Detergents and cleaning agents having an improved cleaning performance against grease-containing stains

Abstract

The invention relates to a detergent and / or cleaning agent, comprising at least one peptide, at least one enzyme having a hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase having a lipolytic activity, particularly preferably lipase, and optionally at least one salt, wherein the peptide is suitable for adhesion to a grease- and / or oil-containing surface or to a surface coated with grease and / or oil or to a surface provided with at least one grease- and / or oil-containing stain, and the surface is selected from hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enameled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably flatware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g. cutlery or pots) or glass and mixtures thereof, particularly preferably flatware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof. The invention further relates to methods for cleaning hard surfaces and / or textiles, to the use of such peptides, and to agents for improving the cleaning performance against at least one grease- and / or oil-containing stain.

Description

[0001] DETERGENT AND CLEANING AGENTS WITH IMPROVED CLEANING PERFORMANCE ON GREASY SOILS

[0002] DESCRIPTION

[0003] The invention relates to a washing and / or cleaning agent, comprising at least one peptide, at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, and optionally at least one salt, wherein the peptide is suitable for adhesion to a fat- and / or oil-containing surface or to a surface coated with fat and / or oil or to a surface provided with at least one fat- and / or oil-containing soil, wherein the surface consists of hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g.cutlery or pots) or glass and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof. Furthermore, the invention relates to methods for cleaning hard surfaces and / or textiles, and to the use of such peptides and agents for improving the cleaning performance on at least one greasy and / or oily soil.

[0004] Peptides that specifically bind to or interact with oxidic surfaces such as metal surfaces, as well as peptides that specifically bind to plastic surfaces, have already been described (WO 2014 / 072313 A1, WO 2023 / 110572 A1). Adhesive peptides are also of interest for many other surfaces, particularly for functionalizing such surfaces or imparting other desired properties.

[0005] It is known to use so-called "functional polymers" in detergents and / or cleaning agents, such as "soil release polymers" in detergents to improve soil removal from textiles or "soil repellent polymers" in detergents to prevent / reduce dirt build-up on textiles. Such soil release polymers (SRPs) are water-soluble or water-dispersible polycondensates based on dicarboxylic acids and diols or cellulose ethers. SRPs can have a positive effect on the ability of oil and grease to be washed out of textiles. Typical SRPs are based, for example, on copolymers of polyester and polyether, also terephthalate, e.g., polypropylene terephthalate. However, these polymers are not biodegradable. Therefore, there is a need for alternative or improved, particularly biodegradable SRPs for use in detergents and / or cleaning agents, and / or alternatives thereto.

[0006] The dispersant polymers used in automatic dishwashing detergents fulfill similar functions to prevent or reduce soil buildup. These are typically (co)polymeric polycarboxylates, such as poly(meth)acrylates or sulfonic acid-containing polymers based on (meth)acrylic acid. However, the biodegradability of such polymers has so far been limited, so readily biodegradable alternatives are being sought for dishwashing detergents.

[0007] Grease and / or oily soils on hard surfaces and / or textiles are among the more stubborn types of soiling that are not easy to remove. In conventional washing and / or cleaning processes, such soiling is removed by first liquefying the fats due to the washing and / or cleaning temperature, usually between approximately 40°C and approximately 60°C, and then detaching them from the surface by surfactants contained in the washing and / or cleaning agents ("roll-up mechanism"). The detached, liquefied fat molecules are then carried away, i.e., rinsed away, by mechanical forces during the washing and / or rinsing process. Additionally or alternatively, grease and / or oily soils can be removed by esterases, lipolytic enzymes, or lipases, in which the enzyme breaks down the fats and / or oils, and the degradation products are then in turn rinsed away.However, the use of lipases after the washing process results in an unpleasant odor on the washed objects, especially textiles, because the lipase is adsorbed by the textiles and continues to hydrolyze fatty acid esters to low molecular weight fatty acids. These low molecular weight fatty acids are then perceived by their unpleasant odor. The intensity of the odor can vary depending on the nature of the textile. Therefore, there is currently no satisfactory alternative for removing greasy and / or oily soils at low temperatures, i.e. at temperatures below 40°C, in particular at, for example, around 20°C or around 30°C, because the fats do not liquefy or only insufficiently liquefy at temperatures below around 30°C or around 40°C.

[0008] The inventors have discovered and developed specific peptides which, surprisingly, are suitable for adhering to fatty and / or oily surfaces, as described herein, enable the removal of at least one fatty and / or oily soil from surfaces, and can thus improve the cleaning performance of washing and / or cleaning agents containing them on at least one fatty and / or oily soil. Furthermore, the inventors have discovered that, in particular, the combination of a lipase and at least one peptide according to the invention leads to improved removal of at least one fatty and / or oily soil from a surface. Furthermore, the inventors have discovered that, in particular, the combination of a lipase and at least one peptide according to the invention in the presence of a salt leads to improved removal of at least one fatty and / or oily soil from a surface.In the context of the present invention, a "fatty and / or oily surface" is understood to mean a surface that contains or consists of fats and / or oils, and / or a surface that is coated with fats and / or oils, and / or a surface that is soiled with at least one fatty and / or oily soil. In the context of the present invention, "fat" or "fats" are understood to mean macromolecules formed from glycerol and fatty acids, in addition to mono- and diglycerides, in particular the so-called triacylglycerols or triglycerides, in which three fatty acids are bonded to the glycerol. Furthermore, according to the invention, all known fatty acids having 8 to 36, preferably 10 to 24, carbon atoms, both mono- and polyunsaturated and saturated fatty acids, are encompassed. In the context of the present invention, "oil" or "oils" are understood to mean fatty acids that are liquid or soluble at room temperature.Flowable fatty substances that do not mix with water are understood. Both synthetic and bio-based fats and / or oils are encompassed within the scope of the invention. Within the scope of the present invention, "fatty and / or oily soiling" is understood to mean soiling on a surface, in particular a hard surface and / or textile surface, that contains or consists of a fat and / or oil. Examples of typical fat and / or oily soiling are fat and / or oily food and food residue soiling, such as vegetable fats (e.g. coconut fat), animal fats (e.g. butter, clarified butter), cooking oils (e.g. olive oil, sunflower oil, rapeseed oil), frying fat, mayonnaise, margarine, frying fat, meat fat (e.g. beef tallow, pork fat, lard), also burnt-in food residues, and / or synthetic fats and / or oils, such asMineral oil(s) and / or greases, engine oil, bicycle chain oil, pigment greases, pigment oils, and / or fats and / or oils from personal care products, such as lipstick, make-up, lotion, cream, and / or body fat deposits, such as sebum, tallow. In preferred embodiments, the fatty surface contains or consists of a fat that is solid at room temperature. In preferred embodiments, the surface coated with fat is coated with a fat that is solid at room temperature. In preferred embodiments, the surface provided with at least one fatty soil is provided or soiled with at least one solid fat, ie the at least one fatty soil preferably contains or consists of a fat that is solid at room temperature.

[0009] In the context of the present invention, the fat- and / or oil-containing surface and / or the surface coated with fat and / or oil and / or the surface provided with at least one fat- and / or oil-containing soil is preferably selected from hard surfaces and / or textiles.

[0010] Preferably, the greasy and / or oil-containing surface and / or the surface coated with grease and / or oil and / or the surface provided with at least one greasy and / or oil-containing soil is a hard surface containing or consisting of ceramic (e.g., porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enameled surfaces, wood, laminate, linoleum, and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or earthenware, as well as plastic), metal (e.g., cutlery or pots), or glass. Preferably, the greasy and / or oil-containing surface and / or the surface coated with grease and / or oil and / or the surface provided with at least one greasy and / or oil-containing soil is a textile surface. The term "textile surface," as used herein, is synonymous with the term "textile" or "textiles." The term "textile" or"Textiles," as used herein, means any textile material, including yarns, yarn precursors, fibers, nonwovens, natural materials, synthetic materials, and all other textile materials, fabrics made from these materials, and products made from fabrics (e.g., garments and other articles). The textile or fabric may be in the form of knits, wovens, denims, nonwovens, felts, yarns, and terry cloth. The textile may be cellulose-based, such as natural cellulose fibers like cotton, flax / linen, jute, ramie, sisal, or coconut fibers, or man-made cellulose fibers (e.g., from wood pulp) such as viscose / rayon, cellulose acetate fibers (Tricell), lyocell, or mixtures thereof. The textile or fabric may also be made of non-cellulose fibers, e.g.,Made from natural polyamides such as wool, camel, cashmere, mohair, rabbit, and silk, or from synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulosic and non-cellulosic fibers. Examples of blends include blends of cotton and / or rayon / viscose with one or more accompanying materials such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and / or cellulosic fibers (e.g., rayon / viscose, ramie, flax / linen, jute, cellulose acetate fibers, lyocell). The fabric may be conventional washable laundry, e.g., soiled household linen. When the term "fabric" or "garment" is used, it is intended to include the broader term "textiles."Textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof are preferred, particularly preferably cotton, polyester or mixtures thereof.

[0011] The invention particularly preferably relates to hard surfaces and / or textiles which are provided with at least one greasy and / or oily soil, ie are greasy soiled, wherein the hard surfaces are preferably selected from tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and the textiles contain or consist of cotton, polyester and mixtures thereof.

[0012] Through the adhesion of substrate-specific peptides to fatty and / or oily surfaces, in particular fatty surfaces as defined herein, i.e. in particular to at least one fatty and / or oily soil on a surface (as described herein), preferably selected from hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, functional groups can be selectively bound to the fat and / or oil molecules on the surface. This can bring about a substrate-specific detachment of the fatty and / or oily soils.Peptides according to the invention which specifically bind to fats and / or oils, preferably solid fats, or fat- and / or oil-containing soils, preferably fat-containing soils, on surfaces can thus be used to specifically remove these fats and / or oils, in particular solid fats, from the surface.

[0013] In particularly preferred embodiments, the peptides according to the invention enable the improvement of the cleaning performance of washing and / or cleaning agents on at least one fatty and / or oil-containing soiling from a surface, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, in particular containing or consisting of cotton, polyester and mixtures thereof.

[0014] The invention therefore relates in a first aspect to a washing and / or cleaning agent comprising

[0015] (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5, and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1, and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably from -1.8 to +1.0; and

[0016] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and

[0017] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0018] In preferred embodiments, the peptide in agents according to the invention has an amino acid sequence which is 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, preferably the peptide has an amino acid sequence according to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, more preferably SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, particularly preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29. In preferred embodiments, the at least one enzyme having hydrolytic activity on an ester bond is a lipase, wherein the lipase is selected from

[0019] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:32,

[0020] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0021] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0022] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

[0023] In preferred embodiments, the at least one salt is selected from

[0024] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts, and / or

[0025] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0026] Particularly preferably, the at least one salt is selected from alkali metal salts with inorganic counterion, very particularly preferred are alkali metal halides, in particular those selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0027] In preferred embodiments, the peptide binds to a fatty surface or to a surface coated with fat or to a surface provided with at least one fatty and / or oily soil, wherein the surface is preferably selected from hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2.

[0028] In further aspects, the invention relates to preferred embodiments of the aforementioned agent as described herein.

[0029] Further objects of the invention relate to

[0030] • Process for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, wherein a washing and / or cleaning agent described herein is used in at least one process step;

[0031] • Process for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, wherein in a first step the at least one peptide is brought into contact with the items to be washed or rinsed and in a second step the at least one lipase is brought into contact with the items to be washed or rinsed;

[0032] • Process for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, wherein it is carried out in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C;

[0033] • Use of an agent described herein for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass;

[0034] • Use of a peptide described herein in a washing and / or cleaning agent to improve the cleaning performance of the washing and / or cleaning agent on at least one fatty and / or oily soil, preferably fatty soil;

[0035] • Use of a peptide described herein in a washing and / or cleaning agent as a soil-removing, in particular grease- and / or oil-removing, active ingredient in a washing or cleaning agent; • Use in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0036] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples.

[0037] Unless otherwise stated, all percentages are by weight (wt%), based on the total weight of the corresponding composition or agent.

[0038] Numerical ranges specified in the format "from x to y" include the specified values. If multiple preferred numerical ranges are specified in this format, it goes without saying that all ranges resulting from the combination of the different endpoints will also be included.

[0039] "At least one," as used herein, means one or more, i.e., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or more. With reference to an ingredient, the statement refers to the type of ingredient and not to the absolute number of molecules. "At least one peptide" thus means, for example, at least one type of peptide, i.e., one type of peptide or a mixture of several different peptides can be meant. Together with weight specifications, the statement refers to all compounds of the specified type contained in a product, i.e., the product typically does not contain any further compounds of this type beyond the stated amount of the corresponding compounds.

[0040] "Approximately" or "approximately" as used herein with reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0041] The term "washing and cleaning agent" or "washing or cleaning agent" as used herein is synonymous with the term "agent" and refers to a composition for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, as explained in the description.

[0042] For the purposes of the invention, the term "room temperature" refers to 20°C at 1,013 mbar, unless explicitly stated otherwise. "Liquid," as used herein, includes liquids and gels, as well as pasty compositions. It is preferred that the liquid compositions be flowable and pourable at room temperature, but it is also possible that they have a yield point.

[0043] A substance, e.g. a composition or an agent, is solid according to the definition of the invention if it is in the solid state at 20°C and 1,013 mbar.

[0044] A substance, e.g., a composition or agent, is liquid according to the invention's definition if it exists in the liquid state at 20°C and 1,013 mbar. Liquid also includes gel.

[0045] The term "N-terminus" or "N-terminal" in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free amino group.

[0046] The term "C-terminus" or "C-terminal" in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free carboxyl group.

[0047] The term "in N- to C-terminal orientation" in the context of this invention refers to an amino acid sequence in which the order of the amino acids is described starting from the N-terminus to the C-terminus.

[0048] When reference is made herein to various linked or individual amino acid sequences, these are always shown in N- to C-terminal orientation unless otherwise stated. Furthermore, the individual amino acids or amino acid sequences are linked to each other via peptide bonds unless otherwise stated.

[0049] In the context of this invention, "adhesion" or "adhesive" refers to an interaction between a peptide and a surface, enabling the peptide to adhere to the surface. Thus, the term "adhesion-promoting" refers to the ability, under suitable conditions, i.e., usually non-denaturing conditions, to interact with and / or adhere to various surfaces, e.g., textile surfaces, in particular those containing or consisting of cotton, polyester, and mixtures thereof, or hard surfaces, such as, in particular, tableware (preferably made of ceramic such as porcelain or earthenware, as well as plastic), metal (e.g., cutlery or pots), or glass. "Fat-binding peptides," as used herein, mean that the peptide binds to fat, e.g., to at least one fatty and / or oily soil on a surface.In preferred embodiments, the binding affinity is greater than that of a reference sequence or a reference molecule that does not exhibit adhesion-promoting properties. The lipid-binding peptides described herein preferably exhibit 10-fold, more preferably 20-fold, 50-fold, or 100-fold higher adhesion to a given surface than a reference molecule (peptide according to SEQ ID NO:32). The term "binding" in the context of this invention preferably refers to "covalent bonds" between the peptide and a surface.A peptide is, in the sense of the invention, a fat-binding peptide in particular if, in a method according to Example 2, the ability of the peptide to adhere to a fat- and / or oil-containing surface and / or to a surface coated with fat and / or oil and / or to at least one fat- and / or oil-containing soil on a surface is demonstrated, wherein the binding affinity is greater than that of a reference molecule (peptide according to SEQ ID NO:32).

[0050] The present invention is based on the surprising discovery of the inventors that specific peptides bind to fatty and / or oily surfaces, as described herein, enable the removal of at least one fatty and / or oily soil from surfaces, and thus improve the cleaning performance of washing and / or cleaning agents containing them on at least one fatty and / or oily soil. Furthermore, the inventors have found that, in particular, the combination of an enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, and a peptide according to the invention leads to improved removal of at least one fatty and / or oily soil from a surface.This is surprising insofar as it has not previously been described that peptides according to the invention can remove fatty and / or oily soils from a surface, i.e., exhibit cleaning performance on at least one fatty and / or oily soil, nor that peptides according to the invention can improve the cleaning performance of an enzyme that exhibits hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipases. Furthermore, it was surprisingly found that the presence of at least one salt further enhances the cleaning performance of the combination of peptide and lipase.

[0051] The invention therefore relates in a first aspect to a washing and / or cleaning agent comprising

[0052] (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and

[0053] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and

[0054] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0055] In a second aspect, the invention relates to a washing and / or cleaning agent comprising

[0056] (A) at least one peptide, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;and / or b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0057] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0058] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0059] X 2 is selected from R, H and K, preferably R and K,

[0060] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0061] X 4 is selected from A, L and V, preferably A and L,

[0062] X 5is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31;

[0063] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and

[0064] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0065] The peptide definitions a), b) and c) are to be understood as alternative or complementary.

[0066] A "peptide" in the context of the present invention is understood to mean a polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, preferably of a linear structure, which has up to 100 amino acids linked to one another via peptide bonds. According to the invention, the peptides of the invention have an amino acid sequence of 4 to 50 amino acids. The amino acids are specified in the context of this invention in a one-letter code, e.g., "C" in the sequence (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 )q] r (X 5 )s(C)t represents a cysteine ​​residue. It is further understood that, unless otherwise stated, the amino acids in an amino acid sequence disclosed herein are linked via peptide bonds and, unless otherwise stated, the sequence is listed in N- to C-terminal orientation.

[0067] Table 1: Proteinogenic amino acids

[0068] Typical acidic or negatively charged amino acids (depending on pH) are D and E. Positively charged or basic amino acids (depending on pH) typically include R, K, and H. Amino acids such as G, A, C, I, L, M, F, V, P, S, T, W, Y, N, and Q are typically uncharged, i.e., neutral amino acids. References herein to "any" amino acids typically refer to one of the 20 naturally occurring proteinogenic amino acids (Table 1).

[0069] Unless otherwise stated, the amino acids are typically L-amino acids. In alternative embodiments, the peptide may also consist of D-amino acids, although it may be preferred that D- and L-amino acids do not occur simultaneously within the peptides described herein. In various embodiments, such an arbitrary amino acid encompasses all of the aforementioned amino acids.

[0070] In various embodiments, the peptide has a theoretically calculated total charge (hereinafter referred to as total charge) of 0 to +12, e.g. 0, +1, +2, +3, +4, +5, +6, +7, +8, +9, +10, +11, +12. The total charge of the peptide is based on the number of amino acids in the peptide that can form a negative or positive charge in a side chain next to the C or N terminus, in particular R, K, H, D and E, and results from the sum of these (theoretically possible) negative and positive charges, with one (theoretically possible) positive and one negative charge canceling each other out. A peptide with 2 R residues and 1 E residue would therefore have a total charge of +1. In preferred embodiments, the total charge of the peptide is 0 to +4.

[0071] In various embodiments, the peptide

[0072] (a1) has a total charge of 0 to +4, or

[0073] (a2) if r > 4, has a total charge of 0 to +4, or

[0074] (a3) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

[0075] In various embodiments,

[0076] (b) the N-terminus comprising the first 1-5 amino acids has a positive net charge; and / or (c1) the C-terminus comprising the last 1-5 amino acids has a negative net charge, so that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than or equal to 0, preferably greater than 0, or

[0077] (c2) the C-terminus comprising the last 1-5 amino acids has a neutral net charge, so that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than 0, preferably greater than 1, or

[0078] (c3) the C-terminus comprising the last 1-5 amino acids has a positive net charge, so that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than 0, preferably greater than 1.

[0079] All of the above features can be implemented individually or in any combination.

[0080] The feature that the peptide has a positive net charge at the N-terminus comprising the first 1-5 amino acids means that the N-terminal 1-5 amino acids comprise more positively charged than negatively charged amino acids. In various embodiments, this feature is met, for example, when the N-terminal 1-5 amino acids comprise 1 or 2 positively charged amino acids, i.e., H, K, or R, preferably K or R, more preferably R, and no negatively charged amino acids, such as E or D. If the N-terminus contains a negatively charged amino acid, the number of positively charged amino acids must be at least 2 for the net charge to remain positive.

[0081] The feature that the peptide has a negative net charge at the C-terminus comprising the last 1-5 amino acids means that the number of charged amino acids must be 0 or the number of negatively charged amino acids, i.e., D and E, must be greater than the number of positively charged amino acids. In various embodiments, this feature is met, for example, if the C-terminal 1-5 amino acids, i.e., within the last 5 amino acids at the C-terminus, have 1 or 2 negatively charged amino acids, i.e., D or E, and no positively charged amino acids, i.e., H, K, or R. An example of such a C-terminal sequence would be, for example, EAL or the double sequence of this motif.

[0082] For the feature that the peptide has a neutral net charge at the C-terminus comprising the last 1-5 amino acids, this means that the number of charged amino acids must be 0 or the number of negatively and positively charged amino acids must be equal.

[0083] The isoelectric point (IEP, pHi or pI) is the pH value at which the number of positive and negative charges of an amphoteric molecule, in this case the peptide, is statistically exactly equal. At this pH value (in an aqueous solution), the respective peptide is externally neutral, i.e., isoelectric.

[0084] The peptides according to the invention have an isoelectric point in a range from 5.0 to 15.0. Preferred peptides have an isoelectric point of 6.0 to 13.0, particularly preferably from 6.5 to 12.0. This has the advantage that the adhesion of the peptides to the fatty surface is particularly stable and the interaction of the peptides with the lipases is also improved.

[0085] Preferred is a peptide which has an isoelectric point in a range of 5.0 to 15.0 and is selected from the peptides according to SEQ ID NO: 1 to 31. Preferred peptides have an isoelectric point of 6.0 to 13.0, particularly preferably of 6.5 to 12.0.

[0086] If the pH of the aqueous solution containing the peptide is above the isoelectric point, the peptide has a negative charge. If the pH of the aqueous solution containing the peptide is below the isoelectric point, the peptide has a positive charge.

[0087] In addition to the total charge mentioned above, which results from the theoretical calculation of the sum of the negative and positive amino acids (i.e. the sum of amino acids that can form a negative or positive charge in a side chain in addition to the C- or N-terminus), whereby a positive and a negative charge cancel each other out, there is also the pH-dependent charge value of a peptide.

[0088] This pH-dependent charge value of the peptide is determined by the actual pKa values ​​of the amino acid residues that can form a negative or positive charge.

[0089] In a further embodiment of the present invention, the peptide according to the invention therefore has a charge value at pH 8 of -3 to +3. Preference is given to a peptide which has a charge value at pH 8 of -3 to +3 and is selected from the peptides according to SEQ ID NO: 1 to 31. A particularly preferred peptide has a charge value at pH 8 of -1.0 to +2.0. A very particularly preferred peptide has a charge value at pH 8 of -1.0 to +2.0 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0090] According to a particularly preferred embodiment, the peptide has a charge value of -0.75 to +1.5 at pH 8. Most preferably, the peptide has a charge value of -0.75 to +1.5 at pH 8 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29,30.

[0091] Furthermore, an embodiment of the present invention is characterized in that the peptide according to the invention has a charge value at pH 9 of -3.0 to +3.0. Preference is given to a peptide which has a charge value at pH 9 of -3 to +3 and is selected from the peptides according to SEQ ID NO: 1 to 31. A particularly preferred peptide has a charge value of -1.5 to +1.5 at pH 9. It is very particularly preferred if the peptide has a charge value of -1.5 to +1.5 at pH 9 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0092] According to a particularly preferred embodiment, a peptide is particularly preferred which has a charge value of -1.1 to +1.1 at pH 9. Most preferably, the peptide has a charge value of -1.1 to +1.1 at pH 9 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0093] In a further embodiment of the present invention, the peptides according to the invention have a charge value at pH 10 of -3 to +3. Preference is given to a peptide which has a charge value at pH 10 of -3 to +3 and is selected from the peptides according to SEQ ID NO: 1 to 31. Particularly preferred peptides have a charge value at pH 10 of -2.0 to +2.0. It is very particularly preferred if the peptide has a charge value at pH 10 of -2.0 to +2.0 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30

[0094] Particularly preferred are peptides which have a charge value of -1.8 to +1.0 at pH 10. Particularly preferred is a peptide which has a charge value of -1.8 to +1.0 at pH 10 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0095] Particularly preferred peptides have a) an isoelectric point of 6.0 to 13.0, particularly preferably of 6.5 to 12.0 and b) a charge value of -1.0 to +2.0 at pH 8 and / or a charge value of -1.5 to +1.5 at pH 9 and / or a charge value at pH 10 of -2.0 to +2.0.

[0096] Very particularly preferred peptides have a) an isoelectric point of 6.5 to 12.0 and b) a charge value of -0.75 to +1.5 at pH 8 and / or a charge value of -1.5 to +1.5 at pH 9 and / or a charge value of -1.8 to +1.0 at pH 10.

[0097] The isoelectric point and the charge values ​​can be calculated using the Henderson-Hasselbalch equation, as described in Kozlowski, LP, “IPC - Isoelectric Point Calculator”. Biol Direct 11 , 55 (2016), https: / / doi.org / 10.1186 / s13062-016-0159-9. In the calculation, the pKa values ​​were used as disclosed in Grimsley GR, Scholtz JM, Pace CN. “A summary of the measured pK values ​​of the ionizable groups in folded proteins”. Protein Sci. 2009 Jan;18(1):247-51. doi: 10.1002 / pro.19. PMID: 19177368; PMCID: PMC2708032.

[0098] The isoelectric points resulting from these calculations for the peptides explicitly disclosed herein as well as the charge values ​​at pH 8.0, pH 9.0 and pH 10.0 are given in Table 2.

[0099] In various embodiments, the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0100] (C)m(X 1 )n(X2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0101] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0102] X 2 is selected from R, H and K, preferably R and K,

[0103] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0104] X 4 is selected from A, L and V, preferably A and L, X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4.

[0105] In various embodiments, in a peptide, when o = 1, p = 0, 1 or 2, q = 2 and r = 4, the sequence (X 2 )0[(X 3 ) P (X 4 ) q ]r(X 5 )s equals Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z 6 ]3(Z 7 ) V , where

[0106] Z 1 like X 2 defined above and selected from R, H and K, preferably R,

[0107] Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined above and selected from A, L and V, preferably A and L,

[0108] Z 4 like X 3 defined above and selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably F, R, E, A, Q and W, u is 1 or 2,

[0109] Z 7 like X 5defined above and selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, v is as defined above and is an integer from 0 to 4.

[0110] In various embodiments

[0111] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0112] (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ.

[0113] In various embodiments, the peptide comprises

[0114] (i) at least one motif selected from RAL and RLA, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 1-3; and / or

[0115] (ii) at least one motif selected from EAL and ELA, preferably EAL, and wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or

[0116] (iii) at least one motif selected from QAL and QI_A, preferably QAL; and / or

[0117] (iv) the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0118] (v) at least one, preferably two or three, RAL motif(s); and / or

[0119] (vi) the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0120] In various embodiments, the peptide comprises a motif selected from RAL, RSI, and RLA, preferably RAL and RLA, more preferably RAL. The N-terminal sequence RAL or RLA not only advantageously has a positive net charge, it also comprises amino acids with a particularly high α-helix-forming potential. In various embodiments, the R residue can also be replaced by K, but the N-terminal R residue is particularly preferred.

[0121] In various embodiments, the peptide comprises amino acids with a high α-helix-forming potential, wherein these amino acids are selected from E, A, L, M, Q, K, R, F, I, H, W and D, more preferably E, A, L, M, Q, K, R, F, I and H, more preferably E, A, L, M, Q, K, R and H.

[0122] In various embodiments, the peptide consists of at least 50%, and increasingly preferably at least 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% of amino acids with a high α-helix-forming potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, W and D, more preferably E, A, L, M, Q, K, R, F, I and H, particularly preferably E, A, L, M, Q, K, R and H.

[0123] In various embodiments, the peptide forms a helical secondary structure, in particular an α-helix structure with an α-helix content of preferably at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. The use of the motif AL or LA in the amino acid sequence of the peptide according to the invention can contribute to the stability of the helix structure because these amino acids have a high α-helix potential.

[0124] In various embodiments, in a peptide, when o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 )0[(X 3 ) P (X 4 ) q ]r equals Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) W Z 16 , where

[0125] Z 11 like X 2defined above and selected from R, H and K,

[0126] Z 12 like X 3 defined above and selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, N, C, Q, G, I, L, M, F, P, S, T, W, Y and V, more preferably M, I, S, T, N, V ​​and F, Z 13 , Z 14 , Z 16 like X 4 defined above and selected from A, L and V, preferably A and L, Z 15 like X 3 defined above and selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably R, K, E, S, Q and N, w is an integer from 3 to 6.

[0127] In various embodiments, a peptide

[0128] (i) Z is 13 Z 14 selected from AL and LA, preferably AL; and / or

[0129] (ii) includes (Z 15 ) wwith w = 3-6 a sequence comprising at least one positively charged amino acid (R, H or K); and / or

[0130] (iii) includes (Z 15 ) w with w = 3-6 a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or

[0131] (iv) Z is 16 selected from A and L, preferably A. In various embodiments, the peptide may have a high proportion of hydrophobic amino acids selected from A, L, F, W, V, M, I and P, in particular A, L, F, W, V, M and I.

[0132] In preferred embodiments, the proportion of hydrophobic amino acids, ie the number of hydrophobic amino acids, based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50% and particularly preferably at least 60%. In various embodiments, the proportion of hydrophobic amino acids in the peptide is at least 30%, and increasingly preferably at least 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69% or 70%. In further preferred embodiments, at least three, preferably at least four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, are located next to one another in the peptide sequence. In particularly preferred embodiments, the proportion of hydrophobic amino acids, iethe number of hydrophobic amino acids, based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and there are at least three, preferably four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, next to one another in the peptide sequence.

[0133] In various embodiments, the peptide has an amino acid sequence having a length of 10 to 24 amino acids, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 18 amino acids.

[0134] In preferred embodiments, the peptide has an amino acid sequence which is 10 to 24 amino acids in length, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 18 amino acids, and the proportion of hydrophobic amino acids, ie the number of hydrophobic amino acids based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and there are at least three, preferably four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, next to one another in the peptide sequence.

[0135] In various embodiments, the peptide has the amino acid cysteine ​​(C) at the C-terminus. In various embodiments, the peptide has the amino acid cysteine ​​at the N-terminus. This amino acid can enable coupling to other molecules, structures, or substrates via the free sulfhydryl group. This amino acid therefore serves as a linkage site but is typically not involved in the desired adhesive effect.

[0136] In preferred embodiments, the peptide has an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with any of the amino acid sequences set forth in SEQ ID NOs: 1-31. In preferred embodiments, the peptide is selected from: HFVKTPARWAWG (SEQ ID NO: 1), IYASNHSHPASY (SEQ ID NO: 2), GHQGHWYGMFRA (SEQ ID NO: 3), SLAFMPAWHASR (SEQ ID NO: 4), HNHHQLALVESY (SEQ ID NO: 5), SQLFNSQRLAYS (SEQ ID NO: 6), WRHPRLRCGNLL (SEQ ID NO: 7), SRARLFWTYHKC (SEQ ID NO: 8), HMISTMNAASRRC (SEQ ID NO: 9), RSIVTFSLRQNRC (SEQ ID NO: 10), RSIVTFSLRQNSEQAC (SEQ ID NO: 11), KSIVTFSLRQNRC (SEQ ID NO: 12), KSIVTFSLKQNRC (SEQ ID NO: 13), RALFRALFEALEALRC (SEQ ID NO: 14), RALFEALQALFRALEALC (SEQ ID NO:15), RALRALFEALEALC (SEQ ID NO:16), RALFEALFRALEALRC (SEQ ID NO:17), RALEALFRALEALC (SEQ ID NO:18), RALFRALWEALFEALC (SEQ ID NO:19),RALFEALWRALFEALC (SEQ ID NQ:20), RALF E ALF RALE ALC (SEQ ID NO:21), SHTWGSQATSSS (SEQ ID NO:22), RALEALWRALEALC (SEQ ID NO:23), RALRALQALEALEALC (SEQ ID NO:24), RALRALQALQALEALC (SEQ ID NO:25), RALRALQALQALEAELC (SEQ ID NO:26), RALARALARALAQALAC (SEQ ID NO:27), RALARALARALARALAC (SEQ ID NO:28), RALRALRALEALEALC (SEQ ID NO:29), RALQALRALQALEALC (SEQ ID NQ:30), RALRALEALQALEALC (SEQ ID NO:31).,

[0137] In preferred embodiments, the peptide has a sequence shown in SEQ ID NO: 1-31, particularly preferably SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, most particularly preferably SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0138] In preferred embodiments, the peptide has an amino acid sequence which is from 10 to 24 amino acids in length, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular from 10 to 18 amino acids, and has an isoelectric point of from 5.0 to 15, preferably from 6.0 to 13.0, particularly preferably from 6.5 to 12.0, and / or a charge value at pH 8 of from -3.0 to +3.0, preferably from -1.0 to +2.0, particularly preferably from -0.75 to +1.5; and / or a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0.

[0139] In preferred embodiments, the peptide has an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, and has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0.

[0140] In preferred embodiments, the peptide has an amino acid sequence having a length of 10 to 24 amino acids, e.g.11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 18 amino acids, wherein the amino acid sequence has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, and has an isoelectric point of 5.0 to 15, preferably from 6.0 to 13.0, particularly preferably from 6.5 to 12.0, and / or a charge value at pH 8 of -3.0 to +3.0, preferably from -1.0 to +2.0, particularly preferably from -0.75 to +1.5; and / or a charge value at pH 9 of -3.0 to +3.0, preferably from -1.5 to +1.5, particularly preferably from -1.1 to +1.1 and / or a charge value at pH 10 of -3.0 to +3.0, preferably from -2.0 to +2.0, particularly preferably from -1.8 to +1.0.

[0141] Preferred peptides according to the invention bind to a surface containing fat and / or oil and / or to a surface coated with fat and / or oil and / or to a surface provided with at least one fatty and / or oil-containing soil, wherein the surface is preferably selected from hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, ie the peptides have the ability under suitable conditions, ieThey are able to adhere to corresponding surfaces under usually non-denaturing conditions and therefore have adhesive properties. Such adhesion / binding of the peptide can occur directly via the terminal N- or C-terminal group. Alternatively or additionally, such adhesion / binding of the peptide can also occur via further functional groups bound N- and / or C-terminally. Furthermore, the peptide can be stably associated N- and / or C-terminally and / or via suitable side chains covalently and / or similar suitable binding mechanisms under the desired application conditions to a carrier substance, in particular to a fat- and / or oil-containing surface and / or to a surface coated with fat and / or oil and / or to a surface provided with at least one fat- and / or oil-containing soil, as described herein.

[0142] In various embodiments, peptides of the invention can be surface-active or non-surface-active. In preferred embodiments, peptides of the invention are non-surface-active.

[0143] Various methods for determining interfacial activity are known to those skilled in the art. Within the scope of the invention, the dynamic surface tension is determined as a measure of interfacial activity, based on the bubble pressure method. Using the SITA science line t100 laboratory tensiometer (formerly SITA Messtechnik GmbH, Dresden), the dynamic surface tension of surfactants or molecules with surfactant-like properties is measured in liquids at pH 8.0 and 20°C. The dynamic surface tension provides, among other things, information on the kinetics of surfactants and is thus a measure of the interfacial activity of, for example, surfactants, but also other molecules (cf. The dynamic surface tension is preferably measured using the bubble pressure method in a concentration range of 0.1 mg / l to 1 g / l of the peptide according to the invention. If the dynamic surface tension remains constant throughout the entire bubble lifetime, the corresponding test substance is not surface-active. Even a deviation of a few mN / m from the ideal surface tension of 72 mN / m for pure water indicates a surfactant effect and would be an indication of surface-active behavior. In the context of the invention, "non-surface-active" is understood to mean a substance in which the dynamic surface tension remains constant throughout the entire bubble lifetime, i.e., the deviation is less than 10 mN / m, preferably less than 8 mN / m, further preferably less than 6 mN / m, particularly preferably less than 5 mN / m, and most preferably less than 2 mN / m.

[0144] In various embodiments, peptides according to the invention can be surface-active or non-surface-active, with the surface activity being determined by the bubble pressure method as described herein, for example as described in Example 6. Preferably, the measurement is carried out at 20°C, in a concentration range of 0.1 mg / l to 1 g / l, at pH 8.0; particularly preferably at 20°C, in a concentration range of 0.1 mg / l to 1 g / l, at pH 8.0 (10 mM Tris-HCl buffer) and with 50 mM KCl).

[0145] In preferred embodiments, peptides according to the invention are not surface-active, wherein the surface activity is determined by the bubble pressure method as described herein, for example as described in Example 6.

[0146] Preferred peptides according to the invention bind to fatty and / or oil-containing surfaces, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. Preferred peptides according to the invention bind to fatty surfaces, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0147] Preferred peptides according to the invention bind to surfaces coated with fat and / or oil, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. Preferred peptides according to the invention bind to surfaces coated with fat, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.Peptides preferred according to the invention bind to at least one fatty and / or oily soil on a surface, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. Peptides preferred according to the invention bind to at least one fatty soil on a surface, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0148] In particularly preferred embodiments, peptides according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soil on textiles. In particularly preferred embodiments, peptides according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soil on textiles, wherein the textile contains or consists of cotton, polyester, or mixtures thereof.

[0149] Good adhesion to textile surfaces, in particular textile surfaces made of synthetic fibers, such as polyester-containing textiles, can be achieved, for example, by a peptide with a pronounced helix structure (in particular a-helix structure) and / or a high arginine content, in particular at one of the termini.

[0150] Preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on polyester textiles have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acids shown in SEQ ID NO: 1, 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 16, 17, 18, 19, 20, 21, 22, 25, 26, 27, 29, 30, 31. Further preferred peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 16, 17, 18, 19, 20, 21, 22, 25, 26, 27, 29, 30, 31.Particularly preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 3, 7, 8, 9, 10, 11, 12, 13, 17, 19, 20, 21, 25, 26, 27, 29, 31. Very particularly preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 8, 10, 21, 25, 26.

[0151] Preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on cotton textiles have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acids shown in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17, 18, 19, 20, 22, 23, 24, 25, 26, 27, 28, 29, 30. Further preferred peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fatty, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17, 18, 19, 20, 22, 23, 24, 25, 26, 27, 28, 29, 30.Particularly preferred peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fat-containing, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 17, 18, 19, 20, 23, 24, 25, 26, 27, 29. Very particularly preferred peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fatty, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 3, 4, 6, 7, 8, 9, 10, 12, 13, 23, 26, 27.

[0152] In particularly preferred embodiments, peptides according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, e.g. fatty and / or oil-containing soiling on dishes, pots, cutlery (metal) or glass.

[0153] Preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO:1-31. Further preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g.cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31. Particularly preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29.Very particularly preferred peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0154] Methods for determining adhesion are known to those skilled in the art, and any suitable methods can be used. Further methods are described in the examples.

[0155] If the peptide used according to the invention is coupled to at least one other (macro)molecule, it can also be referred to as a peptide derivative. The peptide used according to the invention is then derivatized. In such embodiments, the peptide can act as an adhesion tag, which causes the binding of a molecule coupled to it to the desired surface. Such molecules can also be referred to as conjugates.

[0156] In some embodiments, the peptides used according to the invention, which may, for example, have the amino acid cysteine ​​N- or C-terminally for coupling purposes, are coupled with biotin (functionally modified), preferably at a suitable amino acid of the chain and / or N- and / or C-terminally.

[0157] It is also possible for the peptide used according to the invention to be part of a protein or polypeptide. Such proteins and polypeptides can be produced recombinantly, for example, as fusion proteins. In such embodiments, the peptide according to the invention is located either N- or C-terminally to mediate the adhesion of the entire molecule to a surface. In such embodiments, the peptide then also acts as an adhesion tag.

[0158] All of the above features and embodiments can be implemented individually or in any combination.

[0159] Furthermore, the peptide used according to the invention can also be at least one subunit (module) of a larger peptide or polypeptide, wherein the polypeptide can comprise a multimer of the sequences described herein, e.g., 1 to 30 repeats, more preferably 2 to 15 repeats, particularly preferably 2 to 10 repeats, e.g., 2, 3, 4, 5, or 6 repeats of the peptide. The polypeptide can comprise or consist of such multimers. The term "polypeptide" in this context refers in particular to peptides that comprise 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids, unless otherwise described.

[0160] In various embodiments, the peptide used according to the invention is a peptide or polypeptide (multimer) comprising two or more of the peptides as described herein. In various embodiments, the two or more peptides can be linked to one another by at least one spacer; preferably, the at least one spacer comprises or consists of 1 to 10 amino acid residues, in particular 2, 3, or 4 amino acid residues, preferably selected from the group consisting of G, P, I, A, and S or combinations thereof, in particular GPI or GAS. In such embodiments, the individual peptides are optionally linked to one another linearly via peptide bonds, optionally also via a spacer.

[0161] The at least one peptide according to the invention can be present as an aqueous solution. In various embodiments, the peptide content of the solution is preferably 0.00001 to 10 parts by weight of peptide per 100 parts by weight of water, e.g., 0.00001 to 10 wt.%, preferably 0.0001 to 7.5 wt.%, more preferably 0.001 to 5 wt.%, in each case based on the total weight of the solution.

[0162] In addition to the at least one peptide according to the invention, agents according to the invention contain at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase.

[0163] Enzymes that exhibit hydrolytic activity on an ester bond are enzymes capable of hydrolytically breaking down esters into an alcohol and an acid (saponification). They are therefore hydrolases.

[0164] Lipases are enzymes that catalyze the hydrolysis of ester bonds in lipid substrates, particularly in fats and oils. Lipases therefore represent a group of esterases. Lipases are generally versatile enzymes that accept a wide variety of substrates, e.g., aliphatic, alicyclic, bicyclic, and aromatic esters, thioesters, and activated amines. Lipases act, for example, against grease residues in laundry and catalyze their hydrolysis (lipolysis). Lipases with broad substrate spectra are used particularly where inhomogeneous raw materials or substrate mixtures must be converted, such as in detergents and cleaning agents, since soils can consist of differently structured fats and oils. The lipases used in detergents and cleaning agents known from the state of the art are usually of microbial origin and usually originate from bacteria or fungi, e.g.,of the genera Thermomyces, Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma, or Trichosporon. Lipases are usually produced by suitable microorganisms using known biotechnological processes, e.g., by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

[0165] In general, only selected lipases are suitable for use in liquid surfactant preparations. Many lipases do not demonstrate sufficient catalytic performance or stability in such preparations. However, the use of lipases results in an unpleasant odor on the washed items, especially textiles, after the washing process, because the lipase is absorbed by the textiles and continues to hydrolyze fatty acid esters into low-molecular-weight fatty acids. These low-molecular-weight fatty acids are then perceived by their unpleasant odor. The intensity of the odor can vary depending on the nature of the textile.

[0166] Examples of suitable lipases are lipase from Thermomyces, e.g. from T. lanuginosus (formerly Humicola lanuginosa), as described in EP 0258068 and EP 0305216, lipase from strains of Pseudomonas (some of them now renamed Burkholderiae), e.g. P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. sp. strain SD705, P. wisconsinensis, Streptomyces L. pases of the GDSL type, lipase from Thermobifida fusca, lipase from Geobacillus stearothermophilus, lipase from Bacillus subtilis and lipase from Streptomyces griseus and S. pristinaespiralis. The preferred lipases include, for example, the lipases originally obtainable from Humicola lanuginosa (Jhermomyces lanuginosus) or further developed therefrom, in particular those with one or more of the following amino acid exchanges starting from the said lipase in the positions D96L, T213R and / or N233R, particularly preferably T213R and N233R.Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0167] Methods for determining lipase activity are familiar to those skilled in the field of enzyme technology and are routinely used by them (see, for example, Bruno Stellmach, "Bebestimmungsmethoden Enzyme für Pharmazie, Lebensmittelchemie, Technik, Biochemie, Biologie, Medizin", Steinkopff Verlag Darmstadt, 1988, p. 172ff). Lipase-containing samples are added to an olive oil emulsion in emulsifier-containing water and incubated at 30°C and pH 9.0. This releases fatty acids. These are continuously titrated with 0.01 N sodium hydroxide solution using an autotitrator for 20 minutes so that the pH remains constant ("pH-stat titration"). Lipase activity is determined based on the sodium hydroxide consumption by reference to a reference lipase sample. An alternative test for determining the lipolytic activity of the lipases according to the invention is an optical measurement method, preferably a photometric method.The test suitable for this purpose involves the lipase-dependent cleavage of the substrate para-nitrophenol butyrate (pNP-butyrate). This is cleaved by lipase into para-nitrophenolate and butyrate. The presence of para-nitrophenolate can be determined at 405 nm using a photometer, e.g., the Tecan Sunrise device and the XFLUOR software, and thus allows conclusions to be drawn about the enzymatic activity of the lipase.

[0168] In a preferred embodiment, an agent according to the invention comprises at least one lipase selected from

[0169] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0170] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0171] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0172] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0173] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0174] (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, wherein the lipase has an amino acid substitution combination selected from the group consisting of T231R-N233R, P208N-T231 R-N233R, F211 N-T231 R-N233R, T231 R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231 R-N233R-I255A, D96E-T231 R-N233R, N33Q-D96E-T231 R- N233R, N33Q-D111A-T231 R-N233R, N33Q-T231 R-N233R-P256T, N33Q-G38A-G91T-G163K-T231 R- N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-G91T-D96E-D111 A- G163K-T231 R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S,D27R-G38A-G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S, T231 R-N233R-D254S-P256T, G163K-T231 R-N233R-D254S, D27R-N33Q-G38A-G91 T-D96E-G163K- T231 R-N233R-D254S-P256T, D27R-G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D96E- G163K-T231 R-N233R-D254S, D27R-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111A- G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R- G38A-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-D96E-G163K-T231 R-N233R-D254S, D27R-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231 R-N233R- D254S-P256T, D111A-G163K-T231 R-N233R-D254S-P256T, D111A-T231 R-N233R, D111A-T231 R- N233R-D254S-P256T, D27R-D96E-D111 A-G163K-T231 R-N233R, D27R-D96E-D111 A-T231 R-N233R, D27R-N33Q-G38A-D96E-D111A-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-,

[0175] E210Q-T231 R-N233R-D254S-P256T, D27R-T231 R-N233R-D254S-P256T, D96E-D111 A-G163K-T231 R-N233R, D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D96E-D111 A-G163K-T231 R-N233R-P256T, D96E-D111 A-T231 R-N233R, D96E-D111 A-T231 R-N233R-D254S, D96E-D111 A-T231 R-N233R-D254S- P256T, D96E-D111 A-T231 R-N233R-P256T, D96E-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R- N233R-D254S-P256T, D96E-T231 R-N233R-P256T, G38A-D96E-D111A-T231 R-N233R, G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, G91T-D96E-D111A-T231 R-N233R, G91T-D96E-T231 R- N233R, G91T-T231 R-N233R-D254S-P256T, N33Q-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, T231 R-N233R-D254S-P256T and T231 R-N233R-P256T;and / or (c) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical; and / or;

[0176] (d) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or

[0177] (e) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:34 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or

[0178] (f) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:35 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or

[0179] (g) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:36 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or

[0180] (h) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:37 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or

[0181] (i) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:38 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%.

[0182] In a further preferred embodiment, an agent according to the invention comprises at least one lipase which is selected from (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0183] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0184] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0185] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0186] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0187] (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, wherein the lipase has an amino acid substitution combination selected from the group consisting of T231R-N233R, P208N-T231 R-N233R, F211 N-T231 R-N233R, T231 R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231 R-N233R-I255A, D96E-T231 R-N233R, N33Q-D96E-T231 R- N233R, N33Q-D111A-T231 R-N233R, N33Q-T231 R-N233R-P256T, N33Q-G38A-G91T-G163K-T231 R- N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-G91T-D96E-D111 A- G163K-T231 R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S,D27R-G38A-G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S, T231 R-N233R-D254S-P256T, G163K-T231 R-N233R-D254S, D27R-N33Q-G38A-G91 T-D96E-G163K- T231 R-N233R-D254S-P256T, D27R-G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D96E- G163K-T231 R-N233R-D254S, D27R-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111A- G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R- G38A-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-D96E-G163K-T231 R-N233R-D254S, D27R-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231 R-N233R- D254S-P256T, D111A-G163K-T231 R-N233R-D254S-P256T, D111A-T231 R-N233R, D111A-T231 R- N233R-D254S-P256T, D27R-D96E-D111 A-G163K-T231 R-N233R, D27R-D96E-D111 A-T231 R-N233R, D27R-N33Q-G38A-D96E-D111A-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K- E210Q-T231 R-N233R-D254S-P256T, D27R-T231 R-N233R-D254S-P256T, D96E-D111 A-G163K-T231 R- N233R, D96E-D111 A-G163K-T231 R-N233R-D254S-P256T,D96E-D111 A-G163K-T231 R-N233R-P256T, D96E-D111 A-T231 R-N233R, D96E-D111 A-T231 R-N233R-D254S, D96E-D111 A-T231 R-N233R-D254S- P256T, D96E-D111 A-T231 R-N233R-P256T, D96E-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-P256T, G38A-D96E-D111A-T231 R-N233R, G91T-D96E- D111 A-G163K-T231 R-N233R-D254S-P256T, G91T-D96E-D111A-T231 R-N233R, G91T-D96E-T231 R- N233R, G91T-T231 R-N233R-D254S-P256T, N33Q-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, T231 R-N233R-D254S-P256T and T231 R-N233R-P256T; and / or,

[0188] (c) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:34 over its entire length, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%; and / or(d) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical to the amino acid sequence given in SEQ ID NO:34 over its entire length.

[0189] In a particularly preferred embodiment, an agent according to the invention comprises at least one lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical to the amino acid sequence given in SEQ ID NO:33 over its entire length.

[0190] In a very particularly preferred embodiment, an agent according to the invention comprises at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length.

[0191] In a particularly preferred embodiment, an agent according to the invention comprises at least one lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0192] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, wherein the lipase has an amino acid substitution combination selected from the group consisting of T231 R-N233R, P208N- T231 R-N233R, F211 N-T231 R-N233R, T231 R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q- E210Q-T231 R-N233R-I255A, D96E-T231 R-N233R, N33Q-D96E-T231 R-N233R, N33Q-D111A-T231 R- N233R, N33Q-T231 R-N233R-P256T, N33Q-G38A-G91T-G163K-T231 R-N233R-D254S, N33Q-G38A- G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T,D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111 A- G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S, T231 R-N233R-D254S-P256T, G163K-T231 R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R-G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D96E-G163K-T231 R-N233R-D254S, D27R-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K- T231 R-N233R-D254S-P256T, D27R-D96E-G163K-T231 R-N233R-D254S, D27R-D96E-D111 A-G163K- T231 R-N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231 R-N233R-D254S-P256T, D111A-G163K- T231 R-N233R-D254S-P256T, D111 A-T231 R-N233R, D111A-T231 R-N233R-D254S-P256T, D27R-D96E- D111 A-G163K-T231 R-N233R, D27R-D96E-D111 A-T231 R-N233R, D27R-N33Q-G38A-D96E-D111 A- T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D111 A-G163K-E210Q-T231 R-N233R-D254S-P256T,D27R-T231 R-N233R-D254S-P256T, D96E-D111 A-G163K-T231 R-N233R, D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D96E-D111A-G163K-T231 R-N233R-P256T, D96E-D111 A-T231 R-N233R, D96E-D111 A-T231 R-N233R-D254S, D96E-D111 A-T231 R-N233R-D254S-P256T, D96E-D111 A-T231 R-N233R-P256T, D96E-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-P256T, G38A-D96E-D111 A-T231 R-N233R, G91T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, G91T-D96E-D111A-T231 R-N233R, G91T-D96E-T231 R-N233R, G91T-T231 R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, T231 R-N233R-D254S-P256T and T231 R-N233R-P256T existing group is selected.,

[0193] In a very particularly preferred embodiment, an agent according to the invention comprises at least one lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0194] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, wherein the lipase has an amino acid substitution combination selected from the group consisting of T231 R-N233R, P208N-T231 R-N233R, F211 N-T231 R-N233R, T231 R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231 R-N233R-I255A, D96E-T231 R-N233R, N33Q-D96E-T231 R-N233R, N33Q-D111A-T231 R-N233R, N33Q- T231 R-N233R-P256T, N33Q-G38A-G91 T-G163K-T231 R-N233R-D254S, N33Q-G38A-G91 T-D96E-D111 A-G163K-T231 R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231 R-N233R- D254S-P256T,D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-P256T, D27R-N33Q- G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111 A-G163K- T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S, T231 R-N233R-D254S-P256T, G163K- T231 R-N233R-D254S, D27R-N33Q-G38A-G91 T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R- G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, D96E-G163K-T231 R-N233R-D254S, D27R- G163K-T231 R-N233R-D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231 R-N233R-D254S, D27R- G38A-G91T-D96E-G163K-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-T231 R- N233R-D254S-P256T, D27R-D96E-G163K-T231 R-N233R-D254S, D27R-D96E-D111A-G163K-T231 R- N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231 R-N233R-D254S-P256T, D111 A-G163K-T231 R- N233R-D254S-P256T, D111 A-T231 R-N233R, D111 A-T231 R-N233R-D254S-P256T, D27R-D96E-D111 A- G163K-T231 R-N233R, D27R-D96E-D111 A-T231 R-N233R, D27R-N33Q-G38A-D96E-D111 A-T231 R- N233R-D254S-P256T, D27R-G38A-D96E-D111 A-G163K-E210Q-T231 R-N233R-D254S-P256T,D27R-T231 R-N233R-D254S-P256T, D96E-D111A-G163K-T231 R-N233R, D96E-D111A-G163K-T231 R-N233R- D254S-P256T, D96E-D111A-G163K-T231 R-N233R-P256T, D96E-D111A-T231 R-N233R, D96E-D111A-T231 R-N233R-D254S, D96E-D111 A-T231 R-N233R-D254S-P256T, D96E-D111 A-T231 R-N233R-P256T, D96E-G163K-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-D254S-P256T, D96E-T231 R-N233R-P256T, G38A-D96E-D111A-T231 R-N233R, G91T-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, G91T-D96E-D111 A-T231 R-N233R, G91T-D96E-T231 R-N233R, G91T-T231 R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231 R-N233R-D254S-P256T, T231 R-N233R-D254S-P256T and T231 R- N233R-P256T existing group is selected.,

[0195] In preferred embodiments, agents according to the invention contain at least one salt. In preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and the total weight of the agent.

[0196] In preferred embodiments, the at least one salt is selected from

[0197] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0198] In preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and the total weight of the agent, wherein the at least one salt is selected from

[0199] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0200] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0201] In preferred embodiments, the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof.

[0202] In preferred embodiments, agents according to the invention contain at least one salt selected from alkali metal salts with inorganic counterions, particularly preferably alkali metal halides, in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and the total weight of the agent.

[0203] In further preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and the total weight of the agent, wherein the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof.

[0204] In particularly preferred embodiments, the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate and mixtures thereof.

[0205] In particularly preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on active substance and total weight of the agent, wherein the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate and mixtures thereof.

[0206] In further particularly preferred embodiments, the at least one salt is selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0207] In further particularly preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on active substance and total weight of the agent, wherein the at least one salt is selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0208] In particularly preferred embodiments, the at least one salt is selected from sodium chloride, potassium chloride and mixtures thereof.

[0209] In very particularly preferred embodiments, agents according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on active substance and total weight of the agent, wherein the at least one salt is selected from sodium chloride, potassium chloride and mixtures thereof.

[0210] For the purposes of the invention, cleaning performance refers to the ability of a cleaning agent to partially or completely remove existing soiling, in particular the brightening performance of one or more types of soiling on textiles and / or hard surfaces. For the purposes of the invention, both a cleaning agent and the washing and / or cleaning liquor formed by this agent exhibit a respective cleaning performance.

[0211] Washing or cleaning liquor refers to the working solution containing the washing or cleaning agent that acts on the textiles or fabrics or surfaces, especially tableware or household surfaces, and thus comes into contact with the soiling present on the textiles or fabrics or surfaces. The washing or cleaning liquor is usually created when the washing or cleaning process begins and the agent is diluted with water, for example, in a washing machine or dishwasher or in another suitable container.

[0212] The compositions of the washing or cleaning agents according to the invention, as well as the amounts of the ingredients, depend on the respective intended use and the trained specialist is generally familiar with suitable dosages of these components and can obtain these from the relevant specialist literature.

[0213] The washing and / or cleaning agents according to the invention include all conceivable types of washing or cleaning agents, both concentrated and undiluted, for use on a commercial scale, in washing machines or for hand washing or cleaning. These include, for example, washing agents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. These also include, for example, dishwashing detergents for dishwashers (machine dishwashing detergents) or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood, or leather, for which the term "washing agent" is used. Thus, in addition to manual and machine dishwashing detergents, scouring agents, glass cleaners, toilet air fresheners, etc.The washing and cleaning agents within the scope of the invention also include washing aids which are added to the actual washing agent during manual or machine washing of textiles in order to achieve an additional effect. Furthermore, washing and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e. agents with which the item of laundry is brought into contact before the actual washing, e.g. to dissolve stubborn soiling, and also agents which, in a step following the actual textile washing, impart further desirable properties to the laundry such as a pleasant feel, freedom from creasing or low static charge. The latter agents include, among others, fabric softeners. This also includes agents for use in (semi-)automated washing or cleaning systems such as robot mops or wet vacuum cleaners.

[0214] The detergents and / or cleaning agents according to the invention, which may be in powdered or granular solid form, in compacted or recompacted particle form, as homogeneous solutions or suspensions, can contain all known ingredients commonly used in such agents. The agents according to the invention can contain, in particular, surfactants, builders, complexing agents, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators or bleach catalysts, water-miscible organic solvents, enzyme stabilizers, sequestering agents, electrolytes, pH regulators, and / or other auxiliaries such as optical brighteners, graying inhibitors, dye transfer inhibitors, foam regulators, as well as dyes and fragrances.Advantageous ingredients of the compositions according to the invention are disclosed in the international patent application WO 2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly incorporated by reference, and the disclosure content therein is incorporated into the present patent application.

[0215] Agents according to the invention increasingly preferably contain the peptides according to the invention in an amount of 1 x 10 -8 up to 10 wt.%, from 0.00001 to 5 wt.%, from 0.00005 to 2.5 wt.%, from 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.% based on active protein and total weight of the agent.

[0216] In a further embodiment, the agents according to the invention contain an amount of the peptide or peptides according to the invention sufficient for one wash or rinse cycle. Preferably, the peptide or peptides according to the invention are contained in the agents according to the invention or used according to the invention in an amount, based on active protein, of 0.5 to 1500 mg / job, 5 to 500 mg / job and in particular 10 to 200 mg / job (corresponding to the amount contained in one portion sufficient for one rinse or wash cycle). Unless the agents according to the invention are single-use portions, the usual dosage amount of the agent per wash / rinse cycle is to be used as the basis for the calculation.

[0217] Agents according to the invention increasingly preferably contain the lipase according to the invention in an amount of 1 x 10 -8up to 10 wt.%, from 0.00001 to 5 wt.%, from 0.00005 to 2.5 wt.%, from 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.% based on active protein and total weight of the agent.

[0218] The protein concentration can be determined using known methods, e.g., the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall et al., J. Biol. Chem., 1948, 177, 751-766). The active protein concentration can be determined by titrating the active sites using a suitable irreversible inhibitor and determining the residual activity (Bender et al., J. Am. Chem. Soc., 1966, 88, 24, 5890-5913). Those skilled in the art of peptide and protein technology are also familiar with a variety of suitable methods for determining peptide or protein concentration that can be applied within the scope of this invention.

[0219] Further embodiments of the invention include all solid, powdered, liquid, gel-like, or pasty dosage forms of agents according to the invention, which may optionally also consist of multiple phases and may be in compressed or uncompressed form. The agent may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the agent also include extrudates, granules, tablets, or pouches. Alternatively, the agent may also be liquid, gel-like, or pasty, e.g., in the form of a non-aqueous liquid detergent or a non-aqueous paste, or in the form of an aqueous liquid detergent or a water-containing paste. Liquid agents are generally preferred. Furthermore, the agent may be in the form of a one-component system. Such agents consist of one phase. Alternatively, an agent may also consist of multiple phases.Such a remedy is therefore divided into several components.

[0220] When agents according to the invention are in liquid form, they preferably contain more than 20% by weight, preferably 30 to 90% by weight and more preferably 40 to 80% by weight of water, based on their total weight.

[0221] Agents according to the invention can contain one or more surfactants, with particular consideration being given to anionic surfactants, nonionic surfactants, and mixtures thereof, but cationic, zwitterionic, and / or amphoteric surfactants can also be present. The agents preferably contain 0.5 to 70% by weight of surfactant. In textile detergents, preferably 35 to 60% by weight and more preferably 40 to 55% by weight of surfactant is used, based on the total weight of the agent; in preferred embodiments, the agents preferably contain 3 to 35% by weight, preferably 5 to 30% by weight, of surfactant, based on the total weight of the agent.

[0222] Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups, preferably with alkali ions as cations. Suitable soaps are preferably the alkali salts of saturated or unsaturated C12-C18 fatty acids. Such fatty acids can also be used in a non-fully neutralized form. Suitable sulfate-type surfactants include the salts of the sulfuric acid monoesters of C12-C18 fatty alcohols and the sulfation products of the aforementioned nonionic surfactants with a low degree of ethoxylation. The usable surfactants of the sulfonate type include, for example, Cg-u-alkylbenzenesulfonates, alkanesulfonates obtained from Ci2-is-alkanes, for example by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization, Ci2-18-olefinsulfonates, which are formed by the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkanesulfonates, disulfonates, as can be found, for example, infrom C12-18 monoolefins with terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation products, as well as a-sulfofatty acid esters (ester sulfonates) which are formed during the sulfonation of fatty acid methyl or ethyl esters, e.g. a-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

[0223] The agent, in particular textile detergent, preferably contains 2 to 55 wt.%, preferably 3 to 35 wt.%, of anionic surfactant, based on the total weight of the agent. Most preferably, the agent contains 3 to 25 wt.% alkylbenzenesulfonate. Furthermore, the agent may preferably contain further anionic surfactants, in particular alkyl ether sulfates, and nonionic surfactants, in particular fatty alcohol alkoxylates. These may then constitute the remainder of the surfactants. Suitable alkylbenzenesulfonates are preferably selected from linear or branched

[0224] Alkyl benzene sulfonates of the formula in which R' and R" are independently H or alkyl and together contain 6 to 19, preferably 7 to 15 and in particular 9 to 13 C atoms. A particularly preferred representative is sodium dodecylbenzylsulfonate.

[0225] Preferred alk(en)yl sulfates are the alkali metal salts, especially the sodium salts, of the sulfuric acid half-esters of C12-C18 fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or C12-C20 oxo alcohols, and those half-esters of secondary alcohols of these chain lengths. Also preferred are alk(en)yl sulfates of the stated chain length that contain a synthetic, petrochemically produced straight-chain alkyl radical, which exhibit degradation behavior similar to that of equivalent compounds based on oleochemical raw materials. For washing purposes, C12-C18 alkyl sulfates and C12-C15 alkyl sulfates, as well as C11-C15 alkyl sulfates, are preferred.

[0226] Also suitable are the sulfuric acid monoesters of straight-chain or branched C-21 alcohols ethoxylated with 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C9-11 alcohols with an average of 3.5 mol of ethylene oxide (EO) or C12-18 fatty alcohols with 1 to 4 EO.

[0227] Suitable alkyl ether sulfates are, for example, compounds of the formula R 1 -O-(AO) n -SO3 _ X + . In this formula, R 1 represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, more preferably a fatty alcohol radical. Preferred radicals R 1 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, with the representatives having an even number of carbon atoms being preferred. Particularly preferred radicals R 1are derived from C12-18 fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C12-20 oxo alcohols. AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20, and in particular from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7, or 8. X + stands for a monovalent cation or the n-th part of an n-valent cation, preferably the alkali metal ions and among them Na + or K + , where Na + is highly preferred. Other cations X + can be selected from NH4 + , 14 Zn 2+ , 14 mg 2+ , 14 Ca 2+ , 14 minutes 2+ and their mixtures.

[0228] In various embodiments, the alkyl ether sulfate may be selected from

[0229] Fatty alcohol ether sulfates of the formula with k = 11 to 19, n = 2, 3, 4, 5, 6, 7, or 8. Particularly preferred representatives are Na-Ci2-Ci4 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical mean, which can be a whole or fractional number for a specific product. The stated degrees of alkoxylation represent statistical mean, which can be a whole or fractional number for a specific product. Preferred alkoxylates / ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE).

[0230] It has proven beneficial for cold-wash performance if the detergents also contain soap(s). Preferred detergents are therefore characterized by the presence of soap(s). Suitable soaps include saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, as well as, in particular, soap mixtures derived from natural fatty acids, e.g., coconut, palm kernel, or tallow fatty acids.

[0231] A class of preferably used nonionic surfactants, which are used either as the sole nonionic surfactant or in combination with other nonionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably with 1 to 4 C atoms in the alkyl chain, in particular fatty acid methyl esters.

[0232] Another class of nonionic surfactants that can be used advantageously are alkyl polyglycosides (APG). Suitable alkyl polyglycosides satisfy the general formula RO(G) Z in which R is a linear or branched, in particular 2-methyl-branched, saturated or unsaturated, aliphatic radical having 8 to 22, preferably 12 to 18, carbon atoms and G is the symbol which stands for a glycose unit having 5 or 6 carbon atoms, preferably glucose. The degree of glycosidation z is between 1 and 4, preferably between 1 and 2 and in particular between 1.1 and 1.4. Preference is given to using linear alkylpolyglycosides, i.e. alkylpolyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical.

[0233] Nonionic surfactants of the amine oxide type, e.g., N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half that amount.

[0234] Suitable amphoteric surfactants are, for example, betaines of the formula (R''')(R' V )(R V )N + CH2COO _ , in which R'" is an alkyl radical having 8 to 25, preferably 10 to 21 C atoms, optionally interrupted by heteroatoms or heteroatom groups, and R' v and R v identical or different alkyl radicals having 1 to 3 C atoms, in particular Cw-11-alkyldimethylcarboxymethylbetaine and Cn-17-alkylamidopropyldimethylcarboxymethylbetaine. Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R v ')(R vi ')(R v ''')(R'x )N + X _ , in the R vi to R' x represents four identical or different, in particular two long- and two short-chain, alkyl radicals, and X- represents an anion, in particular a halide ion, e.g., didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary surface-active compounds, in particular those containing a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. By using quaternary surface-active compounds with antimicrobial activity, the agent can be given an antimicrobial effect or its existing antimicrobial effect, possibly due to other ingredients, can be improved.

[0235] Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols, each containing 8 to about 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10, alkyl ether groups. Furthermore, corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters, and fatty acid amides, which correspond to the aforementioned long-chain alcohol derivatives with regard to the alkyl moiety, as well as of alkylphenols with 5 to 12 carbon atoms in the alkyl radical, are also suitable.

[0236] As nonionic surfactants, especially in textile detergents, preferably alkoxylated, advantageously ethoxylated, especially primary alcohols with preferably 8 to 18 C atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol are used, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or can contain linear and methyl-branched radicals in the mixture, as are usually present in oxo alcohol radicals. In particular, however, alcohol ethoxylates with linear radicals from alcohols of native origin with 12 to 18 C atoms, e.g. from coconut, palm, tallow or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol are preferred. The preferred ethoxylated alcohols include, for example:C12-C14 alcohols with 3 EO or 4 EO, C8-C14 alcohols with 7 EO, C11-C14 alcohols with 3 EO, 5 EO, 7 EO, or 8 EO, C12-C14 alcohols with 3 EO, 5 EO, or 7 EO, and mixtures thereof, such as mixtures of C12-C14 alcohols with 3 EO and C12-C14 alcohols with 5 EO. The stated degrees of ethoxylation represent statistical averages, which can be a whole or fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohols with 14 EO, 25 EO, 30 EO, or 40 EO.

[0237] For dishwashing detergents, the use of nonionic surfactants is particularly suitable, as explained below. The detergents therefore contain, in particular, one or more nonionic surfactants as surfactants. The proportion of the total weight of the detergent is preferably 0.5 to 30 wt.%, preferably 1.0 to 20 wt.%, more preferably 1.5 to 15 wt.%.

[0238] Examples of nonionic surfactants that can be used either as the sole nonionic surfactant or in combination with other nonionic surfactants are alkoxylated, preferably ethoxylated, or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 C atoms in the alkyl chain. Nonionic surfactants of the amine oxide type, e.g., N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half thereof. These are also used, in particular, in hand dishwashing detergents. Other suitable surfactants are the polyhydroxy fatty acid amides known as PHFA.However, low-foaming non-ionic surfactants are preferably used in dishwashing detergents, in particular alkoxylated, especially ethoxylated, low-foaming non-ionic surfactants. The cleaning agents particularly preferably contain non-ionic surfactants from the group of alkoxylated alcohols. Particular preference is given to non-ionic surfactants that have a melting point above room temperature. Non-ionic surfactants with a melting point above 20°C, preferably above 25°C, more preferably between 25°C and 60°C, and in particular between 26.6°C and 43.3°C, are particularly preferred. Surfactants that are preferably used come from the group of alkoxylated non-ionic surfactants, in particular ethoxylated primary alcohols and mixtures of these surfactants with structurally more complex surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants).Such (PO / EO / PO) nonionic surfactants are also characterized by good foam control. Particularly preferred nonionic surfactants are those containing alternating ethylene oxide and alkylene oxide units. Among these, surfactants with EO-AO-EO-AO blocks are preferred, with one to ten EO or AO groups bonded to each other before a block of the respective other groups follows. These are nonionic surfactants of the general formula: preferred, in the R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical; each group R 2 or R 3 is independently selected from -CHs, -CH2CH3, -CH2CH2-CH3, -CH(CH3)2 and the indices w, x, y, z independently represent integers from 1 to 6.

[0239] Thus, nonionic surfactants which have a Cg-is-alkyl radical with 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units, followed by 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units are particularly preferred.

[0240] Preferred nonionic surfactants are those of the general formula R 1 -CH(OH)CH2O- (AO)w-(A'O)x-(A”O)y-(A'”O) z -R 2 , in the R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical, R 2represents H or a linear or branched hydrocarbon radical having 2 to 26 C atoms, A, A', A" and A'" independently of one another represent a radical from the group -CH2CH2, -CH2CH2-CH2, -CH2-CH(CH3), -CH2-CH2-CH2-CH2, -CH2-CH(CH3)-CH2-, -CH2-CH(CH2-CH3), w, x, y and z represent values ​​between 0.5 and 120, where x, y and / or z can also be 0. Particular preference is given to those end-capped, poly(oxyalkylated) nonionic surfactants which, according to the formula R 1 O[CH2CH2O] X CH2CH(OH)R 2 , besides a remainder R 1 , which represents linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 2 to 30 C atoms, preferably having 4 to 22 C atoms, furthermore a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radical R 2with 1 to 30 C atoms, where x stands for values ​​between 1 and 90, preferably for values ​​between 30 and 80 and in particular for values ​​between 30 and 60.

[0241] Particularly preferred surfactants are those of the formula R 1 O[CH2CH(CH3)O] x [CH2CH2O] y CH2CH(OH)R 2 , in the R 1 represents a linear or branched aliphatic hydrocarbon radical having 4 to 18 C atoms or mixtures thereof, R 2 denotes a linear or branched hydrocarbon radical having 2 to 26 C atoms or mixtures thereof, and x stands for values ​​between 0.5 and 1.5 and y stands for a value of at least 15. The group of these non-ionic surfactants includes, for example, the C2-26 fatty alcohol (PO)i-(EO) 15-40-2-hydroxyalkyl ethers, in particular also the Cs fatty alcohol (PO)i-(EO)22-2-hydroxydecyl ethers.

[0242] Particularly preferred are also those end-capped poly(oxyalkylated) nonionic surfactants of the formula R 1 O[CH2CH2O] x [CH2CH(R 3 )O] y CH2CH(OH)R 2 , in the R 1 and R 2 independently of one another represents a linear or branched, saturated or mono- or polyunsaturated hydrocarbon radical having 2 to 26 C atoms, R 3 is independently selected from -CH3, -CH2CH3, -CH2CH2-CH3, -CH(CH3)2, but preferably represents -CH3, and x and y independently represent values ​​between 1 and 32, wherein nonionic surfactants with R 3 = -CH3 and values ​​for x from 15 to 32 and y from 0.5 to 1.5 are particularly preferred.

[0243] Other preferred nonionic surfactants are the end-capped poly(oxyalkylated) nonionic surfactants of the formula R 1 O[CH2CH(R 3 )O] x [CH2]kCH(OH)[CH2]jOR 2 , in the R 1 and R2 represent linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 1 to 30 C atoms, R 3 represents H or a methyl, ethyl, n-propyl, isopropyl, n-butyl, 2-butyl or 2-methyl-2-butyl radical, x represents values ​​between 1 and 30, k and j represent values ​​between 1 and 12, preferably between 1 and 5. If the value x > 2, each R 3 in the formula R above 1 O[CH2CH(R 3 )O] x [CH2]kCH(OH)[CH2]jOR 2 be different. R 1 and R 2 are preferably linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 6 to 22 C atoms, with radicals having 8 to 18 C atoms being particularly preferred. For the radical R 3H, -CH3 or -CH2CH3 are particularly preferred. Particularly preferred values ​​for x are in the range from 1 to 20, in particular from 6 to 15. As described above, each R 3 in the formula above can be different if x > 2. This allows the alkylene oxide unit in the square brackets to be varied. For example, if x is 3, the radical R 3 selected to produce ethylene oxide (R 3 = H) or propylene oxide (R 3= CH3) units which can be joined together in any order, e.g. (EO)(PO)(EO), (EO)(EO)(PO), (EO)(EO)(EO), (PO)(EO)(PO), (PO)(PO)(EO) and (PO)(PO)(PO). The value 3 for x has been chosen as an example and can certainly be larger, whereby the range of variation increases with increasing x values ​​and includes, for example, a large number of (EO) groups combined with a small number of (PO) groups, or vice versa. Particularly preferred end-capped poly(oxyalkylated) alcohols of the above formula have values ​​of k = 1 and j = 1, so that the above formula R 1 O[CH2CH(R 3 )O]XCH2CH(OH)CH2OR 2 simplified. In the latter formula, R 1 , R 2 and R 3 as defined above and x represents numbers from 1 to 30, preferably from 1 to 20 and in particular from 6 to 18. Particularly preferred surfactants are those in which the radicals R 1 and R 2have 9 to 14 C atoms, R 3 stands for H and x takes values ​​from 6 to 15.

[0244] Finally, the non-ionic surfactants of the general formula R 1 -CH(OH)CH2O-(AO)wR 2 proven in the R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical, R 2 stands for a linear or branched hydrocarbon radical having 2 to 26 C atoms, A stands for a radical from the group CH2CH2, CH2CH2CH2, CH2CH(CH3), preferably CH2CH2, and w stands for values ​​between 1 and 120, preferably 10 to 80, in particular 20 to 40. The group of these non-ionic surfactants includes, for example, the C4-22 fatty alcohol (EO)io-8o-2-hydroxyalkyl ethers, in particular also the Cs-12 fatty alcohol (EO)22-2-hydroxydecyl ethers and the C4-22 fatty alcohol (EO)40-80-2-hydroxyalkyl ethers.

[0245] In various embodiments of the invention, the corresponding non-end-capped hydroxy mixed ethers can also be used instead of the above-defined end-capped hydroxy mixed ethers. These can satisfy the above formulas, where R 2 but hydrogen is and R 1 , R 3 , A, A', A", A'", w, x, y and z are as defined above. In various embodiments, the agents, in particular the automatic dishwashing agents, contain at least one nonionic surfactant from the group of hydroxy mixed ethers.

[0246] Compositions according to the invention preferably further contain builders, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. Builders include, in particular, silicates, carbonates, and organic (co)builders.

[0247] Organic (co)builders include, in particular, polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders, and phosphonates. These classes of substances are described below. Organic cobuilder substances can be contained in agents according to the invention in amounts of up to 60% by weight, based on the total weight of the agent.

[0248] Useful organic builders include, for example, polycarboxylic acids which can be used in the form of the free acid and / or their sodium salts. Polycarboxylic acids are understood to be carboxylic acids which have more than one acid function. Examples include citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethyl inulins; monomeric and polymeric aminopolycarboxylic acids, in particular glycinediacetic acid, methylglycinediacetic acid, glutaminediacetic acid; iminodisuccinates such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid; polymeric hydroxy compounds such as dextrin; and polymeric (poly)carboxylic acids, in particular those obtained by oxidation of polysaccharides orDextrin-accessible polycarboxylates, and / or polymeric acrylic acids, methacrylic acids, maleic acids, and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. In textile washing agents, the organic (co)builders are optionally present in particular in amounts of up to 25% by weight and preferably from 1 to 8% by weight, based on the total weight of the agent. Automatic dishwashing agents preferably contain the organic cobuilders in an amount of 10 to 55% by weight, particularly preferably 15 to 50% by weight, based on the total weight of the agent.

[0249] In addition to their builder effect, the free acids typically also have the property of an acidifying component and thus also serve to adjust a lower and milder pH value of products. Citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof are particularly suitable. Citric acid or citric acid salts are particularly preferably used as the builder substance. Other particularly preferred builders are selected from methylglycinediside acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS), ethylenediamine disuccinate (EDDS), carboxymethylinulin, and polyaspartate.

[0250] In preferred embodiments, citric acid and / or citrate is used as the water-soluble, organic builder. Particular preference is given to using, based on the total weight of the agent, 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% citric acid and / or 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% citrate, preferably alkali citrate, more preferably sodium citrate. Citric acid / citrate can each be used in the form of their hydrates; for example, citric acid can be used in the form of the monohydrate, and citrate in the form of the trisodium citrate dihydrate.

[0251] Another preferred component of agents according to the invention are complexing agents. Particularly preferred complexing agents are phosphonates, provided their use is permitted by regulations. In addition to 1-hydroxyethane-1,1-diphosphonic acid, the complexing phosphonates include a number of different compounds, such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP). Hydroxyalkane and aminoalkanephosphonates are particularly preferred in this application. Among the hydroxyalkanephosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as the sodium salt, with the disodium salt being neutral and the tetrasodium salt being alkaline (pH 9). Preferred aminoalkanephosphonates are ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues. They are preferably used in the form of neutral sodium salts, e.g.as the hexasodium salt of EDTMP or as the hepta- and octasodium salt of DTPMP. HEDP is the preferred builder from the phosphonate class. Aminoalkanephosphonates also possess a pronounced heavy metal binding capacity. Accordingly, it may be preferable, especially if the products also contain bleach, to use aminoalkanephosphonates, especially DTPMP, or mixtures of the aforementioned phosphonates.A preferred agent within the scope of this application contains one or more phosphonate(s) from the group aminotrimethylenephosphonic acid (ATMP) and / or salts thereof; ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or salts thereof; diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and / or salts thereof; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or salts thereof; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or salts thereof; hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and / or salts thereof; nitrilotri(methylenephosphonic acid) (NTMP) and / or salts thereof. Particularly preferred agents are those containing 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates. Of course, agents according to the invention can contain two or more different phosphonates.

[0252] Preferred agents according to the invention are characterized in that the agent contains at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, wherein the weight fraction of the phosphonate in the total weight of the agent is preferably 0.1 to 10.0 wt.%, preferably 0.2 to 8.0 wt.%. In textile detergents, preferably 0.25 to 5.0 wt.%, more preferably 0.3 to 3.0 wt.%, and particularly preferably 0.5 to 2.0 wt.% of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, are used. In automatic dishwashing detergents according to the invention, at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, is preferably used, the weight proportion of the phosphonate in the total weight of the detergent preferably being 0.5 to 8.0 wt.%, preferably 1.0 to 7.0 wt.%, and particularly preferably 1.5 to 6.5 wt.%.

[0253] In further preferred embodiments, agents according to the invention are substantially free of phosphonate-containing compounds. "Substantially free of phosphonate-containing compounds" in this context means that the corresponding agents or compositions contain, based on the total weight of the agent, less than 2 wt.%, preferably less than 1 wt.%, more preferably less than 0.5 wt.%, and particularly preferably less than 0.1 wt.%, of phosphonate-containing compounds. In particularly preferred embodiments, these agents / compositions are free of phosphonate-containing compounds.

[0254] In more preferred embodiments, the complexing agents (builder substances) are selected from aminopolycarboxylic acids, in particular MGDA and GLDA. As used herein, the term "MGDA" includes, among others, methylglycinediacetic acid, α-alaninediacetic acid, N-(l-carboxyethyl)iminodiacetic acid, and N,N-bis(carboxymethyl)-DL-alanine, including the free acid forms and the corresponding salts, preferably alkali metal salts, in particular trisodium salts. As used herein, the term "GLDA" includes, among others, glutamic acid diacetic acid, L-glutamic acid N,N-diacetic acid, and N,N-bis(carboxylatomethyl)-L-glutamate, including the free acid forms and the corresponding salts, preferably alkali metal salts, in particular tetrasodium salts.

[0255] In textile detergents, although higher MGDA or GLDA concentrations are possible, in particular up to 25% by weight, based on the total weight of the detergent, it is particularly preferred to use 0.2 to 5% by weight, preferably 0.25 to 3% by weight, even more preferably 0.5 to 2% by weight of MGDA, preferably MGDA trisodium salt (MGDA-Nas). Even more preferred is the use of 0.2 to 5% by weight, preferably 0.25 to 3% by weight, even more preferably 0.5 to 2% by weight of GLDA, preferably GLDA tetrasodium salt (GLDA-Na4), based on the total weight of the detergent.

[0256] In automatic dishwashing detergents, the amount of MGDA or GLDA, based on the total weight of the detergent, is preferably 2.0 to 40 wt.%, particularly preferably 5.0 to 30 wt.%, in particular 8.0 to 25 wt.%, and most preferably 10.0 to 20 wt.%. The MGDA trisodium salt is preferably used in these amounts.

[0257] A solid composition according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include the above-mentioned organic builders.

[0258] In addition to the aforementioned water-soluble organic builders, the compositions of the invention may also contain inorganic water-soluble builders. Suitable water-soluble inorganic builder materials include, in particular, alkali silicates, alkali carbonates, alkali hydrogen carbonates, alkali phosphates, and / or sesquicarbonates, which may be in the form of their alkaline, neutral, or acidic sodium or potassium salts. Small amounts of calcium carbonates may also be present in solid textile detergents.

[0259] Suitable examples are water-soluble crystalline and / or amorphous alkali silicates. The alkali silicates usable as builders in the agents according to the invention preferably have a molar ratio of alkali oxide to SiO2 of less than 0.95, in particular from 1:1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are sodium silicates, in particular amorphous sodium silicates, with a molar ratio Na2O:SiO2 of 1:2 to 1:2.8. Crystalline silicates, which can be present alone or in a mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na2Si xO2x+ixy H2O, in which x, the so-called modulus, is a number from 1.9 to 22, in particular 1.9 to 4, and y is a number from 0 to 33, and preferred values ​​for x are 2, 3, or 4. Preferred crystalline layered silicates are those in which x in the general formula assumes the values ​​2 or 3. In particular, both ß- and δ-sodium disilicates (Na2Si2O5 xy H2O) is preferred. Also, practically anhydrous crystalline alkali silicates produced from amorphous alkali silicates of the above-mentioned general formula, in which x is a number from 1.9 to 2.1, can be used in agents according to the invention. In a further embodiment of agents according to the invention, a crystalline sodium layered silicate with a modulus of 2 to 3 is used, such as can be produced from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further embodiment of agents according to the invention. In agents containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and in particular 1:1 to 2:1. Crystalline layered silicates of the above-mentioned formula are marketed by Clariant GmbH under the trade name Na-SKS, e.g.Na-SKS-1 (Na2Si22O45 xx H2O, Kenyaite), Na-SKS-2 (Na2Sii4O29. xx H2O, magadiite), Na-SKS-3 (Na2SiOi7 xx H2O) or Na-SKS-4 (Na2Si40g xx H2O, makatite). Of these, Na-SKS-5 (α-Na2SiOs), Na-SKS-7 (β-Na2SiOs, natrosilite), Na-SKS-9 (NaHSiO5x 3 H2O), Na-SKS-10 (NaHSiO5x 3 H2O, kanemite), Na-SKS-11 (β-Na2SiOs) and Na-SKS-13 (NaHSiOs), but especially Na-SKS-6 (δ-Na2SiOs) are particularly suitable. In one embodiment of the inventive compositions, a granular compound of crystalline layered silicate and citrate, of crystalline layered silicate and the above-mentioned (co-)polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate is used, as is commercially available, for example, under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably present in the compositions according to the invention in amounts of 1 to 20 wt. %, in particular 5 to 15 wt. %, based on the total weight of the composition.Furthermore, carbonates (and hydrogen carbonates), especially sodium carbonate, are important as water-soluble inorganic builder substances.

[0260] Alkali carbonate(s), especially sodium carbonate (soda), are preferred as builders in automatic dishwashing detergents. Typical amounts range from 5 to 50 wt.%, preferably 10 to 40 wt.%, especially 15 to 30 wt.%, based in each case on the total weight of the detergent.

[0261] Agents according to the invention are preferably free of phosphate builders, i.e. they contain, based on the total weight of the agent, less than 1% by weight, preferably no deliberately added phosphate builder.

[0262] Agents according to the invention can also contain water-insoluble builder substances. As water-insoluble inorganic builder materials, in particular crystalline or amorphous water-dispersible alkali aluminosilicates are used, in amounts of up to 50 wt. %, preferably not more than 40 wt. %, in particular 3 to 20 wt. % and particularly preferably 1 to 15 wt. %, based on the total weight of the agent. Among these, the crystalline sodium aluminosilicates of detergent quality, in particular zeolite A, zeolite P, zeolite MAP and optionally zeolite X, alone or in mixtures, e.g. in the form of a co-crystallizate of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA), are preferred. Amounts close to the stated upper limit are preferably used in solid, particulate agents. Suitable aluminosilicates in particular do not have particles with a grain size exceeding 30 μm and preferably consist of at least 80 wt.-% of particles with a size of less than 10 pm. Their calcium binding capacity, which can be determined according to DE 2412837 A1, is generally in the range of 100 to 200 mg CaO per gram. In preferred embodiments, agents according to the invention comprise a builder system comprising at least one builder, preferably in an amount of 0.5 to 50 wt.%, more preferably 0.5 to 20 wt.%, particularly preferably 0.5 to 10 wt.-%, based on the total weight of the agent, wherein the builder consists of polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethyl inulins or their salts, monomeric and polymeric aminopolycarboxylic acids such as glycinediacetic acid, methylglycinediacetic acid (MGDA), glutamic acid diacetic acid (GLDA), nitriletriacetic acid, iminodisuccinate such as ethylenediamine-N,N'-disuccinic acid (EDDS) and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid or their salts, polyphosphonic acids such as aminotris(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid), lysinetetra(methylenephosphonic acid), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and 1-hydroxyethane-1 ,1-diphosphonic acid (HEDP) or its salts, polymeric hydroxy compounds such as dextrin, and mixtures thereof.

[0263] In preferred embodiments, agents according to the invention, preferably textile detergents, each based on the total weight of the agent,

[0264] (j) at least 0.0000001 wt.% of at least one peptide according to the invention ii) 0 to 10 wt.%, preferably 1 to 4 wt.% of citric acid and / or citrate, preferably alkali citrate, iii) 0 to 40 wt.%, preferably 0 to 15 wt.%, more preferably 1 to 3 wt.%, alkali carbonate, preferably sodium carbonate, iv) 0 to 20 wt.%, preferably 3 to 10 wt.%, alkali silicate, v) 0 to 10 wt.%, preferably 0.5 to 2 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, vi) 0 to 10 wt.%, preferably 0.5 to 3 wt.%, aminopolycarboxylic acids, preferably MGDA and / or GLDA,

[0265] 0 to 10 wt.%, preferably 0.5 to 2 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP,

[0266] (v) 0 to 10 wt.%, preferably 0.5 to 3 wt.%, of aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0267] In other preferred embodiments, agents according to the invention, preferably automatic dishwashing agents, comprise, in each case based on the total weight of the agent,

[0268] (i) at least 0.0000001 wt.% of at least one peptide according to the invention ii) 0 to 20 wt.%, preferably 1.0 to 15.0 wt.% citric acid and / or citrate, preferably alkali citrate,

[0269] (iii) 0 to 40 wt.%, preferably 5 to 30 wt.%, more preferably 10 to 25 wt.%, alkali carbonate, preferably sodium carbonate,

[0270] (iv) 0 to 20 wt.%, preferably 3 to 10 wt.% alkali silicate, (v) 0 to 10 wt.%, preferably 0.5 to 8 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP,

[0271] (vi) 0 to 25% by weight, preferably 5.0 to 20.0% by weight, of aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0272] Peroxygen compounds suitable for use in the compositions according to the invention include, in particular, organic peracids or peracidic salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid, or salts of diperdodecanedioic acid, hydrogen peroxide, and inorganic salts that release hydrogen peroxide under washing conditions, including perborate, percarbonate, persilicate, and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds, such as H2O2-urea adducts. Hydrogen peroxide can also be produced with the aid of an enzymatic system, i.e., an oxidase and its substrate. If solid peroxygen compounds are to be used, they can be used in the form of powders or granules, which can also be coated in a manner known in principle.The peroxygen compounds can be added to the wash liquor as such or in the form of agents containing them, which in principle can contain all conventional washing, cleaning, or disinfectant ingredients. Particular preference is given to using alkali metal percarbonate or alkali metal perborate monohydrate. If an agent according to the invention contains peroxygen compounds, they are present in amounts of preferably up to 50 wt.%, in particular 5 to 30 wt.%, more preferably 0.1 to 20 wt.%, in each case based on the total weight of the agent.

[0273] Compounds that, under perhydrolysis conditions, yield aliphatic peroxocarboxylic acids with preferably 1 to 10 carbon atoms, especially 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid can be used as bleach activators in the detergents. Suitable substances are those containing O- and / or N-acyl groups with the stated number of carbon atoms and / or optionally substituted benzoyl groups. Preferred are multiply acylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N-acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates or carboxylates or the sulfonic or carboxylic acids thereof, in particular nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS orLOBS), 4-(2-decanoyloxyethoxycarbonyloxy)-benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic acid anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters as well as acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactose, acetylated, optionally N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimidic acids are formed, in particular aminoacetonitrile derivatives with quaternized nitrogen atom, and / or Oxygen-transferring sulfonimines and / or acylhydrazones. Hydrophilically substituted acyl acetals and acyl lactams are also preferred. Combinations of conventional bleach activators can also be used.Such bleach activators can be present, particularly in the presence of the above-mentioned hydrogen peroxide-providing bleaching agents, in the usual amount range, preferably in amounts of 0.5 to 10 wt.%, in particular 1 to 8 wt.%, based on the total weight of the agent, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent.

[0274] In addition to the conventional bleach activators or instead of them, solid detergents, in particular textile detergents, may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0275] Graying inhibitors or soil-release agents (soil release polymers) particularly suitable for textile detergents are cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses and cellulose mixed ethers such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methylcarboxymethylcellulose. Preference is given to using sodium carboxymethylcellulose, hydroxypropylmethylcellulose and mixtures thereof and optionally mixtures thereof with methylcellulose. The commonly used soil-release agents include copolyesters containing dicarboxylic acid units, alkylene glycol units and polyalkylene glycol units. The proportion of graying inhibitors and / or soil-release agents in agents according to the invention generally does not exceed 2% by weight and is preferably 0.5 to 1.5% by weight, particularly preferably 0.5 to 2% by weight, based on the total weight of the agent.

[0276] Derivatives of diaminostilbenedisulfonic acid or its alkali metal salts can be used as optical brighteners in textile detergents, particularly for textiles made from cellulose fibers (e.g., cotton). Suitable brighteners include, for example, salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-ylamino)stilbene-2,2'-disulfonic acid or similarly structured compounds that carry a diethanolamino group, a methylamino group, or a 2-methoxyethylamino group instead of the morpholino group. Furthermore, brighteners of the substituted 4,4'-distyryldiphenyl type, e.g., 4,4'-bis(4-chloro-3-sulfostyryl)diphenyl, can be present. Mixtures of brighteners can also be used. Brighteners of the 1,3-diaryl-2-pyrazoline type, e.g., 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazoline, and similarly structured compounds, are particularly suitable for polyamide fibers. The optical brightener or brightener mixture content of the agent generally does not exceed 1 wt.-%, preferably 0.05 to 0.5 wt.%, based on the total weight of the agent. In a preferred embodiment of the invention, the agent is free of such active ingredients.

[0277] The usual foam regulators that can be used in the agents according to the invention include, for example, polysiloxane-silica mixtures, the finely divided silica contained therein preferably being silanized or otherwise hydrophobicized. The polysiloxanes can consist of linear compounds as well as cross-linked polysiloxane resins and mixtures thereof. Other defoamers are paraffin hydrocarbons, in particular microparaffins and paraffin waxes, whose melting point is above 40°C, saturated fatty acids or soaps with, in particular, 20 to 22 C atoms, e.g. sodium behenate, and alkali metal salts of phosphoric acid mono- and / or dialkyl esters in which the alkyl chains each have 12 to 22 C atoms. Among these, sodium monoalkyl phosphate and / or dialkyl phosphate with Cis-18 alkyl groups is preferably used. The proportion of foam regulators can preferably be 0.2 to 2% by weight, particularly preferably not more than 1% by weight.-%, based on the total weight of the product.

[0278] To adjust the desired pH, agents according to the invention can contain system- and environmentally compatible acids, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid, and / or adipic acid, but also mineral acids, in particular sulfuric acid or alkali metal hydrogen sulfates, or bases, in particular ammonium or alkali metal hydroxides, preferably sodium hydroxide. Such pH regulators are preferably present in the agents according to the invention in amounts of no more than 10% by weight, in particular from 0.5 to 6% by weight, particularly preferably from 0.3 to 2% by weight, based on the total weight of the agent.

[0279] Agents according to the invention preferably have a pH in a range from about 6 to about 11.5, preferably from about 7 to about 11, more preferably from about 7.5 to about 10.5, particularly preferably from about 8 to about 10, in a 1 wt.% solution in deionized water at 20°C. The pH is preferably measured using a standard hydrogen electrode.

[0280] As a further component, agents according to the invention may contain an organic solvent. The addition of organic solvents has a beneficial effect on the enzyme stability and cleaning performance of these agents. Preferred organic solvents come from the group of mono- or polyhydric alcohols, alkanolamines, or glycol ethers.The solvents are preferably selected from ethanol, n- or i-propanol, butanol, glycol, propanediol, butanediol, glycerin, diglycol, propyl diglycol, butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, dipropylene glycol ethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and mixtures of these solvents. The weight proportion of these organic solvents in the total weight of the compositions according to the invention is preferably 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.% and more preferably 0.5 to 5.0 wt.%.A particularly preferred organic solvent that is particularly effective with regard to stabilizing the compositions is glycerin and 1,2-propylene glycol. Liquid compositions preferably comprise at least one polyol, preferably from the group consisting of glycerin and 1,2-propylene glycol, based on the total weight of the composition, preferably in an amount of 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight, and more preferably 0.5 to 5.0% by weight. Further preferred organic solvents are organic amines and alkanolamines. Compositions according to the invention preferably contain these amines in amounts of 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight, and more preferably 0.5 to 5.0% by weight, based on the total weight of the composition. A particularly preferred alkanolamine is ethanolamine. Furthermore, the compositions according to the invention (in particular for automatic dishwashing) can contain bleach catalysts.The bleach catalysts that can be used include, but are not limited to, the group of bleach-enhancing transition metal salts and transition metal complexes, preferably the Mn, Fe, Co, Ru or Mo complexes, particularly preferably from the group of manganese and / or cobalt salts and / or complexes, in particular the cobalt(amine) complexes, the cobalt(acetate) complexes, the cobalt(carbonyl) complexes, the chlorides of cobalt or manganese, the manganese sulfate and the complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Mns-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (M-TACN).

[0281] Preference is given to automatic dishwashing detergents which contain 0.001 to 1% by weight, preferably 0.01 to 0.1% by weight, of bleach catalyst, preferably a Mn complex, in particular a complex of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Mns-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (M-TACN).

[0282] Agents according to the invention can contain further hydrolytic enzymes or other enzymes in a concentration appropriate for the effectiveness of the agent. A further embodiment of the invention thus represents agents which further comprise one or more enzymes. Preferred enzymes are all enzymes which can exhibit catalytic activity in the agent according to the invention, in particular selected from proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, ß-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, and mixtures thereof. Enzymes are advantageously present in the agent in an amount of 1 x 10 -8 to 5 wt.%, based on active protein and total weight of the agent. Increasingly preferably, each enzyme is present in an amount of 1 x 10 -7to 3 wt.%, from 0.00001 to 1 wt.%, from 0.00005 to 0.5 wt.%, from 0.0001 to 0.1 wt.%, and particularly preferably from 0.0001 to 0.05 wt.%, based on the active protein and the total weight of the agent. Enzymes particularly preferably exhibit synergistic cleaning performance against certain soils or stains, i.e., the enzymes contained in the agent composition support each other in their cleaning performance.

[0283] In preferred embodiments, an agent according to the invention contains at least one enzyme and increasingly preferably at least two, three, four or five enzymes, which are preferably selected from the group consisting of proteases, amylases, proteases, cellulases, mannanases, pectate lyases and mixtures thereof, in total in an amount of 0.01 to 10 wt.%, preferably 0.1 to 8 wt.%, particularly preferably 0.2 to 6 wt.%, based on active protein and the total weight of the agent.

[0284] Examples of proteases are subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, protease PB92, subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY, and the enzymes thermitase, proteinase K, and proteases TW3 and TW7, which are classified as subtilases but no longer as subtilisins in the narrower sense. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes. Subtilisins 147 and 309 are marketed by Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants are derived from the protease from Bacillus lentus DSM 5483, described in e.g. WO 95 / 23221, WO 92 / 21760, WO 2013 / 060621 and EP 3660151. Other useful proteases are e.g.the enzymes available under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101 L® and Ovozyme® from Novozymes, the enzymes available under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® from Danisco / DuPont, the enzyme available under the trade name Lavergy pro 104 LS® from BASF, the enzyme available under the trade name Protosol® from Advanced Biochemicals Ltd., the enzyme available under the trade name Wuxi® from Wuxi Snyder Bioproducts Ltd., the enzyme available under the trade names Proleather® and Protease P® from Amano Pharmaceuticals Ltd., and the enzyme available under the name Proteinase K-16 from Kao Corp. The proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in WO 2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697, are also particularly preferably used.

[0285] Examples of amylases are the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus stearothermophilus, and in particular their further developments improved for use in detergents and cleaning agents. The enzyme from Bacillus licheniformis is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. Further developments of this α-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). The α-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derived variants of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also from Novozymes. Furthermore, the a-amylase from Bacillus sp. is used for this purpose.A 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are particularly suitable. Fusion products of all of these molecules can also be used. Furthermore, the further developments of α-amylase from Aspergillus niger and A. oryzae, available under the trade name Fungamyl® from Novozymes, are also suitable. Other commercial products that can be used advantageously include Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, as well as Amplify™ 12L or Amplify Prime™ 100L or Amplify Prime™ 120L, the latter also from Novozymes, and the PREFERENZ S® series from Danisco / DuPont, including PREFERENZ S100®, PREFERENZ S1000®, or PREFERENZ S210®. Variants of these enzymes obtained through point mutations can also be used. Suitable cellulases include those of bacterial or fungal origin.Chemically modified or protein-engineered mutants are included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum. Particularly suitable cellulases are the alkaline or neutral cellulases with color-care properties. Examples of cellulases with endo-1,4-glucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, e.g., those with a sequence of at least 97% identity to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091. Another example may include a GH44 xyloglucanase, e.g., a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903. Other examples of cellulases include the GH45 cellulases described in WO 96 / 29397.Commercially available cellulases include Celluzyme™, Carezyme™, Carezyme Premium™, Celluclean™ (e.g. Celluclean™ 5000L and Cellulclean™ 4000T), Celluclean Classic™, Cellusoft™, Endolase®, Renozyme® and Whitezyme™ (Novozymes A / S), Clazinase™ and Puradax HA™ (Genencor International Inc.), KAC- 500(B)™ (Kao Corporation), Revitalenz™ 1000, Revitalenz™ 2000 and Revitalenz™ 3000 (DuPont), as well as Ecostone® and Biotouch® (AB Enzymes).

[0286] Suitable mannanases are, for example, Bacillus subtilis Endo-b-mannanase, Bacillus sp. I633 Endo-b-mannanase, Bacillus sp. AAI12 Endo-b-mannanase, Bacillus sp. AA349 Endo-b-mannanase, Bacillus agaradhaerens NCIMB 40482 Endo-b-mannanase, Bacillus halodurans Endo-b-mannanase, Bacillus clausii Endo-b-mannanase, Bacillus licheniformis Endo-b-mannanase, Humicola insolens Endo-b-mannanase and Caldocellulosiruptor sp. Endo-b-mannanase (e.g. US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0287] Pectate lyases suitable for detergents and cleaning agents are described, for example, in WO 2003 / 095638 or WO 2015 / 121133. Examples of suitable pectinolytic enzymes include the enzymes and enzyme preparations available under the trade names Gamanase®, Pektinex AR®, X-Pect®, or Pectaway® from Novozymes, under the trade names Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, Rohapect B1 L® from AB Enzymes, and under the trade name Pyrolase® from Diversa Corp.

[0288] The peptides, proteins, and enzymes described herein are preferably mature peptides, proteins, or enzymes, i.e., the catalytically active molecule without signal and / or propeptide(s). Unless otherwise stated, the sequences given also refer to mature (processed) peptides, proteins, or enzymes.

[0289] In various embodiments of the invention, the respective peptide, protein, or enzyme is a free peptide, protein, or enzyme. This means that the peptide, protein, or enzyme can interact directly with all components of the agent and, if the agent is a liquid agent, that the peptide, protein, or enzyme is in direct contact with the agent's solvent (e.g., water). In other embodiments, an agent may contain peptides, proteins, or enzymes that form an interaction complex with other molecules or that contain a "shell." In this case, a single or multiple peptide, protein, or enzyme molecule(s) may be separated from the other components of the agent by a surrounding structure. Such a separating structure may be formed by, but is not limited to, vesicles, such as a micelle or a liposome.However, the surrounding structure can also be a virus particle, a bacterial cell, or a eukaryotic cell. In various embodiments, an agent can contain cells of Bacillus pumilus or Bacillus subtilus that express peptides, proteins, or enzymes, or cell culture supernatants of such cells.

[0290] In the context of the present invention, the feature that a peptide, protein or enzyme has the stated substitution(s) (or deletion or insertion) means that it contains one (of the stated) substitution(s) (or deletion or insertion) at the respective position, i.e. at least the stated positions are not otherwise mutated or deleted, e.g. by fragmentation of the peptide, protein or enzyme. In various embodiments, the peptides, proteins and / or enzymes described herein have the sequence of the respective reference sequence, with the exception of the explicitly mentioned substitutions, i.e. apart from the substituted positions, they are 100% identical to the respective reference sequence.

[0291] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the BLAST algorithm, which is established and commonly used in the state of the art (Altschul et al., Basic local alignment search tool, J. Mol. Biol., 1990, 215, 403-410, and Altschul et al., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 1997, 25, 3389-3402) and is essentially achieved by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences to one another. A tabular assignment of the relevant positions is referred to as an alignment. Another algorithm available in the state of the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. Frequently used algorithms include the Clustal series (Chenna et al., Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 2003, 31 , 3497-3500), T-Coffee (Notredame et al., T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 2000, 302, 205-217) or programs based on these programs or algorithms. Furthermore, sequence comparisons (alignments) are possible with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the given standard parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (use of the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise stated, the sequence identity reported herein is determined using the BLAST algorithm. Such a comparison also allows a statement to be made about the similarity of the compared sequences to each other.It is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the peptide, protein, or enzyme. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes or just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences. Such regions often have identical functions.They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the peptide, protein, or enzyme. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, identity or homology statements in this application refer to the entire length of the respective nucleic acid or amino acid sequence.

[0292] In the context of the present invention, the statement that an amino acid position corresponds to a numerically designated position in SEQ ID NO:1 therefore means that the corresponding position is assigned to the numerically designated position in SEQ ID NO:1 in an alignment as defined above.

[0293] The following convention is used to describe substitutions that affect exactly one amino acid position (amino acid exchanges): first, the naturally occurring amino acid is designated using the internationally accepted single-letter code, followed by the corresponding sequence position, and finally, the inserted amino acid. Multiple or alternative exchanges within the same polypeptide chain are separated by slashes. "130D / V" thus means that position 130 is mutated to D or V. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, e.g., an asterisk or a dash, or an A is indicated in front of the corresponding position.For example, P9T describes the substitution of proline at position 9 by threonine, P9TH the insertion of histidine after the amino acid threonine at position 9, and P9* or AP9 the deletion of proline at position 9. This nomenclature is known to those skilled in the art of enzyme technology.

[0294] Using methods commonly known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, a person skilled in the art can produce the corresponding nucleic acids, including complete genes, based on known DNA and / or amino acid sequences. Such methods are known, for example, from Sambrook, J., Fritsch, EF, and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition, Cold Spring Laboratory Press.

[0295] Furthermore, the peptides, proteins, enzymes, and / or other ingredients contained in the agent can be coated with a substance that is impermeable to the peptide, protein, or enzyme at room temperature or in the absence of water, and which becomes permeable to the peptide, protein, or enzyme under the conditions of use of the agent. Such an embodiment of the invention is thus characterized in that the peptide, protein, or enzyme is coated with a substance that is impermeable to the peptide, protein, or enzyme at room temperature or in the absence of water. Furthermore, the washing or cleaning agent itself can also be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.

[0296] In the compositions described herein, the peptides, proteins, or enzymes to be used can also be formulated together with accompanying substances, for example, from fermentation. In liquid formulations, the peptides, proteins, or enzymes are preferably used as peptide, protein, or enzyme liquid formulation(s).

[0297] The peptides, proteins, or enzymes are generally not provided in the form of pure proteins, but rather in the form of stabilized, storable, and transportable preparations. These prefabricated preparations include, for example, solid preparations obtained by granulation, extrusion, or lyophilization or, particularly in the case of liquid or gel-like products, solutions of the peptides, proteins, or enzymes, preferably as concentrated as possible, with little water content, and / or containing stabilizers or other additives.

[0298] Alternatively, the peptides, proteins, or enzymes can be encapsulated for both solid and liquid dosage forms, e.g., by spray-drying or extrusion of the peptide, protein, or enzyme solution together with a preferably natural polymer, or in the form of capsules, e.g., those in which the peptides, proteins, or enzymes are enclosed as if in a solidified gel, or in core-shell capsules in which an enzyme-containing core is coated with a protective layer impermeable to water, air, and / or chemicals. Additional active ingredients, e.g., stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be applied in superimposed layers. Such capsules are applied using methods known per se, e.g., by shaking or rolling granulation or in fluid-bed processes. Such granules, e.g., by applying polymeric film formers, are advantageously low in dust and, due to the coating, are stable in storage.

[0299] Furthermore, it is possible to package two or more peptides, proteins or enzymes together so that a single granule has multiple enzyme activities.

[0300] The peptides, proteins, or enzymes can also be incorporated into water-soluble films, such as those used, for example, in the packaging of unit-dose detergents and cleaning agents. Such a film allows the release of the peptides, proteins, or enzymes upon contact with water. As used herein, "water-soluble" refers to a film structure that is preferably completely water-soluble. Preferably, such a film consists of (fully or partially hydrolyzed) polyvinyl alcohol (PVA).

[0301] Agents according to the invention can comprise one or more reversible enzyme inhibitors / stabilizers. Agents according to the invention can contain the reversible enzyme inhibitors / stabilizers in a concentration of 0.1 to 2 wt.%, preferably 0.3 to 1.5 wt.%, based on the total weight of the agent. If multiple inhibitors / stabilizers are present, these figures refer to the total concentration. These can be selected in particular from the group consisting of polyols, such as glycerol or 1,2-ethylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters or derivatives, in particular phenylboronic acid derivatives or 4-formylphenylboronic acid (4-FPBA), antioxidants, special peptide compounds, and combinations thereof.

[0302] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent comprising at least one of the fat-binding peptides described herein and at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase.

[0303] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent comprising at least one of the fat-binding peptides described herein, at least one lipase and optionally at least one salt, wherein the lipase is selected from

[0304] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0305] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0306] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0307] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical; and wherein, when present, the salt is selected from

[0308] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0309] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0310] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent which consists of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt are contained in a first phase and the at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is contained in a second phase.

[0311] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent which consists of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt is contained in a first phase and the at least one lipase is contained in a second phase, wherein the lipase is selected from

[0312] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0313] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0314] (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and / or

[0315] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

[0316] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent which consists of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt is contained in a first phase and the at least one lipase is contained in a second phase, wherein the lipase is selected from

[0317] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0318] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0319] (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and / or

[0320] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence set out in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length; and wherein, when present, the salt is selected from

[0321] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0322] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0323] In preferred embodiments, the agent according to the invention is a textile detergent, preferably a multiphase textile detergent. The textile detergent according to the invention is particularly suitable for use on textiles made of plastic and / or with a plastic content (mixed fabric) and / or made of a natural fiber such as cotton.The textile preferably comprises or consists of polyester (PES), polyethylene (PE), polypropylene (PP), polyurethane (PU), polystyrene (PS), polyvinyl chloride (PVC), polycarbonate (PC), polyamide (PA), polyphenylene ether, polyphenylene sulfide, polyoxymethylene (POM), polymethyl methacrylate (PMA), polyethylene terephthalate (PET), polybutylene terephthalate (PBT), polytetrafluoroethylene (PTFE), polyhydroxyalkanoate (PHA), polyhydroxybutyrate (PHB), polyimide (PI), polylactide (PI_A), polyvinylidene fluoride (PVDF), polyether ketone (PEK), and / or copolymers or a blended fabric thereof, even more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or blended fabrics thereof, preferably a cotton / polyester blend with a polyester content of at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, most preferably at least 50%, especially at least 60%, e.g.65% or 70%, or pure polyester or copolymers thereof. The term "mixture" or "blended fabric" refers to textiles with a plastic content, preferably to textiles made of at least one natural fiber and at least one plastic fiber (plastic content). In particular, the mixture or blended fabric consists of cotton and at least one plastic, in particular polyester. In preferred embodiments, a textile with a plastic content or a plastic mixture or blended fabric has a plastic content of at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, very particularly preferably at least 50%, in particular at least 60%, e.g. 65% or 70%.

[0324] In preferred embodiments, the agent is a cleaning agent for hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0325] It is preferred that the peptide according to the invention, particularly when used in washing and / or cleaning agents according to the invention, achieves a dirt-removing, in particular grease- and / or oil-removing, effect, in particular by binding / adhering to at least one grease- and / or oil-containing, preferably fatty, soil on textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. Thus, the washing and / or cleaning agent is preferably used as a detergent in a washing process, in particular in machine washing or hand washing.When used in detergents and / or cleaning agents, the peptides described herein not only improve the cleaning performance of greasy and / or oily soils, but also exhibit a dirt-removing, particularly grease- and / or oil-removing, effect. They thus represent a biodegradable alternative to soil release polymers. These peptides are therefore particularly suitable for use in detergents and cleaning agents and can contribute to improved cleaning performance. Furthermore, they can help reduce or completely eliminate synthetic and chemical substances, e.g., in detergents and / or cleaning agents, by providing a biodegradable alternative. They could also contribute to the stabilization of other ingredients.

[0326] In particularly preferred embodiments, the peptides described herein in washing and / or cleaning agents according to the invention achieve improved cleaning performance on at least one fatty and / or oily soil on textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. The improved cleaning performance is preferably based on a synergistic interaction of the peptide according to the invention and esterase. The improved cleaning performance is particularly preferably based on a synergistic interaction of the peptide according to the invention and lipase.

[0327] It is preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, and the peptide according to the invention, which binds to at least one fatty and / or oil-containing, preferably fatty, soil on a textile, in particular containing or consisting of cotton, polyester and mixtures thereof. It is particularly preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the lipase and the peptide according to the invention, which binds to at least one fatty and / or oil-containing, preferably fatty, soil on a textile, in particular containing or consisting of cotton, polyester and mixtures thereof.

[0328] It is preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, and the peptide according to the invention which binds to at least one fat- and / or oil-containing, preferably fat-containing, soil on a hard surface, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass.It is particularly preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the lipase and the peptide according to the invention, which binds to at least one fat- and / or oil-containing, preferably fat-containing, soil on a hard surface, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0329] It is preferred that the peptide according to the invention has a soil-removing, in particular grease- and / or oil-removing, effect, in particular with regard to at least one grease- and / or oil-containing soil on a textile surface, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surface, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. In particular, the surfaces are freed of this soiling by the presence of the peptide, which binds to at least one grease-containing soil on the textile and / or the hard surface.

[0330] In this context, it is particularly preferred that the peptide according to the invention is surface-active and achieves a soil-removing, in particular fat- and / or oil-removing, effect by binding / adhering to at least one fat- and / or oil-containing, preferably fat-containing, soil on textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, wherein the surface activity is determined according to the bubble pressure method, in particular as described herein, for example as described in Example 6.

[0331] One possible mechanism for the fat-removing effect could be that the peptides described herein are able to adsorb onto solid fats and thereby soften the fatty film. This surfactant-like behavior makes the fatty film easier to remove during the cleaning process. The softened fat can be detached (roll-up mechanism) and / or rinsed away. This mechanism could be explained by the surface-active behavior of peptides according to the invention, with the surface activity being determined as described in Example 6. An example of such a peptide is a peptide with SEQ ID NO: 29.

[0332] Another possible mechanism is that the peptides described herein, especially the non-surface-active peptides of the invention, form a stable layer on the fatty layer. This functionalization of the fatty surface or the binding to the fatty soil on a surface allows other fat-removing and / or fat-dissolving substances or molecules, particularly lipases, to gain easier access to the fatty layer.

[0333] Peptides according to the invention therefore also allow the removal of greasy soils at lower temperatures, e.g., approximately 15°C, approximately 20°C, or approximately 30°C. They thus enable the formulation of high-performance washing and / or cleaning agents which demonstrate good cleaning performance on at least one greasy soil even at low temperatures, e.g., approximately 15°C, approximately 20°C, or approximately 30°C. In preferred embodiments, this effect is also based on the interaction with the lipase. Due to the improved fat removal, in addition to the hydrolysis of the fat molecules by the lipase, the degradation products are also removed more effectively, and the accumulation or persistence of the degradation products on the surface can thus be reduced or even prevented. This reduces the formation of odors, in particular the risk of bad odors caused by the lipase degradation products.All facts, objects, and embodiments described above are also applicable to this subject matter of the invention. Therefore, explicit reference is made here to the disclosure at the corresponding point, with the note that this disclosure also applies to the above-mentioned inventive means.

[0334] A further subject matter of the invention is a method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, which is characterized in that an agent according to the invention is used in at least one method step.

[0335] In preferred embodiments, in a first step, the at least one peptide according to the invention is brought into contact with the laundry or rinse ware, and in a second step, the at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is brought into contact with the laundry or rinse ware. In preferred embodiments, in a first step, the at least one peptide according to the invention is brought into contact with the laundry or rinse ware in the presence of at least one salt, and in a second step, the at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is brought into contact with the laundry or rinse ware.

[0336] In preferred embodiments, in a first step the at least one peptide is brought into contact with the laundry or rinse ware and in a second step the at least one lipase is brought into contact with the laundry or rinse ware, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence (C)m(X; 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0337] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0338] X 2 is selected from R, H and K, preferably R and K,

[0339] X 3is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0340] X 4 is selected from A, L and V, preferably A and L,

[0341] X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-31; and wherein the lipase is selected from

[0342] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0343] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0344] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0345] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

[0346] In preferred embodiments, in a first step the at least one peptide is brought into contact with the laundry or rinse ware in the presence of at least one salt and in a second step the at least one lipase is brought into contact with the laundry or rinse ware, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0347] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0348] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0349] X 2 is selected from R, H and K, preferably R and K,

[0350] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0351] X 4 is selected from A, L and V, preferably A and L,

[0352] X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-31; wherein the lipase is selected from

[0353] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0354] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0355] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0356] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical; and wherein the salt is selected from

[0357] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0358] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular

[0359] In various embodiments, the process described above is characterized in that it is carried out at a temperature of about 5°C to about 100°C, preferably about 10°C to about 60°C, more preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably at about 20°C to about 30°C, most preferably about 20°C.

[0360] In various embodiments, the method described above is characterized in that the at least one salt is present in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, wherein the salt is selected from

[0361] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0362] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0363] This includes both manual and mechanical processes, with mechanical processes being preferred due to their more precise controllability, e.g., with regard to the quantities used and contact times. Processes for cleaning textiles are generally characterized by the fact that various cleaning-active substances are applied to the items to be cleaned in several process steps and are washed off after the contact time, or by the items to be cleaned being treated in some other way with a detergent or a solution or dilution of this detergent. The process preferably relates to a mechanical washing process, in particular in a washing machine, or a hand-washing process. The peptide described herein preferably acts as a soil-repellent and / or soil-removing agent.

[0364] This subject matter of the invention also encompasses a machine dishwashing process. In such a process, the agent according to the invention can be dosed into the cleaning solution, for example, by means of the dosing chamber in the door or by means of an additional dosing container in the interior of the dishwasher. Alternatively, the agent can also be applied directly to the soiled dishes or to one of the interior walls of the dishwasher, for example the inside of the door. The process according to the invention is carried out in the interior of a commercially available dishwasher. In a dishwasher, the cleaning program can generally be selected and set by the consumer before the dishwashing process is carried out. The cleaning program of the dishwasher used in the process according to the invention comprises at least one cleaning cycle.According to the invention, cleaning programs that include additional cleaning or rinsing cycles, e.g., a pre-rinse and / or a final rinse cycle, are preferred. The method according to the invention is particularly preferably a component of a cleaning program comprising an optional pre-rinse cycle, a cleaning cycle, and a final rinse cycle. The method according to the invention is preferably used in conjunction with cleaning programs in which the liquor is heated during the cleaning cycle.

[0365] Alternative embodiments of this subject matter of the invention also include processes for treating textile raw materials or for textile care, in which an agent or peptide according to the invention becomes active in at least one process step. Among these, processes for textile raw materials, fibers, or textiles with natural components are preferred, and especially for those containing wool or silk.

[0366] A further subject matter of the invention is the use of an agent according to the invention for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

[0367] A further subject of the invention is the use of a peptide described herein in a washing and / or cleaning agent according to the invention, preferably a washing and / or cleaning agent containing lipase, for improving the cleaning performance of the agent on at least one greasy and / or oily soil, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0368] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0369] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0370] X 2 is selected from R, H and K, preferably R and K,

[0371] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0372] X 4 is selected from A, L and V, preferably A and L, X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-31; and wherein the lipase is selected from

[0373] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0374] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0375] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0376] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, is identical, preferably in a temperature range of about 10°C to about 80°C, more preferably about 15°C to about 60°C, more preferably about 15°C to 45°C, even more preferably about 15°C to 40°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

[0377] A further subject matter of the invention is the use of a peptide according to the invention as a soil-removing, in particular fat- and / or oil-removing, active ingredient in a washing and / or cleaning agent, preferably in a lipase-containing washing and / or cleaning agent, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0378] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0379] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0380] X 2 is selected from R, H and K, preferably R and K,

[0381] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0382] X 4 is selected from A, L and V, preferably A and L,

[0383] X 5is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31;and wherein the lipase is selected from (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,;

[0384] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0385] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0386] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, is identical, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0387] In various embodiments, the uses described above are characterized in that at least one salt is present in the agent in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, wherein the salt is selected from

[0388] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or

[0389] (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0390] All facts, subject matters, and embodiments described for peptides and agents according to the invention are also applicable to these subject matters of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above-mentioned methods and uses according to the invention.

[0391] PREFERRED EMBODIMENTS

[0392] 1 . Washing and / or cleaning agents comprising

[0393] (A) at least one peptide, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;and / or b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0394] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0395] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0396] X 2 is selected from R, H and K, preferably R and K,

[0397] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0398] X 4 is selected from A, L and V, preferably A and L,

[0399] X 5is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence having at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31; (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0400] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0401] 2. Washing and / or cleaning agents comprising

[0402] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or

[0403] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0404] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0405] 3. Washing and / or cleaning agents comprising

[0406] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0407] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0408] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I, X 2 is selected from R, H and K, preferably R and K,

[0409] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0410] X 4 is selected from A, L and V, preferably A and L,

[0411] X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4;

[0412] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0413] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0414] 4. Washing and / or cleaning agents comprising

[0415] (A) at least one peptide, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;and / or b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence;

[0416] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0417] X 2 is selected from R, H and K, preferably R and K,

[0418] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0419] X 4 is selected from A, L and V, preferably A and L,

[0420] X 5is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31;

[0421] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0422] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0423] 5. Washing and / or cleaning agents comprising

[0424] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or

[0425] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0426] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0427] 6. Washing and / or cleaning agents comprising

[0428] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0429] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0430] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0431] X 2 is selected from R, H and K, preferably R and K,

[0432] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0433] X 4is selected from A, L and V, preferably A and L,

[0434] X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4;

[0435] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0436] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0437] 7. Agent according to point 1, 3, 4 or 6, wherein the peptide according to point 1 b, 3, 4b or 6

[0438] (i) has a total charge of 0 to +4, or

[0439] (ii) if r > 4, has a total charge of 0 to +4, or

[0440] (iii) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

[0441] 8. Agent according to item 1, 3, 4, 6 or 7, wherein in the peptide according to item 1b, 3, 4b or 6, when o = 1, p = 0, 1 or 2, q = 2 and r = 4, the sequence (X 2)o[(X 3 ) P (X 4 ) q ]r(X 5 )s equals Z 1 Z 2 Z 3 [(Z 4 )uZ 5 Z 6 ]3(Z 7 ) v is, where

[0442] Z 1 like X 2 defined in item 1, 3, 4 or 6 and is selected from R, H and K, preferably R,

[0443] Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined in point 1, 3, 4 or 6 and selected from A, L and V, preferably A and L,

[0444] Z 4 like X 3 defined in item 1, 3, 4 or 6 and is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably F, R, E, A, Q and W, u is 1 or 2,

[0445] Z 7 like X 5is as defined in item 1, 3, 4 or 6 and is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, v is as defined in item 1, 3, 4 or 6 and is an integer from 0 to 4.

[0446] 9. Means according to point 8, where,

[0447] (i) if u = 1 , Z 4 is selected from R, E and Q, or

[0448] (ii) if u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0449] 10. Means according to point 8 or 9, where

[0450] (i) the peptide comprises at least one motif selected from RAL and RLA, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 1-3; and / or

[0451] (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, and wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or

[0452] (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or

[0453] (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0454] (v) the peptide comprises at least one, preferably two or three, motif(s) RAL; and / or

[0455] (vi) the peptide comprises the motif RAL at least twice and at least one of QAL or EAL, preferably both. 11. Agent according to item 1, 3, 4, 6 or 7, wherein in the peptide according to item 1b, 3, 4b or 6, when o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 )0[(X 3 ) P (X 4 ) q ]r equals Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) W Z 16 is, where

[0456] Z 11 like X 2defined in point 1, 3, 4 or 6 and selected from R, H and K,

[0457] Z 12 like X 3 defined in item 1, 3, 4 or 6 and selected from A, R, N, D, C, Q, E, G, H, I, L,

[0458] K, M, F, P, S, T, W, Y and V, preferably A, N, C, Q, G, I, L, M, F, P, S, T, W, Y and V, more preferably

[0459] M, I, S, T, N, V ​​and F,

[0460] Z 13 , Z 14 , Z 16 like X 4 defined in point 1, 3, 4 or 6 and selected from A, L and V, preferably A and L,

[0461] Z 15 like X 3 defined in point 1, 3, 4 or 6 and is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably R, K, E, S, Q and N, w is an integer from 3 to 6.

[0462] 12. Means according to point 11 , where,

[0463] (i) z 13 Z 14 is selected from AL and LA, preferably AL; and / or

[0464] (ii) (Z 15 ) w with w = 3-6 comprises a sequence comprising at least one positively charged amino acid (R, H or K); and / or

[0465] (iii) (Z 15 ) w with w = 3-6 comprises a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or

[0466] (iv) Z 16 is selected from A and L, preferably A.

[0467] 13. Washing and / or cleaning agents comprising

[0468] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; and / or

[0469] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0470] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0471] 14. Washing and / or cleaning agents comprising

[0472] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or

[0473] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0474] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0475] 15. Washing and / or cleaning agents comprising

[0476] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or

[0477] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0478] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0479] 16. Washing and / or cleaning agents comprising

[0480] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or

[0481] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0482] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0483] 17. Washing and / or cleaning agents comprising (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; and / or

[0484] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0485] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0486] 18. Washing and / or cleaning agents comprising

[0487] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or

[0488] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0489] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0490] 19. Washing and / or cleaning agents comprising

[0491] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or

[0492] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0493] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0494] 20. Washing and / or cleaning agents comprising

[0495] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or

[0496] (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and / or

[0497] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0498] 21. Agent according to any one of items 1 to 20, wherein the peptide has an amino acid sequence which is 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, preferably SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, more preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0499] 22. Agent according to one of items 1 to 21, wherein the lipase is selected from

[0500] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0501] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and optionally (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, and / or (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

[0502] 23. Washing and / or cleaning agents comprising

[0503] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0504] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0505] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0506] (ii) optionally has, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T

[0507] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0508] 24. Washing and / or cleaning agent, comprising (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0509] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0510] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0511] (ii) optionally has, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T

[0512] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0513] 25. Washing and / or cleaning agents comprising

[0514] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0;

[0515] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0516] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0517] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0518] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0519] 26. Washing and / or cleaning agents comprising

[0520] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;

[0521] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0522] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0523] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0524] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0. 27. Washing and / or cleaning agents, comprising

[0525] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1;

[0526] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0527] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0528] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0529] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0530] 28. Washing and / or cleaning agents comprising

[0531] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0532] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0533] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0534] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0535] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0536] 29. Washing and / or cleaning agents comprising

[0537] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0;

[0538] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0539] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0540] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0541] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0542] 30. Washing and / or cleaning agents comprising

[0543] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0544] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0545] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0546] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0547] 31 . Washing and / or cleaning agents, comprising

[0548] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1;

[0549] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0550] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0551] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0552] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0553] 32. Washing and / or cleaning agents comprising

[0554] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0555] (B) at least one lipase, wherein the lipase is a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0556] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0557] (ii) optionally having at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and

[0558] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0559] 33. Washing and / or cleaning agents comprising

[0560] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0;

[0561] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0562] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0563] 34. Washing and / or cleaning agents comprising

[0564] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;

[0565] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0566] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0567] 35. Washing and / or cleaning agents comprising

[0568] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1;

[0569] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0570] (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0571] 36. Washing and / or cleaning agents comprising

[0572] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0573] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0574] 37. Washing and / or cleaning agents comprising

[0575] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0;

[0576] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0577] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0578] 38. Washing and / or cleaning agents comprising

[0579] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;

[0580] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0581] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0582] 39. Washing and / or cleaning agents comprising

[0583] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably from -1.5 to +1.5, particularly preferably from -1.1 to +1.1; (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0584] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0585] 40. Washing and / or cleaning agents comprising

[0586] (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0;

[0587] (B) at least one lipase which has lipolytic activity and comprises an amino acid sequence which is 100% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length; and

[0588] (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.0.

[0589] 41. Agent according to one of items 1 to 40, wherein the peptide binds to a fatty surface or to a surface coated with fat or to a surface provided with at least one fatty and / or oily soil, wherein the surface is preferably selected from hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2.

[0590] 42. Agent according to any one of items 1 to 41, wherein the peptide is surface-active, wherein the surface activity is determined, preferably by the bubble pressure method, very particularly as described herein, in particular as described in Example 6.

[0591] 43. Agent according to any one of items 1 to 11, wherein the peptide is not surface-active, wherein the surface activity is determined, preferably by the bubble pressure method, especially as described herein, in particular as described in Example 6. 44. Agent according to any one of items 1 to 43, wherein the salt is selected from

[0592] (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0593] 45. Agent according to any one of items 1 to 44, wherein the agent is preferably selected from textile detergent, machine dishwashing detergent, hand dishwashing detergent and hard surface cleaner.

[0594] 46. ​​Agent according to any one of items 1 to 45, wherein the agent has at least two spatially separated compartments, wherein the peptide and optionally the salt are contained in a first compartment and the at least one lipase is contained in a second compartment.

[0595] 47. Agent according to one of claims 1 to 46, wherein the agent comprises the at least one peptide increasingly preferably in an amount, based on active protein, of 0.5 to 1500 mg / job, 5 to 500 mg / job and in particular 10 to 200 mg / job.

[0596] 48. Agent according to one of claims 1 to 46, wherein the agent comprises the at least one peptide in an amount of 1 x 10 -8to 10 wt.%, from 0.00001 to 5 wt.%, from 0.00005 to 2.5 wt.%, from 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.%, based on active protein and total weight of the agent.

[0597] 49. A process for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, characterized in that in at least one process step a washing or cleaning agent according to one of points 1 to 48 is used.

[0598] 50. The method according to item 49, wherein in a first step the at least one peptide and optionally the salt are brought into contact with the items to be washed or rinsed, and in a second step the at least one lipase is brought into contact with the items to be washed or rinsed.

[0599] 51. Process according to item 49 or 50, wherein it is carried out in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C. 52. Use of an agent according to any one of items 1 to 48 for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and also plastic), metal (e.g. cutlery or pots) or glass.

[0600] 53. Use of a peptide in a lipase-containing washing and / or cleaning agent according to one of points 1 to 48 for improving the cleaning performance of the agent on at least one fatty and / or oil-containing soil, preferably fatty soil, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1;and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which has the following sequence in N- to C-terminal orientation;

[0601] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0602] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0603] X 2 is selected from R, H and K, preferably R and K,

[0604] X 3is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0605] X 4 is selected from A, L and V, preferably A and L,

[0606] X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0607] 54. Use of a peptide in a lipase-containing washing and / or cleaning agent according to any one of items 1 to 48 for improving the cleaning performance of the agent on at least one fatty and / or oil-containing soil, preferably fatty soil, wherein the peptide is selected from a peptide having an amino acid sequence identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0608] 55. Use of a peptide in a washing and / or cleaning agent, preferably a washing and / or cleaning agent containing lipase, according to one of points 1 to 48 as a dirt-removing, in particular fat- and / or oil-removing, active ingredient in the agent, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1;and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which has the following sequence in N- to C-terminal orientation;

[0609] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0610] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0611] X 2 is selected from R, H and K, preferably R and K,

[0612] X 3is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0613] X 4 is selected from A, L and V, preferably A and L, X 5 is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L, m and t are each 0 or 1, where m+t = 0 or 1, n and o are each 0 or 1, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0614] 56. Use of a peptide in a washing and / or cleaning agent, preferably a lipase-containing washing and / or cleaning agent, according to one of items 1 to 48 as a dirt-removing, in particular fat- and / or oil-removing, active ingredient in the agent, wherein the peptide is selected from a peptide having an amino acid sequence identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0615] 57. Use according to any one of items 53 to 56, wherein the lipase is selected from

[0616] (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,

[0617] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0618] (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or

[0619] (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical. 58.Use according to any one of items 53 to 57, wherein the lipase is selected from a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33,.

[0620] (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and

[0621] (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0622] 59. Use according to any one of items 52 to 58 in a temperature range from 10°C to 60°C, preferably 15°C to 40°C, particularly preferably 20°C to 30°C, most particularly preferably 20°C.

[0623] EXAMPLES

[0624] Example 1 : Peptide sequences

[0625] The peptides shown in Table 2 were prepared by chemical synthesis.

[0626] Table 2: Peptide names and corresponding amino acid sequences

[0627] The isoelectric point and charge values ​​were calculated using the Henderson-Hasselbalch equation as described in Kozlowski, LP, “IPC - Isoelectric Point Calculator”. Biol Direct 11 , 55 (2016), https: / / doi.org / 10.1186 / s13062-016-0159-9. The pKa values ​​used in the calculation were as disclosed in Grimsley GR, Scholtz JM, Pace CN. “A summary of the measured pK values ​​of the ionizable groups in folded proteins”. Protein Sci. 2009 Jan;18(1):247-51. doi: 10.1002 / pro.19. PMID: 19177368; PMCID: PMC2708032.

[0628] Example 2: Testing the adhesion of peptides with regard to their substrate specificity to fats

[0629] In an initial experiment, the adhesion of various peptides to grease stains on textiles was measured using the fluorescamine method. The protein dye fluorescamine is a fluorescent dye used to quantify minute amounts of proteins and peptides in solution. The fluorescamine reagent reacts rapidly with primary amines. The following pre-soiled textile patches were used (ex. CFT, Center For Test Material): C-FF CS46, Frying Fat, used, Cotton (cooking fat on cotton).

[0630] P-FF PS46, Frying Fat, used, Polyester (frying fat on polyester)

[0631] C-0 C02, Olive Oil with carbon black with thickening agent, Cotton (olive oil on cotton)

[0632] P-0 P02, Olive Oil with carbon black with thickening agent, Polyester (olive oil on polyester)

[0633] CS CS32, Sebum Bey with Carbon black, Cotton (Sebum on cotton)

[0634] P-S PS32, Sebum Bey with Carbon black, Polyester (Sebum auf Polyester)

[0635] For the study, three textile patches (each approximately 10 mm in diameter) were placed twice into the wells of a 48-well microtiter plate. 0.2 ml of peptide solution (0.02 mg / ml in distilled water) was added to the wells of the first plate, and 0.2 ml of distilled water was added to the wells of the second plate. Wells without textile patches served as controls. The microtiter plates were incubated with gentle shaking (750 rpm, Titramax) for 1 h at 20°C. After incubation, 50 μl of supernatant from each well was transferred to wells of a black 96-well microtiter plate. 17 μl of fluorescamine solution (3 mg / ml in DMSO; fluorescamine, ex. AcrosOrganics) was added and mixed for 15 min at 20°C. The fluorescence of the samples in the 96-well plate was measured in a biophotometer (Ex 260 nm, Em 465 nm).Since the fluorescence response is linearly dependent on the peptide concentration, the percentage adhesion of the peptide to the test material can be determined from the final and initial fluorescence values.

[0636] The results are presented in Table 3. The larger the value, the better the adhesion of the peptide to the corresponding surface. Values ​​from 40% to 59% indicate moderate adhesion, values ​​from 60% to 79% indicate good adhesion, and values ​​above 79% indicate very good adhesion. Differences of 5% or more are considered significant.

[0637] Table 3: Adhesion results

[0638] All peptides P1 to P31 exhibit good to very good adhesion to at least one greasy and / or oily soil on polyester and / or cotton textiles. The non-inventive peptide P32 exhibits no adhesion to greasy and / or oily soils.

[0639] Example 3 and 5: QCM-D measurement

[0640] The fat-removing effect was investigated using a quartz crystal microbalance with dissipation monitoring (QCM-D for short; QCM = quartz crystal microbalance; D = dissipation). This surface-sensitive method allows the adsorption and desorption processes of materials or substances (as well as the associated processes, e.g. swelling) on ​​a sensor surface to be monitored in situ with ng resolution. The sensors used for this purpose consist of a thin quartz crystal disc surrounded by two metal electrodes. Due to the piezoelectric properties of the quartz, it can be mechanically deformed when an external electrical voltage is applied (depending on the crystal cut and the sign of the voltage). When an alternating voltage is applied, the quartz sensor begins to oscillate. At a specific frequency, the resonance frequency f, the quartz sensor oscillates in resonance.Since the resonance frequency depends on the thickness of the disk, measuring changes in the resonance frequency over time can be used to draw conclusions about changes in mass or layer thickness for the processes mentioned above. In addition to the change in the resonance frequency Af, the change in dissipation AD (energy loss) is also measured. This parameter describes the energy loss of the oscillating system due to viscoelastic properties of the adsorbed or desorbed material film. By simultaneously measuring Af and AD, viscoelastic models can be created. In simple cases, i.e., with rigid, thin and homogeneously distributed films that are firmly bonded to the quartz crystal surface, mass changes Am due to adsorption and desorption processes can be calculated solely from the frequency change Af (Sauerbrey equation; see, for example, Snabe et al.(2003), Lag phase and hydrolysis mechanisms of triacylglycerol film lipolysis, Chemistry and Physics of Lipids, 125: 69-82; QSense analysis documentation & manufacturer's instructions, available at: https: / / www.biolinscientific.com / qsense / instruments / qsense- pro#knowledqe).

[0641] Carrying out the QCM-D measurement:

[0642] The quartz sensors of the quartz crystal microbalance (QSense Analyzer, QSense Flow module QFM 401, ex. QSense®) were prepared for the test by cleaning the quartz sensors with a hydrogen peroxide-ammonia-Millipore water solution (ratio 1 :1 :5) at 75°C,

[0643] After cleaning, the quartz sensors were spin-coated with a model grease solution (1% tricaprin in toluene, 50 μl at 75 rps). Spin-coating is a method known to those skilled in the art and allows the application of very thin substrate layers with a thickness of just a few nm or mm (see, for example, Diesen et al., Revealing Detergent Efficiency and Mechanism by Real-Time Measurement Using a Novel and Tailored QCM-D Methodology, Tenside Surf. Det. 53 (2016) 5: 488-494). This is done in this way for all examples 3 to 5. The measuring cell was then filled, depending on the test series, with Millipore water or with a buffered Tris / HCl solution (flow rate 50 pL / min), which additionally contained no or 5, 50, or 500 mmol / l potassium chloride, and the frequencies or dissipations of the fundamental tone or the overtones of the grease-coated quartz sensor were measured in Millipore water or the respective buffer at 20°C (baseline).(Termination criterion: temporally constant values ​​for frequency or dissipation, ie the frequency or dissipation was determined over a time course at which the system has adjusted to a stable frequency or dissipation).

[0644] Subsequently, the peptide solution (peptide P2 or peptide P4) was passed through at a flow rate of 50 pl / min and the frequencies or dissipations of the fundamental tone or the overtones of the grease-coated quartz sensors in the peptide solution were measured over time (termination criterion: temporally constant values ​​for frequency or dissipation), see Example 3. Subsequently, each sample was rinsed again with the corresponding buffer system with the respective salt concentration. To measure the fat-removing effect of peptide and lipase (Example 5), after the steps for peptide binding already described under Implementation, the measuring cell was briefly rinsed with the buffered Tris / HCl solution (pH value of 8.0 at 20 °C) (flow rate 50 pl / min), then the lipase solution (lipase according to SEQ ID NO:33) was passed through at a flow rate of 50 pl / min and the frequencies or dissipations of the fundamental tone orThe overtones of the fat-coated quartz sensors in the lipase solution were measured over time (termination criterion: constant values ​​for frequency or dissipation). Subsequently, each sample was rinsed again with the appropriate buffer system at the respective salt concentration.

[0645] To restore the measuring cell, rinse it with a 2% aqueous surfactant solution and then with Millipore water after each measurement has been completed.

[0646] Evaluation principle of the QCM-D measurement:

[0647] The change in the measured frequency values ​​(Af) should be interpreted as follows:

[0648] Values ​​Af < 0 mean that the sensor is becoming heavier, meaning that material is adsorbing onto it, in this case the peptide on the fat layer. The larger the value, the more peptide mass binds to the fat on the sensor.

[0649] Values ​​Af > 0 mean that the sensor becomes lighter, meaning that material is being detached from it—in this case, the fat layer. The larger the value, the more fat mass is being detached from the sensor.

[0650] Values ​​= 0 means that the mass of the sensor does not change (in this case this is the mass of the sensor coated with grease).

[0651] Initially, the frequency (Af) is lowered below the baseline (Af = 0) by the added mass of the adhering peptide, i.e., the peptide adheres or adsorbs to the fat applied to the sensor. Subsequently, the frequency (Af) remains stable for several hours.

[0652] Based on the temporal progression of the measured frequency values, the adsorption rate of the peptide to the fat layer can be determined (adsorption rate; Example 3). This is calculated from the sudden change in frequency after peptide addition and the time required for this change (v ads,s). A continuous, but slower peptide adsorption can be observed via further frequency changes and also related to the time required (v a ds,l). If the frequencies and dissipations are constant over time, the test can be switched to the corresponding measurement solution (without peptide). Once frequencies and dissipations are constant again, the test can be terminated or started with lipase. In the latter case, the reaction times for the removal of the grease coating on the sensor can also be determined after adding lipase. The reaction time for grease removal is calculated from the difference between the time of the onset of the frequency change after adding lipase (= lipase detaches the grease layer from the sensor) and the time of temporally constant frequencies and dissipations after adding lipase. Example 3: Adhesion of peptides to grease on hard surfaces:

[0653] Peptide P2 and peptide P4 were tested as exemplary peptides. The adsorption rate of the respective peptide (P2 and P4, respectively) at the lipid surface was determined for 0 mM, 5 mM, 50 mM, and 500 mM KCl in 10 mM TRIS / HCl buffer at pH 8 by measuring the slope of the frequency jump after peptide addition (Hz / min).

[0654] Fig. 3 shows a QCM-D measurement with the addition of a peptide (as an example). As described above, a sudden change in frequency after peptide addition can be observed as a function of time (v a ds,s). Furthermore, a slower peptide adsorption ((v a ds,l) is observed.

[0655] Table 4: QCM-D measurements with 10 pM peptide P2 or P4 in 10 mM TRIS / HCl buffer at pH 8.0 (average values ​​from 3 measurements, overtones 5, 7 and 9 were used)

[0656] It has been shown that the addition of a salt solution, for example, a potassium chloride solution, improves the adhesion of the peptides to the fatty layer. The higher the adsorption rate, the faster the peptide binds to the fatty surface. This is particularly important for technical applications in washing machines or dishwashers, so that the peptide adheres to the fatty surface as early and as completely as possible. The subsequent interaction between lipase / peptide and the fatty layer can thus occur particularly quickly, while other interactions between the enzyme or peptide components and active ingredients can be avoided.

[0657] Example 4: Streaming potential measurement: The sensors were spin-coated using the method described above and inserted into the gap measurement cell. Streaming potential measurements were performed using 10 pM of peptide P2 or peptide P4 in 10 mM TRIS / HCl at pH 8.0 in the presence of 5 mM potassium chloride at 20 °C.

[0658] First, the zeta potential is determined in mV in an equilibrated state with buffer and saline solution (zeta potential without peptide). In the next step, the respective peptide is added. The zeta potential then undergoes a significant jump. For evaluation, the maximum value of the zeta potential after peptide addition is determined. However, the negative charges of the peptide also accumulate up to this maximum value, lowering the zeta potential again with continued peptide adsorption.

[0659] When the zeta potential no longer changes significantly or reaches a baseline (here approximately 50 min after peptide addition), the peptide final value of the streaming potential is determined.

[0660] Fig. 2 shows the streaming potential measurement for an uncoated and coated gold sensor as a function of pH. The streaming potential measurement values ​​(for peptide P2) shown graphically in Fig. 1 were presented numerically in Table 5:

[0661] Table 5: Streaming potential measurement of peptide P2 and P4 in mV

[0662] The difference between the maximum zeta potential value with the peptide and the final zeta potential value (jump 2) is examined. It is observed that different difference values ​​result depending on the charge value of the respective peptide at pH 8 (P2 (-0.6) or P4 (+0.37)).

[0663] Example 5: Determining the fat-removing effect by combining peptide and lipase

[0664] Table 4 shows the reaction times in the QCM-D measurement with 10 pM peptide (P2 or P4) or without peptide and 20 μl lipase in 50 ml buffer solution (TRIS, pH 8.0) (lipase according to SEQ ID NO: 33; concentration: 5.8 mg / ml total protein content, determined by BCA assay, μl=4.7). The mean values ​​of three measurements are shown (overtones 5, 7, and 9 were used to evaluate the reaction times).

[0665] Table 6: Reaction time of fat detachment

[0666] As can be seen from the data, fat is removed more quickly when using the inventive combination of peptide and lipase. Surprisingly, this effect can be further enhanced by adding salt, especially KCl.

[0667] The QCM-D measurements described above also correspond to observations that can be made with the naked eye. Before the coated quartz sensor comes into contact with the peptide and lipase, or with the lipase alone, the presence of the fatty layer is detectable. After the measurement, the fatty layer is completely removed, and the gold layer of the sensor is visi...

Claims

PATENT CLAIMS 1 . Washing and / or cleaning agents comprising (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5, and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1, and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably from -1.8 to +1.0; and (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, more preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in 1 wt.% solution in deionized water at 20°C preferably has a pH in a range from 6.0 to 11.5, preferably from 7.0 to 11.0, more preferably from 7.5 to 10.5, particularly preferably from 8.0 to 10.

0.

2. Agent according to claim 1, wherein the peptide has an amino acid sequence which is 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31, preferably SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, more preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

3. Agent according to one of claims 1 to 2, wherein the lipase is selected from (a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70%, and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33, (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

4. Agent according to one of claims 1 to 3, wherein the salt is selected from (a) alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

5. Agent according to one of claims 1 to 4, wherein the peptide binds to a fatty surface or to a surface coated with fat or to a surface provided with at least one fatty and / or oily soil, wherein the surface is preferably selected from hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2.

6. A composition according to any one of claims 1 to 5, wherein the composition is preferably selected from textile detergent, machine dishwashing detergent, hand dishwashing detergent and hard surface cleaner.

7. Agent according to one of claims 1 to 6, wherein the agent has at least two spatially separated compartments, wherein the peptide, and optionally at least one salt, is contained in a first compartment and the at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is contained in a second compartment.

8. Agent according to one of claims 1 to 7, wherein the agent contains the at least one peptide increasingly preferably in an amount, based on active protein, of 0.5 to 1500 mg / job, 5 to 500 mg / job and in particular 10 to 200 mg / job and / or in an amount of in each case 1 x 10 -8to 10 wt.%, from 0.00001 to 5 wt.%, from 0.00005 to 2.5 wt.%, from 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.%, based on active protein and total weight of the agent.

9. A process for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, characterized in that in at least one process step a washing or cleaning agent according to one of claims 1 to 8 is used.

10. The method according to claim 9, wherein in a first step the at least one peptide and optionally at least one salt is brought into contact with the laundry or rinse ware and in a second step the at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is brought into contact with the laundry or rinse ware.

11. The process according to claim 9 or 10, wherein it is carried out in a temperature range of 10°C to 80°C, preferably 15°C to 60°C, further preferably 15°C to 45°C, more preferably 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

12. Use of an agent according to one of claims 1 to 8 for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass.

13. Use of a peptide in a lipase-containing washing and / or cleaning agent according to one of claims 1 to 8 for improving the cleaning performance of the agent on at least one fatty and / or oil-containing soil, preferably fatty soil, wherein the at least one peptide is selected from a peptide comprising or consisting of an amino acid sequence from 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably from 6.0 to 13.0, particularly preferably from 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably from -1.0 to +2.0, particularly preferably from -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.

0.

14. Use of a peptide in a washing and / or cleaning agent, preferably a washing and / or cleaning agent containing lipase, according to one of claims 1 to 8 as a dirt-removing, in particular fat- and / or oil-removing, active ingredient in the agent, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5;and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; 15. Use according to one of claims 13 or 14, wherein the lipase is selected from a) a lipase which has lipolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:33 over its entire length and, in each case based on the numbering according to SEQ ID NO:33, (i) at the positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256; and / or (b) a lipase which has lipolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%, preferably 100%, identical.

16. Use according to any one of claims 12 to 15 in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.