Peptides with textile care properties for textile detergents

Abstract

The invention relates to peptides as described herein. The invention also relates to textile detergents comprising at least one peptide as defined herein. The invention further relates to a method for cleaning textiles using said textile detergent, and to the use of a peptide, as a textile care active ingredient when washing textiles, for improving the washing performance of a textile detergent containing said peptide. In particular, the invention relates to the use of peptides described herein for improving the moisture regulation and / or dimensional stability of textiles.

Description

[0001] Henkel AG & Co. KGaA

[0002] Dr. Dieckmann / BLO

[0003] 2024P00405WG

[0004] December 16, 2025

[0005] PEPTIDES WITH FABRIC-CARE PROPERTIES FOR FABRIC DETERGENT

[0006] DESCRIPTION

[0007] Introduction

[0008] The invention relates to peptides as described herein. The invention further relates to textile detergents comprising at least one peptide as defined herein. The invention also relates to a method for cleaning textiles using said textile detergent and to the use of a peptide as a textile conditioning agent in the washing of textiles, as well as for improving the washing performance of a textile detergent containing this peptide. In particular, the invention relates to the use of peptides described herein for improving the moisture regulation and / or dimensional stability of textiles.

[0009] Polyester has become increasingly important in textile production in recent years. It is well known that polyester textiles have the disadvantage of having comparatively hydrophobic fiber surfaces. This results in lower wearing comfort for pure polyester or polyester blends compared to, for example, pure cotton textiles, as polyester fibers have a significantly lower capacity to absorb moisture.

[0010] For consumers, the durability and comfort of textiles play a major role. Consumers therefore expect a good textile detergent not only to clean effectively, but also to care for textiles (e.g., clothing, tablecloths, bed linens, towels, etc.) and maintain their quality. When textiles look newer for longer, they are worn longer and replaced less frequently. This leads to a reduction in the carbon footprint and is highly beneficial in terms of sustainability.

[0011] It is common practice to use "soil release polymers" to improve dirt removal or "soil repellent polymers" to prevent / reduce dirt adhesion in detergents for cleaning textiles. These soil release and / or soil repellent polymers (hereinafter referred to as SRP polymers) are water-soluble or water-dispersible polycondensates based on dicarboxylic acids and diols or cellulose ethers. SRP polymers are suspended in the wash liquor by surfactants. As the wash liquor is diluted during the rinsing process, the polymer adheres to the textile, so that the hydrophilic sides of the polymer face outwards, while the hydrophobic sides bind to the fiber surface. This forms a hydrophilic protective layer around the textile fiber, limiting the extent to which dirt can adhere to the fiber or penetrate the textile, making it easier to remove in the next wash.This effect becomes particularly noticeable when a textile is soiled that has already been washed several times with a product containing SRP polymers. The SRP polymers only reach their full effectiveness after several washes. Typical SRP polymers can be based, for example, on copolymers of polyester and polyether, or on terephthalates, such as polypropylene terephthalate. However, these polymers are typically not biodegradable.

[0012] It is known that cationic polymers, such as polyquaternium-7, are used in textile care products. Due to their cationic structure and the formation of a protective film, these cationic polymers can improve stretch recovery, allowing textiles to retain their original shape and elasticity even after multiple washes.

[0013] There is a need for alternative or improved, especially biodegradable, polymer alternatives for use in textile detergents. In particular, there is a need for alternative or improved, especially biodegradable, polymer alternatives for use as textile conditioning agents in textile detergents.

[0014] In the context of the invention, "textile care agents" means agents that have a soil-release effect and / or a soil-repellent effect, and / or agents that positively influence the moisture management of textiles, and / or agents that improve the dimensional stability of textiles, and / or agents that prevent color fading and / or transfer from colored textiles, and / or anti-pilling agents and / or de-pilling agents. In the context of the invention, textile care agents that positively influence, and in particular improve, the moisture management of textiles and / or improve the dimensional stability of textiles are particularly relevant.

[0015] In the context of the invention, "moisture regulation" encompasses, in particular, the aspects of moisture absorption, moisture wicking, and drying time. Moisture-regulating agents can be integrated into or applied to textiles. This allows them to absorb moisture (e.g., perspiration) from the skin and promote evaporation, and / or to transport the absorbed moisture (e.g., perspiration) along the surface of the textile by capillary action, thus distributing it over a larger area to enable faster evaporation. Improved wicking of absorbed moisture (e.g., perspiration) can accelerate the drying process of textiles. These aspects are fundamentally relevant for all textiles but are particularly advantageous for functional clothing, such as sportswear or outdoor clothing made of synthetic fibers.Improved moisture transport and faster evaporation allow for better regulation of body temperature and reduce discomfort caused by excessive moisture buildup in the fabric. This improved and faster evaporation keeps the wearer dry and comfortable.

[0016] In connection with the invention, the term "dimensional stability" means the ability of a textile to return to its original shape after mechanical and / or thermal stress, whereby the textile has the lowest possible residual elongation (measured according to DIN 53835 T13).

[0017] Intensive research is being conducted on the development of adhesive peptides. In particular, peptides that specifically bind to or interact with oxide surfaces, such as metal surfaces, have already been described (WO 2014 / 072313). However, adhesive peptides are also of interest for many other surfaces whose material or surface properties make treatment or the application of other objects, substances, or compounds difficult. Surfaces with low surface energies, such as those often found in certain plastics, are particularly problematic. These plastics are also referred to in the prior art as low surface energy polymers (LSEPs) and include, for example, many polyolefins or polymers with ester functional groups. Textile-binding peptides are described in WO 2023 / 110575.WO 2024 / 256090 describes peptides that can represent a biodegradable alternative to SRP polymers, particularly with regard to their grease-dissolving properties. DE 102024202185 describes grease-binding peptides that can contribute to the removal of greasy soiling.

[0018] It has now been surprisingly discovered that certain peptides can also positively influence the moisture regulation and / or dimensional stability of textiles. These peptides are suitable for use in textile detergents and can contribute to improved cleaning performance and / or impart special properties to the textiles. Furthermore, they could help to reduce or completely eliminate synthetic and chemical substances, e.g., in textile detergents, by providing a biodegradable alternative. Such peptides can exert their effects particularly well at low temperatures. These peptides surprisingly exhibit comparable or improved effects compared to conventional (non-biodegradable) SRP polymers. Therefore, the peptides according to the invention represent good and biodegradable alternatives to conventional SRP polymers and can thus contribute to the sustainability of textile detergents.

[0019] The invention therefore relates in a first aspect to a textile detergent comprising at least one peptide, wherein the at least one peptide is selected from

[0020] (a) a peptide with the following amino acid sequence

[0021] (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t,

[0022] where

[0023] X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I,

[0024] X 2 selected from R, H and K, preferably R and K,

[0025] X 3 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

[0026] X 4 selected from A, L and V, preferably A and L,

[0027] X 5selected 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.

[0028] m and t are each 0 or 1, where m+t = 0 or 1,

[0029] n is an integer from 0 to 2,

[0030] o 0 or 1 is,

[0031] p is an integer from 0 to 9,

[0032] q is an integer from 0 to 2,

[0033] r is an integer from 1 to 4, and

[0034] s is an integer from 0 to 4; where the peptide improves the moisture regulation of textiles and / or where the peptide improves the dimensional stability of textiles,

[0035] or

[0036] b) a peptide having an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0037] In preferred embodiments, the peptide according to 1a)

[0038] (a1) a total charge of 0 to +7, or

[0039] (a2) if r> 4, a total charge of 0 to +4 on, or

[0040] (a3) if r < 4, a total charge of +1 to +7.

[0041] In preferred embodiments

[0042] (b) the peptide according to 1a) has a total charge of 0 to +7, preferably 0 to +4, and / or

[0043] (c) the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge, and / or

[0044] (d1) the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net negative charge and preferably comprises at least one negatively charged amino acid, in particular E, or

[0045] (d2) the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a neutral net charge, or

[0046] (d3) the C-terminus of the peptide according to a) comprising the last 1-5 amino acids has a net positive charge, and / or

[0047] (e1) if the total charge is less than +4, the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge, and the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net negative charge and preferably includes at least one negatively charged amino acid, in particular E, or (e2) if the total charge is greater than +4, the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net positive charge.

[0048] In preferred embodiments, in the peptide according to 1a), if 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 Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z 6 ]3(Z7 ) V ,

[0049] where

[0050] Z 1 like X 2 previously defined and selected from R, H and K, preferably R,

[0051] Z 2 , Z 3 , Z 5 and Z 6 like X 4 previously defined and selected from A, L and V, preferably A and L,

[0052] Z 4 like X 3 previously defined 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.

[0053] u 1 or 2 is,Z 7 like X 5 previously defined and 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.

[0054] v is defined as s previously and is an integer from 0 to 4.

[0055] In preferred embodiments,

[0056] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0057] (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ.

[0058] In preferred embodiments, it comprises

[0059] (i) the peptide comprising at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids at positions 1-3; and / or

[0060] (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or

[0061] (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or

[0062] (iv) the peptide, the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0063] (v) the peptide at least one, preferably two or three, motif(s) RAL; and / or

[0064] (vi) the peptide the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0065] In preferred embodiments, the peptide has an amino acid sequence that is 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-58; and / or the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0066] In preferred embodiments, the at least one peptide is suitable for adhesion and / or binding to textiles. In preferred embodiments, the at least one peptide is suitable for adhesion and / or binding to textiles, wherein the adhesion to textiles is determined as described in Example 2.

[0067] In particularly preferred embodiments, the at least one peptide exhibits textile-conditioning properties. In particularly preferred embodiments, the at least one peptide improves the moisture regulation of textiles and / or the dimensional stability of textiles.

[0068] In particularly preferred embodiments, the at least one peptide is suitable for adhesion and / or bonding to textiles and exhibits textile-conditioning properties. In particularly preferred embodiments, the at least one peptide is suitable for adhesion and / or bonding to textiles and improves the moisture regulation and / or dimensional stability of textiles.In preferred embodiments, the agent is essentially free of conventional soil-release polymers, wherein conventional soil-release polymers are in particular composed of cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, cellulose mixed ethers such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methyl carboxymethylcellulose, sodium carboxymethylcellulose, hydroxypropylmethylcellulose, copolyesters containing dicarboxylic acid, alkylene glycol and / or polyalkylene glycol units, polymers of phthalic acid and / or terephthalic acid, their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates, and / or their anionically and / or nonionically modified derivatives, copolymers of polyester and polyether, including terephthalate, e.g.

[0069] Polypropylene terephthalate, as well as mixtures thereof, are selected from the existing group.

[0070] Further aspects of the invention relate to

[0071] • A method for cleaning textiles characterized in that an agent described herein is used in at least one process step,

[0072] • Method for improving the moisture regulation of textiles, characterized in that an agent described herein is used in at least one process step,

[0073] • Method for improving the dimensional stability of textiles, characterized in that an agent described herein is used in at least one process step,

[0074] • Use of any agent described herein for cleaning textiles.

[0075] • Use of a peptide described herein in a textile detergent to improve the moisture regulation of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3a.

[0076] • Use of a peptide contained herein in a textile detergent to improve the dimensional stability of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3b.

[0077] In preferred embodiments, the methods and uses described herein are carried out in a temperature range of about 20°C to about 60°C, preferably about 20°C to about 40°C.

[0078] These and other aspects, features, and advantages of the invention will become apparent to the person skilled in the art upon studying the following detailed description and claims. Each feature from one aspect of the invention can be used in any other aspect of the invention. Furthermore, it is understood that the examples contained herein are intended to describe and illustrate the invention, but do not limit it, and in particular, the invention is not limited to these examples. Definitions

[0079] Unless otherwise stated, all percentages are weight percent (wt%), based on the total weight of the respective composition / agent.

[0080] Numeric ranges specified in the format "from x to y" include the stated values. If multiple preferred numeric ranges are specified in this format, it is understood that all ranges resulting from the combination of the different endpoints are also included.

[0081] "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. When referring to an ingredient, the statement refers to the type of ingredient and not the absolute number of molecules. Thus, "at least one peptide," for example, means at least one type of peptide, i.e., it may refer to one type of peptide or a mixture of several different peptides. When used 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 that type beyond the specified amount of the relevant compounds.

[0082] "Approximately" or "about" as used herein in reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0083] "Substantially free of", as used herein and unless otherwise specified, means that the composition or agent contains less than 0.2 wt.%, preferably less than 0.1 wt.%, further preferably less than 0.05 wt.% and particularly preferably less than 0.01 wt.%, of the corresponding substance, based on the total weight of the composition / agent.

[0084] The term "textile detergent" or "detergent", 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, as explained in the description.

[0085] The term "textile," as used herein, refers to any textile material, including yarns, yarn precursors, fibers, nonwovens, natural materials, synthetic materials, and all other textile materials; textile fabrics made from these materials; and products constructed from textile fabrics (e.g., garments and other articles). The textile or fabric may be in the form of knitted, woven, nonwoven, felted, knitted, terry, and terry cloth. The textile may be cellulose-based, such as natural cellulose fibers like cotton, flax / linen, jute, ramie, sisal, or coconut fibers, or artificially produced cellulose fibers (e.g., from wood pulp) such as viscose / rayon, cellulose acetate fibers (Tricell), lyocell, or mixtures thereof. The textile or fabric may also consist of non-cellulose fibers, e.g.,Fabrics are made from natural protein fibers such as wool, camel, cashmere, mohair, rabbit, and silk, or from synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulose and non-cellulose fibers. Examples of blends include cotton and / or rayon / viscose blends with one or more accompanying materials such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and / or cellulose-containing fibers (e.g., rayon / viscose, ramie, flax / linen, jute, cellulose acetate fibers, lyocell). The fabric may be conventional washable laundry, such as soiled household linen. When the term "fabric" or "garment" is used, it should also encompass the broader term "textiles."

[0086] Unless explicitly stated otherwise, the term "room temperature" within the scope of the invention is understood to mean 20°C at 1013 mbar.

[0087] A substance, e.g. a composition or a means, is, according to the definition of the invention, solid if it is in the solid state at 25°C and 1,013 mbar.

[0088] A substance, e.g., a composition or agent, is liquid according to the definition of the invention if it exists in the liquid state at 25°C and 1013 mbar. "Liquid" here also includes gel-like states. "Liquid," as used herein, includes liquids and gels as well as pasty compositions. It is preferred that the liquid compositions are free-flowing and pourable at room temperature, but it is also possible that they exhibit a yield point.

[0089] In the context of the present invention, the term "N-terminus" or "N-terminal" typically describes the end of the amino acid chain of a peptide which has a free amino group.

[0090] In the context of the present invention, the term "C-terminus" or "C-terminal" typically describes the end of the amino acid chain of a peptide which has a free carboxyl group.

[0091] In the context of this invention, the expression "in N- to C-terminal orientation" refers to an amino acid sequence in which the order of the amino acids is described starting from the N-terminus towards the C-terminus.

[0092] When reference is made herein to various interconnected or individual amino acid sequences, these are always shown in an N- to C-terminal orientation, unless otherwise stated. Furthermore, the individual amino acids or amino acid sequences are linked to each other via peptide bonds, unless otherwise stated.

[0093] The term "variant", as used herein, refers to variants of an enzyme, protein or peptide which retain the functionality of the original molecule but differ from the original sequence by one or more sequence deviations, e.g. 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more sequence deviations, e.g. a substitution, deletion or insertion. The sequence identity of such variants can be in the range of 80% based on the total length of the starting peptide, and can be at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, or 99.5%. In the context of this invention, "adhesion" or "adhesive" refers to an interaction between a peptide and a surface, enabling the peptide to adhere to the surface. Thus, the term "adhesion-mediating" denotes the ability, under suitable conditions, i.e.,Typically non-denaturing conditions, to interact with various surfaces, e.g., textile surfaces, particularly those containing or consisting of cotton, polyester, and mixtures thereof, and / or to adhere to a specific surface. In this context, the term "textile-binding" refers to the ability of a molecule, particularly a peptide, to adhere to textile surfaces. In connection with the present invention, adhesion or textile bonding is determined as described in Example 2.

[0094] Detailed description

[0095] The present invention is based on the inventors' surprising discovery that certain peptides can positively influence, and in particular improve, the moisture regulation and / or dimensional stability of textiles. These peptides are suitable for use in textile detergents and can contribute to improved cleaning performance and / or impart special properties to the textiles. Furthermore, they could help to reduce or completely eliminate synthetic and chemical substances, e.g., in textile detergents, by providing a biodegradable alternative. Such peptides can exert their effects particularly well at low temperatures.

[0096] This is particularly surprising because such peptides have not previously been associated with textile care properties, especially moisture regulation and / or shape stability of textiles.

[0097] Peptides

[0098] In the context of the present invention, a "peptide" is understood to be a preferably linear polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, comprising up to 100 amino acids linked together by peptide bonds. According to the invention, the peptides have an amino acid sequence of 4 to 50 amino acids. The amino acids are indicated in the context of this invention by a single-letter code (Table 1). It is further understood that, unless otherwise stated, the amino acids in any amino acid sequence disclosed herein are linked by peptide bonds and that, unless otherwise stated, the sequence is shown in an N- to C-terminal orientation.

[0099] Table 1: Proteinogenic amino acids

[0100]

[0101]

[0102] 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. When reference is made herein to "any" amino acid, this usually refers to one of the 20 naturally occurring proteinogenic amino acids (Table 1).

[0103] Unless otherwise specified, the amino acids are typically L-amino acids. In alternative embodiments, the peptide may also consist of D-amino acids, although it may be preferred that D- and L-amino acids do not occur simultaneously within the peptides described herein. In various embodiments, such an arbitrary amino acid encompasses all of the aforementioned amino acids.

[0104] In various embodiments, the peptide used according to the invention 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, whereby one positive and one negative charge cancel each other out. A peptide with two R residues and one E residue would thus have a total charge of +1. In preferred embodiments, the total charge of the peptide is 0 to +7.

[0105] In various embodiments, the peptide used according to the invention exhibits

[0106] (a1) has a total charge of 0 to +7, or (a2) if r > 4, has a total charge of 0 to +4, or

[0107] (a3) if r < 4 has a total charge of +1 to +4, preferably +2 or +3.

[0108] In various embodiments

[0109] (b) the N-terminus comprising the first 1-5 amino acids carries a net positive charge; and / or

[0110] (c1) the C-terminus comprising the last 1-5 amino acids has a net negative charge such 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

[0111] (c2) the C-terminus comprising the last 1-5 amino acids has a neutral net charge such 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

[0112] (c3) the C-terminus comprising the last 1-5 amino acids has a net positive charge such 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; and / or

[0113] (d) if the total charge is greater than +4, the N-terminus comprising the first 1-5 amino acids has a net positive charge and the C-terminus comprising the last 1-5 amino acids has a net positive charge.

[0114] All of the aforementioned features (a) to (d) can be realized individually or in any combination.

[0115] The feature that the peptide has a net positive charge at the N-terminus comprising the first 1-5 amino acids means that the N-terminal 1-5 amino acids contain more positively charged than negatively charged amino acids. In various embodiments, this feature is fulfilled, for example, when the N-terminal 1-5 amino acids contain one or two positively charged amino acids, i.e., H, K, or R, preferably K or R, even 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 two for the net charge to remain positive.

[0116] The feature that the peptide has a net negative 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 (D and E) must be greater than the number of positively charged amino acids. In various embodiments, this feature is fulfilled, for example, when the C-terminal 1-5 amino acids (i.e., within the last 5 amino acids at the C-terminus) contain 1 or 2 negatively charged amino acids (D or E) and no positively charged amino acids (H, K, or R). An example of such a C-terminal sequence would be EAL or the double sequence of this motif.

[0117] The feature that the peptide has a "neutral 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 and positively charged amino acids must be equal. In various embodiments, the peptide used according to the invention has an amino acid sequence which, in an 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

[0118] where

[0119] X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I,

[0120] X 2 selected from R, H and K, preferably R and K,

[0121] X 3selected 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

[0122] X 4 selected from A, L and V, preferably A and L,

[0123] X 5 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.

[0124] m and t are each 0 or 1, where m+t = 0 or 1,

[0125] n is an integer from 0 to 2,

[0126] o 0 or 1 is,

[0127] p is an integer from 0 to 9,

[0128] q is an integer from 0 to 2,

[0129] r is an integer from 1 to 4,

[0130] s is an integer from 0 to 4.

[0131] In various embodiments, in a peptide used according to the invention, 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 Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z 6 ]3(Z 7 ) V , where

[0132] Z 1 like X 2 The above is defined and selected from R, H and K, preferably R.

[0133] Z 2 , Z 3 , Z 5 and Z 6 like X 4 The above defined and selected are from A, L and V, preferably A and L.

[0134] Z 4 like X 3 The above is defined 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.

[0135] u 1 or 2 is,

[0136] Z 7 like X 5 The above is defined and 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.

[0137] vwie s defined above and is an integer from 0 to 4.

[0138] In various embodiments

[0139] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0140] (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ.

[0141] In various embodiments, the peptide used according to the invention comprises

[0142] (i) at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids of positions 1-3; and / or (ii) at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or

[0143] (iii) at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) the RAL motif and at least one of QAL or EAL, preferably both; and / or (v) at least one, preferably two or three, RAL motif(s); and / or

[0144] (vi) the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0145] In various embodiments, the peptide used according to the invention comprises a motif selected from RAL, RSI, and RLA, preferably RAL and RLA, and more preferably RAL. In various embodiments, the motif selected from RAL, RSI, and RLA is localized at the N-terminus, preferably in the N-terminal amino acids at positions 4-7 and at least 6-7 amino acids away from the C-terminus. The N-terminal sequence RAL or RLA not only advantageously has a net positive charge, but also comprises amino acids with a particularly high α-helix forming potential. In various embodiments, the R residue can also be replaced by K; however, the N-terminal R residue is particularly preferred.

[0146] In various embodiments, the peptide used according to the invention comprises a motif selected from EAL, LEA, and ELA, preferably EAL. In various embodiments, the motif selected from EAL, LEA, and ELA is localized at the C-terminus, preferably not in the N-terminal amino acids at positions 1-6.

[0147] In various embodiments, the peptide used according to the invention comprises a motif selected from EQA, QAL, LQA and QLA, preferably EQA, QAL and QLA, more preferably QAL. In various embodiments, the motif selected from EQA, QAL, LQA and QLA is not localized in the N-terminal amino acids at positions 1-6 or 1-11.

[0148] In various embodiments, when the sequence (X 2 )0[(X 3 )p(X 4 )q]r(X 5 ) s equal Z 1 Z 2 Z 3 [(Z 4 )UZ 5 Z 6 ]3(Z7 ) V is, includes Z 1 Z 2 Z 3 the motif RAL and [(Z 4 ) U Z 5 Z 6 ]3(Z 7 ) V The motif includes QAL and / or EAL.

[0149] In such embodiments, the peptide has the sequence (C)mRAL(Y 1 ) a QAL(Y 2 )bEAL(Y 3 )c(C)t or

[0150] (C)mRAL(Y 1 ) a EAL(Y 2 )bQAL(Y 3 )c(C)t,

[0151] where

[0152] m and t are each 0 or 1, where m+t = 0 or 1,

[0153] Y 1 and Y 2 any amino acid independently of one another, preferably with the exception of P, further preferably with the exception of P and G,

[0154] Y 3 any uncharged amino acid, preferably Q, A or L, further preferably A or L,

[0155] a and b are 0 or an integer from 1-10, preferably 0, 1, 2 or 3,

[0156] c 0 or 1 is, and a+b+c = 0-21 , preferably 0-15 or 0-9 or 1-15 or 1-9 or 1-6 or 0-6 or 0-3 or 1-3.

[0157] In various embodiments, the peptide used according to the invention can additionally comprise at least one further (second) sequence RAL. This sequence can, in various embodiments, follow directly C-terminally to the first RAL sequence or be separated from it by 1-3 amino acids, e.g., by 1 or 3 amino acids. In various embodiments, the peptide used according to the invention can comprise two sequences RAL and at least one sequence EAL and / or QAL. In various embodiments, such peptides can have the following sequences:

[0158] RALRAL(Y 1 ) a QAL(Y 2 )bEAL(Y 3 )c,

[0159] RALRAL(Y 1 ) a EAL(Y 2)bQAL(Y 3 )c,

[0160] RAL(Y 1 ) a RALQAL(Y 2 )bEAL(Y 3 )c,

[0161] RAL(Y 1 )aRALEAL(Y 2 ) b QAL(Y 3 )c,

[0162] RAL(Y 1 ) a QALRAL(Y 2 )bEAL(Y 3 )c,

[0163] RAL(Y 1 )aEALRAL(Y 2 ) b QAL(Y 3 )c,

[0164] where

[0165] Y 1 and Y 2 any amino acid independently of each other, preferably excluding P, further preferably excluding P and G, e.g. W or F or other motifs QAL or EAL,

[0166] Y 3 any uncharged amino acid, preferably Q, A or L, further preferably A or L,

[0167] a and b are 0 or an integer from 1 to 6, preferably 0, 1, 2 or 3,

[0168] c 0 or 1 is, preferably 0, and

[0169] a+b = 0-9, preferably 0-6 or 0-3 or 1-9 or 1-6 or 1-3.

[0170] In various embodiments, the peptide used according to the invention 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.

[0171] In various embodiments, the peptide used according to the invention 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, further preferably E, A, L, M, Q, K, R, F, I and H, particularly preferably E, A, L, M, Q, K, R and H.

[0172] In various formulations, the peptide used according to the invention 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 used according to the invention can contribute to the stability of the helical structure because these amino acids have a high α-helix potential.

[0173] In various embodiments, in a peptide used according to the invention, 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

[0174] Z11 like X 2 The above is defined and selected from R, H and K.

[0175] Z 12 like X 3 The above is defined 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.

[0176] Z 13 , Z 14 , Z 16 like X 4 The above defined and selected are from A, L and V, preferably A and L, Z 15 like X 3 The above is defined 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.

[0177] w is an integer from 3 to 6.

[0178] In various embodiments in a peptide used according to the invention

[0179] (i) is z 13 Z 14 selected from AL and LA, preferably AL; and / or

[0180] (ii) includes (Z 15 )w with w = 3-6 a sequence that includes at least one positively charged amino acid (R, H or K); and / or

[0181] (iii) includes (Z 15 ) w with w = 3-6 a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, further preferably RQN; and / or

[0182] (iv) is Z 16 selected from A and L, preferably A.

[0183] In various embodiments, the peptide used according to the invention can 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.

[0184] In various embodiments, the peptide used according to the invention has an amino acid sequence that is 10 to 24 amino acids long, e.g., 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, or 24 amino acids, in particular 12 to 18 amino acids. In preferred embodiments, the peptide used according to the invention has an amino acid sequence that is 12 to 18 amino acids long.

[0185] In various embodiments, the peptide used according to the invention has the amino acid cysteine ​​(C) at its C-terminus. In various embodiments, the peptide used according to the invention has the amino acid cysteine ​​at its 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.

[0186] In preferred embodiments, the peptide used according to the invention has an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0187] In preferred embodiments, the peptide used according to the invention is selected from: HFVKTPARWAWG (SEQ ID NO:1), IYASNHSHPASY (SEQ ID NO:2), GHQGHWYGMFRA (SEQ ID NO:3), SLAFMPAWHASR (SEQ ID NO:4), HNHHQLALVESY (SEQ ID NO:5), SQLFNSQRLAYS (SEQ ID NO:6), WRHPRLRCGNLL (SEQ ID NO:7), SRARLFWTYHKC (SEQ ID NO:8), HMISTMNAASRRC (SEQ ID NO:9), RSIVTFSLRQNRC (SEQ ID NO:10), RSIVTFSLRQNSEQAC (SEQ ID NO:11), KSIVTFSLRQNRC (SEQ ID NO:12), KSIVTFSLKQNRC (SEQ ID NO:13), RALFRALFEALEALRC (SEQ ID NO:14), RALFEALQALFRALEALC (SEQ ID NO:15), RALRALFEALEALC (SEQ ID NO:16), RALFEALFRALEALRC (SEQ ID NO:17), RALEALFRALEALC (SEQ ID NO:18), RALFRALWEALFEALC (SEQ ID NO:19), RALFEALWRALFEALC (SEQ ID NQ:20), 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), RALRALRALEALEALALC (SEQ ID NO:29),RALQALRALQALEALC (SEQ ID NQ:30), RALRALEALQALEALC (SEQ ID NO:31), QNRSPRRTRKRR (SEQ ID NO:32), RALRALRALQALQAL (SEQ ID NO:33), RALRALRALQALEAL (SEQ ID NO:34), RALRALEALQALEA (SEQ ID NO:35), RALFEALQALFRALEAL (SEQ ID NO:36), RALFEALFRALEALR (SEQ ID NO:37), RALRALQALEALEAL (SEQ ID NO:38), RALRALRALEALEAL (SEQ ID NO:39), RALRALFRALEEAL (SEQ ID NQ:40), RALFEALFRALEAL (SEQ ID NO:41), RALEALFRALEAL (SEQ ID NO:42), RALRALFEALEAL (SEQ ID NO:43), RALEALFRALQALEAL (SEQ ID NO:44), RALEALWRALQALEAL (SEQ ID NO:45), RALEALWRALEAL (SEQ ID NO:46), RALARALARALAQALA (SEQ ID NO:47), RSIVTFSLRQNAQLA (SEQ ID NO:48), RSIVTFSLRQNSEQA (SEQ ID NO:49), GLHTSATNLYLH (SEQ ID NQ:50), QHSIRLLTIKKP (SEQ ID NO:51), QQSIRIMTIKHP (SEQ ID NO:52), QKSRNRMTRTHP (SEQ ID NO:53), SRARLFVVTYHK (SEQ ID NO:54), HMISTMNAASRR (SEQ ID NO:55), RSIVTFSLRQNR (SEQ ID NO:56), RNTIRIRTIKHP (SEQ ID NO:57), RHSSTLRYRPLP (SEQ ID NO:58).,

[0188] In preferred embodiments, the peptide used according to the invention has a sequence that is represented in SEQ ID NO: 1-58, particularly preferably SEQ ID NO: 10, 14-21, 23-47, most preferably SEQ ID NO: 10, 25, 32.

[0189] Variants of the peptides used according to the invention, whose amino acid sequence exhibits at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences corresponding to the sequences in SEQ ID NO:1-58, preferably differ in a maximum of 3 positions, more preferably in a maximum of 2 positions, and particularly preferably in a maximum of 1 position from one of the amino acid sequences according to SEQ ID NO:1-58. For example, if one position is different, either one of the amino acids in the respective sequence may have been exchanged, or the sequences may be the same, but an amino acid within the amino acid chain or at the N- or C-terminus may have been added or omitted. For example, a cysteine ​​(C) may have been added at the C- or N-terminus.

[0190] The peptides preferably used according to the invention are textile-binding peptides, i.e., peptides that have the ability to adhere to textile surfaces under suitable conditions, i.e., typically non-denaturing conditions, and thus exhibit adhesive properties. Methods for determining adhesion are known to those skilled in the art, and any suitable method can be used. Preferably, the method described in Example 2 is used.

[0191] Peptides preferably used according to the invention have textile-conditioning properties.

[0192] Peptides used according to the invention are particularly preferred for improving the moisture regulation of textiles and / or the dimensional stability of textiles.

[0193] The peptides preferably used according to the invention are textile-binding peptides and exhibit textile-conditioning properties. The peptides particularly preferably used according to the invention are textile-binding peptides and improve the moisture regulation and / or dimensional stability of textiles. The peptides particularly preferably used according to the invention are textile-binding peptides and improve the moisture regulation of textiles. The peptides particularly preferably used according to the invention are textile-binding peptides and improve the dimensional stability of textiles. The peptides particularly preferably used according to the invention are textile-binding peptides and improve the moisture regulation and dimensional stability of textiles.

[0194] 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 in the art and commonly used (see, e.g., Altschul et al. (1990) Basic local alignment search tool, J. Mol. Biol., 215:403-410, and Altschul et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25:3389-3402). In principle, it is performed by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences. A tabular assignment of the relevant positions is called an alignment. Another algorithm available in the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are performed using computer programs. Frequently used programs include, for example, the Clustal series (see, e.g., Chenna et al.).(2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 31:3497-3500), T-Coffee (see, e.g., Notredame et al. (2000) T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 302:205-217) or programs based on these programs or algorithms. Sequence comparisons (alignments) are also possible using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the predefined standard parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (using the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise stated, the sequence identity given herein is determined using the BLAST algorithm. Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually expressed as a percentage identity, i.e.,Homology is expressed as the proportion of identical nucleotides or amino acid residues at the same positions or positions corresponding to each other in an alignment. The broader concept of homology, when applied to 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 protein. 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 only for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are thus 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.Often, such small regions perform essential functions for the overall activity of the protein. It can therefore be useful to refer to sequence similarities only in individual, possibly small, regions. Unless otherwise stated, however, identity or homology claims in this application refer to the total length of the respective nucleic acid or amino acid sequence.

[0195] The peptide or protein concentration can be determined using known methods, e.g., the BCA method (bicinchoninic acid; 2,2'-bicinolyl-4,4'-dicarboxylic acid) or the Biuret method (Gornall et al., J. Biol. Chem., 1948, 177:751-766). Those skilled in the art of peptide and protein technology are aware of a variety of suitable methods for determining the peptide or protein concentration that can be applied within the scope of this invention.

[0196] Peptides according to the invention can exhibit amino acid modifications, in particular amino acid substitutions, insertions, or deletions. Such peptides are further developed, for example, by targeted genetic modification, i.e., by mutagenesis, and optimized for specific applications or with regard to special properties (e.g., their stability, binding, etc.). For example, targeted mutations such as substitutions, insertions, or deletions can be introduced into known molecules to modify certain properties. In particular, the surface charges and / or the isoelectric point of the molecules, and thus their interactions with a surface, can be altered. For example, the net charge of the peptides can be changed to influence substrate binding. Alternatively or additionally, one or more corresponding mutations can, for example, increase the stability or adsorption of the peptide.The advantageous properties of individual mutations, e.g., individual substitutions, can complement each other.

[0197] Thus, the invention also includes peptides characterized in that they are obtainable from a peptide as described above as a starting molecule, e.g., from a molecule with one of the amino acid sequences according to SEQ ID NO:1-58, on which, for example, one or more amino acid substitutions, including one or more conservative amino acid substitutions, have been carried out, wherein the resulting peptide has a content of at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%. exhibits 98%, 98.5%, 99%, 99.5% and less than 100% sequence identity with one of the amino acid sequences according to SEQ ID NO:1-58.

[0198] The term "conservative amino acid substitution" means the exchange (substitution) of one amino acid residue for another, whereby this exchange does not lead to a change in polarity or charge at the position of the exchanged amino acid, e.g., the exchange of one nonpolar amino acid residue for another nonpolar amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G=A=S, l=V=L=M, D=E, N=Q, K=R, Y=F, S=T, G=A=I=V=L=M=Y=F=W=P=S=T. However, it may be preferred that such substitutions do not involve glycine or tyrosine as the target amino acid, or, for example, an amino acid with a low alpha-helix-forming potential.

[0199] In preferred embodiments, peptides according to the invention can also be modified. Preferred modifications can, for example, involve coupling the peptide with certain other molecules or chemical groups, e.g., organic (macro)molecules, e.g., via a covalent bond or a linker / spacer via a suitable amino acid of the chain and / or at the N- and / or C-terminal.

[0200] Furthermore, peptides 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 multimerder of the sequences described herein, e.g., 1 to 30 repeats, more preferably 2 to 15 repeats, and 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. In this context, the term "polypeptide" refers in particular to peptides comprising 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids, unless otherwise specified.

[0201] 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 together by at least one spacer, preferably comprising or consisting 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 linearly to one another via peptide bonds, possibly also via a spacer.

[0202] The peptides used according to the invention can be chemically synthesized in various embodiments and / or produced recombinantly by means of protein design. Short peptides are now easily synthesized, e.g., via solid-phase synthesis. Longer peptides and polypeptides, such as enzymes, are, on the other hand, often also produced recombinantly in host organisms, e.g., in bacteria or yeast.

[0203] It is preferred that peptides used according to the invention be produced by recombinant methods. These methods include all genetic engineering or microbiological processes based on the introduction of the genes for the peptides of interest into a host organism suitable for production, where they are transcribed and translated (collectively referred to within the scope of this invention as biotechnological processes). For example, the introduction of the genes in question is carried out via vectors, in particular expression vectors; but also via vectors that enable the gene of interest to be inserted into an existing genetic element in the host organism, such as a chromosome or other vectors. The functional unit consisting of the gene and promoter, and possibly other genetic elements, is typically referred to as an expression cassette. However, it does not necessarily have to exist as a physical unit.

[0204] Particularly preferably, peptides used according to the invention are produced as polypeptides (multimers) and subsequently cleaved into the functional peptides. Particularly preferred multimers comprise 1 to 30 peptide units (each according to the invention), each separated from the others by spacers of 1 to 10 amino acids in length (e.g., 1, 2, 3, or 4 amino acids). Alternatively, the spacers can also be or include cleavage sites for specific proteases / peptidases, in particular endopeptidases, or together with parts of the peptide, form such a cleavage site.

[0205] Using methods now widely known, such as chemical synthesis or polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemistry techniques, a specialist can synthesize the corresponding nucleic acids, even complete genes, from known DNA and / or amino acid sequences. Such methods are described, for example, in Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition Cold Spring Laboratory Press.

[0206] In particularly preferred embodiments, the peptides described herein are produced using biotechnological methods as described above.

[0207] Textile detergent

[0208] Preferably, the at least one peptide used according to the invention is suitable for adhesion and / or bonding to textiles, as described herein.

[0209] It is particularly preferred that the peptide used according to the invention, especially when used in textile detergents according to the invention, imparts textile-care properties, particularly through binding and / or adhesion to textiles, preferably polyester-containing textiles and / or polyester / cotton blends, in particular improving the moisture regulation and / or dimensional stability of textiles. Thus, the textile detergent is used in a washing process, particularly in machine washing or hand washing.

[0210] In various embodiments, the peptides described herein are used in textile detergents according to the invention, without being limited thereto, in a concentration of approximately 0.00001 to approximately 5 wt.%, e.g., in a concentration of approximately 0.0001 to approximately 2 wt.% or approximately 0.001 to approximately 1 wt.%. In preferred embodiments, the peptides according to the invention achieve their effect when used in a concentration of approximately 0.075 wt.% to approximately 0.75 wt.%, based on the active ingredient content and total weight of the agent. In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is not more than approximately 0.1 wt.%, in particular not more than approximately 0.09 wt.%, based on the active ingredient content and total weight of the agent.In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is not less than approximately 0.075 wt.% and not more than approximately 0.09 wt.%, based on the active ingredient content and total weight of the agent. In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is not more than approximately 0.75 wt.%, in particular not more than approximately 0.64 wt.%, based on the active ingredient content and total weight of the agent. In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is not less than approximately 0.75 wt.%, in particular not less than approximately 0.64 wt.%, based on the active ingredient content and total weight of the agent. In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is approximately 0.09 wt.%.-%, based on the active ingredient content and total weight of the product. In various embodiments, it may be preferred that the concentration of the peptides according to the invention in textile detergents is approximately 0.64% by weight, based on the active ingredient content and total weight of the product.

[0211] Textile detergents according to the invention are particularly suitable for use on textiles made of plastic and / or with a plastic component (mixed fabrics) and / or made of a natural fiber such as cotton.Preferably, the textile 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), polyetherketone (PEK), and / or copolymers or a mixture thereof, more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or mixtures thereof, preferably a cotton / polyester blend with a polyester content of at least 10%, more preferably at least 20%, more preferably at least 30%, and even more preferably at least 40%, particularly preferably at least 50%, most preferably at least 60%, e.g.65%, or pure polyester or copolymers thereof.

[0212] The term "mixture" or "blended fabric" refers to textiles containing a synthetic fiber and / or plastic component, preferably textiles made of at least one natural fiber and at least one synthetic fiber and / or plastic component. In particular, the mixture or blended fabric consists of cotton and at least one plastic, especially polyester. In preferred embodiments, a textile containing a plastic component or a plastic mixture or blended fabric has a plastic component of at least 10%, preferably at least 20%, more preferably at least 30%, even more preferably at least 40%, particularly preferably at least 50%, and most preferably at least 60%, e.g., 65%. Detergents according to the invention include all conceivable types of detergents, both concentrates and undiluted agents, for use on a commercial scale, in washing machines, or for hand washing. These include, for example...Detergents for textiles, carpets, or natural fibers, for which the term "detergent" is used. Detergents within the scope of the invention also include washing aids that are added to the actual detergent during manual or machine washing of textiles to achieve an additional effect. Furthermore, detergents within the scope of the invention also include textile pre- and post-treatment agents, i.e., agents with which the garment is brought into contact before the actual washing, e.g., to loosen stubborn stains, and also agents that, in a step following the actual washing process, impart further desirable properties to the laundry, such as a pleasant feel, wrinkle resistance, or low static charge. Fabric softeners are among the latter types of agents.

[0213] Textile detergents according to the invention, which may be in the form of powdered or granular solids, in compacted or post-compacted particle form, as homogeneous solutions or suspensions, may contain all known ingredients commonly found in such products. In particular, products according to the invention may contain 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, sequestrants, electrolytes, pH regulators and / or other additives such as optical brighteners, anti-graying agents, dye transfer inhibitors, foam regulators, as well as dyes and fragrances.The composition of the textile detergents according to the invention, as well as the quantities of the ingredients, depends on the respective intended use, and a trained person skilled in the art is generally familiar with suitable dosages of these components and can obtain them from the relevant technical literature. Advantageous ingredients of the detergents according to the invention are disclosed, for example, in WO 2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly referenced, and its content is incorporated into the present patent application.

[0214] Further embodiments include all solid, powdered, liquid, gel-like, or pasty dosage forms of textile detergents according to the invention, which may optionally consist of several phases and may be in compressed or uncompressed form. Textile detergents according to the invention can be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1,200 g / l, and more specifically 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of textile detergents according to the invention also include extrudates, granules, tablets, or pouches. Alternatively, textile detergents according to the invention can 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 compositions are generally preferred.Furthermore, textile detergents according to the invention can be in the form of a single-component system. Such detergents consist of one phase. Alternatively, textile detergents according to the invention can also consist of several phases. Such a detergent is therefore divided into several components. In various embodiments, textile detergents according to the invention are liquid textile detergents. In various embodiments, textile detergents according to the invention are solid textile detergents. Liquid textile detergents are preferred.

[0215] The viscosity of liquid textile detergents according to the invention is preferably 5 to about 100,000 mPa s, more preferably about 10 to about 5,000 mPa s, and particularly preferably about 100 to about 750 mPa s, measured with a Brookfield rotational viscometer of type LVT or LVDV-II+ with small sample adapter at a rotational speed of 30 rpm. -1, wherein the spindle used as a measuring element is selected according to Brookfield such that the torque is within a favorable range and the measuring range is not exceeded. In this context, spindle 31 is preferred and – if required for viscosities above approximately 240 mPa s – spindle 25 is preferably used.

[0216] In other preferred embodiments, textile detergents according to the invention are pre-portioned textile detergents, in particular detergent portion units comprising a liquid detergent preparation according to the invention and a water-soluble film that completely encloses the detergent preparation. The water-soluble film in which the detergent preparation is packaged can comprise one or more structurally different water-soluble polymers. Particularly suitable as water-soluble polymers are polymers from the group of (optionally acetalized) polyvinyl alcohols (PVALs) and their copolymers. Water-soluble films are preferably based on a polyvinyl alcohol or a polyvinyl alcohol copolymer whose molecular weight is in the range of about 10,000 to about 1,000,000 g / mol, preferably about 20,000 to about 500,000 g / mol, particularly preferably about 30,000 to about 100,000 g / mol and particularly about 40,000 to about 80,000 g / mol.Suitable biopolymers, e.g., based on casein or starch, are also an option. Suitable water-soluble films are available from companies such as MonoSol LLC, for example under the designations M8630, M8720, M8310, C8400, or M8900. Films such as Solublon® PT, Solublon® GA, Solublon® KC, or Solublon® KL from Aicello Chemical Europe GmbH, or the VF-HP films from Kuraray, are also suitable.

[0217] When compositions according to the invention are in liquid form, they preferably contain more than about 40 wt.%, preferably about 50 to about 90 wt.% and particularly preferably about 60 to about 85 wt.% water based on their total weight.

[0218] The composition according to the invention can contain one or more surfactants, in particular anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and / or amphoteric surfactants. The composition according to the invention preferably contains about 5 to about 70 wt.%, more preferably about 7.5 to about 60 wt.% and further preferably about 10 to about 50 wt.% surfactant. In preferred embodiments, the total surfactant content is not more than about 20 wt.%, in particular about 7.5 to about 15 wt.%, and more preferably about 10 to about 12 wt.%.

[0219] Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups with preferably alkali ions as cations. Usable soaps are preferably the alkali salts of saturated or unsaturated C₆s fatty acids. Such fatty acids can also be used in a partially neutralized form. Suitable sulfate-type surfactants include the salts of the sulfuric acid half-esters of C₆s fatty alcohols and the sulfation products of the aforementioned nonionic surfactants with a low degree of ethoxylation. Usable sulfonate-type surfactants include, for example, Cg-14 alkylbenzenesulfonates, alkanesulfonates obtained from Ci2-is alkanes by sulfochlorination or sulfoxidation followed by hydrolysis or neutralization, Cs-olefin sulfonates formed by the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkanesulfonates, and disulfonates, such as those found, for example, in...from 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 α-sulfofaticial esters (ester sulfonates) that are formed by the sulfonation of fatty acid methyl or ethyl esters, e.g. α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

[0220] Preferably, compositions according to the invention comprise about 2 to about 50 wt.%, preferably about 5 to about 35 wt.%, more preferably about 10 to about 25 wt.%, anionic surfactant. Most preferably, compositions according to the invention comprise about 1 to about 25 wt.%, preferably about 2 to about 10 wt.%, more preferably about 2.5 to about 5 wt.%, alkylbenzenesulfonate. Furthermore, compositions according to the invention may preferably also contain other anionic surfactants, in particular alkyl ether sulfates, as well as non-ionic surfactants, in particular fatty alcohol alkoxylates. These may then constitute the remainder of the surfactants.

[0221] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula

[0222]

[0223] In which R' and R" are independently H or alkyl and together contain 6 to 19, preferably 7 to 15 and particularly 9 to 13 carbon atoms. A particularly preferred representative is sodium dodecylbenzylsulfonate.

[0224] The alkali and, in particular, the sodium salts of the sulfuric acid half-esters of the Ci2-18 fatty alcohols, e.g., from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or the Ci2-20 oxo alcohols, and those half-esters of secondary alcohols of these chain lengths are preferred as alk(en)yl sulfates. Also preferred are alk(en)yl sulfates of the aforementioned chain lengths which contain a synthetic, petrochemically produced, straight-chain alkyl group and which exhibit analogous degradation behavior to the corresponding compounds based on fatty chemical raw materials. For detergent applications, the C1e alkyl sulfates, Ci2-15 alkyl sulfates, and C1s alkyl sulfates are preferred.

[0225] 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 Cg-n alcohols with an average of 3.5 mol of ethylene oxide (EO) or C s fatty alcohols with 1 to 4 EO, are also suitable.

[0226] Suitable alkyl ether sulfates are, for example, compounds of formula R 1 -O-(AO) n -SO3- X + .

[0227] In this formula, R is represented by 1 for a linear or branched, substituted or unsubstituted alkyl group, preferably for a linear, unsubstituted alkyl group, particularly preferably for a fatty alcohol group. Preferred groups R 1 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and eicosyl groups and mixtures thereof, with representatives having an even number of carbon atoms being preferred. Particularly preferred groups R 1are derived from C₆s fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C₆O₂ 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 particularly 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 nth part of an n-valent cation, preferably the alkali metal ions and among them Na + or K + , where Na + is extremely preferred. Further cations X + can be selected from NHT, % Zn 2+ , % Mg 2+ , % Ca 2+ , % Mn 2+ and their mixtures.

[0228] In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula

[0229]

[0230] "

[0231] with k = 11 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 average, which may be a whole number or a fraction for a specific product. The stated degrees of alkoxylation represent statistical averages, which may be a whole number or a fraction for a specific product. Preferred alkoxylates / ethoxylates exhibit a narrow range of homologs (nre ethoxylates).

[0232] For cold washing performance, it has proven advantageous if the agents additionally contain soap(s). Preferred agents are therefore characterized by the fact that they contain soap(s).

[0233] Suitable are 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 soap mixtures derived from natural fatty acids, e.g. coconut, palm kernel or tallow fatty acids.

[0234] Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols, each with 8 to approximately 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 respect to the alkyl moiety, as well as of alkylphenols with 5 to 12 carbon atoms in the alkyl group, are also suitable.

[0235] Preferably, alkoxylated, advantageously ethoxylated, and especially primary alcohols with preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol are used as nonionic surfactants. The alcohol residue in these alcohols may be linear or, preferably, methyl-branched at the 2-position, or the mixture may contain both linear and methyl-branched residues, as is commonly found in oxo alcohol residues. However, alcohol ethoxylates with linear residues derived from native alcohols with 12 to 18 carbon atoms, e.g., from coconut, palm, tallow, or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol, are particularly preferred. Preferred ethoxylated alcohols include, for example, Ci2-14 alcohols with 3 EO or 4 EO, Cg-n alcohol with 7 EO, Ci3-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C s alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of Ci2-14 alcohol with 3 EO and C12-18 alcohol with 5 EO.The stated degrees of ethoxylation represent statistical averages, which may be whole numbers or fractions for a specific product. Preferred alcohol ethoxylates exhibit a narrow range of homologs (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.

[0236] Another class of preferably used non-ionic surfactants, which are 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, in particular fatty acid methyl esters.

[0237] Another class of nonionic surfactants that can be used advantageously are the alkyl polyglycosides (APGs). Suitable alkyl polyglycosides satisfy the general formula RO(G) Z ,

[0238] In the formula, R represents a linear or branched, particularly 2-position methyl-branched, saturated or unsaturated, aliphatic residue with 8 to 22, preferably 12 to 18, carbon atoms, and G is the symbol for a glucose unit with 5 or 6 carbon atoms, preferably glucose. The degree of glycosylation z is between 1 and 4, preferably between 1 and 2, and particularly between 1.1 and 1.4. Linear alkyl polyglycosides are preferably used, i.e., alkyl polyglycosides in which the polyglycosyl residue is a glucose residue and the alkyl residue is an n-alkyl residue.

[0239] Non-ionic surfactants of the amine oxide type, e.g., N-cocosalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these non-ionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, and in particular not more than half of it.

[0240] Suitable amphoteric surfactants include, for example, betaines of the formula

[0241] (R iii )(R iv )(R v )N + CH2COO-,

[0242] in the R'" an alkyl group, optionally interrupted by heteroatoms or heteroatom groups, with 8 to 25, preferably 10 to 21 carbon atoms and R iv as well as R v similar or different alkyl groups with 1 to 3 carbon atoms, in particular C10-18-alkyldimethylcarboxymethyl betaine and Cn-17-alkylamidopropyldimethylcarboxymethyl betaine.

[0243] Suitable cationic surfactants include, among others, the quaternary ammonium compounds of the formula (R vi )(R vii )(R viii )(R ix )N + X',

[0244] in the R vi to R ix for four identical or different, in particular two long-chain and two short-chain, alkyl groups and X - for an anion, especially a halide ion, e.g. didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride and their mixtures.

[0245] Other suitable cationic surfactants are quaternary surfactants, particularly those with a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. By using quaternary surfactants with antimicrobial activity, the product can be formulated with antimicrobial properties, or its existing antimicrobial effect, if present due to other ingredients, can be enhanced.

[0246] Another preferred component of compositions according to the invention are complexing agents. Particularly preferred complexing agents are phosphonates, provided their use is permitted under regulations. A composition preferred within the scope of this application contains one or more phosphonates from the group consisting of aminotrimethylenephosphonic acid (ATMP) and / or its salts;

[0247] Ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or its salts;

[0248] 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. Particularly preferred are compositions containing 1-Hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates.

[0249] Preferred compositions according to the invention are characterized in that they contain at least one complexing agent from the group of phosphonates, preferably HEDP or DTPMP, wherein the weight fraction of the phosphonate to the total weight of the composition is preferably about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, further preferably about 0.3 to about 3.0 wt.% and particularly preferably about 0.5 to about 2.0 wt.%.

[0250] In various embodiments, the compositions according to the invention are essentially free of phosphonate-containing compounds. "Essentially free of phosphonate-containing compounds" in this context means that the compositions contain less than 0.2 wt.%, preferably less than 0.1 wt.%, more preferably less than 0.05 wt.%, and particularly preferably less than 0.01 wt.%, phosphonate-containing compounds, based on the total weight of the composition. In particularly preferred embodiments, these compositions are completely free of phosphonate-containing compounds.

[0251] The composition according to the invention further preferably comprises a builder, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The builders include, in particular, silicates, carbonates, and organic co-builders.

[0252] Examples of organic (co-)builders include polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic (co-)builders, and phosphonates. These classes of substances are described below. Organic co-builder substances can be present, if desired, in amounts up to approximately 40% by weight, particularly up to approximately 25% by weight, and preferably approximately 0.1 to approximately 8% by weight. Suitable organic framework substances include, for example, polycarboxylic acids that can be used in the form of the free acid and / or their sodium salts, where polycarboxylic acids are understood to be those carboxylic acids that carry 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 carboxymethylinulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycine diacetic acid, methylglycine diacetic acid, glutamine diacetic acid, nitrilotriacetic acid (NTA), iminodisuccinates such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid, polyphosphonic acids, in particular aminotris(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid), lysinetetra(methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly)carboxylic acids, in particular by oxidation of polysaccharides or...Dextrin-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. Such organic builder substances may be present in amounts up to approximately 50 wt.%, particularly up to approximately 25 wt.%, preferably approximately 10 to approximately 20 wt.%, and most preferably approximately 0.1 to approximately 5 wt.%. In addition to their builder action, the free acids typically also possess the property of an acidifying component and thus also serve to adjust the pH of the compounds to a lower and milder value. Citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof are particularly suitable. Citric acid or salts of citric acid are especially preferred as the builder substance.Further particularly preferred scaffold materials are selected from methylglycine disidic acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS), ethylenediamine disuccinate (EDDS), carboxymethylinulin, and polyaspartate. In preferred embodiments, citric acid and / or citrate are used as the water-soluble, organic builder. Particularly preferred is the use of about 0.1 to about 10 wt.%, preferably about 0.2 to about 5 wt.%, more preferably about 0.25 to about 2 wt.% citric acid and / or about 0.1 to about 10 wt.%, preferably about 0.2 to about 5 wt.%, more preferably about 0.25 to about 2 wt.% citrate, preferably alkali citrate, and 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.

[0253] Suitable scaffold materials also include polymeric polycarboxylates, such as the alkali metal salts of polyacrylic acid or polymethacrylic acid, e.g., those with a relative molecular mass of approximately 500 to approximately 70,000 g / mol. For the purposes of this application, the molar masses specified for polymeric polycarboxylates are weight-average molar masses (Mw) of the respective acid form, which were generally determined by gel permeation chromatography (GPC) using a UV detector. The measurement was performed against an external polyacrylic acid standard, which, due to its structural similarity to the polymers under investigation, provides realistic molar mass values. These values ​​differ significantly from the molar mass values ​​obtained when polystyrenesulfonic acids are used as a standard. The molar masses measured against polystyrenesulfonic acids are generally considerably higher than the molar masses specified in this application.Suitable polymers are, in particular, polyacrylates, preferably having a molecular weight of about 2,000 to about 20,000 g / mol. Due to their superior solubility, short-chain polyacrylates from this group, with molecular weights of about 2,000 to about 10,000 g / mol, and preferably about 3,000 to about 5,000 g / mol, are particularly advantageous. Copolymers of polycarboxylates are also suitable, especially those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid. Copolymers of acrylic acid with maleic acid containing about 50 to about 90 wt% acrylic acid and about 50 to about 10 wt% maleic acid have proven to be particularly suitable. Their relative molecular mass, based on free acids, is generally about 2,000 to about 70,000 g / mol, preferably about 20,000 to about 50,000 g / mol and particularly about 30,000 to about 40,000 g / mol.

[0254] Solid agents according to the invention preferably contain at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include the organic scaffolding substances mentioned above.

[0255] In addition to the aforementioned water-soluble organic builders, solid compositions according to 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 present in the form of their alkaline, neutral, or acidic sodium or potassium salts. Small amounts of calcium carbonate may also be present in solid textile detergents. Suitable examples include water-soluble crystalline and / or amorphous alkali silicates. The alkali silicates suitable as builders in compositions according to the invention preferably have a molar ratio of alkali oxide to SiO₂ below 0.95, in particular from 1:1.1 to 1:12, and may 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 may be present alone or in mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na2Si. xThe general formula O2x+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 aforementioned general formula takes the values ​​2 or 3. In particular, both β- and β-sodium disilicates (Na2Si2Ü5 • y H2O) are preferred. Practically anhydrous crystalline alkali silicates of the above-mentioned general formula, in which x is a number from 1.9 to 2.1, prepared from amorphous alkali silicates, can also be used in compositions according to the invention. In a further embodiment of compositions 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. In another embodiment of the invention, crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used.In compositions containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and particularly 1:1 to 2:1. Crystalline layered silicates of the formula (I) given above are marketed by Clariant GmbH under the trade name Na-SKS, e.g. Na-SKS-1 (Na2Si22O45 • x H2O, Kenyaite), Na-SKS-2 (Na2Sii4O29 • x H2O, Magadiite), Na-SKS-3 (Na2SisOi7 • x H2O) or Na-SKS-4 (Na2Si4Ü9 • x H2O, Makatite). Of these, Na-SKS-5 (a-Na2Si2O5), Na-SKS-7 (ß-Na2Si2O5, Natrosilite), Na-SKS-9 (NaHSi2O5• 3 H2O), Na-SKS-10 (NaHSi2O5• 3 H2O, Kanemite), Na-SKS-11 (t-Na2Si2O5) and Na-SKS-13 (NaHSi2O5), but especially Na-SKS-6 (ö-Na2Si2C>5), are particularly suitable.In one embodiment of the composition according to the invention, a granular compound of crystalline layered silicate and citrate, of crystalline layered silicate and the aforementioned (co-)polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate is used, such as that commercially available under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably contained in compositions according to the invention in amounts of about 1 to about 20 wt.%, in particular about 5 to about 15 wt.%. Furthermore, carbonates (and hydrocarbon carbonates), in particular sodium carbonate, and phosphonic acids / phosphonates are also important as water-soluble inorganic builder substances.

[0256] Solid agents according to the invention may also contain water-insoluble builder substances. In particular, crystalline or amorphous water-dispersible alkali aluminosilicates are used as water-insoluble inorganic builder materials, in amounts of up to about 50 wt.%, preferably not exceeding about 40 wt.%, particularly about 3 to about 20 wt.%, and preferably about 1 to about 15 wt.%. Among these, crystalline sodium aluminosilicates of detergent quality, especially zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, alone or in mixtures, e.g., in the form of a co-crystallizate of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA), are preferred. Amounts close to the aforementioned upper limit are preferably used in solid, particulate agents. Suitable aluminosilicates, in particular, do not contain particles with a particle size greater than 30 pm 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.

[0257] The inventive means are preferably free of phosphate builders, i.e., contain less than 1 wt.%, preferably less than 0.5 wt.%, more preferably less than 0.1 wt.%, and most preferably no deliberately added phosphate builder.

[0258] In addition to the previously described base materials, cleaning-active polymers may be included in the compositions according to the invention. The weight fraction of cleaning-active polymers in the total weight of the compositions according to the invention is—if present—preferably about 0.1 to about 20 wt.%, more preferably about 1.0 to about 15 wt.%, and more preferably about 2.0 to about 12 wt.%.

[0259] Suitable peroxygen compounds for use in compositions according to the invention include, in particular, organic peracids or pericy 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 the washing conditions, including perborate, percarbonate, persilicate and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds, such as H2G2 urea adducts.

[0260] Hydrogen peroxide can also be generated using an enzymatic system, i.e., an oxidase and its substrate. If solid peroxygen compounds are to be used, these can be in the form of powders or granules, which may also be coated in a known process. The peroxygen compounds can be added to the washing liquor as such or in the form of agents containing them, which in principle can contain all conventional detergent components. Alkali percarbonate or alkali perborate monohydrate is particularly preferred. If agents according to the invention contain peroxygen compounds, these are present in amounts preferably up to about 50 wt.%, in particular about 5 to about 30 wt.%, and preferably about 0.1 to about 20 wt.%.

[0261] The bleaching activators used in the composition according to the invention can be compounds which, under perhydrolysis conditions, yield aliphatic peroxocarboxylic acids with preferably 1 to 10 carbon atoms, in particular 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those bearing O- and / or N-acyl groups of the aforementioned 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-acylides, 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 or iso-NOBS).LOBS), 4-(2-Decanoyloxyethoxycarbonyloxy)benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic 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 a quaternary nitrogen atom, and / or Oxygen-transferring sulfonimines and / or acylhydrazones. Hydrophilically substituted acylacetals and acyllactams are also preferred. Combinations of conventional bleaching activators can also be used.Such bleach activators, if present, may be contained in the usual quantity range, preferably in amounts of about 0.5 to about 10 wt.%, particularly about 1 to about 8 wt.%, based on the total product, especially in the presence of the aforementioned hydrogen peroxide-supplying bleaching agents, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent.

[0262] In addition to or as an alternative to conventional bleach activators, solid agents may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0263] In preferred embodiments, the composition according to the invention is free of bleach, i.e., free of deliberately added peroxygen compounds, bleach activators, etc.

[0264] Suitable anti-graying agents or soil-release polymers are cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, and cellulose mixtures such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, and methyl carboxymethylcellulose. Sodium carboxymethylcellulose, hydroxypropylmethylcellulose, and mixtures thereof, and optionally mixtures thereof with methylcellulose, are preferably used. Commonly used soil-release polymers include copolyesters containing dicarboxylic acid units, alkylene glycol units, and polyalkylene glycol units. Other soil-release polymers that may be present include, for example, non-ionic cellulose ethers such as methylcellulose and methylhydroxypropylcellulose with a methoxyl group content of approximately 15 to 30 wt.% and a hydroxypropoxyl group content of approximately 1 to 15 wt.%.-%, each based on the nonionic cellulose ether, as well as polymers of phthalic acid and / or terephthalic acid or their derivatives with monomeric and / or polymeric diols known from the prior art, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates or anionically and / or nonionically modified derivatives thereof. Such are commercially available, for example, under the trade name Texcare®. Typical soil release polymers for polyester-containing textiles can be based, for example, on copolymers of polyester and polyether, including terephthalate, e.g., polypropylene terephthalate. Examples of commercially available soil release polymers include, for example, the polymers marketed by Rhodia under the trade name Repel-O-Tex, such as Repel-O-Tex SRP 4, Repel-O-Tex SRP 6, Repel-O-Tex PF, Repel-O-Tex PF 594, and the polymers marketed by BASF under the trade name Sokalan, such as...Sokalan SR 100, the polymers marketed by Sasol under the trade name Marloquest SL, and the polymers marketed by Clariant under the trade name TexCare, such as TexCare SRN-170, TexCare SRN-240, and TexCare SRN-325, are not suitable. However, these polymers are typically not biodegradable, and their use is therefore not preferred from a sustainability perspective. The content of the agent for graying inhibitors, soil-release agents, and soil-release polymers—if present—generally does not exceed approximately 1% by weight and is preferably approximately 0.05% to approximately 0.5% by weight. In preferred embodiments, the agent according to the invention is free of such agents, and in particular, free of conventional soil-release polymers.In connection with the invention, "conventional soil-release polymers" refers in particular to the following SRP polymers: cellulose ethers, such as carboxymethylcellulose, methylcellulose, hydroxyalkylcellulose; cellulose mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methylcarboxymethylcellulose; sodium carboxymethylcellulose; hydroxypropylmethylcellulose; copolyesters containing dicarboxylic acid, alkylene glycol and / or polyalkylene glycol units; polymers of phthalic acid and / or terephthalic acid, their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates, and / or their anionically and / or nonionically modified derivatives; copolymers of polyester and polyether, including terephthalate, e.g.

[0265] Polypropylene terephthalate, and mixtures thereof, consisting of the group.

[0266] Optical brighteners, particularly for textiles made from cellulose fibers (e.g., cotton), can include derivatives of diaminostilbene disulfonic acid or its alkali metal salts. Suitable examples are salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-yl-amino)stilbene-2,2'-disulfonic acid or similarly structured compounds that, instead of the morpholino group, contain a diethanolamino group, a methylamino group, or a 2-methoxyethylamino group.

[0267] Furthermore, optical brighteners of the substituted 4,4'-distyryldiphenyl type may be present, e.g., 4,4'-bis-(4-chloro-3-sulfostyryl)diphenyl. Mixtures of optical brighteners may also be used. For polyamide fibers, optical brighteners of the 1,3-diaryl-2-pyrazoline type are particularly suitable, e.g., 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazolin and similarly structured compounds. The content of optical brighteners or brightener mixtures in the composition—if present—generally does not exceed approximately 1% by weight, preferably approximately 0.05 to approximately 0.5% by weight. In preferred embodiments, compositions according to the invention are free of such active ingredients.

[0268] Conventional defoamers that can be used in compositions according to the invention include, for example, polysiloxane-silica mixtures, wherein the finely divided silica contained therein is preferably silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as cross-linked polysiloxane resins and mixtures thereof. Other defoamers include paraffin hydrocarbons, in particular microparaffins and paraffin waxes with a melting point above 40°C, saturated fatty acids or soaps with, in particular, 20 to 22 carbon atoms, e.g., sodium behenate, and alkali 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 C6-18 alkyl groups is preferably used. The proportion of the defoamers, if present, can preferably be about 0.001 to about 1% by weight.

[0269] In various embodiments, the compositions according to the invention can contain dye transfer inhibitors, preferably DTI (dye transfer inhibiting) polymers. Suitable DTI polymers include, for example, homo- or copolymers based on vinylic, nitrogen-containing, preferably heterocyclic monomers, such as N-vinylpyrrolidone, N-vinylimidazole, N-vinylcaprolactam, and 4-vinylpyridine. These compounds are typically not biodegradable. Examples of commercially available DTIs are known from US 2012 / 0225025. Other examples of DTI polymers include, but are not limited to, polyvinylpyrrolidone (e.g., Sokalan® HP 50 / BASF, PVP-K types® / ISP), vinylpyrrolidone-vinylimidazole copolymers (e.g., Sokalan® HP 56 / BASF), poly(4-vinylpyridine N-oxide) (e.g., Chromabond® S-403E / ISP), and poly(4-vinylpyridine N-carboxymethyl betaine) (e.g., Chromabond® S 400 / ISP). The proportion of DTIs, if present, may preferably be approximately 0.001 to approximately 1 wt%.

[0270] Preferably, compositions according to the invention contain at least one perfume or fragrance substance, or optionally a mixture of different perfumes or fragrance substances. Individual odorant compounds, e.g., synthetic products of the ester, ether, aldehyde, ketone, alcohol, and hydrocarbon type, can be used as perfume oils or fragrance substances. However, mixtures of different fragrance substances that together produce an appealing scent are preferred. Such perfume oils can also contain natural fragrance mixtures such as those available from plant sources, e.g., pine, citrus, jasmine, patchouli, rose, or ylang-ylang oil. Suitable fragrance and perfume substances, or mixtures thereof, are known to those skilled in the art in the field of detergent manufacturing. In preferred embodiments, compositions according to the invention can contain one or more fragrance substances in an amount typically up to about 15% by weight, preferably about 0.01% to about 5% by weight.-%, in particular about 0.3 to about 3 wt.%, based on the total weight of the composition. To adjust the desired pH value, compositions 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 hydrogen sulfates, or bases, in particular ammonium or alkali hydroxides, preferably sodium hydroxide. Such pH regulators are preferably not present in compositions according to the invention—if present—in excess of about 10 wt.%, in particular about 0.5 to about 6 wt.%, and most preferably about 0.3 to about 2 wt.%.

[0271] As a further component, compositions according to the invention can contain at least one organic solvent or a mixture of organic solvents. The addition of organic solvents has a beneficial effect on the enzyme stability and the cleaning performance of these compositions. Preferred organic solvents are from the group consisting of monohydric or polyhydric alcohols, alkanolamines, or glycol ethers.Preferably, the solvents are selected from ethanol, n- or i-propanol, butanol, glycol, propanediol, butanediol, glycerin, diglycylene glycol, propyldiglycylene glycol, butyldiglycylene glycol, 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 fraction of these organic solvents in the total weight of the composition according to the invention is - if present - preferably about 0.1 to about 10 wt.%, preferably about 0.2 to about 8.0 wt.% and further preferably about 0.5 to about 5.0 wt.%.A particularly preferred organic solvent, especially effective for stabilizing the composition, is glycerin and 1,2-propylene glycol. Liquid compositions preferably comprise at least one polyol, preferably from the group consisting of glycerin and 1,2-propylene glycol, based on the total weight of the composition—if present—preferably in amounts of about 0.1 to about 10 wt.%, more preferably about 0.2 to about 8.0 wt.%, and further preferably about 0.5 to about 5.0 wt.%. Other preferred organic solvents are the organic amines and alkanolamines. Compositions according to the invention contain these amines—if present—preferably in amounts of about 0.1 to about 10 wt.%, more preferably about 0.2 to about 8.0 wt.%, and further preferably about 0.5 to about 5.0 wt.%, in each case based on their total weight. A particularly preferred alkanolamine is ethanolamine.

[0272] The composition according to the invention can contain enzymes in a concentration suitable for the efficacy of the composition. Preferably, all enzymes that can exhibit catalytic activity in compositions according to the invention can be used, in particular selected from protease, lipase, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, β-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase, and mixtures thereof. If present, enzymes in such compositions are advantageously present in an amount of approximately 1 x 10⁻⁶. -8 up to approximately 5 wt% based on active protein. Increasingly preferred is each enzyme in an amount of approximately 1 x 10⁻⁵. -7The enzymes are contained in the composition according to the invention in amounts of up to approximately 3 wt.%, approximately 0.00001 to approximately 1 wt.%, approximately 0.00005 to approximately 0.5 wt.%, approximately 0.0001 to approximately 0.1 wt.%, and particularly preferably approximately 0.0001 to approximately 0.05 wt.%, based on active protein. The enzymes particularly preferably exhibit synergistic cleaning performance against certain soils or stains; that is, the enzymes contained in the composition mutually support each other in their cleaning performance.

[0273] Examples of proteases include 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 not as subtilisins in the strict sense. Subtilisin Carlsberg is available in an advanced form under the trade name Alcalase® from Novozymes. subtilisins 147 and 309 are marketed by Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants derived from the protease in Bacillus lentus DSM 5483 are described, for example, in WO 95 / 23221, WO 92 / 21760, WO 2013 / 060621, and EP 3660151. Other useful proteases include, for example...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 enzymes 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. Proteases from Bacillus gibsonii and Bacillus pumilus, disclosed in WO 2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697, are also particularly favored.

[0274] Examples of amylases include the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, and Bacillus stearothermophilus, as well as their improved formulations for use in detergents. The enzyme from Bacillus licheniformis is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. Further developments of this α-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). The α-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derivatives of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also by Novozymes. Furthermore, α-amylase from Bacillus sp. is suitable for this purpose.A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are particularly noteworthy. Fusion products of all the aforementioned molecules can also be used. Furthermore, the advanced versions of α-amylase from Aspergillus niger and A. oryzae, available under the trade names Fungamyl® from Novozymes, are suitable. Other advantageous commercial products include, for example, Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, as well as Amplify™ 12L or Amplify Prime™ 100L, the latter also from Novozymes, and the PREFERENZ S® series from Danisco / DuPont, including, for example, PREFERENZ S100®, PREFERENZ S1000®, and PREFERENZ S210®. Variants of these enzymes obtained through point mutations can also be used according to the invention.

[0275] Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are included. Suitable cellulases are those from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4435307, US 5648263, US 5691178, US 5776757, and WO 89 / 09259. Particularly suitable cellulases are alkaline or neutral cellulases with color-preserving properties. Examples of such cellulases are those described in EP 0495257, EP 0531372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940. Examples of cellulases with endo-1,4-glucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, e.g., those with a sequence of at least 97% identity to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091.Another example may include a GH44 xyloglucanase, e.g., a xyloglucanase enzyme with 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 Celluclean™ 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).

[0276] Suitable lipases include, for example, those from Thermomyces, e.g., from T. lanuginosus (formerly Humicola lanuginosa), as described in EP 0258068 and EP 0305216; lipase from strains of Pseudomonas (some of which are now renamed Burkholderia), e.g., P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. sp. strain SD705, P. wisconsinensis; Streptomyces lipases of the GDSL type; lipase from Thermobifida fusca; lipase from Geobacillus stearothermophilus; lipase from Bacillus subtilis; and lipase from Streptomyces griseus and S. pristinaespiralis. Preferred lipases include, for example, those originally obtained from or further developed from Humicola lanuginosa (Thermomyces lanuginosus), in particular those with one or more of the following amino acid substitutions starting from the aforementioned lipase at positions D96L, T213R and / or N233R, especially T213R and N233R.Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0277] Suitable mannanases are, for example, 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 insolensEndo-ß-mannanase and Caldocellulosiruptor sp. Endo-ß-mannanase (cf. e.g. US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0278] Pectate lyases suitable for detergents are described, for example, in WO 2003 / 095638 or WO 2015 / 121133. Other examples of suitable pectinolytic enzymes include those available under the trade names Gamanase®, Pectinex 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.

[0279] In the detergents described herein, the enzymes to be used may also be formulated together with accompanying substances, for example from fermentation. In liquid formulations, the enzymes are preferably used as liquid enzyme formulation(s).

[0280] Furthermore, it is possible to combine two or more enzymes so that a single granule has multiple enzyme activities.

[0281] The enzymes can also be incorporated into water-soluble films, such as those used in the formulation of unit-dose detergents. Such a film enables the release of the 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).

[0282] The composition according to the invention may comprise one or more reversible enzyme inhibitor(s) / stabilizer(s), preferably in a concentration of about 0.1 to about 2 wt%, preferably about 0.2 to about 1.5 wt%, based on the total weight of the composition. If several inhibitors / stabilizers are included, these values ​​refer to the total concentration. These may 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, specific peptide compounds, and combinations thereof.

[0283] In preferred embodiments, the detergents according to the invention are essentially free of boron-containing compounds. "Essentially free of boron-containing compounds" in this context means that the compositions according to the invention contain less than 0.2 wt.%, preferably less than 0.1 wt.%, more preferably less than 0.05 wt.%, and particularly preferably less than 0.01 wt.%, boron-containing compounds, based on the total weight of the composition. In particularly preferred embodiments, the compositions according to the invention are free of boron-containing compounds, i.e., they contain, in particular, no boric acid and / or phenylboronic acid derivatives.

[0284] If detergents according to the invention are formulated in multiple phases, they may contain one or more phase separation aids. Suitable phase separation aids, besides citric acid or citrates, include, for example, alkali metal and alkaline earth metal halides, in particular chlorides and sulfates, as well as nitrates, in particular sodium and potassium chloride and sulfate, and ammonium chloride and sulfate, or mixtures thereof. As strong electrolytes that increase ion strength, such salts support phase separation through the salt effect. Sodium chloride has proven particularly effective in this regard, while sodium sulfate and, in particular, magnesium sulfate have a less pronounced phase-separating effect. According to the invention, compositions may contain phase separation aids—if present—in amounts, based on the total weight of the composition, of approximately 0.01 to approximately 30 wt.%, preferably approximately 0.1 to approximately 20 wt.%, e.g., approximately 1 to approximately 15 wt.% or approximately 1 to approximately 5 wt.%.

[0285] To adjust the viscosity, the composition according to the invention can contain one or more thickening agents, if present, preferably in an amount of about 0.01 to about 5 wt.%, more preferably about 0.05 to about 2.5 wt.%, and even more preferably about 0.1 to about 1 wt.%. Suitable thickeners include, for example, organic natural thickeners (agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar gum, locust bean gum, starch, dextrins, gelatin, casein), organic modified natural substances (carboxymethylcellulose and other cellulose ethers, hydroxyethyl and hydroxypropyl cellulose and the like, bean gum ethers), organic fully synthetic thickeners (polyacrylic and polymethacrylic compounds, vinyl polymers, polycarboxylic acids, polyethers, polyimines, polyamides) and inorganic thickeners (polysilicic acids, clay minerals such as montmorillonite, zeolites, silicic acids).

[0286] Exemplary compositions and suitable ingredients are described, for example, in WO 2001 / 44433 and WO 2016 / 091650.

[0287] An exemplary composition of a detergent according to the invention, in particular a liquid detergent, comprises, in addition to the peptides described herein, the following components:

[0288] • Water; and

[0289] • Surfactants, in particular anionic and / or non-ionic surfactants; and / or

[0290] • Enzymes; and / or

[0291] • Fragrances; and / or

[0292] • Complexing agents, e.g., phosphonates, especially HEDP and / or DTPMP; and / or

[0293] • Builders, e.g. citric acid and / or citrate; and / or

[0294] • Antifoaming agent.

[0295] A detergent according to the invention, in particular a liquid textile detergent, preferably comprises, in addition to the peptides according to the invention, the following components, each based on the total weight of the agent:

[0296] • at least one surfactant, preferably in a concentration of 0.5 to 15 wt.%, wherein the total surfactant content is preferably 10 to 12 wt.%; and / or

[0297] • at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%; and / or at least one enzyme, preferably in a concentration of 0.00001 to 5 wt.%; and / or

[0298] • at least one fragrance or perfume ingredient and / or at least one fragrance storage substance, preferably in a concentration of 0.0001 to 2 wt.%, more preferably 0.1 to 1 wt.%; and / or

[0299] • at least one antifoaming agent, preferably in a concentration below 1 wt.%, e.g. below 0.1 wt.% or below 0.01 wt.%; and / or

[0300] • Water.

[0301] Washing performance

[0302] Within the scope of the invention, washing performance is understood to mean the ability of a means to partially or completely remove existing soiling, in particular the brightening performance of one or more soilings on textiles. The washing performance is preferably determined as described below.

[0303] The term "wash liquor" refers to the solution containing the detergent that comes into contact with the textiles or fabrics, thus interacting with the soiling present on them. The wash liquor is typically created when the washing process begins and the detergent is diluted with water, for example, in a washing machine or other suitable container.

[0304] The washing performance can be determined in a washing system containing a detergent in a dosage between 2.0 and 8.0 grams per liter of washing liquor, as well as the peptides to be tested.

[0305] A liquid reference detergent for such a washing system can, for example, be composed as follows (all values ​​in weight percent (wt%)): 4.4% alkylbenzenesulfonic acid, 5.6% other anionic surfactants, 2.4% C12-18 sodium salts of fatty acids (soaps), 4.4% non-ionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% sodium hydroxide (NaOH), 0.01% defoamer, 2% glycerin, 0.08% preservatives, 1% ethanol, remainder demineralized water. Preferably, the dosage of the liquid detergent is between 3.0 and 6.0 grams per liter of wash liquor, e.g., 3.0, 3.2, 3.5, 3.7, 4.0, 4.5, 4.7, 4.9, or 5.9 grams per liter of wash liquor. Washing is preferably carried out in a pH range between pH 7 and pH 10.5, preferably between pH 8 and pH 9.

[0306] Washing performance is determined by measuring the degree of cleanliness of the washed textiles, based on the degree of soiling on the fabric. For example, the washing process can take place for 60 minutes at a temperature of 40°C, with the water having a hardness between 15.5°dH and 16.5°dH (German hardness).

[0307] The degree of whiteness, i.e., the lightening of the soiling, as a measure of the washing performance, is determined using optical measurement methods, preferably photometrically. A suitable device for this purpose is, for example, the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably a supplied white standard. Preferred embodiments of the inventive means achieve such advantageous washing performances even at low temperatures, particularly in the temperature ranges between about 10°C and about 60°C, preferably about 15°C to about 50°C, and most preferably about 20°C to about 40°C, e.g., at 20°C, 25°C, 30°C, or 40°C.

[0308] Methods and uses

[0309] Another object of the invention is a method for cleaning textiles which is characterized in that an agent according to the invention is used in at least one process step.

[0310] In various embodiments, the above-described method is characterized by being carried out at a temperature of 0°C to approximately 100°C, preferably approximately 20°C to approximately 60°C, and particularly preferably approximately 20°C to approximately 40°C, e.g., at 20°C, 25°C, 30°C, or 40°C. 20°C represents a low washing temperature, while 40°C is the preferred / average washing temperature in Europe.

[0311] This includes both manual and machine-based methods, with machine-based methods being preferred due to their more precise controllability, for example, regarding the quantities used and contact times. Methods for cleaning textiles are generally characterized by the fact that, in several process steps, various cleaning agents are applied to the item to be cleaned and rinsed off after the contact time, or that the item to be cleaned is treated in some other way with a detergent or a solution or dilution thereof.

[0312] The method preferably relates to a machine washing process, in particular in a washing machine, or a hand washing process. The peptide described herein preferably acts as a textile conditioning agent.

[0313] Alternative embodiments of this invention also include methods for treating textile raw materials or for textile care, in which an agent according to the invention is active in at least one process step. Methods for textile raw materials, fibers, or textiles with natural components are preferred, and especially for those containing wool or silk.

[0314] Another aspect of the invention is the use of an agent according to the invention for cleaning textiles, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C, e.g. at 20°C, 25°C, 30°C or 40°C.

[0315] Another aspect of the invention is the use of a peptide described herein in a detergent according to the invention to improve the cleaning performance of the detergent, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C, e.g. at 20°C, 25°C, 30°C or 40°C.

[0316] In preferred embodiments, the use of peptides according to the invention leads to a textile conditioning effect, i.e., peptides according to the invention have a textile conditioning effect on textiles, preferably during the washing process, more preferably as a component of a detergent.

[0317] In particular, the presence of the peptide, which preferably binds to and / or adheres to textiles, preferably textiles containing synthetic fibers and / or plastics, preferably polyester-containing textiles, or blended fabrics, improves the textiles' ability to wick away moisture and / or protects them from excessive deformation due to wear and washing, etc. The textile-conditioning effect of the peptides becomes particularly pronounced after several washes, as it is a continuously accumulating effect. After several washes, typically after just 3 or more, e.g., 4, 5, 6, 7, 8, 9, 10 or more, the effect becomes increasingly stronger. The adhering peptides improve the moisture regulation of the textiles. The adhering peptides improve the dimensional stability of the textiles.The attached peptides improve the moisture regulation and / or shape retention of textiles. They enhance moisture regulation by absorbing moisture (e.g., perspiration) from the skin and promoting evaporation, and / or by transporting the absorbed moisture (e.g., perspiration) along the textile surface via capillary action, thus distributing it over a larger area for faster evaporation. Improved wicking of absorbed moisture (e.g., perspiration) accelerates the drying process of textiles. These aspects are generally relevant for all textiles, but are particularly beneficial for functional clothing, such as sportswear or outdoor apparel made from synthetic fibers.Improved moisture transport and faster evaporation allow for better regulation of body temperature and reduce discomfort caused by excessive moisture buildup in the fabric. This improved and faster evaporation keeps the wearer dry and comfortable.

[0318] In another aspect, the invention relates to the use of a peptide described herein in a textile detergent to improve the moisture regulation of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer.

[0319] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the moisture regulation of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3a.

[0320] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the moisture regulation of textiles, wherein the improvement compared to a textile detergent without such a peptide is determined as described in Example 3a.

[0321] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the moisture regulation of textiles, wherein the improvement is determined in comparison to a textile detergent with a conventional SRP polymer as described in Example 3a.

[0322] In another aspect, the invention relates to the use of a peptide described herein in a textile detergent to improve the dimensional stability of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer.

[0323] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the dimensional stability of textiles, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3b.

[0324] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the dimensional stability of textiles, wherein the improvement compared to a textile detergent without such a peptide is determined as described in Example 3b.

[0325] In preferred embodiments, the invention relates to the use of a peptide described herein in a textile detergent to improve the dimensional stability of textiles, wherein the improvement is determined in comparison to a textile detergent with a conventional SRP polymer as described in Example 3b.

[0326] In preferred embodiments, the peptides according to the invention achieve the effect according to the invention when used in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C, e.g. at 20°C, 25°C, 30°C or 40°C.

[0327] All circumstances, objects, and embodiments described for peptides and agents according to the invention are also applicable to these inventions. Therefore, explicit reference is made here to the disclosure at the relevant point, with the note that this disclosure also applies to the aforementioned use according to the invention. PREFERRED EMBODIMENTS

[0328] 1. Textile detergent, comprehensive

[0329] (A) at least one peptide, in a concentration of about 0.00001 to about 5 wt.%, preferably about 0.0001 to about 2 wt.%, more preferably about 0.001 to about 1 wt.%, particularly preferably about 0.075 wt.% to about 0.75 wt.%,

[0330] where at least one peptide is selected from

[0331] (a) a peptide with the following amino acid sequence (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t,

[0332] where

[0333] X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I,

[0334] X 2 selected from R, H and K, preferably R and K,

[0335] X 3 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

[0336] X 4 selected from A, L and V, preferably A and L,

[0337] X 5 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.

[0338] m and t are each 0 or 1, where m+t = 0 or 1,

[0339] n is an integer from 0 to 2,

[0340] o 0 or 1 is,

[0341] p is an integer from 0 to 9,

[0342] q is an integer from 0 to 2,

[0343] r is an integer from 1 to 4, and

[0344] s is an integer from 0 to 4;

[0345] wherein the peptide improves the moisture regulation of textiles and / or wherein the peptide improves the dimensional stability of textiles,

[0346] or

[0347] b) a peptide having an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58;

[0348] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0349] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0350] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%; and / or (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, more preferably 0.001 to 1 wt.%; and

[0351] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0352] 2. Means according to point 1 , wherein the peptide according to 1 a)

[0353] (a1) has a total charge of 0 to +7, or

[0354] (a2) if r > 4, has a total charge of 0 to +4, or

[0355] (a3) if r < 4, has a total charge of +1 to +7.

[0356] 3. Means according to point 1 or 2, wherein

[0357] (b) the peptide according to 1a) has a total charge of 0 to +7, preferably 0 to +4, and / or

[0358] (c) the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge, and / or

[0359] (d1) the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net negative charge and preferably comprises at least one negatively charged amino acid, in particular E, or

[0360] (d2) the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a neutral net charge, or

[0361] (d3) the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net positive charge, and / or

[0362] (e1) if the total charge is less than +4, the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net negative charge and preferably includes at least one negatively charged amino acid, in particular E, or (e2) if the total charge is greater than +4, the N-terminus of the peptide according to 1a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to 1a) comprising the last 1-5 amino acids has a net positive charge.

[0363] 4. Means according to one of points 1 to 3, wherein in the peptide according to 1 a), if 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 Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z 6 ]3(Z 7 ) V is, whereby

[0364] Z 1 like X 2 In point 1, defined and selected from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4 The following are defined and selected in point 1 from A, L and V, preferably A and L,

[0365] Z 4 like X 3 defined and selected in point 1 is 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.

[0366] u 1 or 2 is,

[0367] Z 7 like X 5 defined and selected in point 1 is 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, as defined in point 1 and is an integer from 0 to 4.

[0368] 5. Means according to point 4, wherein,

[0369] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0370] (ii) if u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0371] 6. Means according to point 4 or 5, wherein

[0372] (i) the peptide comprises at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids at positions 1-3; and / or

[0373] (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or

[0374] (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or

[0375] (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0376] (v) the peptide comprises at least one, preferably two or three, motif(s) RAL; and / or

[0377] (vi) the peptide comprises the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0378] 7. Means according to any of points 1 to 6, wherein the peptide has an amino acid sequence that is 80% and increasingly preferentially at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-58; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0379] 8. Textile detergent, comprehensive

[0380] (A) at least one peptide, in a concentration of about 0.00001 to about 5 wt%, preferably about 0.0001 to about 2 wt%, more preferably about 0.001 to about 1 wt%, particularly preferably about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that 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 peptides listed in SEQ ID NOs: 1-58 exhibits amino acid sequences;

[0381] (B) at least one surfactant selected from anionic and / or nonionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%; (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0382] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0383] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0384] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0385] 9. Textile detergent, comprehensive

[0386] (A) at least one peptide, in a concentration of about 0.00001 to about 5 wt%, preferably about 0.0001 to about 2 wt%, more preferably about 0.001 to about 1 wt%, particularly preferably about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that has 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-58;

[0387] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0388] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0389] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0390] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0391] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0392] 10. Textile detergent, comprehensive

[0393] (A) at least one peptide in a concentration of about 0.00001 to about 5 wt%, preferably about 0.0001 to about 2 wt%, more preferably about 0.001 to about 1 wt%, particularly preferably about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that has 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 10, 25 or 32;

[0394] (B) at least one surfactant selected from anionic and / or nonionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%; (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0395] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0396] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0397] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0398] 11. Textile detergent, comprehensive

[0399] (A) at least one peptide, in a concentration of about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that has 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 10, 25 or 32;

[0400] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0401] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0402] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0403] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0404] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0405] 12. Textile detergent, comprehensive

[0406] (A) at least one peptide, in a concentration of not more than 0.1 wt%, preferably not more than 0.09 wt%, wherein the at least one peptide has an amino acid sequence which has 100% sequence identity with the amino acid sequence specified in SEQ ID NO:10;

[0407] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0408] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%; (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0409] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0410] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0411] 13. Textile detergent, comprehensive

[0412] (A) at least one peptide in a concentration of about 0.075 wt% to about 0.75 wt%, in particular 0.09 wt% or 0.64 wt%, preferably not more than 0.1 wt%, further preferably not more than 0.09 wt%, wherein the at least one peptide has an amino acid sequence which has 100% sequence identity with the amino acid sequence specified in SEQ ID NO:25;

[0413] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0414] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0415] (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0416] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0417] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0418] 14. Textile detergent, comprehensive

[0419] (A) at least one peptide in a concentration of about 0.075 wt% to about 0.75 wt%, in particular 0.09 wt% or 0.64 wt%, preferably not less than 0.75 wt%, further preferably not less than 0.64 wt%, wherein the at least one peptide has an amino acid sequence which has 100% sequence identity with the amino acid sequence specified in SEQ ID NO:32;

[0420] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0421] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%; (D) optionally, at least one complexing agent, in particular selected from HEDP and / or DTPMP, preferably in a concentration of about 0.1 to about 8.0 wt.%, more preferably about 0.2 to about 5.0 wt.%, particularly preferably about 0.3 to about 3.0 wt.% and most preferably about 0.5 to about 2.0 wt.%;

[0422] (E) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0423] (F) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0424] 15. Agent according to any of points 1 to 14, wherein the at least one peptide is suitable for adhesion and / or binding to textiles, wherein the adhesion to textiles is determined as described in Example 2.

[0425] 16. A composition according to any one of points 1 to 14, wherein the composition is substantially free of conventional soil-release polymers, wherein conventional soil-release polymers are in particular composed of cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, cellulose mixed ethers such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methyl carboxymethylcellulose, sodium carboxymethylcellulose, hydroxypropylmethylcellulose, copolyesters containing dicarboxylic acid, alkylene glycol and / or polyalkylene glycol units, polymers of phthalic acid and / or terephthalic acid, their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates, and / or their anionically and / or nonionically modified derivatives, copolymers of polyester and polyether, including terephthalate, e.g.

[0426] Polypropylene terephthalate, as well as mixtures thereof, are selected from the existing group.

[0427] 17. Use of a peptide in a textile detergent to improve the moisture regulation of textiles, wherein the peptide is selected from

[0428] (a) a peptide with the following amino acid sequence (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t,

[0429] where

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

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

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

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

[0434] X 5selected 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.

[0435] m and t are each 0 or 1, where m+t = 0 or 1,

[0436] n is an integer from 0 to 2,

[0437] o 0 or 1, p is an integer from 0 to 9,

[0438] q is an integer from 0 to 2,

[0439] r is an integer from 1 to 4, and

[0440] s is an integer from 0 to 4;

[0441] or

[0442] b) a peptide having an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0443] 18. Use of a peptide in a textile detergent to improve the dimensional stability of textiles, wherein the peptide is selected from

[0444] (a) a peptide with the following amino acid sequence (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t,

[0445] where

[0446] X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I,

[0447] X 2 selected from R, H and K, preferably R and K,

[0448] X 3 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

[0449] X 4 selected from A, L and V, preferably A and L,

[0450] X 5selected 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.

[0451] m and t are each 0 or 1, where m+t = 0 or 1,

[0452] n is an integer from 0 to 2,

[0453] o 0 or 1 is,

[0454] p is an integer from 0 to 9,

[0455] q is an integer from 0 to 2,

[0456] r is an integer from 1 to 4, and

[0457] s is an integer from 0 to 4;

[0458] or

[0459] b) a peptide having an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0460] 19. Use according to point 17 or 18, wherein the peptide according to 17a) and / or 18a) (a1) has a total charge of 0 to +7, or

[0461] (a2) if r > 4, has a total charge of 0 to +4, or

[0462] (a3) if r < 4, has a total charge of +1 to +7. 20. Use according to any of points 17 to 19, wherein

[0463] (b) the peptide according to 17a) and / or 18a) has a total charge of 0 to +7, preferably 0 to +4, and / or

[0464] (c) the N-terminus of the peptide according to 17a) and / or 18a) comprising the first 1-5 amino acids has a net positive charge, and / or

[0465] (d1) the C-terminus of the peptide according to 17a) and / or 18a) comprising the last 1-5 amino acids has a net negative charge and preferably includes at least one negatively charged amino acid, in particular E, or

[0466] (d2) the C-terminus of the peptide according to 17a) and / or 18a) comprising the last 1-5 amino acids has a neutral net charge, or

[0467] (d3) the C-terminus of the peptide according to 17a) and / or 18a) comprising the last 1-5 amino acids has a net positive charge, and / or

[0468] (e1) if the total charge is less than +4, the N-terminus of the peptide according to 17a) and / or 18a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to 17a) and / or 18a) comprising the last 1-5 amino acids has a net negative charge and preferably comprises at least one negatively charged amino acid, in particular E, or

[0469] (e2) if the total charge is greater than +4, the N-terminus of the peptide according to 17a) and / or 18a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to 17a) and / or 18a) comprising the last 1-5 amino acids has a net positive charge.

[0470] 21. Use according to any of points 17 to 20, wherein in the peptide according to 17a) and / or 18a), if 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 Z 1 Z 2 Z 3 [(Z 4 )UZ 5 Z 6 ]3(Z 7 ) V is,

[0471] where

[0472] Z 1 like X 2 defined in point 17 or 18 and selected from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4defined and selected in point 17 or 18 are from A, L and V, preferably A and L,

[0473] Z 4 like X 3 defined in point 17 or 18 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,

[0474] u 1 or 2 is,

[0475] Z 7 like X 5 defined in point 17 or 18 and 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,

[0476] vwie s is defined in point 17 or 18 and is an integer from 0 to 4.

[0477] 22. Use according to point 21, wherein,

[0478] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0479] (ii) if u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0480] 23. Use according to any one of points 21 or 22, wherein (i) the peptide comprises at least one motif selected from RAL and RLA, preferably RAL, and wherein this sequence is preferably localized in the N-terminal amino acids at positions 1-3; and / or

[0481] (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or

[0482] (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or

[0483] (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0484] (v) the peptide comprises at least one, preferably two or three, motif(s) RAL; and / or

[0485] (vi) the peptide comprises the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0486] 24. Use according to any of points 17 to 23, wherein the peptide has an amino acid sequence that is 80% and increasingly preferentially at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-58; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-58.

[0487] 25. Use according to any of points 17 to 24, wherein the peptide has an amino acid sequence according to one of the amino acid sequences mentioned in SEQ ID NOs: 10, 25 or 32.

[0488] 26. Use according to any of points 17 to 25, wherein the at least one peptide is suitable for adhesion and / or bonding to textiles, wherein the adhesion to textiles is determined as described in Example 2.

[0489] 27. Use according to one of points 17 to 26, wherein the means comprises

[0490] (A) containing at least one peptide in a concentration of about 0.00001 to about 5 wt.%, preferably about 0.0001 to about 2 wt.%, more preferably about 0.001 to about 1 wt.%, particularly preferably about 0.075 wt.% to about 0.75 wt.%,

[0491] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0492] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0493] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and (E) water in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0494] 28. Use according to any of points 17 to 27, wherein the means comprises

[0495] (A) at least one peptide in a concentration of about 0.00001 to about 5 wt%, preferably about 0.0001 to about 2 wt%, more preferably about 0.001 to about 1 wt%, particularly preferably about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that has 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 10, 25 or 32;

[0496] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0497] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0498] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0499] (E) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0500] 29. Use according to one of points 17 to 28, wherein the means comprises

[0501] (A) at least one peptide, in a concentration of about 0.075 wt% to about 0.75 wt%, wherein the at least one peptide is selected from a peptide having an amino acid sequence that has 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 10, 25 or 32;

[0502] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0503] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0504] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0505] (E) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0506] 30. Use according to one of points 17 to 29, wherein the means comprises

[0507] (A) at least one peptide, in a concentration of not more than 0.1 wt%, preferably not more than 0.09 wt%, wherein the at least one peptide has an amino acid sequence that has 100% sequence identity with the amino acid sequence specified in SEQ ID NQ:10; (B) at least one surfactant, selected from anionic and / or nonionic surfactants, each in a concentration of 0.5 to 12 wt%, preferably 0.5 to 7.5 wt%, wherein the total surfactant content is 7.5 to 15 wt%, preferably 10 to 12 wt%;

[0508] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0509] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0510] (E) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0511] 31. Use according to one of points 17 to 30, wherein the means comprises

[0512] (A) at least one peptide in a concentration of about 0.075 wt% to about 0.75 wt%, in particular 0.09 wt% or 0.64 wt%, preferably not more than 0.1 wt%, further preferably not more than 0.09 wt%, wherein the at least one peptide has an amino acid sequence which has 100% sequence identity with the amino acid sequence specified in SEQ ID NO:25;

[0513] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0514] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0515] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0516] (E) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.

[0517] 32. Use according to one of points 17 to 31, wherein the means comprises

[0518] (A) at least one peptide in a concentration of about 0.075 wt% to about 0.75 wt%, in particular 0.09 wt% or 0.64 wt%, preferably not less than 0.75 wt%, further preferably not less than 0.64 wt%, wherein the at least one peptide has an amino acid sequence which has 100% sequence identity with the amino acid sequence specified in SEQ ID NO:32;

[0519] (B) at least one surfactant selected from anionic and / or non-ionic surfactants, each in a concentration of 0.5 to 12 wt.%, preferably 0.5 to 7.5 wt.%, wherein the total surfactant content is 7.5 to 15 wt.%, preferably 10 to 12 wt.%;

[0520] (C) at least one builder, preferably citric acid and / or citrate, in a concentration of 0.1 to 10 wt.%, in particular 0.2 to 5 wt.% or 0.25 to 2 wt.%;

[0521] (D) at least one enzyme in a concentration of 0.00001 to 5 wt.%, preferably 0.0001 to about 2 wt.%, further preferably 0.001 to 1 wt.%; and

[0522] (E) Water, in a concentration of more than 40 wt.%, preferably about 50 to about 90 wt.%, further preferably about 60 to about 85 wt.%.33.Use according to any one of claims 17 to 32, wherein the agent is substantially free of, preferably free of, conventional soil-release polymers, wherein conventional soil-release polymers are in particular composed of cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, cellulose mixed ethers such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methyl carboxymethylcellulose, sodium carboxymethylcellulose, hydroxypropylmethylcellulose, copolyesters containing dicarboxylic acid, alkylene glycol and / or polyalkylene glycol units, polymers of phthalic acid and / or terephthalic acid, their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates, and / or their anionically and / or nonionically modified derivatives, copolymers of polyester and polyether, including terephthalate, e.g.

[0523] Polypropylene terephthalate, as well as mixtures thereof, are selected from the existing group.

[0524] 34. Use according to any of points 17 to 33, wherein the improvement is determined in comparison to a textile detergent without such peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3a.

[0525] 35. Use according to any of points 17 to 34 in a temperature range of about 20°C to about 60°C, preferably about 20°C to 40°C. EXAMPLES

[0526] Example 1: Materials

[0527] Table 2: Peptide sequences

[0528]

[0529] The peptides listed in Table 2 were produced by chemical synthesis.

[0530] Table 3: Textiles used

[0531]

[0532] Table 4: Detergent matrix used

[0533]

[0534] All figures are given in wt.%, based on the total weight of the product.

[0535] Example 2: Adhesion test of peptides on polyester and blended fabrics

[0536] The adhesion of peptides 1 to 3 according to Table 2 to textile C was checked.

[0537] Test setup: Direct measurement method with pBCA in a 48-well microtiter plate with fabric swabs with a diameter of 10 mm.

[0538] Three patches of each peptide dilution were placed in a 48-well microtiter plate, and 0.2 ml of peptide solution (0.02 mg / ml in distilled water) was added to each patch. The mixture was incubated for 1 hour at room temperature, shaking at 750 rpm. The patches were then washed three times with 0.5 ml of distilled water, shaking at 750 rpm for 5 minutes each. Afterward, 0.2 ml of distilled water and 0.2 ml of BCA reagent were added, and the mixture was incubated for 60 minutes at 60°C. Immediately following this, the absorbance was measured at 562 nm. Table 4 shows the percentage of the applied amount (100%) of peptide that adheres to the respective textile. The higher the value, the higher the binding affinity.

[0539] Table 5: Adhesion of peptides to test tissue

[0540]

[0541] Peptides 1 and 2 exhibit high binding affinity. Peptide 3 exhibits low binding affinity. Peptides 1 to 3 are textile-binding peptides.

[0542] Example 3: Determining textile care properties

[0543] In a detergent matrix according to Table 4, either a conventional soil release polymer (CP propylene glycol terephthalate liquid; 0.06% active substance) (V2) or a peptide according to the invention (peptides 1 to 3; 0.088 wt.% and 0.637 wt.% active substance in the formulation, respectively; E1 to E6) was incorporated. As a further control, V1 = matrix according to Table 4 without any further additives was used.

[0544] Table 6: Experimental approaches

[0545]

[0546] Test fabrics according to Table 2 (2.5 kg, including ballast fabric) were washed ten times each in a front-loading washing machine (Miele WCI 360WTL) using 50 ml of detergent (preparations according to Table 6) in the easy-care program (100 min) at 40°C. The textiles were air-dried between washes and after the final wash.

[0547] After the 5th and 10th washes, the moisture management and elasticity of the washed and dried test textiles were determined. Example 3a: Determination of moisture management

[0548] To assess the moisture regulation of textiles, the absorption rate of textile surfaces with respect to water is determined using the so-called "rise height method" according to DIN 539242020-09. For this purpose, textile strips to be tested (5 pieces per test, 250 mm long, 35 mm wide) are stretched vertically in an apparatus so that the lower end is immersed in a tray containing test liquid (colored water). After 1, 3, 5, and 10 minutes, the extent to which the test liquid has risen in the textile strips is measured.

[0549] The results are shown in Table 7 (mean of 5 measurements per approach, with standard deviation).

[0550] Table 7: Results of humidity regulation

[0551]

[0552]

[0553] New and unwashed textile

[0554] The peptides P1 to P3 according to the invention improve the moisture regulation of polyester-cotton blend fabric (textile A) and polyester fabric (textile B), the effect being comparable to or better than that of a detergent with a conventional SRP (V2).

[0555] Example 3b: Determining textile shape stability

[0556] To assess textile dimensional stability, the tensile elastic behavior of textile fabrics is determined under a single tensile stress between constant yield strengths according to DIN 53835 Part 13, unless explicitly stated otherwise. This allows the residual elongation to be determined, which provides an indication of the expected dimensional stability behavior. For this purpose, textile strips to be tested (220 mm long, with a marked test section of 100 mm, 50 mm wide; 5 pieces per test) are clamped in an apparatus under the influence of a pre-tension force of 0.22 Newtons with a velocity pre-force of 100 mm / s. The total elongation depends on the textile and the maximum tensile force; the value should be > 50 Newtons. Textile A: total elongation 45%, Textile B: total elongation 60%.

[0557] Each textile strip under investigation undergoes a stress cycle, the stress cycle comprising the following steps.

[0558] 1) Stretching the test specimen to the defined total elongation

[0559] 2) Defined dwell time in the stretched state, here 1 min,

[0560] 3) The sample is taken from the unloaded state and relaxed for a specified recovery period (3 min).

[0561] The residual elongation is determined using the following formula: length increase x 100 / initial value. The results are shown in Table 8 (mean value from 5 measurements per approach, with standard deviation).

[0562] Table 8: Results of textile shape stability

[0563]

[0564]

[0565] New and unwashed textile

[0566] The peptides P1 to P3 according to the invention improve textile shape stability, i.e., they exhibit lower residual elongation. On polyester-cotton blends (textile A), the shape stability of the detergents containing peptides (E1 to E6) according to the invention is better than when using a detergent without SRP (V1) and comparable to a detergent with a conventional SRP (V2). On polyester fabrics (textile B), the shape stability of the detergents containing peptides (E1 to E6) according to the invention is better than when using a detergent without SRP (V1) or a detergent with a conventional SRP (V2).

[0567] In summary, the peptides P1 to P3 according to the invention lead to improved moisture regulation and improved textile shape stability. Improved moisture regulation ensures comfortable wear. Good textile shape stability means that the textiles retain their shape and do not deform even after several wear and wash cycles. This improves the durability of the textiles.

[0568] The peptides P1 to P3 according to the invention also represent good, if not improved, and sustainable alternatives to conventional SRP polymers.

Claims

1. PATENT CLAIM 1. Textile detergent comprising at least one peptide, where at least one peptide is selected from (a) a peptide with the following amino acid sequence (C) m (X 1 )n(X 2 )o[(X 3 )p(X 4 ) q ]r(X 5 )s(C)t, where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, X 3 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 selected from A, L and V, preferably A and L, X 5 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 is an integer from 0 to 2, o 0 or 1 is, p is an integer from 0 to 9, q is an integer from 0 to 2, r is an integer from 1 to 4, and s is an integer from 0 to 4; wherein the peptide improves the moisture regulation of textiles and / or wherein the peptide improves the dimensional stability of textiles, or b) a peptide having an amino acid sequence that has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-58.

2. Means according to claim 1, wherein the peptide according to claim 1a) (a1) has a total charge of 0 to +7, or (a2) if r > 4, has a total charge of 0 to +4, or (a3) if r < 4, has a total charge of +1 to +7.

3. Means according to claim 1 or 2, wherein (b) the peptide according to claim 1a) has a total charge of 0 to +7, preferably 0 to +4, and / or (c) the N-terminus of the peptide according to claim 1a) comprising the first 1-5 amino acids has a net positive charge, and / or (d1) the C-terminus of the peptide according to claim 1a) comprising the last 1-5 amino acids has a net negative charge and preferably comprises at least one negatively charged amino acid, in particular E, or (d2) the C-terminus of the peptide according to claim 1a) comprising the last 1-5 amino acids has a neutral net charge, or (d3) the C-terminus of the peptide according to claim 1a) comprising the last 1-5 amino acids has a net positive charge, and / or (e1) if the total charge is less than +4, the N-terminus of the peptide according to claim 1a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to claim 1a) comprising the last 1-5 amino acids has a net negative charge and preferably comprises at least one negatively charged amino acid, in particular E, or (e2) if the total charge is greater than +4, the N-terminus of the peptide according to claim 1a) comprising the first 1-5 amino acids has a net positive charge and the C-terminus of the peptide according to claim 1a) comprising the last 1-5 amino acids has a net positive charge.

4. Composition according to any one of claims 1 to 3, wherein in the peptide according to claim 1 a), if 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 Z 1 Z 2 Z 3 [(Z4 ) U Z 5 Z 6 ]3(Z 7 ) V is, whereby Z 1 like X 2 The term defined in claim 1 is selected from R, H and K, preferably R, Z. 2 , Z 3 , Z 5 and Z 6 like X 4 The following are defined and selected in claim 1 from A, L and V, preferably A and L, Z 4 like X 3 as defined in claim 1 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably F, R, E, A, Q and W, u 1 or 2 is, Z 7 like X 5 as defined in claim 1 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, vwie s is defined in claim 1 and is an integer from 0 to 4.

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

6. Use according to claim 4 or 5, wherein (i) the peptide comprises at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids at positions 1-3; and / or (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids at 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.

7. Composition according to any one of claims 1 to 6, 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%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-58; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-58.

8. Composition according to any one of claims 1 to 7, wherein the at least one peptide is suitable for adhesion and / or bonding to textiles, wherein the adhesion to textiles is determined as described in Example 2.

9. Composition according to any one of claims 1 to 8, wherein the composition is substantially free of conventional soil-release polymers, wherein conventional soil-release polymers are in particular composed of cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, cellulose mixed ethers such as methylhydroxyethylcellulose, methylhydroxypropylcellulose and methyl carboxymethylcellulose, sodium carboxymethylcellulose, hydroxypropylmethylcellulose, copolyesters containing dicarboxylic acid, alkylene glycol and / or polyalkylene glycol units, polymers of phthalic acid and / or terephthalic acid, their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates, and / or their anionically and / or nonionically modified derivatives, copolymers of polyester and polyether, including terephthalate, e.g. Polypropylene terephthalate, as well as mixtures thereof, are selected from the existing group.

10. Method for cleaning textiles characterized in that in at least one process step an agent according to one of claims 1 to 9 is used, 11. Method for improving the moisture regulation of textiles, characterized in that in at least one method step an agent according to one of claims 1 to 9 is used.

12. A method for improving the dimensional stability of textiles, characterized in that an agent according to one of claims 1 to 9 is used in at least one method step.

13. A method according to one of claims 10 to 12, wherein the method is carried out in a temperature range of about 20°C to about 60°C, preferably about 20°C to 40°C.

14. Use of an agent according to any one of claims 1 to 9 for cleaning textiles.

15. Use of a peptide in a textile detergent to improve the moisture regulation of textiles, wherein the peptide is defined as in any one of claims 1 to 8, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3a.

16. Use of a peptide in a textile detergent to improve the dimensional stability of textiles, wherein the peptide is defined as in any one of claims 1 to 8, wherein the improvement is determined in comparison to a textile detergent without such a peptide and / or in comparison to a textile detergent with a conventional SRP polymer as described in Example 3b.

17. Use according to any one of claims 14 to 16 in a temperature range of about 20°C to about 60°C, preferably about 20°C to 40°C

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