Method for removing grease and / or grease- and / or oil-containing stains

Abstract

The invention relates to a method for removing grease and / or grease- and / or oil-containing stains from a grease- and / or oil-containing surface or on a surface coated with grease and / or oil or on a surface provided with at least one grease- and / or oil-containing stain, wherein the surface is selected from hard surfaces and / or textiles. The invention also relates to corresponding agents.

Description

[0001] .Process for removing grease and / or greasy and / or oily soils

[0002] The invention relates to a method for removing grease and / or greasy and / or oily soils from a greasy and / or oily surface or from a surface coated with grease and / or oil or from a surface provided with at least one greasy and / or oily soil, wherein the surface is selected from hard surfaces and / or textiles, as well as corresponding agents.

[0003] 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, there is currently no satisfactory alternative for removing grease and / or oily soiling at low temperatures, ie at temperatures below 50°C, preferably below 45°C, particularly preferably below 40°C, in particular at, for example, about 20°C or about 30°C, since the greases do not liquefy or only insufficiently liquefy at temperatures below about 30°C or about 40°C.

[0004] Peptides are readily biodegradable. 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 in the prior art (WO 2014 / 072313 A1, WO 2023 / 110572 A1).

[0005] The task was therefore to develop a process in which grease or greasy and / or oily soiling or coatings can be removed from surfaces even at low temperatures and at the same time more environmentally friendly agents can be used.

[0006] A first aspect of the invention is a method for removing grease, grease- and / or oil-containing soiling and / or greasy deposits from surfaces, characterized by the following steps: i) Providing at least one peptide ii) Bringing the peptide into contact with a grease- and / or oil-containing surface iii) Subsequently rinsing the surface with water or an aqueous solution; characterized in that 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 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0007] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0008] X 1is 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,

[0009] X 2 is selected from R, H and K, preferably R and K,

[0010] 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,

[0011] X 4 is selected from AL and V, preferably A and L,

[0012] 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; or b) 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0013] Surprisingly, it was found that these peptides are capable of adhering to fat adhering to surfaces, thus enabling the removal of the fat from these surfaces and partially detaching or removing it.

[0014] This process allows for grease removal with minimal amounts (or even without) of surfactants and / or at lower temperatures. This is ecologically advantageous, as the presence of peptides in wastewater is not critical and the peptides' biodegradability is very high.

[0015] The applicability in washing and / or rinsing processes at low temperatures is also suitable, in particular at temperatures of 10 to 50°C, preferably 15 to 45°C, and particularly 20 to 40°C, since the peptides enable grease removal even at these temperatures, although the solubility of fats or greasy soils in the liquor is significantly lower than at temperatures above these values. For example, the at least one peptide used according to the invention can be dosed at a time when the washing or rinsing water is not (yet) heated or is only slightly heated, in order to promote the detachment of the greasy soils from the surfaces. The greasy and / or oily soils thus dissolved can then enter the rinsing liquor even below the melting temperature and, if necessary, can thus be removed from the rinsing liquor earlier.As a result, these fats do not re-deposit on the surface or only to a reduced extent.

[0016] This also helps reduce grease deposits in areas where water movement is reduced, such as in the drainage pipes and / or filters. Larger amounts of grease often accumulate there, which are then removed from the liquor. However, these greasy residues are not dissolved or solubilized, or only partially, and thus cannot be transported completely or residue-free to the sewer system. Instead, they solidify or freeze again in the filters and / or drainage pipes, potentially clogging these machine parts or pipes / sewage lines.

[0017] It is therefore particularly preferred to use the at least one peptide used according to the invention for cleaning water-conducting machines, in particular dishwashers or washing machines, or their drainage systems and / or filters.

[0018] In step i) of the process according to the invention, a peptide to be used according to the invention is provided.

[0019] The preparation is carried out by dissolving the peptide or the peptide-containing agent in a suitable solvent. This solvent preferably comprises water. Particularly preferably, the solvent comprises at least 50 wt.%, in particular at least 60 wt.%, particularly preferably at least 70 wt.%, and very particularly preferably at least 80 wt.% water. According to a very particularly preferred embodiment, the solvent comprises at least 90 wt.% water.

[0020] It is preferred that the water be of drinking water quality. For example, the water may be supplied from industrial water reservoirs, drinking water reservoirs, or drinking water pipes.

[0021] Preferably, the solvent, especially water, used to dissolve the peptide is placed in a container. This is done by adding the solvent, especially water, to the container or by filling the container with the solvent, especially water. The peptide is added during or after the process. However, it is also possible within the scope of the invention to initially introduce the peptide and then add the solvent, especially water.

[0022] In water-conducting machines, especially water-conducting household appliances, the provision is achieved by making at least one peptide available directly in the water-conducting machine. The peptide is dosed into the machine and dissolved by the water flowing into the machine.

[0023] According to the invention, it is preferred that in the water-conducting machines, in particular household machines, the surfaces to be cleaned are already in the machine before the peptide is dissolved by the solvent.

[0024] According to a preferred embodiment, the peptide is provided simultaneously with the provision of a washing or cleaning agent. Particularly preferably, the peptide is provided in step i) in a washing or cleaning agent, which is initially introduced and dissolved or dosed and dissolved.

[0025] Particularly preferably, the peptide can be contained in a washing and / or cleaning agent that is dosed into the water in the water-carrying machine. It is also possible for the peptide to be dosed separately from the washing or cleaning agent.

[0026] In another embodiment, the peptide is dosed before and / or after the dosage of a washing or cleaning agent, preferably with a dosing time difference of at least 1 minute, preferably of at least 5 minutes, particularly preferably of at least 10 minutes. In step ii), the at least one peptide is brought into contact with a fat- and / or oil-containing surface. This is preferably done by bringing this surface into contact with the washing or cleaning liquor.

[0027] The term "washing or cleaning liquor" refers to the working solution containing the peptide, or the peptide and the washing or cleaning agent, which acts on the textiles or fabrics or surfaces, especially dishes 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 typically created when the washing or cleaning process begins and the agent is diluted with the solvent, preferably water, e.g., in a washing machine or dishwasher or in another suitable container.

[0028] 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 provided with at least one fatty and / or oily soil (preferably soiled). 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. According to the invention, all known fatty acids with 8 to 36, preferably 10 to 24, carbon atoms, both mono- or polyunsaturated and saturated fatty acids, are also 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 include 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, deep-fryer fat, meat fat (e.g., beef tallow, pork fat, lard), even burnt-in food residues, and / or synthetic fats and / or oils, such as, for example,Mineral 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.

[0029] 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.

[0030] Preferably, the greasy and / or oil-containing surface and / or the surface coated with greasy and / or oil and / or the surface provided with at least one greasy and / or oil-containing soiling 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 enamelled surface, wood, laminate, linoleum and mixtures thereof, particularly preferably crockery (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass.

[0031] Preferably, 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 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, refers to 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 can be in the form of knits, wovens, denims, nonwovens, felts, yarns, and terry cloth. The textile can be cellulose-based, such asNatural cellulose fibers such as 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 blends thereof. The textile or fabric can also be made of non-cellulose fibers, e.g., natural polyamides such as wool, camel, cashmere, mohair, rabbit, and silk, or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulose fibers and non-cellulose fibers. Examples of blends are blends of cotton and / or rayon / viscose with one or more accompanying materials such as wool, synthetic fibers (e.g. polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) and / or cellulosic fibers (e.g. rayon / viscose, ramie, flax / linen, jute, cellulose acetate fibers, lyocell).The fabric can 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, with cotton, polyester, or mixtures thereof being particularly preferred.

[0032] The invention particularly preferably relates to hard surfaces and / or textiles that are provided with at least one greasy and / or oily soil, i.e., are greasy. 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. Surfaces to be cleaned are preferably hard surfaces that come into contact with foodstuffs, eating, and / or drinking.

[0033] 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 used 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.

[0034] In particularly preferred embodiments, the peptides used according to the invention enable the improvement of the cleaning performance of washing and / or cleaning agents on at least one greasy and / or oily 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.

[0035] In step iii), the surface is rinsed with water or an aqueous solution. This is suitable for removing or transporting away the grease or greasy soils dissolved by the peptide adhesion. This step preferably takes place simultaneously and / or subsequently to step ii). This subsequent rinsing or rinsing also serves to remove non-adhered peptides and any residues of detergent or cleaning agents from the surface.

[0036] 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.

[0037] 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.

[0038] Unless otherwise stated, all percentages are by weight (wt%), based on the total weight of the corresponding composition or agent.

[0039] 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.

[0040] "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.

[0041] "Approximately" or "approximately" as used herein with reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0042] 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.

[0043] In the context of the invention, the term "room temperature" is understood to mean 20°C at 1,013 mbar, unless explicitly stated otherwise.

[0044] "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.

[0045] 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.

[0046] 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.

[0047] 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.

[0048] 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.

[0049] 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.

[0050] When reference is made herein to various interconnected 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 one another via peptide bonds, unless otherwise stated. In the context of this invention, "adhesion" or "adhesive" is understood to mean an interaction between a peptide and a surface, whereby the peptide can adhere to the surface. Thus, the term "adhesion-promoting" refers to the ability, under suitable conditions, i.e., usually non-denaturing conditions, to adhere to various surfaces, e.g., textile surfaces, in particular containing or consisting of cotton, polyester, and mixtures thereof, or hard surfaces, such as, in particular, tableware (preferably made of ceramics such as porcelain or earthenware, as well as plastic), metal (e.g.,cutlery or pots) or glass, and / or to adhere to a specific surface. "Fat-binding peptides," as used herein, mean that the peptide binds to fat, e.g., to at least one fatty and / or oil-containing 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 fat-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).

[0051] 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 presented in N- to C-terminal orientation.

[0052] Table 1: Proteinogenic amino acids

[0053] 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 acid usually refer to one of the 20 naturally occurring proteinogenic amino acids (Table 1).

[0054] The amino acids are, unless otherwise stated, 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, any such amino acid encompasses all of the aforementioned amino acids. In various embodiments, the peptide has a 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 positively and negatively charged amino acids in the peptide, in particular R, K, H, D and E, and results from the sum of the negative and positive charges, with one 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.

[0055] In various embodiments, the peptide

[0056] (a1) has a total charge of 0 to +4, or

[0057] (a2) if r > 4, has a total charge of 0 to +4, or

[0058] (a3) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

[0059] In various embodiments,

[0060] (b) the N-terminus comprising the first 1-5 amino acids has a positive net charge; and / or

[0061] (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

[0062] (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

[0063] (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.

[0064] All of the above features can be implemented individually or in any combination.

[0065] 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.

[0066] 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.

[0067] 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.

[0068] In various embodiments, the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0069] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0070] 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,

[0071] X 2 is selected from R, H and K, preferably R and K,

[0072] 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,

[0073] X 4 is selected from A, L and V, preferably A and L,

[0074] 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.

[0075] 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 equal to Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z 6 ]3(Z 7 ) V , where

[0076] Z 1 like X 2 defined above and selected from R, H and K, preferably R,

[0077] Z 2 , Z 3 , Z 5 and Z 6 like X 4defined above and selected from A, L and V, preferably A and L, 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,

[0078] Z 7 like X 5 defined 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.

[0079] In various embodiments

[0080] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0081] (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ.

[0082] In various embodiments, the peptide comprises

[0083] (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

[0084] (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

[0085] (iii) at least one motif selected from QAL and QLA, preferably QAL; and / or

[0086] (iv) the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0087] (v) at least one, preferably two or three, RAL motif(s); and / or

[0088] (vi) the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0089] 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.

[0090] 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.

[0091] 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.

[0092] 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 helical structure because these amino acids have a high α-helix potential.

[0093] 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

[0094] Z 11 like X 2defined above and selected from R, H and K,

[0095] 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,

[0096] S, T, N, V ​​and F,

[0097] Z 13 , Z 14 , Z 16 like X 4 defined above and selected from A, L and V, preferably A and L,

[0098] 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,

[0099] T, W, Y and V, preferably R, K, E, S, Q and N, w is an integer from 3 to 6.

[0100] In various embodiments, a peptide

[0101] (i) is z 13 Z 14 selected from AL and LA, preferably AL; and / or

[0102] (ii) includes (Z 15 )w with w = 3-6 a sequence comprising at least one positively charged amino acid (R, H or K); and / or

[0103] (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

[0104] (iv) Z is 16 selected from A and L, preferably A.

[0105] 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.

[0106] In various 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 various 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 various 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.

[0107] 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.

[0108] In various 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.

[0109] 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.

[0110] 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 set forth in SEQ ID NOs: 1-31.

[0111] 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), SRARLFVVTYHKC (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), RALFEALFRALEALC (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).

[0112] In preferred embodiments, the peptide has a sequence which is 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, very particularly preferably SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29, very particularly preferably SEQ ID NOs: 1, 3, 5, 9, 10, 12, 29.

[0113] Surprisingly, it was found that these particularly preferred peptides are suitable for adhering to fat adhering to surfaces and, moreover, for partially detaching or removing the fat from these surfaces, even without additional excipients and / or active substances.

[0114] In preferred embodiments, the peptides according to the invention are surface-active.

[0115] 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 (also known as the bubble differential 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, particularly aqueous solutions, 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. https: / / www.sita-messtechnik.de / wissen / oberflaechenspannung). If the dynamic surface tension remains constant over the entire lifetime of the bubble, 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 over the entire bubble lifetime, i.e., the deviation is less than 10 mN / m, preferably less than 8 mN / m, more preferably less than 6 mN / m, particularly preferably less than 5 mN / m, and most preferably less than 2 mN / m. Conversely, the peptides according to the invention are surface-active if, in the bubble pressure method, the dynamic surface tension does not remain constant over the entire bubble lifetime, i.e., the deviation is 2 mN / m or more, preferably 5 mN / m or more, more preferably 6 mN / m or more, particularly preferably 8 mN / m or more, and most preferably 10 mN / m or more.

[0116] In preferred embodiments, peptides according to the invention are surface-active, wherein the surface activity is determined according to the bubble pressure method as described herein, and wherein the dynamic surface tension over the entire bubble lifetime shows a deviation of 2 or more mN / m, preferably of 5 or more mN / m, more preferably of 6 mN / m or more, particularly preferably of 8 mN / m or more, and most preferably of 10 or more mN / m (preferably measured at 20°C, in a concentration range of 0.1 mg / l to 1 g / l, at pH 8.0; particularly preferably measured 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).

[0117] Surprisingly, it was found that these particularly preferred surfactant peptides are suitable for adhering to fat adhering to surfaces and, moreover, for partially detaching or removing the fat from these surfaces, even without additional excipients and / or active substances.

[0118] Peptides preferably used 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, ieusually non-denaturing conditions, to adhere to corresponding surfaces, thus exhibiting adhesive properties.

[0119] 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 additional 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.

[0120] Peptides preferably used 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. Peptides preferably used 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.

[0121] Peptides preferably used 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. Peptides preferably used 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.

[0122] Peptides preferably used 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 preferably used 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.

[0123] In particularly preferred embodiments, peptides used according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soil on textiles. In particularly preferred embodiments, peptides used 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.

[0124] 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. 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 have the amino acid sequences given.Further preferred peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fat-containing, 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 fat- and / or oil-containing, preferably fat-containing, 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 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: 8, 10, 21, 25, 26.

[0125] 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.

[0126] In particularly preferred embodiments, peptides used 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.

[0127] 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, very particularly preferably SEQ ID NOs: 1, 3, 5, 9, 10, 12, 29.

[0128] Methods for determining adhesion are known to those skilled in the art, and any suitable methods may be used. Further methods are described in the examples.

[0129] 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.

[0130] 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 to a suitable amino acid of the chain and / or N- and / or C-terminally. 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, for example, be produced recombinantly as fusion proteins. In such embodiments, the peptide according to the invention is located either N- or C-terminally in order to mediate the adhesion of the entire molecule to a surface. In such embodiments, the peptide then also acts as an adhesion tag.

[0131] All of the above features and embodiments can be implemented individually or in any combination.

[0132] 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.

[0133] 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.

[0134] The at least one peptide used according to the invention can be present as an aqueous solution. In various embodiments, the peptide content of the solution is preferably 0.000001 to 10 parts by weight of peptide per 100 parts by weight of solvent, preferably 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.

[0135] The present invention further relates to agents used in a method according to the invention. All facts, objects, and embodiments described above are also applicable to this subject matter 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 agents according to the invention.

[0136] Therefore, a further subject of the invention is a cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, containing at least one peptide, characterized in that 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 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0137] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0138] 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,

[0139] X 2 is selected from R, H and K, preferably R and K,

[0140] 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,

[0141] X 4 is selected from AL and V, preferably A and L,

[0142] 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; or b) 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0143] Agents according to the invention increasingly preferably contain the peptides used 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.

[0144] 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.

[0145] 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.

[0146] 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 "cleaning 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.

[0147] 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.

[0148] Agents according to the invention increasingly preferably contain the peptides used 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.

[0149] In various embodiments, agents according to the invention contain an amount of the peptide according to the invention sufficient for one wash or rinse cycle. The peptide according to the invention is preferably contained in agents according to the invention in an amount, based on active protein, of 0.5 to 1,500 mg / job, 5 to 500 mg / job, and in particular 10 to 200 mg / job. Unless the agents according to the invention are single-dose units, the usual dosage amount of the agent per wash / rinse cycle is to be used for the calculation.

[0150] 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.

[0151] 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.

[0152] If agents used according to the invention are in liquid form, they preferably contain, based on their total weight, more than 20% by weight, preferably 30 to 90% by weight and particularly preferably 40 to 80% by weight of water.

[0153] 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.

[0154] 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 C s-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 C s-fatty alcohols and the sulfation products of the aforementioned nonionic surfactants with a low degree of ethoxylation. The surfactants of the sulfonate type that can be used include, for example, Cg-14-alkylbenzenesulfonates, alkanesulfonates obtained from Cs-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 C s-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.

[0155] The agent, in particular the textile detergents, 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 other anionic surfactants, in particular alkyl ether sulfates, as well as nonionic surfactants, in particular fatty alcohol alkoxylates. These can then make up the remainder of the surfactants.

[0156] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates 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.

[0157] 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 C10-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-C16 alkyl sulfates and C18-C16 alkyl sulfates, as well as C18-C16 alkyl sulfates, are preferred.

[0158] Also suitable are the sulfuric acid monoesters of straight-chain or branched C7-2i alcohols ethoxylated with 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C5-n alcohols with an average of 3.5 mol of ethylene oxide (EO) or C12-18 fatty alcohols with 1 to 4 EO. Suitable alkyl ether sulfates are, for example, compounds of the formula

[0159] R 1 -O-(AO) n -SO3- X + .

[0160] In this formula, R 1 represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly 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 C s fatty alcohols, e.g., from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C 10-20 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, preferred are the alkali metal ions and among them Na + or K + , where Na + is highly preferred. Other cations X + can be selected from NHT, % Zn 2+ , % Mg 2+ , % Ca 2+ , % Mn 2+ and their mixtures.

[0161] In various embodiments, the alkyl ether sulfate may be selected from fatty alcohol ether sulfates of the formula with k = 1 from 1 to 19, n = 2, 3, 4, 5, 6, 7, or 8. Particularly preferred representatives are Na-Ci2-14 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).

[0162] 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.

[0163] 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 having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

[0164] Another class of nonionic surfactants that can be used advantageously are alkyl polyglycosides (APG). Suitable alkyl polyglycosides satisfy the general formula

[0165] 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 representing 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 alkyl polyglycosides, i.e. alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical.

[0166] 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.

[0167] Suitable amphoteric surfactants are, for example, betaines of the formula

[0168] (R iii )(R iv )(R v )N + CH2COO-, in which R'" is an alkyl radical having 8 to 25, preferably 10 to 21 carbon atoms, optionally interrupted by heteroatoms or heteroatom groups, and R iv and R v identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C10-18-alkyldimethylcarboxymethylbetaine and Cn-17-alkylamidopropyldimethylcarboxymethylbetaine.

[0169] Suitable cationic surfactants include the quaternary ammonium compounds of the formula

[0170] (R vi )(R vii )(R viii )(R ix )N + X-, in the R vi to R ix 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.

[0171] 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.

[0172] 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-n-alcohols with 7 EO, C13-C15 alcohols with 3 EO, 5 EO, 7 EO, or 8 EO, C15-s-alcohols with 3 EO, 5 EO, or 7 EO, and mixtures of these, such as mixtures of C12-C14 alcohols with 3 EO and C12-C18 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.

[0173] 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.%.

[0174] Examples of non-ionic surfactants that can be used either as the sole non-ionic surfactant or in combination with other non-ionic surfactants are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably with 1 to 4 carbon atoms in the alkyl chain.

[0175] Nonionic surfactants of the amine oxide type, for example 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. These are also used in particular in hand dishwashing detergents. Other suitable surfactants are the polyhydroxy fatty acid amides known as PHFA.

[0176] However, low-foaming non-ionic surfactants are preferred in dishwashing detergents, especially alkoxylated, especially ethoxylated, low-foaming non-ionic surfactants. The detergent portion units particularly preferably contain non-ionic surfactants from the group of alkoxylated alcohols.

[0177] Particularly preferred are nonionic surfactants with a melting point above room temperature. Nonionic surfactants with a melting point above 20°C, preferably above 25°C, particularly preferably between 25 and 60°C, and especially between 26.6 and 43.3°C, are particularly preferred.

[0178] Preferred surfactants come from the group of alkoxylated nonionic surfactants, especially 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.

[0179] 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, where one to ten EO or AO groups are bonded to one another before a block of the 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 -CH3, -CH2CH3, -CH2CH2-CH3, CH(CH3)2 and the indices w, x, y, z independently represent integers from 1 to 6.

[0180] Thus, nonionic surfactants which have a Cg-15 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.

[0181] Preferred nonionic surfactants are those of the general formula R 1 - CH(OH)CH2O-(AO)w-(A'O)x-(A”O)y-(A'”O)zR 2 , in the

[0182] R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical;

[0183] R 2 represents H or a linear or branched hydrocarbon radical having 2 to 26 carbon atoms;

[0184] A, A', A” and A'” independently represent a residue from the group

[0185] -CH2CH2, -CH2CH2-CH2, -CH2-CH(CH3), -CH2-CH2-CH2-CH2, -CH2-CH(CH3)-CH2-, -CH2-CH(CH2-CH3), w, x, y and z stand for values ​​between 0.5 and 120, where x, y and / or z can also be 0.

[0186] Particularly preferred are 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 carbon atoms, preferably having 4 to 22 carbon atoms, furthermore a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radical R 2 having 1 to 30 carbon 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.

[0187] Particularly preferred surfactants are those of the formula

[0188] 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 carbon atoms or mixtures thereof, R 2 denotes a linear or branched hydrocarbon radical having 2 to 26 carbon atoms or mixtures thereof and x stands for values ​​between 0.5 and 1.5 and y for a value of at least 15.

[0189] 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 the Cs-io fatty alcohol (PO)i-(EO)22-2-hydroxydecyl ethers.

[0190] 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 R2 independently of one another represents a linear or branched, saturated or mono- or polyunsaturated hydrocarbon radical having 2 to 26 carbon 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.

[0191] 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 R 2 represent linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 1 to 30 carbon atoms, R 3represents 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 carbon atoms, with radicals having 8 to 18 carbon atoms being particularly preferred. For the radical R 3 H, -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.

[0192] As described above, each R 3in 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) to form units that can be joined together in any order, for example (EO)(PO)(EO), (EO)(EO)(PO), (EO)(EO)(EO), (PO)(EO)(PO),

[0193] (PO)(PO)(EO) and (PO)(PO)(PO). The value 3 for x has been chosen as an example and can be considerably larger, with the range of variation increasing with increasing x values, for example, including a large number of (EO) groups combined with a small number of (PO) groups, or vice versa.

[0194] 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 1O[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 2 have 9 to 14 C atoms, R 3 stands for H and x takes values ​​from 6 to 15.

[0195] Finally, the non-ionic surfactants of the general formula R 1 -CH(OH)CH2O-(AO) W -R 2 proven in the

[0196] R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical;

[0197] R 2 represents a linear or branched hydrocarbon radical having 2 to 26 carbon atoms;

[0198] A represents a radical from the group CH2CH2, CH2CH2CH2, CH2CH(CH3), preferably CH2CH2, and w represents values ​​between 1 and 120, preferably 10 to 80, in particular 20 to 40.

[0199] The group of these non-ionic surfactants includes, for example, the C4-22 fatty alcohol (EO)iso-2-hydroxyalkyl ethers, in particular the C8-12 fatty alcohol (EO)22-2-hydroxydecyl ethers and the C4-22 fatty alcohol (EO)40-80-2-hydroxyalkyl ethers.

[0200] 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.

[0201] 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.

[0202] 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.

[0203] 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, nitrilotriacetic acid (NTA); 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 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 detergents, the organic (co)builders are optionally present in particular in an amount of up to 25% by weight and preferably from 1 to 8% by weight, based on the total weight of the detergent. Automatic dishwashing detergents 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 detergent.

[0204] 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 agents. In particular, citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid and any mixtures thereof are to be mentioned here. Citric acid or salts of citric acid are particularly preferably used as the builder substance. Other particularly preferred builders are selected from methylglycine diacetate (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS) and ethylenediamine disuccinate (EDDS), carboxymethylinulin and polyaspartate. In preferred embodiments, citric acid and / or citrate are used as the water-soluble, organic builder. The use of 0.5 to 25 wt., based on the total weight of the agent, is particularly preferred.-%, 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, even 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.

[0205] A further 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 preferably used as a builder from the phosphonate class. Aminoalkanephosphonates also possess a pronounced heavy metal binding capacity. Accordingly, it may be preferable, particularly if the agents also contain bleach, to use aminoalkanephosphonates, in particular DTPMP, or mixtures of the phosphonates mentioned. A preferred agent within the scope of this application contains one or more phosphonate(s) from the group consisting of aminotrimethylenephosphonic acid (ATMP) and / or salts thereof.

[0206] Ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or its salts; diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and / or its salts; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or its salts; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or its salts; hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and / or its salts; nitrilotri(methylenephosphonic acid) (NTMP) and / or its salts.

[0207] Particularly preferred are agents which contain 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates.

[0208] Of course, agents according to the invention can contain two or more different phosphonates.

[0209] 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 between 0.1 and 10.0 wt.%, preferably between 0.2 and 8.0 wt.%. In textile detergents, preferably between 0.25 and 5.0 wt.%, more preferably between 0.3 and 3.0 wt.%, and particularly preferably between 0.5 and 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 from 0.5 to 8.0 wt.%, preferably from 1.0 to 7.0 wt.%, and particularly preferably 1.5 to 6.5 wt.%.

[0210] 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.

[0211] 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-(1-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 corresponding salts, preferably alkali metal salts, in particular tetrasodium salts.

[0212] 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.

[0213] 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. A solid detergent 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.

[0214] 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.

[0215] 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+i • y H2O is used, 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 mentioned takes on the values ​​2 or 3. In particular, both β- and δ-sodium disilicates (Na2Si2O5 • y H2O) are preferred. Practically anhydrous crystalline alkali silicates produced from amorphous alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, can also 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 the compositions according to the invention.In agents that contain 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 formula given above are sold by Clariant GmbH under the trade name Na-SKS, e.g. Na-SKS-1 (Na2Si2O45 • x H2O, Kenyaite), Na-SKS-2 (Na2SiO2O49 • x H2O, Magadiite), Na-SKS-3 (Na2SiO17 • x H2O) or Na-SKS-4 (Na2SiO4O5 • x H2O, Makatite). Of these, Na-SKS-5 (α-Na2Si2O5), Na-SKS-7 (β-Na2Si2O5, Natrosilite), Na-SKS-9 (NaHSi2O5• 3 H2O), Na-SKS-10 (NaHSi2O5• 3 H2O, Kanemite), Na-SKS-11 (β-Na2Si2O5) and Na-SKS-13 (NaHSi2O5), but especially Na-SKS-6 (δ-Na2Si2O5) are particularly suitable.In one embodiment of the inventive agents, a granular compound of crystalline phyllosilicate and citrate, of crystalline phyllosilicate 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 inventive agents in amounts of 1 to 20 wt.%, in particular 5 to 15 wt.%, based on the total weight of the agent. Other important water-soluble inorganic builder substances are carbonates (and hydrogen carbonates), in particular sodium carbonate. Alkali carbonate(s) are preferred as builders in automatic dishwashing agents, in particular sodium carbonate (soda). Typical amounts are in the range of 5 to 50 wt.%, preferably 10 to 40 wt.%, in particular 15 to 30 wt.%, in each case based on the total weight of the agent.

[0216] 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.

[0217] Agents according to the invention can also contain water-insoluble builder substances. As water-insoluble inorganic builder materials, 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 from 3 to 20 wt. % and particularly preferably from 1 to 15 wt. %, based on the total weight of the agent. Among these, preference is given to 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). 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.

[0218] 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.%, 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.

[0219] In preferred embodiments, agents according to the invention, preferably textile detergents, comprise, in each case based on the total weight of the agent,

[0220] (a) at least 0.0000001% by weight of at least one peptide according to the invention ii) 0 to 10% by weight, preferably 1 to 4% by weight of citric acid and / or citrate, preferably alkali citrate, iii) 0 to 40% by weight, preferably 0 to 15% by weight, more preferably 1 to 3% by weight, alkali carbonate, preferably sodium carbonate, iv) 0 to 20% by weight, preferably 3 to 10% by weight of alkali silicate, v) 0 to 10% by weight, preferably 0.5 to 2% by weight, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, and / or vi) 0 to 10% by weight, preferably 0.5 to 3% by weight, aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0221] (v)

[0222] 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,

[0223] (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,

[0224] (iii) 0 to 40 wt.%, preferably 5 to 30 wt.%, more preferably 10 to 25 wt.%, alkali carbonate, preferably sodium carbonate,

[0225] (iv) 0 to 20 wt.%, preferably 3 to 10 wt.% alkali silicate,

[0226] (v) 0 to 10 wt.%, preferably 0.5 to 8 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, and / or

[0227] (vi) 0 to 25% by weight, preferably 5.0 to 20.0% by weight, of aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0228] Peroxygen compounds suitable for use in agents 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 from 5 to 30 wt.%, more preferably from 0.1 to 20 wt.%, in each case based on the total weight of the agent.

[0229] 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. However, they are preferably completely absent when percarboxylic acid is used as the sole bleaching agent. In addition to the conventional bleach activators, or instead of them, solid agents, especially textile detergents, can also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0230] Graying inhibitors or soil-release active ingredients (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 active ingredients include copolyesters containing dicarboxylic acid units, alkylene glycol units and polyalkylene glycol units. The proportion of graying inhibitors and / or soil-release active ingredients 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.

[0231] 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 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.

[0232] The conventional foam regulators that can be used in the compositions according to the invention include, for example, polysiloxane-silica mixtures, the finely divided silica contained therein preferably being silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as crosslinked 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 carbon 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 carbon atoms. Among these, sodium monoalkyl phosphate and / or dialkyl phosphate with C16-18 alkyl groups is preferably used. The proportion of foam regulators may preferably be 0.2 to 2 wt.%, particularly preferably not more than 1 wt.-%, based on the total weight of the product.

[0233] 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.

[0234] 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 glycerol and 1,2-propylene glycol. Liquid compositions preferably comprise at least one polyol, preferably from the group consisting of glycerol and 1,2-propylene glycol, based on the total weight of the composition, preferably in an amount of 0.1 to 10 wt. %, preferably 0.2 to 8.0 wt. %, and more preferably 0.5 to 5.0 wt. %. 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 wt. %, preferably 0.2 to 8.0 wt. % and more preferably 0.5 to 5.0 wt. % based on the total weight of the composition. A particularly preferred alkanolamine is ethanolamine.

[0235] Furthermore, the agents according to the invention (in particular for automatic dishwashing) can contain bleach catalysts. The usable bleach catalysts include, but are not limited to, the group of bleach-enhancing transition metal salts and transition metal complexes, preferably Mn, Fe, Co, Ru, or Mo complexes, particularly preferably from the group of manganese and / or cobalt salts and / or complexes, in particular cobalt (ammine) complexes, cobalt (acetate) complexes, cobalt (carbonyl) complexes, cobalt or manganese chlorides, manganese sulfate, and complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Mn5-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Mn4-TACN).

[0236] 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).

[0237] 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.

[0238] 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.

[0239] 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 AlcalaseO 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.

[0240] Examples of amylases include the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus stearothermophilus, as well as their improved versions 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.

[0241] 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 derivatives of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also from Novozymes. Other products suitable for this purpose include the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948). Fusion products of all of these molecules can also be used. In addition, the further developments of α-amylase from Aspergillus niger and A. oryzae, available under the trade name Fungamyl® from Novozymes, are 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, as well as 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.

[0242] 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 comprise 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).

[0243] Common mannanases are from the Bacillus subtilis Endo-ß-mannanase, Bacillus sp. I633 Endo-ß-Mannanase, Bacillus sp. AAI12 Endo-ß-Mannanase, Bacillus sp. AA349 Endo-ß- Mannanase, Bacillus agaradhaerens NCIMB 40482 Endo-ß-Mannanase, Bacillus halodurans Endo-ß-Mannanase, Bacillus clausii Endo-ß-Mannanase, Bacillus licheniformis Endo-ß- Mannanase, Humicola insolens Endo-ß-Mannanase and Caldocellulosiruptor sp. Endo-ß-mannanase (ZB US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0244] 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.

[0245] 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.

[0246] 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.

[0247] 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.

[0248] 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, sequence identity reported herein is determined using the BLAST algorithm.

[0249] Such a comparison also allows a statement to be made about the similarity of the compared sequences. This 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 exhibit 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.

[0250] 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.

[0251] 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.

[0252] 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.

[0253] 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.

[0254] 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).

[0255] 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.

[0256] 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.

[0257] Furthermore, it is possible to package two or more peptides, proteins or enzymes together so that a single granule has multiple enzyme activities.

[0258] The peptides, proteins, or enzymes can also be incorporated into water-soluble films, such as those used 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).

[0259] 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% by weight, preferably 0.3 to 1.5% by weight, based on the total weight of the agent. If multiple inhibitors / stabilizers are present, these values ​​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.

[0260] 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 fabrics) 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 (PLA), 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%.

[0261] 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.

[0262] It is preferred that the peptide used according to the invention, in particular 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.

[0263] 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 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 and plastic), metal (e.g. cutlery or pots) or glass, wherein the surface activity is determined according to the bubble pressure method as described herein.

[0264] Particularly preferred are dishwashing detergents, preferably automatic dishwashing detergents, which contain at least one peptide as described above. In particular, the dishwashing detergents contain at least one peptide in an amount of 0.000001 to 3.5 wt.%, preferably 0.00001 to 2.5 wt.%, in particular 0.00001 to 2.0 wt.%, based on the total weight of the detergent.

[0265] Very particularly preferred dishwashing detergents contain at least one active ingredient selected from builders, preferably selected from carbonates, bicarbonates, silicates and / or citrates; complexing agents, preferably selected from phosphonic acid and / or aminopolycarboxylic acids and their salts; bleaching agents, bleach activators and / or bleach catalysts.

[0266] A very particularly preferred cleaning agent, preferably dishwashing detergent, in particular automatic dishwashing detergent, comprises a) a cleaning agent preparation A which is liquid at 20°C and contains a1) builder; a2) complexing agent b) a cleaning agent preparation B which is different from the cleaning agent preparation A and is liquid at 20°C and has a water content above 1% by weight, containing b1) at least one cleaning-active enzyme, preferably 0.00001 to 2.0% by weight, preferably 0.0001 to 1.5, in particular 0.001 to 1.0% by weight of active protein based on the total weight of the cleaning agent preparation B; b2) at least one peptide according to the invention, preferably in an amount of 0.000001 to 8.0 wt.%, preferably 0.00001 to 5.0 wt.%, in particular 0.00001 to 4.0 wt.%, based on the total weight of the cleaning agent preparation B. and a packaging means in which the cleaning agent preparations A and B are present separately from one another.

[0267] This cleaning agent, preferably dishwashing agent, in particular automatic dishwashing agent, is characterized in particular in that the cleaning agent preparation A, based on its total weight, contains 2 to 50 wt.%, preferably 6 to 45 wt.% and in particular 10 to 40 wt.% builder and / or the builder a1) is selected from the group of carbonates, bicarbonates, citrates, silicates and polymeric carboxylates.

[0268] In a preferred embodiment, the complexing agent a2) is selected from the group consisting of hydroxyethylethylenediaminetriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, glutamic acid diacetic acid, in particular L-glutamic acid A / . / V-diacetic acid, iminodisuccinic acid, hydroxyimino-disuccinic acid, methylglycinediacetic acid, aspartic acid diacetic acid, hydroxyethane-1,1-diphosphonic acid or diethylenetriaminepenta(methylenephosphonic acid) and salts thereof or mixtures thereof, preferably L-glutamic acid A / . / V-diacetic acid and / or methylglycinediacetic acid and salts thereof and / or the cleaning agent preparation A contains 2 to 60% by weight, preferably 4 to 55% by weight and in particular 8 to 50% by weight of complexing agent.

[0269] According to a preferred embodiment of the cleaning agent, the cleaning agent preparation B contains a cleaning-active enzyme from the group of amylases and / or proteases and / or cellulases and / or hemicellulases and / or lipases, in particular amylases and / or proteases.

[0270] According to a further preferred embodiment, the cleaning agent preparation B contains surfactants in an amount of 1 to 35 wt.%, in particular 3 to 30 wt.%, based on the total weight of the preparation B.

[0271] A particularly preferred embodiment is when the cleaning agent, in addition to the cleaning agent preparations A and B, c) comprises a cleaning agent preparation C which is liquid at 20°C and different from the cleaning agent preparation A and B, containing c1) an acidifying agent, c2) a glass corrosion inhibitor, c3) optionally a non-ionic surfactant, c4) optionally a hydrotrope, and c5) optionally less than 1% by weight, preferably less than 0.5% by weight, in particular less than 0.1% by weight of enzyme preparation, and d) a packaging means in which the cleaning agent preparations A, B and C are present separately from one another.

[0272] The cleaning agent preparation B preferably contains, based on its total weight, 30 wt.% and less, preferably 25 wt.% and less, in particular 15 wt.% and less of water and / or the cleaning agent preparation B contains organic solvent, preferably selected from glycerol, 1,2-propylene glycol, 1,3-propylene glycol, dipropylene glycol and polyethylene glycols, in particular 1,2-propylene glycol, wherein the weight fraction of the 1,2-propylene glycol, based on the total weight of the cleaning agent preparation, is preferably 5 to 80 wt.%, preferably 10 to 60 wt.% and in particular 20 to 50 wt.%.

[0273] The cleaning agent preparation C preferably contains the acidifying agent c1) selected from formic acid, tartaric acid, succinic acid, malonic acid, adipic acid, maleic acid, fumaric acid, oxalic acid and / or polyacrylic acid, in particular formic acid, acetic acid and / or citric acid, and / or the cleaning agent preparation C preferably contains the acidifying agent c1) in amounts of 0.1 to 12% by weight, particularly preferably 0.2 to 10% by weight and in particular 0.3 to 8.0% by weight, in each case based on the total weight of the cleaning agent preparation C.

[0274] In a preferred embodiment, the cleaning agent presentation form further comprises a liquid cleaning agent preparation C, wherein the cleaning agent preparation C is different from the cleaning agent preparations A and B.

[0275] In the detergent formulation according to the invention or in the automatic dishwashing processes according to the invention, detergent preparations A and B are used in combination with at least one further detergent preparation C. Detergent preparation C is liquid (20°C), phosphate-free, and contains at least one acidifying agent and one glass corrosion inhibitor. Detergent preparations C according to the invention contain at least one acidifying agent. Acidifying agents can be added to the detergent preparations C according to the invention to lower the pH of the liquor in the final rinse cycle. Both inorganic and organic acids are suitable for this purpose, provided they are compatible with the other ingredients. For reasons of consumer protection and handling safety, solid mono-, oligo-, and polycarboxylic acids are particularly suitable.From this group, formic acid, citric acid, tartaric acid, succinic acid, malonic acid, adipic acid, maleic acid, fumaric acid, oxalic acid, and polyacrylic acid are preferred. Organic sulfonic acids such as amidosulfonic acid can also be used. Sokalan® DCS (trademark of BASF), a mixture of succinic acid (max. 31 wt.%), glutaric acid (max. 50 wt.%), and adipic acid (max. 33 wt.%), is commercially available and also preferably used as an acidifying agent in the context of the present invention. Cleaning agent preparations C which, based on the total weight of the cleaning agent preparation C, contain one or more acidifying agents, preferably mono-, oligo- and polycarboxylic acids, particularly preferably formic acid, tartaric acid, succinic acid, malonic acid, adipic acid, maleic acid, fumaric acid, oxalic acid and polyacrylic acid and in particular formic acid, acetic acid and / or citric acid in amounts of 0.1 to 12% by weight, preferably 0.2 to 10% by weight.-% and in particular 0.3 to 8.0 wt.% are preferred embodiments of the present invention.

[0276] The use of formic acid is preferred because, in addition to its acid function in improving the final rinse result, it also has a positive influence on the storage stability of cleaning preparation C, which, as explained above, is subject to strong temperature fluctuations due to storage in the interior of the dishwasher. Furthermore, it has a disinfecting effect, so that when formic acid is used in the final rinse cycle, the number of bacteria is reduced. This applies both to bacteria found in the rinse liquor of the final rinse cycle and to those found in the rinse liquor remaining in the sump of the dishwasher during and after the wash cycle, as well as the interior of the dishwasher. This can also reduce the number of residual germs on the washed dishes.

[0277] Furthermore, the cleaning agent preparations C according to the invention and optionally A and / or B contain at least one glass corrosion inhibitor. Particularly preferably, preparation(s) C and optionally preparation(s) A contain a corresponding amount of glass corrosion inhibitor(s). These glass corrosion inhibitors are preferably selected from water-soluble zinc salts, preferably zinc chloride, zinc sulfate and / or zinc acetate, particularly preferably zinc acetate, polyalkyleneimines, in particular polyethyleneimines.

[0278] The preparations according to the invention, in particular preparations A and / or C, contain, in a preferred embodiment, as a further constituent at least one zinc salt, in particular inorganic or organic, as a glass corrosion inhibitor. The inorganic zinc salt is preferably selected from the group consisting of zinc bromide, zinc chloride, zinc iodide, zinc nitrate, and zinc sulfate. The organic zinc salt is preferably selected from the group consisting of zinc salts of monomeric or polymeric organic acids, in particular from the group consisting of zinc acetate, zinc acetylacetonate, zinc benzoate, zinc formate, zinc lactate, zinc gluconate, zinc ricinoleate, zinc abietate, zinc valerate, and zinc p-toluenesulfonate. In a particularly preferred embodiment according to the invention, zinc acetate is used as the zinc salt.

[0279] The zinc salt is present in cleaning agent preparations according to the invention preferably in an amount of 0.01 wt.% to 5 wt.%, particularly preferably in an amount of 0.05 wt.% to 3 wt.%, in particular in an amount of 0.1 wt.% to 2 wt.%, based on the total weight of the respective cleaning agent preparation, in particular the respective cleaning agent preparation A or C.

[0280] Polyethylenimines, such as those available under the name Lupasol® (BASF), are preferably used as glass corrosion inhibitors in an amount of 0 to 5 wt.%, in particular 0.01 to 2 wt.%, based on the total weight of the respective preparation.

[0281] It is very particularly preferred if the cleaning agent preparation C contains a zinc salt preferably in an amount of 0.01 wt.% to 5 wt.%, particularly preferably in an amount of 0.05 wt.% to 3 wt.%, in particular in an amount of 0.1 wt.% to 2 wt.%, based on its total weight.

[0282] The cleaning agent preparation preferably contains a non-ionic surfactant. By using a surfactant-containing cleaning agent preparation C, the final rinse performance achieved in the dishwashing processes according to the invention carried out with products according to the invention can be improved. This applies in particular to those preferred variants in which the dosing of the cleaning agent preparations A, B and C takes place at different times. The non-ionic surfactants described above are particularly suitable as surfactant additives for the cleaning agent preparation C. However, non-ionic surfactants of the general formula R1 -CH(OH)CH2O-(AO)w-(A'O)x-(A”O)y-(A'”O)zR 2 , in the

[0283] R 1 represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical;

[0284] R 2 represents a linear or branched hydrocarbon radical having 2 to 26 carbon atoms;

[0285] A, A', A” and A'” independently represent a residue from the group

[0286] -CH2CH2, -CH2CH2-CH2, -CH2-CH(CH3), -CH2-CH2-CH2-CH2, -CH2-CH(CH3)-CH2-, -CH2-CH(CH2-CH3), w, x, y and z stand for values ​​between 0.5 and 120, where x, y and / or z can also be 0. Non-ionic surfactants of the general formula R have proven particularly effective. 1 -CH(OH)CH2O-(AO) W -R 2 proven in the

[0287] R 1represents a straight-chain or branched, saturated or mono- or polyunsaturated Ce-24 alkyl or alkenyl radical;

[0288] R 2 represents a linear or branched hydrocarbon radical having 2 to 26 carbon atoms;

[0289] A represents a radical from the group CH2CH2, -CH2CH2-CH2, -CH2- CH(CH3), and w represents values ​​between 1 and 120, preferably 10 to 80, in particular 20 to 40.

[0290] The group of these non-ionic surfactants includes, for example, the C4-22 fatty alcohol (EO)io-ao-2-hydroxyalkyl ethers, in particular the C8-12 fatty alcohol (EO)22-2-hydroxydecyl ethers and the C4-22 fatty alcohol (EO)40-80-2-hydroxyalkyl ethers.

[0291] The weight proportion of the non-ionic surfactant in the total weight of the cleaning agent preparation C is preferably from 1.0 to 20 wt.%, preferably from 2.0 to 18, particularly preferably from 4.0 to 15 wt.% and in particular from 6.0 to 12 wt.%.

[0292] In a further particularly preferred embodiment, at least one cleaning agent preparation, in particular at least one cleaning agent preparation further comprising a nonionic surfactant, particularly preferably at least cleaning agent preparation B and / or D, contains at least one hydrotrope (hereinafter also referred to as solubilizer). Preferred hydrotropes are xylenesulfonate, cumenesulfonate, urea and / or AAmethylacetamide, particularly preferably cumenesulfonate and / or xylenesulfonate, in particular cumenesulfonate. It has been found that the use of hydrotropes, in particular cumenesulfonate, enormously improves phase stability with regard to temperature fluctuations. This is particularly observed for preparations containing at least one nonionic surfactant.It is particularly preferred that at least the cleaning agent preparation C, in particular the cleaning agent preparations C and B, contains at least one hydrotrope, preferably xylenesulfonate, cumenesulfonate, urea and / or A / - methylacetamide, particularly preferably cumenesulfonate and / or xylenesulfonate, in particular cumenesulfonate, preferably in an amount of 2 to 25% by weight, in particular of 4 to 20% by weight and particularly preferably in an amount of 6 to 15, for example of 7 to 12% by weight, based on the total weight of the respective cleaning agent preparation.

[0293] The weight ratio of the at least one non-ionic surfactant to the at least one hydrotrope, preferably xylenesulfonate, cumenesulfonate, urea and / or A / - methylacetamide, particularly preferably cumenesulfonate and / or xylenesulfonate, in particular cumenesulfonate, is preferably 2:1 to 1:2, in particular 1.6:1 to 1:1. The cleaning agent preparation C preferably contains less than 1% by weight, preferably less than 0.5% by weight, in particular less than 0.1% by weight of enzyme preparation and / or less than 2 mg of active enzyme protein / g of composition, preferably less than 1 mg of active enzyme protein / g of composition, in particular less than 0.5 mg of active enzyme protein / g of composition, particularly preferably the cleaning agent preparation C contains less than 0.1 mg of active enzyme protein / g of composition. Most preferably the cleaning agent preparation C contains no enzyme preparation.

[0294] The combination of cleaning agents described above is packaged using a packaging medium in which the cleaning agent preparations A, B, and C are separated from one another. This separation can be achieved, for example, by separate compartments, each of which contains one of the combined cleaning agents. Examples of such packaging forms are cartridges with two, three, four, or more separate compartments, for example, two-, three-, four-, or multi-chamber bottles. By separating the cleaning agents of different compositions, undesirable reactions due to chemical incompatibility can be excluded.

[0295] A further subject matter of the present application is a cleaning agent offer form, comprising a) a cleaning agent preparation A according to the invention in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; b) at least one further cleaning agent preparation B different from A in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; c) optionally a further cleaning agent preparation C different from A and B in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; e) a cartridge for the cleaning agent preparations A and B orA, B and C, in which the cleaning agent preparations A, B or A, B, C are present in separate receiving chambers.

[0296] The present application further provides a detergent dosing system comprising a) a detergent preparation A according to the invention in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; b) at least one further detergent preparation B different from A in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; c) optionally a detergent preparation C different from A and B in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; d) a cartridge for the detergent preparations A and B orA, B and C, in which the cleaning agent preparations A and B or A, B and C are present in separate receiving chambers; e) a dosing device detachably connected to the cartridge.

[0297] In a preferred embodiment, the previously described cartridges of the cleaning agent packages are provided with a dosing device that can be detachably connected to the cartridge. Such a dosing device can be connected to the cartridge, for example, by means of an adhesive, locking, snap-in, or plug-in connection. Separating the cartridge and dosing device simplifies, for example, filling the cartridge. Alternatively, the detachable connection between the cartridge and dosing device allows the cartridges to be replaced at the dosing device. Such a replacement may be necessary, for example, when changing the cleaning program or after the cartridge has been completely emptied.

[0298] A particularly preferred subject matter of this application is a detergent dosing system comprising a) a detergent dosage form according to the invention, comprising a quantity of detergent preparations A and B or A, B and C sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; b) a dosing device detachably connected to the detergent dosage form.

[0299] Of course, cleaning agent delivery forms are also conceivable in which the cartridge and the dosing device are inseparably connected to one another.

[0300] The present application further provides a detergent dosing system, comprising a) a detergent dosage form according to the invention, comprising a quantity of detergent preparations A and B or B which is sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times.A, B and C; b) a dosing device permanently connected to the cleaning agent packaging The aforementioned cleaning agent dosing systems, comprising the cleaning agent packaging according to the invention (and optionally one or two further compositions different from the cleaning agent preparations A and B and C according to the invention, a cartridge and a dosing device detachably connected to the cartridge are, in a preferred embodiment, present in a common outer packaging, wherein the filled cartridge and the dosing device are particularly preferably contained separately from one another in the outer packaging. The outer packaging serves for the storage, transport and presentation of the cleaning agent packaging according to the invention and protects it from soiling, impact and shock. In particular for the purpose of presentation, the outer packaging should be at least partially transparent.

[0301] Alternatively, or in addition to outer packaging, it is of course possible to market the cleaning agent packaging according to the invention in conjunction with a dishwasher. Such a combination is particularly advantageous in cases where the course of the automatic dishwashing process (e.g., duration, temperature profile, water supply) and the cleaning agent formulation or the control electronics of the dosing device are coordinated.

[0302] The dosing system according to the invention consists of the basic components of a cartridge filled with the cleaning agent according to the invention and a dosing device that can be coupled to the cartridge, which in turn is formed from further components, such as a component carrier, actuator, closure element, sensor, energy source and / or control unit.

[0303] It is preferred that the dosing system according to the invention be movable. Movable in the sense of this application means that the dosing system is not permanently connected to a water-conducting device such as a dishwasher or the like, but rather can be removed from a dishwasher by the user or positioned in a dishwasher, i.e., can be handled independently.

[0304] According to an alternative embodiment of the invention, it is also conceivable that the dosing device is not detachably connected to a water-conducting device such as a dishwasher or the like for the user and only the cartridge is movable.

[0305] Since the preparations to be dispensed can have a pH value between 2 and 14, in particular between 2 and 12, depending on their intended use, all components of the dispensing system that come into contact with the preparations should have appropriate acid and / or alkali resistance. Furthermore, these components should be largely chemically inert, for example, against non-ionic surfactants, enzymes and / or fragrances, through a suitable selection of materials. A cartridge within the meaning of this application is understood to be a packaging means suitable for enclosing or holding together flowable or spreadable preparations and which can be coupled to a dispensing device for dispensing the preparation. In particular, a cartridge can also comprise several chambers that can be filled with different compositions. It is also conceivable for a plurality of containers to be arranged to form a cartridge unit.

[0306] It is advantageous for the cartridge to have at least one outlet opening arranged in such a way that a gravity-induced release of the preparation from the container can be achieved when the dosing device is in the use position. This eliminates the need for additional conveying means to release the preparation from the container, thus keeping the design of the dosing device simple and manufacturing costs low.

[0307] In a preferred embodiment of the invention, at least one second chamber is provided for accommodating at least one second flowable or spreadable preparation, wherein the second chamber has at least one outlet opening arranged such that gravity-induced product release from the second chamber is achieved in the use position of the dosing device. The provision of a second chamber is particularly advantageous when preparations are stored in the separate containers that are not usually stable together, such as bleaching agents and enzymes.

[0308] Furthermore, according to the invention, it is necessary that more than two, in particular three, four, or five chambers are provided in or on a cartridge. In particular, at least one of the chambers for releasing active ingredient(s) C, such as a glass corrosion inhibitor, a fragrance, or in particular an odor neutralizer, into the environment is designed to have openings through which the rinsing solution and / or air can flow.

[0309] In a further embodiment of the invention, the cartridge is formed in one piece. This allows the cartridges to be produced cost-effectively in a single manufacturing step, particularly using suitable blow-molding processes. The chambers of a cartridge can be separated from one another, for example, by webs or material bridges.

[0310] The cartridge can also be formed from multiple pieces made of injection-molded components that are subsequently assembled. Furthermore, it is conceivable for the cartridge to be formed from multiple pieces such that at least one chamber, preferably all chambers, can be individually removed from the dosing device or inserted into the dosing device. This makes it possible, if a preparation is consumed at different levels from one chamber, to replace an already empty chamber while the others, which may still be filled with preparation, remain in the dosing device. This allows for targeted and needs-based refilling of the individual chambers or their preparations.

[0311] The chambers of a cartridge can be secured to one another by suitable connection methods, forming a container unit. The chambers can be releasably or permanently secured to one another by a suitable positive, non-positive, or material connection.

[0312] In particular, the fixation can be achieved by one or more of the following connection types: snap-in connections, hook-and-loop connections, press connections, melt connections, adhesive connections, welded connections, soldered connections, screw connections, wedge connections, clamp connections, or impact connections. In particular, the fixation can also be achieved by a shrink tube (so-called sleeve), which is pulled over the entire cartridge or sections of it in a heated state and tightly encloses the chambers or cartridge when cooled.

[0313] To ensure advantageous residual emptying properties of the chambers, the bottom of the chambers can be funnel-shaped and inclined toward the dispensing opening. Furthermore, the inner wall of a chamber can be designed, through a suitable choice of material and / or surface configuration, to minimize adhesion of the preparation to the inner chamber wall. This measure can also further optimize the residual emptying properties of a chamber.

[0314] The chambers of a cartridge can have the same or different filling volumes. In a two-chamber configuration, the container volume ratio is preferably 5:1, and in a three-chamber configuration, it is preferably 4:1:1. These configurations are particularly suitable for use in dishwashers.

[0315] As mentioned above, the cartridge preferably has 3, 4, 5, or 6 chambers. For use of such a cartridge in a dishwasher, it is particularly preferred that the first chamber contains an alkaline cleaning preparation, the second chamber an enzymatic preparation, and the third chamber a rinse aid, with the volume ratio of the chambers being approximately 4:1:1. The fourth chamber contains the at least one active ingredient composition, comprising the at least one active ingredient and a carrier material, preferably a water-insoluble carrier material.

[0316] A dosing chamber can be formed in or on a chamber, upstream of the outlet opening in the direction of flow of the preparation. The dosing chamber determines the amount of preparation to be released from the chamber into the environment. This is particularly advantageous if the closure element of the dosing device, which releases the preparation from a chamber to the environment, can only be set to a release and a closed state without control of the release amount. The dosing chamber then ensures that a predefined amount of preparation is released without direct feedback of the released amount of preparation. The dosing chambers can be formed as a single piece or in multiple pieces.

[0317] According to a further advantageous development of the invention, one or more chambers each have a liquid-tight sealable chamber opening in addition to an outlet opening. This chamber opening makes it possible, for example, to refill the preparation stored in this chamber.

[0318] To ventilate the cartridge chambers, ventilation options can be provided, particularly in the head area of ​​the cartridge, to ensure pressure equalization between the interior of the cartridge chambers and the environment as the fill level drops. These ventilation options can be designed, for example, as a valve, particularly a silicone valve, micro-openings in the cartridge wall, or the like.

[0319] If, according to a further embodiment, the cartridge chambers are not ventilated directly, but rather via the dosing device, or no ventilation is provided, e.g., when using flexible containers such as bags, this has the advantage that, at elevated temperatures during a dishwasher cycle, the heating of the chamber contents builds up pressure, which pushes the preparations to be dispensed toward the outlet openings, thus ensuring good residual emptying of the cartridge. Furthermore, with such air-free packaging, there is no risk of oxidation of the preparation's substances, which makes bag packaging or bag-in-bottle packaging particularly suitable for oxidation-sensitive preparations.

[0320] The cartridge typically has a filling volume of <5,000 ml, in particular <1,000 ml, preferably <500 ml, particularly preferably <250 ml, most particularly preferably <50 ml.

[0321] The cartridge can take on any spatial shape. For example, it can be cube-shaped, spherical, or plate-shaped.

[0322] The cartridge and the dosing device can in particular be designed with regard to their spatial shape in such a way that they ensure the lowest possible loss of useful volume, in particular in a dishwasher.

[0323] To use the dosing device in dishwashers, it is particularly advantageous to design the device to resemble dishes to be cleaned in dishwashers. For example, these can be plate-shaped, roughly the size of a plate. This allows the dosing device to be positioned in a space-saving manner, for example in the lower basket of the dishwasher. Furthermore, the plate-like shape makes the correct positioning of the dosing unit immediately and intuitively clear to the user. The cartridge preferably has a height:width:depth ratio of between 5:5:1 and 50:50:1, particularly preferably of approximately 10:10:1. The “slim” design of the dosing device and the cartridge makes it possible, in particular, to position the device in the lower cutlery basket of a dishwasher in the receptacles provided for plates.This has the advantage that the preparations dispensed from the dosing device go directly into the dishwashing water and cannot adhere to other items being washed.

[0324] Commercially available household dishwashers are typically designed to accommodate larger items, such as pans or large plates, in the lower basket. To prevent the user from positioning the dosing system incorrectly in the upper basket, an advantageous embodiment of the invention allows the dosing system to be positioned only in the designated receptacles of the lower basket. For this purpose, the width and height of the dosing system can be selected, in particular, between 150 mm and 300 mm, and particularly preferably between 175 mm and 250 mm.

[0325] However, it is also conceivable to design the dosing unit in the shape of a cup with an essentially circular or square base.

[0326] In order to protect heat-sensitive components of a preparation contained in a cartridge from the effects of heat, it is advantageous to manufacture the cartridge from a material with low thermal conductivity.

[0327] Another possibility for reducing the influence of heat on a preparation in a chamber of the cartridge is to insulate the chamber by suitable measures, e.g. by using thermal insulation materials such as polystyrene, which completely or partially enclose the chamber or the cartridge in a suitable manner.

[0328] In a preferred embodiment of the invention, the cartridge has an RFID label that contains at least information about the contents of the cartridge and that can be read by the sensor unit.

[0329] This information can be used to select a dosing program stored in the control unit. This ensures that the optimal dosing program for a specific preparation is always used. It can also be configured that if an RFID label is not present, or if the RFID label contains an incorrect or faulty identifier, the dosing device will not dispense any liquid and instead generate a visual or acoustic signal to alert the user to the error.

[0330] To prevent misuse of the cartridge, the cartridges can also have structural elements that interact with corresponding elements of the dosing device according to the key-lock principle, so that, for example, only cartridges of a specific type can be coupled to the dosing device. Furthermore, this design makes it possible for information about the cartridge coupled to the dosing device to be transmitted to the control unit, allowing the dosing device to be controlled in a way that is tailored to the contents of the corresponding container.

[0331] The cartridge is particularly designed to hold flowable cleaning agents. Such a cartridge particularly preferably has a plurality of chambers for spatially separating different preparations of a cleaning agent. The cartridge can be designed so that it can be arranged detachably or permanently in or on the dishwasher. The control unit, sensor unit, and at least one actuator required for operation are integrated into the dosing device. A power source is also preferably arranged in the dosing device.

[0332] Preferably, the dosing device consists of a splash-proof housing that prevents splash water from penetrating into the interior of the dosing device, such as can occur when used in a dishwasher.

[0333] It is particularly preferred that the dosing device comprises at least one first interface which interacts with a corresponding interface formed in or on a water-conducting device, in particular a water-conducting household appliance, preferably a dishwasher, in such a way that a transmission of electrical energy from the water-conducting device to the dosing device is realized.

[0334] In one embodiment of the invention, the interfaces are formed by connectors. In a further embodiment, the interfaces can be designed to enable wireless transmission of electrical energy.

[0335] In an advantageous further development of the invention, a second interface is formed on the dosing device and the water-conducting device, such as a dishwasher, for transmitting electromagnetic signals which represent, in particular, operating state, measurement and / or control information of the dosing device and / or the water-conducting device, such as a dishwasher.

[0336] An adapter allows for easy connection of the dosing system to a water-using household appliance. The adapter serves to mechanically and / or electrically connect the dosing system to the water-using household appliance.

[0337] The adapter is preferably permanently connected to a water line of the household appliance. However, it is also conceivable to position the adapter in or on the household appliance, where it is exposed to the water flow and / or spray jet of the household appliance.

[0338] The adapter makes it possible to implement a dosing system in both a standalone and a built-in version. It is also possible to configure the adapter as a charging station for the dosing system, where, for example, the dosing device's power source is charged or data is exchanged between the dosing device and the adapter.

[0339] The adapter can be arranged in a dishwasher on one of the inner walls of the washing chamber, in particular on the inner side of the dishwasher door. However, it is also conceivable for the adapter as such to be positioned in the water-conducting household appliance so that it is not accessible to the user, so that the dosing device is inserted into the adapter, for example, during assembly of the household appliance, wherein the adapter, the dosing device, and the household appliance are designed such that a cartridge can be coupled to the dosing device by the user. The cleaning agent packaging forms according to the invention are suitable for use in dishwashing; however, the use of a cleaning agent packaging form according to the invention or a cleaning agent dosing system for dishwashing in a machine dishwashing process is preferred.

[0340] As stated at the outset, the cleaning agents according to the invention are characterized by particular physical and chemical stability, particularly with respect to temperature fluctuations. The cleaning agents according to the invention are therefore exceptionally suitable for dosing using a dosing system located in the interior of a dishwasher. Such a dosing system, which can be integrated immovably into the interior of the dishwasher (machine-integrated dosing device), but can of course also be introduced into the interior as a movable device (self-contained dosing device), contains several times the amount of cleaning agent required to carry out a machine cleaning process.

[0341] Movable within the meaning of this application means that the dispensing and dosing system is not permanently connected to a device such as a dishwasher or the like, but is, for example, removable from a dishwasher or positionable in a dishwasher.

[0342] The use of a detergent dosage form according to the invention for filling i) a cartridge of a dosing system that is immovably integrated into the interior of a dishwasher or ii) a movable cartridge of a dosing system that is intended to be positioned in the interior of a dishwasher with a quantity of this detergent dosage form that is sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times are also the subject matter of this application.

[0343] An example of a fixed cartridge is a container that is permanently integrated into the interior of a dishwasher, for example, into the side panel or the interior panel of the door. An example of a movable cartridge is a container that is inserted into the interior of the dishwasher by the consumer and remains there throughout the entire cleaning cycle. Such a cartridge can be integrated into the interior, for example, by simply placing it in the cutlery or dish basket, but can also be removed from the interior of the dishwasher by the consumer.

[0344] As described above, the detergent or detergent combination is preferably dispensed from the cartridge into the dishwasher's interior using a dosing device that can be removed from the cartridge. Such a dosing device can be connected to the cartridge using an adhesive, locking, snap-in, or plug-in connection. However, cartridges with a permanently attached dosing device are also acceptable.

[0345] The use of a detergent formulation according to the invention as a detergent reservoir for i) a dosing device fixedly integrated into the interior of a dishwasher or ii) a movable dosing device intended for positioning in the interior of a dishwasher is preferred.

[0346] The use of a detergent dosing system according to the invention as a detergent reservoir for a dishwasher is a further subject of the present application.

[0347] Two further subjects of this application are the use of a cleaning agent offer form according to the invention, comprising a) a cleaning agent preparation A according to the invention in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; b) at least one further cleaning agent preparation B different from A in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; c) optionally a further cleaning agent preparation C different from A and B in an amount sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; d) a cartridge for the cleaning agent preparations A and B orA, B and C, in which the detergent preparations A, B or A, B, C are present in separate receiving chambers as a detergent reservoir for i) a dosing device fixedly integrated into the interior of a dishwasher or ii) a movable dosing device intended for positioning in the interior of a dishwasher.

[0348] The cleaning agents and cleaning agent combinations according to the invention are, as previously stated, preferably used as automatic dishwashing detergents.

[0349] Automatic dishwashing method using a detergent dispenser or a detergent dosing system according to one of the preceding claims, in the course of which a cartridge located in the interior of the dishwasher

[0350] - a partial amount a of the detergent preparation A contained in the cartridge is dosed into the interior of the dishwasher, whereby a residual amount of the detergent preparation contained in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount a; and

[0351] - a partial amount b of the detergent preparation B contained in the cartridge is dosed into the interior of the dishwasher, whereby a residual amount of the detergent preparation in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount b; and

[0352] - optionally a partial amount c of the cleaning agent preparation C contained in the cartridge is dosed into the interior of the dishwasher, wherein a residual amount of the active ingredient contained in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount c.

[0353] In the dishwashing processes according to the invention, it is of course possible to use not only the detergent delivery forms according to the invention, but also the detergent dosing systems according to the invention.

[0354] In a preferred embodiment, the dosage of cleaning agent preparation A and cleaning agent preparation B and optionally cleaning agent preparation C takes place at different times of the cleaning cycle.

[0355] A further preferred subject matter of this application is therefore a machine dishwashing process using a detergent dosage form according to the invention or a detergent dosing system according to the invention, in the course of which a) at a time t1 a partial amount a of the detergent preparation A according to the invention located in the cartridge is dosed into the interior of the dishwasher from a cartridge located in the interior of the dishwasher, wherein a residual amount of the detergent located in the cartridge remains in the cartridge until the end of the dishwashing process, which residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount a;b) at least one further time t2 11, a partial amount b of the cleaning agent preparation B, which is different from the cleaning agent preparation A according to the invention and is located in the second cartridge, is dosed into the interior of the dishwasher from a cartridge located in the interior of the dishwasher, wherein a residual amount of the cleaning agent located in this cartridge remains in the cartridge until the end of the dishwashing process, which residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount b;c) optionally at at least one further time t3 t2 11 a partial amount d of the detergent preparation C, which is different from the detergent preparations A and B according to the invention and is located in a further cartridge is dosed into the interior of the dishwasher from a cartridge located in the interior of the dishwasher, wherein a residual amount of the detergent located in this cartridge remains in the cartridge until the end of the dishwashing process, which residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount c.;

[0356] In preferred embodiments of the previously described automatic dishwashing processes with time-delayed dosing of the cleaning agent preparations A and B or A, B and C, the time t2 is at least 1 minute, preferably at least 2 minutes and in particular between 3 and 30 minutes, in particular between 3 and 20 minutes, before or after, preferably before the time t1. In preferred embodiments of the previously described automatic dishwashing processes with time-delayed dosing of the minute, preferably at least 2 minutes and in particular between 3 and 30 minutes, in particular between 3 and 20 minutes, before or after, preferably after the time t1.

[0357] In a preferred embodiment, cleaning preparation B is added to the interior at a temperature of 20-35°C, followed by cleaning preparation A at a temperature of 30-60°C and then cleaning preparation C at a temperature below 20°C.

[0358] In particularly preferred embodiments, the peptides described herein in the process according to the invention or in washing and / or cleaning agents according to the invention achieve improved cleaning performance on at least one greasy 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 and plastic), metal (e.g. cutlery or pots) or glass.

[0359] It is preferred that the improved cleaning performance of the method is based on the interaction of the peptide used according to the invention with a washing or cleaning agent which binds to at least one fat- and / or oil-containing, preferably fat-containing, soil on a textile, in particular containing or consisting of cotton, polyester and mixtures thereof, and preferably also removes this at least partially from the surface.

[0360] It is preferred that the improved cleaning performance of the method is based on the interaction of the peptide used according to the invention with a washing or cleaning agent which binds to at least one greasy and / or oil-containing, preferably greasy, soiling 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, and preferably also at least partially removes it from the surface.

[0361] It is preferred that the peptide used 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.

[0362] It is particularly preferred that the peptide according to the invention is surface-active and 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, wherein the surface activity is determined according to the bubble pressure method as described herein. In particular, the surfaces are freed of this soiling by the presence of the peptide, which is surface-active and binds to at least one grease-containing soil on the textile and / or the hard surface, wherein the surface activity is determined according to the bubble pressure method as described herein.

[0363] 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 fat film. This surfactant-like behavior makes the fat film easier to remove during the cleaning process. The softened fat can be detached (roll-up mechanism) and / or rinsed off. This mechanism could be explained by the surface-active behavior of peptides according to the invention, which is determined using the bubble pressure method as described herein. An example of such a peptide is a peptide with SEQ ID NO: 29.

[0364] Peptides used 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 that exhibit 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.

[0365] 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.

[0366] 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.

[0367] 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 80°C, more preferably about 15°C to about 60°C, particularly preferably at about 15°C to about 45°C, most preferably 20°C to about 30°C, especially preferably about 20°C.

[0368] 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.

[0369] 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.

[0370] 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.

[0371] Particularly suitable embodiments are described in the following points:

[0372] 1 . A method for removing grease, grease- and / or oil-containing soiling and / or greasy deposits from surfaces, characterized by the following steps: i) providing at least one peptide ii) bringing the peptide into contact with a grease- and / or oil-containing surface iii) rinsing the surface with water or an aqueous solution; characterized in that 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 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence

[0373] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0374] X1 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,

[0375] X 2 is selected from R, H and K, preferably R and K,

[0376] 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,

[0377] X 4 is selected from AL and V, preferably A and L,

[0378] 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; or b) 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0379] 2. Method according to point 1 , wherein the peptide

[0380] (i) has a total charge of 0 to +4, or

[0381] (ii) if r > 4, has a total charge of 0 to +4, or

[0382] (iii) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

[0383] 3. The method according to claim 1 or 2, wherein in the peptide according to point 1 a), 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 equal to Z 1 Z 2 Z 3 [(Z 4 )UZ 5 Z 6 ]3(Z 7 ) V is, where

[0384] Z 1 like X 2 defined in point 1 and selected from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined in point 1 and selected from A, L and V, preferably A and L,

[0385] Z 4 like X 3 defined in point 1 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,

[0386] Z 7 like X 5is defined in point 1 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 as s is defined in point 1 and is an integer from 0 to 4.

[0387] 4. Procedure according to point 3, whereby,

[0388] (i) if u = 1 , Z 4 is selected from R, E and Q, or

[0389] (ii) if u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0390] 5. Procedure according to point 3 or 4, whereby

[0391] (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

[0392] (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

[0393] (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or

[0394] (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0395] (v) the peptide comprises at least one, preferably two or three, RAL motif(s); and / or (vi) the peptide comprises the RAL motif at least twice and at least one of QAL or EAL, preferably both.

[0396] 6. The method according to claim 1 or 2, wherein in the peptide according to point 1a) or 2a), 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 )WZ 16 is, where

[0397] Z 11 like X 2 defined in point 1 or 2 and selected from R, H and K,

[0398] Z 12like X 3 defined in point 1 or 2 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,

[0399] Z 13 , Z 14 , Z 16 like X 4 defined in point 1 or 2 and selected from A, L and V, preferably A and L,

[0400] Z 15 like X 3 defined in item 1 or 2 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.

[0401] 7. Procedure according to point 6, whereby,

[0402] (i) z 13 Z 14 is selected from AL and LA, preferably AL; and / or

[0403] (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

[0404] (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

[0405] (iv) Z 16 is selected from A and L, preferably A.

[0406] 8. The method according to any one of items 1 to 7, 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.

[0407] 9. The method according to any one of points 1 to 8, 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, most preferably SEQ ID NOs: 1, 3, 5, 9, 10, 12, 29.

[0408] 10. The method according to items 1 to 8, 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 according to 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, most preferably SEQ ID NOs: 1, 3, 5, 9, 10, 12, 29. The method according to any one of items 1 to 10, wherein the peptide is surface-active. The method according to item 11, wherein the surface activity is determined by the bubble pressure method, preferably as described herein.Process according to item 11 or 12, wherein the dynamic surface tension shows a deviation of 2 or more mN / m, preferably of 5 or more mN / m, more preferably of 6 mN / m or more, particularly preferably of 8 mN / m or more, and most preferably of 10 or more mN / m. Process according to items 11 to 13, wherein the dynamic surface tension, measured using the bubble pressure method (preferably measured at 20°C, in a concentration range from 0.1 mg / l to 1 g / l, at pH 8.0), shows a deviation of 2 or more mN / m, preferably of 5 or more mN / m, more preferably of 6 mN / m or more, particularly preferably of 8 mN / m or more, and most preferably of 10 or more mN / m over the entire bubble lifetime. Method according to one of points 1 to 14, characterized in that the provision of the peptide in step i) takes place simultaneously with a washing or cleaning agent.Method according to item 15, characterized in that the provision of the peptide in step i) takes place in a washing or cleaning agent. Method according to one of items 1 to 16, characterized in that the dosage of the peptide takes place before and / or after the dosage of a washing or cleaning agent, preferably with a time difference of at least 1 minute, preferably of at least 5 minutes, particularly preferably of at least 10 minutes. Method according to one of items 1 to 17, characterized in that at least one of steps ii) or iii), preferably both steps ii) and iii), is carried out in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, in particular about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, for example about 20°C.Method according to one of the preceding points, characterized in that at least 1 minute, preferably at least 5 minutes, in particular at least 10 minutes, very particularly preferably at least 15 minutes, lie between the start of step ii) and the start of step iii). Method according to one of the preceding points, characterized in that the surface is selected from textiles and / or hard surfaces, wherein the textiles preferably consist of or contain natural and / or synthetic fibers, preferably cotton, viscose, silk, wool, and / or polyester, polyamide, polyurethane, and mixtures thereof; and / or wherein the hard surfaces preferably consist of or contain ceramic, metal, steel, stainless steel, plastic, glass, and mixtures thereof. Method according to one of the preceding points, characterized in that at least one, preferably all, of steps ii) and iii) are carried out in a water-conducting machine.Method according to one of the preceding points, characterized in that step i) is carried out in a water-conducting machine. Method according to point 22, characterized in that.

[0409] In step i), an aqueous solution comprising the peptide in an amount of 0.000001 ppm to 100 ppm is provided. Method according to one of the preceding points, characterized in that it is a method for dishwashing, preferably for manual and / or machine dishwashing, and the hard surfaces are selected from, consist of, or contain ceramic, metal, steel, stainless steel, plastic, synthetic material, glass, and mixtures thereof. Method according to point 24, characterized in that the soiled hard surfaces are dishes (preferably selected from earthenware, porcelain, plastic), glasses, pots, and / or pans. Method according to one of points 1 to 25, characterized in that it is a method for textile cleaning, in particular a machine textile cleaning method, in particular a machine textile washing method.Cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, characterized in that it is used in a method according to one of the preceding points. Cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, containing at least one peptide, characterized in that 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 12 to 18 amino acids, wherein the peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence.

[0410] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t where

[0411] 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,

[0412] X 2 is selected from R, H and K, preferably R and K,

[0413] 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,

[0414] X 4 is selected from AL and V, preferably A and L,

[0415] 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

[0416] 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; or b) 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. A cleaning agent, preferably a dishwashing agent, particularly preferably an automatic dishwashing agent, characterized in that it contains at least one peptide as defined in any one of points 1 to 14, or as described in a process of the above points 1 to 14, or as used in any one of the processes of the above processes according to points 1 to 14.Cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, according to items 27 to 29, characterized in that it contains at least one peptide in an amount of 0.000001 to 3.5 wt. %, preferably 0.00001 to 2.5, in particular 0.00001 to 2.0 wt. %. 31. Cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, according to items 27 or 30, characterized in that it contains at least one active ingredient selected from builders, preferably selected from carbonates, bicarbonates, silicates and / or citrates; complexing agents, preferably selected from phosphonic acid and / or aminopolycarboxylic acids and their salts; bleaching agents, bleach activators and / or bleach catalysts.

[0417] 32. Cleaning agent, preferably dishwashing agent, in particular automatic dishwashing agent, preferably according to one of points 27 to 31, comprising a) a cleaning agent preparation A which is liquid at 20°C and contains a1) builder; a2) complexing agent b) a cleaning agent preparation B which is different from the cleaning agent preparation A and is liquid at 20°C and has a water content above 1% by weight, containing b1) at least one cleaning-active enzyme, preferably 0.00001 to 2.0% by weight, preferably 0.0001 to 1.5, in particular 0.001 to 1.0% by weight of active protein based on the total weight of the cleaning agent preparation B; b2) contains at least one peptide according to one of points 1 to 10, preferably in an amount of 0.000001 to 8.0 wt.%, preferably 0.00001 to 5.0 wt.%, in particular 0.00001 to 4.0 wt.%, based on the total weight of the cleaning agent preparation B.and a packaging in which the cleaning agent preparations A and B are present separately from each other.

[0418] 33. Cleaning agent according to item 32, characterized in that the cleaning agent preparation A, based on its total weight, contains 2 to 50 wt.%, preferably 6 to 45 wt.% and in particular 10 to 40 wt.% builder and / or the builder a1) is selected from the group of carbonates, hydrogen carbonates, citrates, silicates and polymeric carboxylates.

[0419] 34. Cleaning agent according to one of points 32 or 33, characterized in that the complexing agent a2) is selected from the group consisting of hydroxyethylethylenediaminetriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, glutamic acid diacetic acid, in particular L-glutamic acid A / . / V-diacetic acid, iminodisuccinic acid, hydroxyiminodisuccinic acid, methylglycinediacetic acid, aspartic acid diacetic acid, hydroxyethane-1,1-diphosphonic acid or diethylenetriaminepenta(methylenephosphonic acid) and salts thereof or mixtures thereof, preferably L-glutamic acid A / . / V-diacetic acid and / or methylglycinediacetic acid and salts thereof and / or the cleaning agent preparation A contains 2 to 60% by weight, preferably 4 to 55% by weight and in particular 8 to 50% by weight of complexing agent.

[0420] 35. Cleaning agent according to one of items 32 to 34, characterized in that the cleaning agent preparation B contains a cleaning-active enzyme from the group of amylases and / or proteases and / or cellulases and / or hemicellulases and / or lipases, in particular amylases and / or proteases.

[0421] 36. Cleaning agent according to one of items 32 to 35, characterized in that the cleaning agent preparation B contains surfactants in each case in an amount of 1 to 35 wt.%, in particular 3 to 30 wt.%, based on the total weight of the preparation B.

[0422] 37. Cleaning agent according to one of points 32 to 36, characterized in that the cleaning agent preparation B, based on its total weight, contains 30 wt.% and less, preferably 25 wt.% and less, in particular 15 wt.% and less of water and / or the cleaning agent preparation B contains organic solvent, preferably selected from glycerol, 1,2-propylene glycol, 1,3-propylene glycol, dipropylene glycol and polyethylene glycols, in particular 1,2-propylene glycol, wherein the weight fraction of the 1,2-propylene glycol, based on the total weight of the cleaning agent preparation, is preferably 5 to 80 wt.%, more preferably 10 to 60 wt.% and in particular 20 to 50 wt.%.

[0423] 38. Cleaning agent presentation form, comprising cleaning agent preparations A and B according to any one of points 32 to 36 and additionally c) a cleaning agent preparation C which is liquid at 20°C and different from the cleaning agent preparations A and B, containing c1) an acidifying agent, c2) a glass corrosion inhibitor, c3) optionally a non-ionic surfactant, c4) optionally a hydrotrope, and c5) optionally less than 1% by weight, preferably less than 0.5% by weight, in particular less than 0.1% by weight of enzyme preparation, and d) a packaging means in which the cleaning agent preparations A, B and C are present separately from one another.

[0424] 39. Cleaning agent packaging according to item 38, characterized in that the cleaning agent preparation C contains the acidifying agent c1) selected from formic acid, tartaric acid, succinic acid, malonic acid, adipic acid, maleic acid, fumaric acid, oxalic acid and / or polyacrylic acid, in particular formic acid, acetic acid and / or citric acid, and / or the cleaning agent preparation C contains the acidifying agent c1) preferably in amounts of 0.1 to 12% by weight, particularly preferably 0.2 to 10% by weight and in particular 0.3 to 8.0% by weight, in each case based on the total weight of the cleaning agent preparation C.

[0425] 40. Cleaning agent packaging according to one of claims 38 to 39, characterized in that the cleaning agent preparation C, the glass corrosion inhibitor c2) is selected from polyalkyleneimines, in particular polyethyleneimines, and / or water-soluble zinc salts, preferably zinc chloride, zinc sulfate and / or zinc acetate, particularly preferably zinc acetate, and / or the cleaning agent preparation C contains the glass corrosion inhibitor c2) preferably in amounts of 0.01 wt.% to 5 wt.%, particularly preferably 0.05 wt.% to 3 wt.%, in particular 0.1 wt.% to 2 wt.%, based on the total weight of the cleaning agent preparation C.

[0426] 41. Cleaning agent packaging according to one of items 38 to 40, characterized in that the cleaning agent preparation C, the hydrotrope c3) is selected from xylenesulfonate, cumenesulfonate, urea and / or / V-methylacetamide, particularly preferably cumenesulfonate and / or xylenesulfonate, in particular cumenesulfonate, and / or the cleaning agent preparation C contains the hydrotrope c3) in an amount of 2 to 25 wt.%, in particular of 4 to 20 wt.% and particularly preferably in an amount of 6 to 15, for example of 7 to 12 wt.%, based on the total weight of the cleaning agent preparation C.

[0427] 42. Cleaning agent packaging according to one of items 38 to 41, characterized in that the cleaning agent preparation C contains surfactants, preferably non-ionic surfactants in an amount of 1 to 35 wt.%, in particular 3 to 30 wt.%, particularly preferably 7 to 12 wt.%, based on the total weight of the cleaning agent preparation C.

[0428] 43. Use of a cleaning agent according to any one of claims 28 to 37 or a cleaning agent presentation form according to any one of points 38 to 42 as a cleaning agent reservoir for i) a dosing device fixedly integrated into the interior of a dishwasher or ii) a movable dosing device intended for positioning in the interior of a dishwasher.

[0429] 44. Use of a cleaning agent according to any one of points 28 to 37 or a cleaning agent packaging according to any one of points 38 to 42 for filling i) a cartridge of a dosing system which is immovably integrated into the interior of a dishwasher or ii) a movable cartridge of a dosing system which is intended to be positioned in the interior of a dishwasher with a quantity of this cleaning agent packaging which is sufficient for carrying out a machine dishwashing process or a machine textile washing process at least twice, preferably at least four times and in particular at least eight times.

[0430] 45. Detergent dosing system, comprising a) a detergent according to any one of items 28 to 37 or a detergent packaging according to any one of items 38 to 42, comprising a quantity of detergent preparations A and B or A, B and C sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times, and in particular at least eight times; b) a dosing device detachably connected to the detergent packaging.

[0431] 46. ​​Use of a cleaning agent, preferably dishwashing agent, particularly preferably automatic dishwashing agent, according to one of items 28 to 37, a cleaning agent presentation form according to one of items 38 to 42 or a cleaning agent dosing system according to item 45 for cleaning dishes in an automatic dishwashing process.

[0432] 47. Automatic dishwashing process using a detergent according to one of points 28 to 37, a detergent packaging form according to one of points 38 to 42 or a detergent dosing system according to point 45, in the course of which a partial amount a of the detergent preparation A contained in the cartridge is dosed into the interior of the dishwasher from a cartridge located in the interior of the dishwasher, wherein a residual amount of the detergent preparation in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount a;and a partial amount b of the cleaning agent preparation B contained in the cartridge is dosed into the interior of the dishwasher, wherein a residual amount of the cleaning agent preparation contained in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of partial amount b; and optionally a partial amount c of the cleaning agent preparation C possibly contained in the cartridge is dosed into the interior of the dishwasher, wherein a residual amount of the cleaning agent preparation contained in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of partial amount c.

[0433] EXAMPLES

[0434] Example 1 : Peptide sequences

[0435] The peptides shown in Table 2 were prepared by chemical synthesis.

[0436] Table 2: Peptide names and corresponding amino acid sequences

[0437] Example 2: Testing the adhesion of peptides with regard to their substrate specificity to fats

[0438] 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.

[0439] The following pre-soiled textile rags were used (ex. CFT, Center For Test Material):

[0440] C-FF CS46, Frying Fat, used, Cotton (frying fat on cotton)

[0441] P-FF PS46, Frying Fat, used, Polyester (frying fat on polyester)

[0442] CO2, Olive Oil with carbon black with thickening agent, Cotton (olive oil on cotton)

[0443] PO P02, Olive Oil with carbon black with thickening agent, Polyester (olive oil on polyester)

[0444] CS CS32, Sebum Bey with Carbon black, Cotton (Sebum on cotton)

[0445] PS PS32, Sebum Bey with Carbon black, Polyester (Sebum on Polyester)

[0446] For the study, three textile patches (each approximately 10 mm in diameter) were placed twice in 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.

[0447] The results are shown 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. A difference of 5% or more is considered significant.

[0448] Table 3: Adhesion results

[0449] 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. Peptide P32, which was not used according to the invention, exhibits no adhesion to greasy and / or oily soils.

[0450] Example 3: Testing the adhesion of peptides to fats and subsequent fat detachment

[0451] In another experiment, the substrate specificity of some peptides with regard to their adhesion to fat was investigated using a quartz crystal microbalance with dissipation monitoring (QCM-D for short; QCM = quartz crystal microbalance; D = dissipation). Using this surface-sensitive method, the adsorption and desorption processes of materials or substances (as well as the associated processes, e.g., swelling) on ​​a sensor surface can 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 (thin gold layer on both sides). 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 disc, by measuring changes in the resonance frequency over time, conclusions can be drawn 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.eom / qsense / instruments / qsense-pro#knowledqe).

[0452] Implementation:

[0453] The quartz sensors of the quartz crystal microbalance (QSense Analyzer in the QSense Flow module QFM 401, ex. QSense®) were prepared for the investigation by cleaning the quartz sensors with a hydrogen peroxide-ammonia-Millipore water solution (ratio 1:1:5) at 75°C, the frequencies and dissipations of the fundamental tone and the overtones of the cleaned quartz sensors were measured in air at 20°C (termination criterion: temporally constant values ​​for frequency and dissipation, ie the frequency and dissipation were determined over a time course at which the system had adjusted to a stable frequency and dissipation).

[0454] The quartz sensors were then spin-coated with a model grease solution (1% tricaprin in toluene). 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, Olesen 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). Subsequently, the frequencies and dissipations of the fundamental tone and the overtones of the grease-coated quartz sensors were measured in air.

[0455] The measuring cell was then filled with Millipore water and the frequencies and dissipations of the fundamental tone and the overtones of the grease-coated quartz sensors were measured in water at 20°C (baseline). The respective solution of the peptide in Millipore water was then passed through at 20°C and a flow rate of 50 pl / min. The frequencies and dissipations of the fundamental tone and the overtones of the grease-coated quartz sensors were measured over time (termination criterion: temporally constant values ​​for frequency and dissipation).

[0456] To restore the sensor, the measuring cell is rinsed with a 2% aqueous surfactant solution after the measurement has been completed.

[0457] As exemplary peptides, peptides P12 and P29 were tested in different concentrations (from 0.07 mg / l to 0.4 mg / l).

[0458] Evaluation:

[0459] The average amount of fat mass applied to the sensor can be determined from the QCM-D measurement in air as the difference between the frequencies of the coated and uncoated sensors using the Sauerbrey equation (average value over all oscillations, ie the average value over the frequencies of the fundamental tone or the overtones).

[0460] Am = -C— n (Sauerbrey equation)

[0461] 4m: Change in mass per cm 2 ;

[0462] 4f: change in resonance frequency; n: number of the oscillation (fundamental or overtone);

[0463] C: mass sensitivity constant;

[0464] Figure 1 below shows the difference between the QCM-D measurements with the peptide P12 and the measurement without peptide (fat layer in Millipore water). The average mass of the applied fat layer / cm 2 , calculated according to the Sauerbrey equation, was 2300 ng / cm 2The concentration of the peptide solution was 0.364 mg / l.

[0465] The frequency changes as well as the dissipation due to the adhesion of the peptides to the fat layer (as well as the detachment of the fat layer from the sensor itself) are clearly visible (approx. 1 h).

[0466] Initially, the frequency or dissipation is reduced below the baseline by the added mass of the adhering peptide (the greater the magnitude of this frequency change, the greater the added mass of peptide on the sensor). As the experiment progresses, a progressive change in the frequency or dissipation beyond the baseline can be observed. This increase in frequency (or dissipation) means that the fat layer is increasingly detaching from the sensor (the mass on the sensor is reduced).

[0467] Thus, detachment / removal of the fatty and / or oily soiling from the surface is achieved by bringing it into contact with the peptides according to the invention. The QCM-D measurements described above also correspond to the observations that could be made with the naked eye with the peptides according to SEQ ID NO: 1, 3, 5, 9, 10, 12, 29. Before the coated quartz sensor comes into contact with the peptide, the presence of the fatty layer is visible. After the end of the measurement (before rinsing), the fatty layer is completely detached and the gold layer of the sensor is visible again. This also shows that the peptides used according to the invention act on fatty and / or oily soiling that adheres to a surface and additionally cause the fat to be removed from this surface.

[0468] Example 4: Determining the interfacial activity

[0469] 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 in liquids will be measured. 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. In this case, the dynamic surface tension is determined using the bubble pressure method. For this purpose, a volume flow of air is introduced into the liquid to be measured through a capillary, creating an air bubble. The pressure curve of the bubble formation can then be used to draw conclusions about the dynamic surface tension using the Young-Laplace equation.

[0470] First, the science line t100 laboratory tensiometer is calibrated with distilled water. Once a constant value of 72.7 mN / m is measured over various bubble lifetimes (72.7 mN / m corresponds to the reference value of water at 20°C, source: https: / / www.sita-messteclmik.de / wissen / oberflaechensDannung), the sample fluid can be measured. To do this, the capillary is immersed in the sample fluid and the measurement is started over various bubble lifetimes. The following parameters were used for the measured sample fluids: pH = 8.0 (10 mM TRIS-HCl buffer); CKCl = 50 mM; cpeptide = 10 pM (peptide); T = 22°C

[0471] 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. It is advisable to increase the concentration of the peptide in the measurement solution, unless obvious surface activity is already present (concentration series). 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 of the invention.

[0472] In the context of the invention, "surface-active" is understood to mean a substance in which the dynamic surface tension, determined using the bubble pressure method, shows a deviation of 2 or more mN / m, preferably of 5 or more mN / m, more preferably of 6 mN / m or more, particularly preferably of 8 mN / m or more, and most preferably of 10 or more mN / m over the entire bubble lifetime (preferably measured at 20 °C, in a concentration range of 0.1 mg / l to 1 g / l, at pH 8.0; particularly preferably measured 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).

[0473] Example 5: Exemplary detergent and cleaning agent formulations

[0474] The at least one peptide according to the invention can be used in various washing and cleaning compositions and realize its effect.

[0475] Table 4: Liquid detergents Table 5: Solid detergents

[0476] Table 6: Two-phase solid dishwasher detergents

[0477]

[0478] Table 7: Solid dishwasher detergents

[0479] Active ingredient content in % by weight (unless otherwise stated), based on the

[0480] Table 8: Single-phase liquid dishwasher detergents

[0481]

[0482] Table 9: Two-phase liquid automatic dishwashing detergents in separate compartments (wt% active ingredient)

[0483] The respective enzyme phase is mixed with the respective alkali phase in a ratio of 1 :1, total weight 30 g, from a two-chamber bottle directly into the dosing chamber of an automatic dishwasher and

[0484] Table 10: Multiphase, liquid detergent combination. Suitable for automatic dosing, preferably in dishwashers in separate compartments.

[0485] Active ingredient content in wt.%, based on the total weight of the respective phase (cleaning agent C according to this table may, but does not necessarily have to, be included)

[0486]

[0487] Table 11 : Cleaning agents for hard surfaces pH = 10 was achieved by adding NaOH

[0488] Table 12: Hand dishwashing detergents

[0489] Table 13: Cleaning agents for hard surfaces, preferred for glass cleaning

[0490] In addition, the above-mentioned compositions were provided with amine oxide and a fatty alcohol ethoxylate with 7 EO units as additional surfactants in an amount of 0.2 wt.% each.

Claims

Patent claims: 1 . A method for removing grease, grease- and / or oil-containing soiling and / or greasy deposits from surfaces, characterized by the following steps: i) providing at least one peptide ii) bringing the peptide into contact with a grease- and / or oil-containing surface iii) rinsing the surface with water or an aqueous solution; characterized in that 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 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 X 1is 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, 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, X 4 is selected from AL and V, preferably A and L, 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; or b) 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

2. The method according to claim 1, wherein the peptide (i) has a total charge of 0 to +4, or (ii) if r > 4, has a total charge of 0 to +4, or (iii) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

3. The method according to claim 1 or 2, wherein in the peptide according to claim 1 a), 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 equal to Z 1 Z 2 Z 3 [(Z 4 )UZ 5 Z 6 ]3(Z 7 ) V is, where Z 1 like X 2 defined in claim 1 and selected from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined in claim 1 and selected from A, L and V, preferably A and L, Z 4 like X 3 defined in claim 1 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, Z 7 like X 5defined in claim 1 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 in claim 1 and is an integer from 0 to 4.

4. The method according to claim 3, wherein, (i) if u = 1 , Z 4 is selected from R, E and Q, or (ii) if u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

5. The method according to claim 3 or 4, wherein (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 (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 (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or (v) the peptide comprises at least one, preferably two or three, motif(s) RAL; and / or (vi) the peptide comprises the motif RAL at least twice and at least one of QAL or EAL, preferably both.

6. The method according to claim 1 or 2, wherein in the peptide according to claim 1 a), 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 )WZ 16 is, where Z 11 like X 2 defined in claim 1 or 2 and selected from R, H and K, Z 12 like X 3defined in claim 1 or 2 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 in claim 1 or 2 and selected from A, L and V, preferably A and L, Z 15 like X 3 defined in claim 1 or 2 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.

7. The method according to claim 6, wherein, (i) z 13 Z 14 is selected from AL and LA, preferably AL; and / or (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 (iii) (Z 15 ) wwith w = 3-6 comprises a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or (iv) Z 16 is selected from A and L, preferably A.

8. The method according to any one of claims 1 to 7, 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.

9. The method according to any one of claims 1 to 8, 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, most preferably SEQ ID NOs: 1, 3, 5, 9, 10, 12, 29.

10. The method according to any one of claims 1 to 9, characterized in that the peptide is surface-active, preferably measured by the bubble pressure method, wherein the dynamic surface tension determined by the bubble pressure method over the entire bubble lifetime preferably shows a deviation of 2 and more mN / m, preferably of 5 and more mN / m, more preferably of 6 mN / m and more, particularly preferably of 8 mN / m and more, and most preferably of 10 and more mN / m. 1 1. Method according to one of claims 1 to 10, characterized in that the provision of the peptide in step i) takes place in a washing or cleaning agent.

2. The method according to any one of claims 1 to 11, characterized in that at least one of steps ii) or iii), preferably both steps ii) and iii), is carried out in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, in particular about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, for example about 20°C.

13. Method according to one of the preceding claims, characterized in that at least one, preferably step ii) and iii), in particular steps i) to iii) are carried out in a water-conducting machine.

14. Method according to one of the preceding claims, characterized in that it is a method for dishwashing, preferably for manual and / or machine dishwashing, and the hard surfaces are selected from, consist of, or contain ceramic, metal, steel, stainless steel, plastic, plastic, glass and mixtures thereof.

15. Cleaning agent, preferably dishwashing agent, in particular automatic dishwashing agent, characterized in that it contains at least one peptide as defined in one of claims 1 to 10, preferably in an amount of 0.000001 to 3.5% by weight, preferably 0.00001 to 2.5, in particular 0.00001 to 2.0% by weight.

16. Cleaning agent, preferably dishwashing agent, in particular automatic dishwashing agent, comprising a) a cleaning agent preparation A which is liquid at 20°C and contains a1) builder; a2) complexing agent b) a cleaning agent preparation B which is different from the cleaning agent preparation A and is liquid at 20°C and has a water content above 1% by weight, containing b1) at least one cleaning-active enzyme, preferably 0.00001 to 2.0% by weight, preferably 0.0001 to 1.5, in particular 0.001 to 1.0% by weight of active protein based on the total weight of the cleaning agent preparation B; b2) at least one peptide according to one of claims 1 to 14, preferably in an amount of 0.000001 to 8.0% by weight, preferably 0.00001 to 5.0% by weight, in particular 0.00001 to 4.0% by weight, based on the total weight of the cleaning agent preparation B, and a packaging means in which the cleaning agent preparations A and B are present separately from one another.

17. Cleaning agent according to claim 16, additionally comprising c) a cleaning agent preparation C which is liquid at 20°C and different from the cleaning agent preparations A and B, containing c1) an acidifying agent, c2) a glass corrosion inhibitor, c3) optionally a non-ionic surfactant, c4) optionally a hydrotrope, and c5) optionally less than 1% by weight, preferably less than 0.5% by weight, in particular less than 0.1% by weight of enzyme preparation, and d) a packaging means in which the cleaning agent preparations A, B and C are present separately from one another.

18. Detergent dosing system, comprising a) a detergent dosage form according to one of claims 15 or 17, comprising a quantity of detergent preparations A and B or A, B and C sufficient for carrying out a machine dishwashing process at least twice, preferably at least four times and in particular at least eight times; b) a dosing device detachably connected to the detergent dosage form.

19. Automatic dishwashing process using a detergent or a detergent dosing system according to one of claims 15 to 18, in the course of which a partial amount a of the detergent preparation A located in the cartridge is dosed into the interior of the dishwasher from a cartridge located in the interior of the dishwasher, wherein a residual amount of the detergent preparation located in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount a;and a partial amount b of the cleaning agent preparation B contained in the cartridge is dosed into the interior of the dishwasher, wherein a residual amount of the cleaning agent preparation contained in the cartridge remains in the cartridge until the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount b; and optionally a partial amount c of the cleaning agent preparation C possibly contained in the cartridge is dosed into the interior of the dishwasher, wherein a residual amount of the cleaning agent preparation contained in the cartridge remains up to; remains in the cartridge at the end of the dishwashing process, characterized in that this residual amount corresponds to at least twice, preferably at least four times and in particular at least eight times the amount of the partial amount c.