (Tyr), tryptophan (Trp), and valine (Val). Specific examples of B3 are leucine, phenylalanine, tyrosine, and tryptophan.

[0379] The linker group L may be absent or selected from the group consisting of -C(=O)-, -C(=O)-C(=O)-, -C(=S)-, -C(=S)-C(=S)-, or -C(=S)-C(=O)-. A particular embodiment of the invention is where L is absent or where L is a carbonyl group -C(=O)-.

[0380] When present, A1 is linked to L via the N-terminus of the amino acid and can be an aliphatic amino acid, an aromatic amino acid, a hydrophobic amino acid, a neutral amino acid, and / or a polar amino acid. Examples of A1 include alanine (Ala), arginine (Arg), capreomycin (Cpd), glycine (Gly), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), threonine (Thr), tyrosine (Tyr), tryptophan (Trp), and valine (Val). Specific examples of A1 include alanine, arginine, glycine, leucine, phenylalanine, tyrosine, tryptophan, and valine. A particular embodiment is when B2 is leucine, phenylalanine, tyrosine, or tryptophan.

[0381] A2, if present, is linked to A1 via the N-terminus of the amino acid and can be a large aliphatic amino acid, an aromatic amino acid, a hydrophobic amino acid, and / or a neutral amino acid. Examples of A2 include arginine (Arg), isoleucine (Ile), leucine (Leu), norleucine (Nle), norvaline (Nva), phenylalanine (Phe), phenylglycine, tyrosine (Tyr), tryptophan (Trp), and valine (Val). Specific examples of A2 include phenylalanine and tyrosine.

[0382] The N-terminal protecting group P (if present) may be selected from formyl, acetyl (Ac), benzoyl (Bz), trifluoroacetyl, methoxysuccinyl, aromatic and aliphatic urethane protecting groups such as fluorenylmethyloxycarbonyl (Fmoc), methoxycarbonyl (Moc), (fluoromethoxy)carbonyl, benzyloxycarbonyl (Cbz), t-butyloxycarbonyl (Boc), and adamantyloxycarbonyl; p-methoxybenzylcarbonyl, benzyl (Bn), p-methoxybenzyl (PMB), p-methoxyphenyl (PMP), methoxyacetyl, methylaminocarbonyl, methylsulfonyl, ethylsulfonyl, benzylsulfonyl, methylphosphoramidyl (MeOP(OH)(=O)), and benzylphosphoramidyl (PhCHOP(OH)(=O)).

[0383] Suitable peptide aldehydes are described in WO 94 / 04651, WO 95 / 25791, WO 98 / 13458, WO 98 / 13459, WO 98 / 13460, WO 98 / 13461, WO 98 / 13462, WO 07 / 141736, WO 07 / 145963, WO 09 / 118375, WO 10 / 055052, and WO 11 / 036153.More specifically, the peptide aldehydes include Cbz-Arg-Ala-Tyr-H, Ac-Gly-Ala-Tyr-H, Cbz-Gly-Ala-Tyr-H, Cbz-Gly-Ala-Tyr-CF3, Cbz-Gly-Ala-Leu-H, Cbz-Val-Ala-Leu-H, Cbz-Val-Ala-Leu-CF3, Moc-Val-Ala-Leu-CF3, Cbz-Gly-Ala-Phe-H, Cbz-Gly-Ala-Phe-CF3, Cbz-Gly-Ala-Va l-H, Cbz-Gly-Gly-Tyr-H, Cbz-Gly-Gly-Phe-H, Cbz-Arg-Val-Tyr-H, Cbz-Leu-Val-Tyr-H, Ac-Leu-Gly-Ala-Tyr-H (SEQ ID NO: 21), Ac-Phe-Gly-Ala-Tyr-H (SEQ ID NO: 22), Ac-Tyr-Gly-Ala-Tyr-H (SEQ ID NO: 23), Ac-Phe-Gly-Ala-Leu-H (SEQ ID NO: 24), Ac-Phe-Gly-Ala-Phe-H (SEQ ID NO: 25) ), Ac-Phe-Gly-Val-Tyr-H (SEQ ID NO: 26), Ac-Phe-Gly-Ala-Met-H (SEQ ID NO: 27), Ac-Trp-Leu-Val-Tyr-H (SEQ ID NO: 28), MeO-CO-Val-Ala-Leu-H, MeNCO-Val-Ala-Leu-H, MeO-CO-Phe-Gly-Ala-Leu-H (SEQ ID NO: 29), MeO-CO-Phe-Gly-Ala-Phe-H (SEQ ID NO: 30), MeSO-Phe-Gly-Ala-Leu-H (SEQ ID NO: 31), MeSO-Val-Ala-Leu-H, PhCHO-P(OH)(O)-Val-Ala-Leu-H, EtSO-Phe-Gly-Ala-Leu-H (SEQ ID NO: 32), PhCHSO-Val-Ala-Leu-H, PhCHO-P(OH)(O)-Leu-Ala-Leu-H, PhCHO-P(OH)(O)-Phe-Ala-Leu-H, or MeO-P(OH)(O)-Leu-Gly-Ala-Leu-H (SEQ ID NO: 33). A preferred stabilizer for use in the liquid compositions of the present invention is Cbz-Gly-Ala-Tyr-H, or a hydrosulfite adduct thereof, wherein Cbz is benzyloxycarbonyl.

[0384] Further examples of such peptide aldehydes include α-MAPI, β-MAPI, Phe-C(=O)-Arg-Val-Tyr-H, Phe-C(=O)-Gly-Gly-Tyr-H, Phe-C(=O)-Gly-Ala-Phe-H, Phe-C(=O)-Gly-Ala-Tyr-H, Phe-C(=O)-Gly-Ala-LH, Phe-C(=O)-Gly-Ala-Nva- ... Gly-Ala-Nle-H, Tyr-C(=O)-Arg-Val-Tyr-H, Tyr-C(=O)-Gly-Ala-Tyr-H, Phe-C(=S)-Arg-Val-Phe-H, Phe-C(=S)-Arg-Val-Tyr-H, Phe-C(=S)-Gly-Ala-Tyr-H, antipain, GE20372A, GE20372B, chym...

Claims

1. 1. A detergent composition comprising: (i) a polypeptide having catalase activity and having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 1, 2, 3, 4 or 5; and (ii) A detergent composition comprising a polypeptide having α-amylase activity.

2. the α-amylase is an α-amylase variant comprising a modification at one or more positions corresponding to positions 1, 54, 56, 72, 109, 113, 116, 134, 140, 159, 167, 169, 172, 173, 174, 181, 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391, 395, 439, 469, 444, 473, 476 or 477 of SEQ ID NO:4, and the α-amylase variant has a nucleotide sequence at least 60%, e.g.

2. The detergent composition of claim 1, wherein the α-amylase variant has at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the α-amylase variant, and wherein the α-amylase variant has α-amylase activity.

3. 2. The detergent composition of claim 1, wherein the α-amylase comprises one or more modifications selected from the group consisting of H1, N54, V56, K72, G109, F113, R116, T134, W140, W159, W167, Q169, Q172, L173, A174, R181, G182, D183, G184, W189, E194, N195, V206, G255, N260, F262, A265, W284, F289, S304, G305, W347, K391, Q395, W439, W469, R444, F473, G476, and G477, wherein the positions correspond to positions in SEQ ID NO:

6.

4. 2. The detergent composition of claim 1, wherein the at least one α-amylase variant comprises a deletion at positions corresponding to 181+182, 181+183, 181+184, 182+183, 182+184, or 183+184 of SEQ ID NO:

6.

5. The α-amylase variant in (i) H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K; H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S +G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K; H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1* + N54S + V56T + K72R + G109A + A174S + G182* + D183* + N195F + V206L + G255A + K391A + G476K and H1* + N54S + V56T + G109A + W167F + Q172E + L173P + A174K + G182* + D183* + N195F + V206L + K391A + G476K, and wherein the α-amylase variant has a sequence identity of at least 60%, such as at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 81%, or at least 90% relative to SEQ ID NO: 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20.

5. The detergent composition of claim 1, wherein the α-amylase variants have at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the α-amylase variants, and wherein the α-amylase variants have α-amylase activity.

6. The composition of any one of claims 1 to 5, wherein the composition further comprises a detergent component.

7. 7. The composition of claim 6, wherein the detergent ingredients are selected from the group consisting of surfactants, builders, chelating agents or chelating agents, bleaching systems or ingredients, polymers, suds boosters, suds suppressors, dyes, fragrances, tan inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, corrosion inhibitors, enzyme stabilizers, enzyme inhibitors or activators, one or more transferases, hydrolases, oxidoreductases, antireflective agents and fluorescent dyes, antioxidants and solubilizers.

8. The composition of any one of claims 1 to 7, wherein the composition further comprises an additional enzyme.

9. 9. The composition of claim 8, wherein the additional enzyme is selected from the group consisting of a protease, lipase, cutinase, a second amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, a licheninase, a laccase, and / or a peroxidase.

10. 10. The composition of any one of claims 1 to 9, wherein the composition is a detergent, and the detergent composition is a liquid laundry detergent composition, a powder laundry detergent composition, a liquid dishwashing detergent composition, or a powder dishwashing detergent composition.

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

12. A method for removing stains from a fabric or hard surface comprising contacting said fabric or hard surface contaminated with the stain with a composition according to any one of claims 1 to 10.

13. 11. A method of washing dishes in an automatic dishwashing machine using a composition according to any one of claims 1 to 10, comprising the steps of adding the detergent composition to a detergent composition compartment of the automatic dishwashing machine and discharging the detergent composition during a main wash cycle.

14. 11. A method of washing clothes in an automatic washing machine using a composition according to any one of claims 1 to 10, comprising the steps of adding said detergent composition to a detergent composition compartment of said automatic washing machine and discharging said detergent composition during a main wash cycle.

15. 1. A method for treating a surface, comprising: a. forming an aqueous cleaning solution using the composition of any one of claims 1 to 10; b. treating the surface with the aqueous cleaning solution, preferably at a temperature in the range of 5°C to 60°C; c. rinsing said surface; A method comprising:

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