DE102016209406A1 - Stabilized enzyme-containing detergents and cleaners - Google Patents

Abstract

The present invention relates to detergents or cleaners, preferably liquid detergents containing at least one protease, at least one compound of formula (I) and / or of formula (II), which acts as a protease inhibitor and thus is a suitable enzyme stabilizer, and a salt of Formula (III) that enhances the action of the protease inhibitor. Also part of the invention are the corresponding washing and cleaning methods, the use of the agents described herein and the use of a salt to increase the effect of a peptide stabilizer in a protease-containing detergent or cleaning agent.

Description

The present invention relates to detergents or cleaners, preferably liquid detergents containing at least one protease, at least one compound of formula (I) and / or of formula (II), which acts as a protease inhibitor and thus is a suitable enzyme stabilizer, and a salt of Formula (III), which enhances the action of the protease inhibitor. Also part of the invention are the corresponding washing and cleaning methods, the use of the agents described herein and the use of a salt to increase the effect of a peptide stabilizer in a protease-containing detergent or cleaning agent.

The use of enzymes in detergents and cleaners has been established in the art for decades. They serve to extend the range of services of the funds concerned according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three hydrolyze proteins, starches and fats and thus contribute directly to soil removal. Cellulases are used in particular because of their tissue effect. Another group of washing and cleaning agent enzymes are oxidative enzymes, in particular oxidases, which, if appropriate, in combination with other components, are preferably used to bleach soiling or to produce the bleaching agents in situ. In addition to these enzymes, which are subjected to constant optimization, further enzymes are constantly being made available for use in detergents and cleaners in order to be able to optimally address particular soiling, such as pectinases, β-glucanases, mannanases or other hemicellulases (glycosidases) Hydrolysis in particular of special vegetable polymers.

The enzymes which are the longest established and are contained in virtually all modern, powerful detergents and cleaners are proteases and, among these, in particular serine proteases, to which the subtilases according to the invention are also calculated. They serve the degradation of protein-containing stains on the cleaning material. However, they also hydrolyze themselves (autoproteolysis) and all other proteins contained in the agents concerned, i. especially enzymes. This happens especially during the cleaning process, i. in the aqueous wash liquor, if comparatively favorable reaction conditions are present. This occurs to a lesser extent but also during storage of the agents concerned, which is why a long storage always accompanied by a certain loss of protease activity and the activities of other enzymes. This is particularly problematic in gel or liquid and especially in water-containing formulations, because in this with the water contained both the reaction medium and the hydrolysis reagent available.

One goal in the development of detergent formulations is to stabilize the enzymes contained, especially during storage. This is understood as protection against various unfavorable influences, such as denaturation or decay by physical influences or oxidation. One focus of these developments is the protection of the contained proteins and / or enzymes against proteolytic cleavage. This can be done by the construction of physical barriers, such as by encapsulation of the enzymes in special enzyme granules or by packaging the means in two- or multi-chamber systems. The other many pathway is to add chemical compounds that inhibit the proteases and thus act collectively as stabilizers for proteases and the other proteins and enzymes contained. It must be reversible protease inhibitors, since the protease activity is only temporarily, especially during storage, but not be suppressed during the cleaning process.

Polyols, in particular glycerol and 1,2-propylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters are established as reversible protease inhibitors in the prior art. These include, in particular, derivatives with aromatic groups, for example ortho, meta or para-substituted phenylboronic acids, in particular 4-formylphenylboronic acid, or the salts or esters of the compounds mentioned. A particularly good protection results when boric acid derivatives are used together with polyols, since these can then form a complex stabilizing the enzyme. Also peptide aldehydes, that is, oligopeptides with reduced C-terminus, especially those of 2 to 50 monomers are described for this purpose. Among the peptidic reversible protease inhibitors include ovomucoid and leupeptin. Also, specific, reversible peptide inhibitors and fusion proteins from proteases and specific peptide inhibitors are used for this purpose.

Other established enzyme stabilizers are amino alcohols such as mono-, di-, triethanol- and -propanolamine and mixtures thereof, aliphatic carboxylic acids up to C ₁₂ , such as succinic acid, other dicarboxylic acids or salts of said acids. End-capped fatty acid amide alkoxylates are also established for this purpose. Certain organic acids used as builders are capable of, as in WO 97/18287 discloses, in addition to its builder function, also to stabilize an enzyme.

As detergency and detergent proteases various protease classes are established, for example metalloproteases. However, among the detergent and detergent proteases, subtilisin-type proteases (subtilases, subtilopeptidases, EC 3.4.21.62) occupy an outstanding position due to their favorable enzymatic properties such as stability or pH optimum. They are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family offers for example the Article "Subtilases: Subtilisin-like Proteases" by R. Siezen, pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996 , Subtilases are naturally produced by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.

It is therefore particularly worked to provide reversible inhibitors just this class of enzymes available. In this case, polyols such as glycerol and 1,2-propylene glycol have proved to be unfavorable due to their high necessary use concentrations, because the other active ingredients of the respective agents can thus be contained only in proportionally smaller proportions.

Boric acid derivatives occupy an outstanding position among the serine protease inhibitors (stabilizers), which are effective at a comparatively low concentration. However, regardless of their stabilizing effect, the boric acid derivatives have a significant disadvantage: many of them, such as borate, form undesirable by-products with some other detergent ingredients, so that they are no longer available in the agents concerned for the desired cleaning purpose, or even remain as an impurity on the laundry.

Peptide-based protease stabilizers do not have the disadvantages mentioned for boric acid derivatives. However, peptide-based protease stabilizers, when used in moderate concentrations, have significantly reduced protease stabilizer performance compared to the boric acid standard stabilizer (1 wt% boric acid based on the total weight of the agent).

The object of the present invention was therefore to identify compounds which increase the protease stabilizer performance of peptide-based protease stabilizers and are suitable for use in detergents and cleaners. Here, the use in total liquid, gel or pasty detergents and cleaning agents of particular interest, and including in particular those containing water.

• (I) der allgemeinen Strukturformel (I) Z-A-NH-CH(R)-C(O)-X (I), wobei A ein Aminosäurerest ist; X Wasserstoff ist; Z ein N-Verkappungsrest ausgewählt aus Phosphoramidat [(R'O)₂(O)P-], Sulfenamid [(SR')₂-], Sulfonamid [(R'(O)₂S-], Sulfonsäure [SO₃H], Phosphinamid [(R')₂(O)P-], Sulfamoyl Derivaten [R'O(O)₂S-], Thioharnstoff [(R')₂N(O)C-], Thiocarbamat [R'O(S)C-], Phosphonat [R'-P(O)OH], Amidophosphat [R'O(OH)(O)P-], Carbamat (R'O(O)C-) und Harnstoff (R'NH(O)C-) ist, wobei jedes R' unabhängig ausgewählt wird aus geradkettigen oder verzweigten C1-C6 unsubstituierten Alkyl-, Phenyl-, C7-C9 Alkylaryl- und Cycloalkyl-Resten, wobei der Cycloalkylring ein C4-C8 Cycloalkylring sein kann und ein oder mehrere Heteroatome enthalten kann, die ausgewählt werden aus O, N, und S; und R ausgewählt wird aus geradkettigen oder verzweigten C1-C6 unsubstituierten Alkyl-, Phenyl und C7-C9 Alkylarylresten; und Stereoisomeren, Tautomeren und Salzen davon; oder
• (II) der allgemeinen Strukturformel (II) Y-B₁-B₀-X (II), wobei X Wasserstoff ist; B₁ ein einzelner D- oder L-Aminosäurerest ist; B₀ ein Aminosäurerest ist und Y aus einem oder mehreren, bevorzugt ein oder zwei, Aminosäureresten und optional aus einem N-Verkappungsrest besteht, wobei der N-Verkappungsrest wie unter (I) definiert ist; und wobei das mindestens eine Salz der allgemeinen Strukturformel (III) (C^E+)_p(D^F–)_q (III) entspricht, wobei C ein Kation ausgewählt aus der Gruppe bestehend aus Al³⁺, Ca²⁺, Li⁺, Mg²⁺, Mn²⁺, Ni²⁺, K⁺, NR''4⁺ und Na⁺ ist, wobei jedes R'' unabhängig voneinander für H oder eine lineare oder verzweigte, substituierte oder unsubstituierte Alkyl-, Aryl- oder Alkenylgruppe steht, die alle optional ein oder mehrere Heteroatom(e) enthalten können; E eine ganze Zahl von 1 bis 3 ist und der Valenz/Wertigkeit des Kations entspricht; p der Anzahl an Kationen im Salz entspricht; D ein Anion ausgewählt aus der Gruppe bestehend aus CH₃COO^–, Br^–, CO₃ ^2–, Cl^–, C₃H₅O(COO)₃ ^3–, HCOO^–, HCO₃ ^–, HSO₄ ^–, C₂O₄ ^2–, SO₄ ^2– und SO₃ ^2– ist; F eine ganze Zahl von 1 bis 3 ist und der Valenz/Wertigkeit des Anions entspricht; q der Anzahl an Anionen im Salz entspricht; wobei die Nettoladung des Salzes 0 ist, d.h. es gilt ((E)·p) – ((F)·q) = 0.

This object is achieved by detergents or cleaners which contain at least one protease, at least one enzyme stabilizer and at least one salt, wherein the at least one enzyme stabilizer is selected from compounds

• (I) the general structural formula (I) ZA-NH-CH (R) -C (O) -X (I), wherein A is an amino acid residue; X is hydrogen; Z is an N-capping moiety selected from phosphoramidate [(R'O) ₂ (O) P-], sulfenamide [(SR ') ₂ -], sulfonamide [(R' (O) ₂ S-], sulfonic acid [SO ₃ H ], Phosphinamide [(R ') ₂ (O) P-], sulfamoyl derivatives [R'O (O) ₂ S-], thiourea [(R') ₂ N (O) C-], thiocarbamate [R'O (S) C-], phosphonate [R'-P (O) OH], amidophosphate [R'O (OH) (O) P-], carbamate (R'O (O) C-) and urea (R ') NH (O) C-), wherein each R 'is independently selected from C1 -C6 straight or branched unsubstituted alkyl, phenyl, C7-C9 alkylaryl and cycloalkyl radicals wherein the cycloalkyl ring may be a C4-C8 cycloalkyl ring and one or more heteroatoms selected from O, N, and S; and R is selected from C1 to C6 straight or branched unsubstituted alkyl, phenyl and C7 to C9 alkylaryl radicals, and stereoisomers, tautomers and salts thereof;
• (II) the general structural formula (II) YB ₁ -B ₀ -X (II), wherein X is hydrogen; B _{1 is} a single D or L amino acid residue; B _{0 is} an amino acid residue and Y consists of one or more, preferably one or two, amino acid residues and optionally an N-capping residue, wherein the N-capping residue is as defined under (I); and wherein the at least one salt of the general structural formula (III) (C ^{E +} ) _p (D ^F- ) _q (III) where C is a cation selected from the group consisting of Al ³⁺ , Ca ²⁺ , Li ⁺ , Mg ²⁺ , Mn ²⁺ , Ni ²⁺ , K ⁺ , NR''4 ⁺ and Na ⁺ , each R '' is independently H or a linear or branched, substituted or unsubstituted alkyl, aryl or alkenyl group, all of which may optionally contain one or more heteroatom (s); E is an integer from 1 to 3 and corresponds to the valency of the cation; p is the number of cations in the salt; D represents an anion selected from the group consisting of CH ₃ COO ^-, Br ^-, CO ₃ ^2-, Cl ^-, C ₃ H ₅ O (COO) ₃ ^3-, HCOO ^-, HCO ₃ ^-, HSO ₄ ^-, C ₂ O _{4 is} ^2- , SO _{4 is} ^2- and SO _{3 is} ^2- ; F is an integer from 1 to 3 and corresponds to the valency of the anion; q corresponds to the number of anions in the salt; where the net charge of the salt is 0, that is, ((E) .p) - ((F) .q) = 0.

Preferred radicals R are selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C ₆ H ₅ , -CH ₂ -C ₆ H ₅ , and -CH ₂ -CH ₂ -C ₆ H ₅ , so that the part -NH-CH (R) -C (O) -X of the compound of formula (I) is derived from the amino acids Ala, Val, Ile, Leu, PGly (phenylglycine), Phe and HPhe (homophenylalanines) by the Carboxyl group is converted into an aldehyde or Trifluoromethylketongruppe. Therefore, although such residues are not amino acids (although they may be synthesized from an amino acid precursor), for the sake of simplicity, the aldehyde portion of the inhibitors derived from the corresponding amino acids in the exemplified enzyme stabilizers will be identified by the suffix "H" after the analogous Denotes amino acid (eg, "-AlaH" represents the radical "-NHCH (CH ₃ ) C (O) H"). Trifluoromethyl ketones are identified in the same way by the addition "CF ₃ " after the analogous amino acid (eg, "-AlaCF ₃ " is the radical "-NHCH (CH ₃ ) C (O) CF ₃ ").

These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Further, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular that the invention is not limited to these examples. All percentages are by weight unless otherwise specified. Numeric ranges indicated in the format "from x to y" include the above values. If multiple preferred numeric ranges are specified in this format, it is understood that all ranges resulting from the combination of the various endpoints are also captured.

The aldehydes of the present invention can be prepared from the corresponding amino acids by converting the C-terminal carboxyl group of the amino acid into an aldehyde group. Such aldehydes can be prepared by known methods, such as in US Pat. No. 5015627 . EP 0 185 930 . EP 0 583 534 and DE 3200812 described.

The trifluoromethyl ketones can also be prepared from the corresponding amino acids by converting the C-terminal carboxyl group into a trifluoromethyl ketone group. Such trifluoromethyl ketones can be synthesized by known methods, such as those described in U.S. Pat EP 0 583 535 described, are produced.

In preferred embodiments, the substituent A is selected from Ala, Gly, Val, Ile, Leu, Phe and Lys.

The N-terminal end of the enzyme stabilizers of formula (I), and optionally that of the enzyme stabilizers of formula (II) is protected by a protecting group capping the N-terminus, the group being selected from carbamates, ureas, sulfonamides, phosphonamides , Thioureas, sulfenamides, sulfonic acids, phosphinamides, thiocarbamates, amidophosphates and phosphonamides. However, in a preferred embodiment, the N-terminal end is replaced by a methyl, ethyl or benzyl carbamate group [CH ₃ O- (O) C-; CH ₃ CH ₂ O- (O) C-; or C ₆ H ₅ CH ₂ O- (O) C-], a methyl, ethyl or benzyl urea group [CH ₃ NH- (O) C-; CH ₃ CH ₂ NH- (O) C-; or C ₆ H ₅ CH ₂ NH- (O) C-], a methyl, ethyl or Benzylsulfonamide group [CH ₃ SO ₂ -; CH ₃ CH ₂ SO ₂ -; or C ₆ H ₅ CH ₂ SO ₂ -], or a methyl, ethyl or benzylamidophosphate group [CH ₃ O (OH) (O) P-; CH ₃ CH ₂ O (OH) (O) P-; or C ₆ H ₅ CH ₂ O (OH) (O) P-].

The synthesis of the N-capping groups can be found, for example, in the following documents: Protective Groups in Organic Chemistry, Greene, T., Wuts, P., John Wiley & Sons, New York, 1991, pp 309-405 ; March, J, Advanced Organic Chemistry, Wiley Interscience, 1985, pp. 445, 469 . Carey, F. Sundberg, R., Advanced Organic Chemistry, Part B, Plenum Press, New York, 1990, p. 686-89 ; Atherton, E., Sheppard, R., Solid Phase Peptide Synthesis, Pierce Chemical, 1989, pp. 3-4 ; Grant, G., Synthetic Peptides, WH Freeman & Co. 1992, pp. 77-103 ; Stewart, J., Young, J., Solid Phase Peptide Synthesis, 2nd Edition, IRL Press, 1984, pp. 3,5,11,14-18, 28-29 , Bodansky, M., Principles of Peptide Synthesis, Springer-Verlag, 1988, pp. 62, 203, 59-69 ; Bodansky, M., Peptide Chemistry, Springer-Verlag, 1988, pp. 74-81 . Bodansky, M., Bodansky, A., The Practice of Peptide Synthesis, Springer-Verlag, 1984, pp. 9-32 ,

The agents according to the invention include salts of the formula (III). These salts are in the agents described herein in a concentration of 50-2000 mM, preferably in a concentration of 70-1500 mM, more preferably in a concentration of 100-1000 mM, even more preferably in a concentration of 150-500 mM and further preferably in a concentration of 200 mM. In further embodiments of the invention, the salt according to structural formula (III) is Na ₂ SO ₄ .

The term "alkyl" as used herein refers to an aliphatic hydrocarbon group which may be straight or branched and comprises 1 to 20 carbon atoms in the chain. The term "aryl" as used herein refers to an aromatic monocyclic or multicyclic ring system comprising 6 to 14 carbon atoms. The term "alkenyl" as used herein refers to an aliphatic hydrocarbon group containing at least one carbon-carbon double bond and which may be straight or branched and comprises from 2 to 15 carbon atoms in the chain.

The agents according to the invention may contain, alternatively or in addition to the enzyme stabilizer of the formula (I), an enzyme stabilizer of the formula YB ₁ -B ₀ -X (II) where X is hydrogen; B _{1 is} a single D or L amino acid residue; B _{0 is} an amino acid residue and Y consists of one or more, preferably one or two, amino acid residues and optionally an N-capping residue, wherein the N-capping residue is as defined above.

In preferred embodiments, B _{0 is} a D or L amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile, and Nle, and / or B ₁ is a D. or L-amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. In further preferred embodiments YB is ₂ , B ₃ -B ₂ , ZB ₂ , ZB ₃ -B ₂ , wherein B ₂ and B _{3 are} each independently an amino acid residue and Z is an N-capping residue, wherein the N-capping residue is as is defined above. In further preferred embodiments, B _{2 is} selected from Val, Gly, Ala, Arg, Leu, Phe and Thr, and / or B _{3 is} selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Ile.

Unless otherwise indicated, the amino acids in the above formulas are linked via peptide bonds and all peptides or peptide-like compounds are always shown from the N to the C terminus unless otherwise specified.

The agents according to the invention may contain the at least one enzyme stabilizer according to structural formula (I) and / or (II) in a concentration of 0.01-50 mM, preferably in a concentration of 0.05-5 mM, more preferably in a concentration of 0, 1-0.5 mM included. If several enzyme stabilizers of formulas (I) and / or (II) are included, this information refers to the total concentration.

Exemplary enzyme stabilizers of formulas (I) and (II) which can be used in the present invention include, but are not limited to, Cbz-Arg-Ala-Tyr-H, Ac-Gly-Ala-Tyr-H, Cbz-Gly-Ala -Tyr-H, Cbz-Gly-Ala-Tyr-H, Cbz-Val-Ala-Tyr-H, Cbz-Gly-Ala-Phe-H, Cbz-Gly-Ala-Val-H, Cbz-Gly-Gly -Tyr-H, Cbz-Gly-Gly-Phe-H, Cbz-Arg-Val-Tyr-H, Cbz-Leu-Val-Tyr-H, Ac-Leu-Gly-Ala-Tyr-H, Ac-Phe Gly-Ala-Tyr-H, Ac-Tyr-Gly-Ala-Tyr-H, Ac-Phe-Gly-Ala-Leu-H, Ac-Phe-Gly-Ala-Phe-H, Ac-Phe-Gly -Val-Tyr-H, Ac-Phe-Gly-Ala-Met-H, Ac-Trp-Leu-Val-Tyr-H, MeO-CO-Val-Ala-Leu-H, MeNCO-Val-Ala-Leu -H, MeO-CO-Phe-Gly-Ala-Leu-H, MeO-CO-Phe-Gly-Ala-Phe-H, MeSO ₂ -Phe-Gly-Ala-Leu-H, MeSO ₂ -Val-Ala Le-H, PhCH ₂ O (OH) (O) P-Val-Ala-Leu-H, EtSO ₂ -Phe-Gly-Ala-Leu-H, PhCH ₂ SO ₂ -Val-Ala-Leu-H, PhCH ₂ O (OH) (O) P-Leu-Ala-Leu-H, PhCH ₂ O (OH) (O) P-Phe-Ala-Leu-H, MeO (OH) (O) P-Leu-Gly -Ala-Leu-H, α-MAPI, β-MAPI, Phe-urea-Arg-Val-Tyr-H, Phe-urea-Gly-Gly-Tyr-H, Phe-urea-Gly-Ala-Phe-H , Phe-urea-Gly-Ala-Tyr-H, Phe-urea-Gly-Ala-Leu-H, Phe-urea- Gly-Ala-Nva-H, Phe-urea-Gly-Ala-Nle-H, Tyr-urea-Arg-Val-Tyr-H, Tyr-urea-Gly-Ala-Tyr-H, Phe-Cys-Ser Arg-Val-Phe-H, Phe-Cys-Ser-Arg-Val-Tyr-H, Phe-Cys-Ser-Gly-Ala-Tyr-H, Antipain, GE20372A, GE20372B, Chymostatin A, Chymostatin B and Chymostatin C ,

As used herein, the term "Cbz" refers to the benzyloxycarbonyl group having the empirical formula C ₇ H ₇ O. This is used as a protecting group. Other terminal groups in the enzyme stabilizers of the present invention may be: "Ph": phenyl; "Ac": acetyl and "Me": methyl. The term "urea" as used herein is synonymous with urea.

In various embodiments, the invention also includes all stereoisomers, in particular enantiomers and diastereomers, tautomers and salts of the compounds described above.

Under a detergent or cleaning agent according to the invention are all means that are suitable for washing or cleaning of particular textiles and / or solid surfaces. Other suitable ingredients are described in detail below.

According to the invention, a protease is to be understood as meaning all enzymes which are capable of hydrolyzing acid amide linkages of proteins. The proteases are also described in detail below.

Without wishing to be bound by theory, it is believed that the addition of a salt of formula (III) stabilizes the enzyme-peptide stabilizer complex by removing free reactive water molecules. This increases the binding efficiency of the peptide stabilizer to the enzyme and / or increases the ionic strength, ultimately stabilizing the enzyme-peptide stabilizer complex.

The first advantage of the prior art compounds over the prior art is that the above-mentioned advantages of peptide stabilizers can be utilized (e.g., avoiding the formation of undesirable by-products in the composition of the invention by the unwanted reactions of the stabilizer with other ingredients of the composition). By using at least one salt of the formula (III), it is surprisingly possible to use the peptide stabilizers in moderate concentrations (0.01-50 mM) without the agent having a significantly reduced protease stabilizer performance in comparison to the standard stabilizer (boric acid). The protease and optionally other proteins contained, in particular other enzymes are protected in this way against proteolysis by this enzyme (stabilized against proteolysis) and are thus fully efficient even after storage.

Furthermore, the compounds relevant to the invention have good solubility in water, so that they can easily be incorporated into corresponding agents and precipitation during storage is avoided.

The said enzyme inhibitors (stabilizers) presumably act as reversible inhibitors because they are structurally adapted to the conditions of the binding pocket, similar to the substrate of the proteases. This applies in particular to serine proteases, as has been shown on the basis of the examples of the present application with the positive effect of the compounds experimentally described there on the basis of serine proteases, specifically subtilases, even more specific subtilisins.

• – Wasch- oder Reinigungsverfahren, in dem eine Protease zur Wirkung kommt, die mit den oben beschriebenen Verbindungen (A) der Formel (I) und/oder (II) und (B) der Formel (III) inhibiert und/oder stabilisiert ist;
• – die Verwendung eines erfindungsgemäßen Wasch- oder Reinigungsmittels zum Waschen und/oder Reinigen von Textilien und/oder harten Oberflächen; sowie
• – die Verwendung einer Protease und der oben beschriebenen Verbindungen nach (A) Formel (I) und/oder (II) und (B) Formel (III) zur Herstellung eines Wasch- oder Reinigungsmittels.

Further objects of the present invention relate to:

• - Washing or cleaning method in which a protease comes into action, which is inhibited and / or stabilized with the above-described compounds (A) of the formula (I) and / or (II) and (B) of the formula (III);
• The use of a washing or cleaning agent according to the invention for washing and / or cleaning textiles and / or hard surfaces; such as
• The use of a protease and the compounds described above according to (A) formula (I) and / or (II) and (B) formula (III) for the preparation of a washing or cleaning agent.

In detergents or cleaners according to the invention, which in one embodiment are in predominantly solid form and in another embodiment in predominantly liquid, pasty or gel form, the enzyme, i. the protease in an amount of 0.05-5% by weight, preferably 0.05-2% by weight, and the enzyme stabilizer in an amount of 0.05-15% by weight, preferably 0.05- 5 wt .-%, based on the total weight of the washing or cleaning agent contained in this.

In various embodiments, the enzyme and the enzyme stabilizer may be pre-formulated in an enzyme composition. As can be seen from the previous comments, the enzyme protein forms only a fraction of the total weight of conventional enzyme preparations. Preferably used protease preparations contain between 0.1 and 40 wt .-%, preferably between 0.2 and 30 wt .-%, particularly preferably between 0.4 and 20 wt .-% and in particular between 0.8 and 10 wt .-% of the enzyme protein. In such compositions, the enzyme stabilizer may be contained in an amount of 0.05-35% by weight, preferably 0.05-10% by weight, based on the total weight in the enzyme composition. This enzyme composition, which is also a constituent of the present invention, can then be used in detergents or cleaners according to the invention in amounts which lead to the above-mentioned final concentrations in the washing or cleaning agent.

The protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method. The determination of the active protein concentration takes place in this respect via a titration of the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)) and determination of the residual activity (see. Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), p. 5890-5913 ).

In addition to the enzyme stabilizer according to the general formula given above, an agent according to the invention may contain at least one further stabilizer, in particular a polyol, such as glycerol or 1,2-ethylene glycol, and / or an antioxidant.

The proteases used are alkaline serine proteases. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are located inside peptides or proteins and thereby cause degradation of proteinaceous soils on the items to be cleaned. Their pH optimum is usually in the clearly alkaline range.

• – der Alkalischen Protease aus Bacillus amyloliquefaciens (BPN‘),
• – der Alkalischen Protease aus Bacillus licheniformis (Subtilisin Carlsberg),
• – der Alkalischen Protease PB92,
• – Subtilisin 147 und/oder 309 (Savinase)
• – der Alkalischen Protease aus Bacillus lentus, vorzugsweise aus Bacillus lentus (DSM 5483),
• – der Alkalischen Protease aus Bacillus alcalophilus (DSM 11233),
• – der Alkalischen Protease aus Bacillus gibsonii (DSM 14391) oder einer hierzu mindestens zu 70% identischen Alkalischen Protease,
• – der Alkalischen Protease aus Bacillus sp. (DSM 14390) oder einer hierzu mindestens zu 98,5% identischen Alkalischen Protease, und
• – der Alkalischen Protease aus Bacillus sp. (DSM 14392) oder einer hierzu mindestens zu 98,1 % identischen Alkalischen Protease.

The protease stabilized or reversibly inhibited according to the invention is therefore preferably a serine protease, in particular a subtilase, more preferably a subtilisin. The subtilisin may be a wild-type enzyme or a subtilisin variant, wherein the wild-type enzyme or the starting enzyme of the variant is preferably selected from one of the following:

• The alkaline protease from Bacillus amyloliquefaciens (BPN '),
• The alkaline protease from Bacillus licheniformis (subtilisin Carlsberg),
• The alkaline protease PB92,
• Subtilisin 147 and / or 309 (Savinase)
• The alkaline protease from Bacillus lentus, preferably from Bacillus lentus (DSM 5483),
• The alkaline protease from Bacillus alcalophilus (DSM 11233),
• The alkaline protease from Bacillus gibsonii (DSM 14391) or an at least 70% identical alkaline protease,
• The alkaline protease from Bacillus sp. (DSM 14390) or an at least 98.5% identical alkaline protease, and
• The alkaline protease from Bacillus sp. (DSM 14392) or an at least 98.1% identical alkaline protease.

In various embodiments of the invention, the protease stabilized according to the invention is a protease selected from the group of proteases according to SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3. In alternative embodiments, combinations of two or three proteases according to SEQ ID NO: 1 / SEQ ID NO: 2; SEQ ID NO: 1 / SEQ ID NO: 3; SEQ ID NO: 2 / SEQ ID NO: 3 or SEQ ID NO: 1 / SEQ ID NO: 2 / SEQ ID NO: 3 stabilized according to the invention.

Although reference will always be made hereinafter to a protease, it is of course also possible to use a combination of two or more proteases.

"Variant" as used herein in the context of proteases refers to naturally or artificially produced variations of a native protease that have an amino acid sequence that is modified from the reference form. Such a variant may have single or multiple point mutations, ie substitutions of one amino acid naturally occurring at the corresponding position by another, insertions (insertion of one or more amino acids) and / or deletions (removal of one or more amino acids), in particular one or more point mutations. Such variants preferably have at least 50, preferably 60 or more, more preferably 70, 80, 90, 100 % or more of the enzyme activity of the reference form. In various embodiments, such a variant has an amino acid sequence identical to the reference sequence over its total length of at least 70, preferably 75, 80, 85, 90, 95, 96, 97, 98, or 99%. The variants preferably have the same length as the reference sequence. Variants may be distinguished from the reference form by improved properties, such as, for example, higher enzyme activity, higher stability, altered substrate specificity, etc.

The identity of nucleic acid or amino acid sequences is determined by a sequence comparison. This sequence comparison is based on the BLAST algorithm established in the prior art and commonly used (cf., for example, US Pat Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215: 403-410 , and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs "; Nucleic Acids Res., 25, pp. 3389-3402 ) and in principle occurs in that similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences are assigned to each other. A tabular assignment of the respective positions is referred to as alignment. Another algorithm available in the prior art is the FASTA algorithm.

Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. The broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, as these usually perform similar chemical activities within the protein. Therefore, the similarity of the sequences compared may also be stated as percent homology or percent similarity. Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such areas often have identical functions. They can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert essential functions for the overall activity of the protein. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless otherwise indicated, identity or homology information in the present application, however, refers to the total length of the particular nucleic acid or amino acid sequence indicated.

"Functional fragments" as used herein refers to enzymatically active polypeptides that are truncated N- and / or C-terminally by at least one, preferably two or more, amino acids as compared to the reference sequence. The activity of such fragments is at least 50%, preferably at least 60, 70, 80, 90, 95 or 100% of the activity of the reference enzyme.

In general, the measurement of the enzyme activity - matched to the particular type of enzyme - can be carried out in the customary manner. Methods for determining activity are familiar to the expert in the field of enzyme technology and are routinely used by him. Methods for determining the protease activity are disclosed, for example, in Surfactants, Vol. 7 (1970), pp. 125-132 , The proteolytic activity can also be determined by the release of the chromophore para-nitroaniline (pNA) from the substrate suc-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide (suc-AAPF-pNA ). The protease cleaves the substrate and releases pNA. The release of the pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of the enzymatic activity (cf. Del Mar et al., 1979 ). The measurement can be carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm. The measuring time can be 5 min. amount to a measuring interval of 20s to 60s.

In the agents described herein, the enzymes to be used may also be formulated together with adjuncts, such as from fermentation. In liquid formulations, the enzymes are preferably used as enzyme liquid formulation (s).

The proteases are generally not provided in the form of the pure protein but rather in the form of stabilized, storage and transportable preparations. Such prefabricated preparations include, for example, the solid preparations obtained by granulation, extrusion or lyophilization or, especially in the case of liquid or gel-form detergents, solutions of the enzymes, advantageously as concentrated as possible, low in water and / or added with stabilizers or further auxiliaries.

Alternatively, the enzymes may be encapsulated for both the solid and liquid dosage forms, for example by spray-drying or extruding the enzyme solution together with a preferably natural polymer or in the form of capsules, for example those in which the enzymes are entrapped as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer. In deposited layers, further active ingredients, for example stabilizers, emulsifiers, pigments, bleaches or dyes, may additionally be applied. Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes. Advantageously, such granules, for example by applying polymeric film-forming agent, low in dust and storage stable due to the coating.

Furthermore, it is possible to assemble two or more enzymes together so that a single granule has several enzyme activities.

Agents according to the invention may contain, in addition to the protease, one or more further enzymes, in particular from the following group: amylases, hemicellulases, cellulases, lipases and oxidoreductases.

The amylase (s) is preferably an α-amylase. The hemicellulase is preferably a β-glucanase, a pectinase, a pullulanase and / or a mannanase. The cellulase is preferably a cellulase mixture or a one-component cellulase, preferably or predominantly an endoglucanase and / or a cellobiohydrolase. The oxidoreductase is preferably an oxidase, in particular a choline oxidase, or a perhydrolase.

The compositions described herein include all conceivable types of detergents or cleaners, both concentrates and neat agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers, for which the term detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, ie in addition to manual and machine Dishwashing agents, for example, scouring agents, glass cleaners, toilet scenters, etc. The washing and cleaning agents in the invention also include washing aids which are added to the actual detergent in the manual or machine textile laundry to achieve a further effect. Furthermore, laundry detergents and cleaners in the context of the invention also include textile pre-treatment and post-treatment agents, ie those agents with which the laundry item is brought into contact before the actual laundry, for example to dissolve stubborn soiling, and also agents which are in one of the actual Textile laundry downstream step to give the laundry further desirable properties such as comfortable grip, crease resistance or low static charge. Among the latter, i.a. calculated the fabric softener.

Embodiments of the present invention include all solid, powdered, liquid, gelatinous or pasty administration forms of agents described herein, which if appropriate can also consist of several phases and can be present in compressed or uncompressed form. The agent can be present as a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. The solid dosage forms of the composition also include extrudates, granules, tablets or pouches. Alternatively, the agent can also be liquid, gelatinous or pasty, for example in the form of a non-aqueous liquid washing or dishwashing detergent or a non-aqueous paste or in the form of an aqueous liquid washing or dishwashing detergent or a water-containing paste. Furthermore, the agent may be present as a one-component system. Such funds consist of one phase. Alternatively, an agent can also consist of several phases. Such an agent is therefore divided into several components.

The detergents or cleaners described herein, which may be in the form of powdered solids, in densified particulate form, as homogeneous solutions or suspensions, may further additionally contain all known ingredients customary in such compositions, preferably at least one further ingredient being present in the composition. In particular, the agents described herein may contain surfactants, builders, bleaches or bleach activators. In addition, they may include water-miscible organic solvents, sequestering agents, electrolytes, pH regulators and / or other auxiliaries such as optical brighteners, grayness inhibitors, foam regulators and colorants and fragrances and combinations thereof.

Advantageous ingredients of the agents described herein are disclosed in the international patent application WO2009 / 121725 starting there on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. Exemplary formulations of detergents or cleaners which may contain the protease, enzyme stabilizer and salt described herein are in the patents US6165966 Example 1, 2 and 3; WO2009118375 , Example 1 and WO2013004636 , Table 1 and 3 discloses. This disclosure is incorporated herein by reference and the disclosure is incorporated herein by reference.

A further subject of the invention is a method for the cleaning of textiles or hard surfaces, which is characterized in that in at least one method step a means described herein is used.

These include both manual and mechanical processes, with mechanical processes being preferred. Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned and washed off after the contact time, or that the items to be cleaned are otherwise treated with a detergent or a solution or dilution of this product. The same applies to processes for cleaning all other materials than textiles, especially hard surfaces. All conceivable washing or cleaning methods can be enriched in at least one of the method steps by the use of a washing or cleaning agent described herein and then represent embodiments of the present invention.

Another subject of the invention is the use of an agent described herein for cleaning or washing textiles or for cleaning hard surfaces.

All aspects, objects, and embodiments described for means described herein are also applicable to the aforementioned methods and uses. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above described methods and uses.

Examples

Example 1:

Used peptide stabilizer:

The peptide-stabilizer / peptide inhibitor (PI) used is the peptide methoxycarbonyl-Val-Ala-leu-aldehyde, which was synthesized by Bachem (Bubendor, Switzerland).

Enzyme-kinetics assay with the substrate AAPF:

The proteolytic activity was determined by the release of the chromophore para-nitroaniline (pNA) from the substrate suc-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide (suc-AAPF-pNA). The protease cleaves the substrate and releases pNA. The release of the pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of the enzymatic activity (cf. Del Mar et al., 1979 ). The measurement is carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm. The measuring time is 5 min. at a measuring interval of 20s to 60s.

Results on protease stabilizer performance:

The stabilizing effect of the peptide stabilizer / peptide inhibitor was measured in comparison to the effect of Na borate at various concentrations (by incubating the formulation at 30 ° C for the indicated number of days): Incubation period (in days) 7 14 28 42 % RA % RA % RA % RA 1% protease acc. SEQ ID NO: 1 with: 1% borate 90 90 84 86 0.1 mM PI 89 84 80 80 0.5 mM PI 91 83 78 80 1% protease acc. SEQ ID NO: 2 with: 1% borate 95 0.1 mM PI 91 1% protease acc. SEQ ID NO: 3 with: 1% borate 90 0.1 mM PI 87 0.5 mM PI 84

As can be seen above, the storage stability of the proteases is reduced by the change of boric acid to the peptide inhibitor (PI).

To test the effect of the model salt (Na ₂ SO ₄ ) on the peptide inhibitor (stabilizer), the respective proteases (SEQ ID Nos. 1-3) were stored with borate or with the peptide inhibitor, wherein the storage with peptide inhibitor under Use of the model salt took place.

The relative stability of the enzyme in both approaches (1. with peptide inhibitor, 2. with peptide inhibitor and salt) was calculated in terms of stability with borate. Incubation period (in days) 7 14 28 42 % RA % RA % RA % RA 1% protease acc. SEQ ID NO: 1 with: 0.1 mM PI 99 93 96 93 0.5 mM PI 101 93 94 93 200mM Na ₂ SO ₄ , 0.1mM PI 108 103 110 121 200mM Na ₂ SO ₄ , 0.5mM PI 120 114 118 130 1% protease acc. SEQ ID NO: 2 with: 0.1 mM PI 96 96 99 200mM Na ₂ SO ₄ , 0.1mM PI 94 100 102 1% protease acc. SEQ ID NO: 3 with: 0.5 mM PI 93 200mM Na ₂ SO ₄ , 0.5mM PI 113

As can be seen above, the addition of salt causes increased stability of the enzyme in the presence of the peptide inhibitor to a level even greater than that observed with borate stabilization.

Example 2:

Exemplary detergent formulations:

Unless indicated, the formulations given below may be supplemented with a protease, an enzyme stabilizer and a salt as described above. (A) Wt .-% pure substance thickener 0.3-0.5 Anti-foaming agents 0.2-0.4 glycerin 1-7 ethanol 1-7 Anionic surfactants 1-10 Nonionic surfactants 0-20 fatty acids 0-10 Sodium citrate (dihydrate) 0.5-4 soda 0.5-4 HEDP 0.5-4 PVP 0.1-4 Optical brighteners 0-2 dye 0 to 0.0001 water rest (B) A B C D e F G H C9-13-Alkylbenzenesulfonate, Na salt 9 10 6 7 5 15 15 9 C12-18 fatty alcohol with 7 EO 8th 9 6 7 5 6 11 10 C12-18 fatty alcohol sulfate with 2 EO - - 8th 7 10 2 2 5 C12-18 fatty acid, Na salt 4 3 3 3 4 2 4 7 citric acid 2 3 3 2 2 2 2 3 Sodium hydroxide, 50% 3 3 2 3 3 3 3 4 Enzymes (amylase, protease, cellulase) + + + + + + + + Perfume 1 0.5 0.5 1 1 1 1 1 propanediol - - - - - 5 5 - ethanol 1.5 1.5 1.5 1.5 1.5 1.5 1.5 5 PVA / maleic acid copolymer 0.1 - 0.1 - - - - - Optical brightener - 0.1 - 0.1 0.2 0.2 0.2 0.2 opacifiers 0.2 - - - - - - - Phosphonic acid, Na salt 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 polymer 2 2 2 2 2 2 2 2 water on 100

This is followed by a sequence protocol according to WIPO St. 25. This can be downloaded from the official publication platform of the DPMA.

QUOTES INCLUDE IN THE DESCRIPTION

This list of the documents listed by the applicant has been generated automatically and is included solely for the better information of the reader. The list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions.

Cited patent literature

• WO 97/18287 [0006]
• US 5015627 [0015]
• EP 0185930 [0015]
• EP 0583534 [0015]
• DE 3200812 [0015]
• EP 0583535 [0016]
• WO 2009/121725 [0058]
• US 6165966 [0058]
• WO 2009118375 [0058]
• WO 2013004636 [0058]

Cited non-patent literature

• Article "Subtilases: Subtilisin-like Proteases" by R. Siezen, pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996 [0007]
• Organic Chemistry, Greene, T., Wuts, P., John Wiley & Sons, New York, 1991, pp 309-405 [0019]
• March, J, Advanced Organic Chemistry, Wiley Interscience, 1985, pp. 445, 469 [0019]
• Carey, F. Sundberg, R., Advanced Organic Chemistry, Part B, Plenum Press, New York, 1990, p. 686-89 [0019]
• Atherton, E., Sheppard, R., Solid Phase Peptide Synthesis, Pierce Chemical, 1989, pp. 3-4 [0019]
• Grant, G., Synthetic Peptides, WH Freeman & Co. 1992, pp. 77-103 [0019]
• Stewart, J., Young, J., Solid Phase Peptide Synthesis, 2nd Edition, IRL Press, 1984, pp. 3,5,11,14-18, 28-29 [0019]
• Bodansky, M., Principles of Peptide Synthesis, Springer-Verlag, 1988, pp. 62, 203, 59-69 [0019]
• Bodansky, M., Peptide Chemistry, Springer-Verlag, 1988, pp. 74-81 [0019]
• Bodansky, M., Bodansky, A., The Practice of Peptide Synthesis, Springer-Verlag, 1984, pp. 9-32 [0019]
• Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), pp. 5890-5913 [0038]
• Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." Biol. 215: 403-410 [0045]
• Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs "; Nucleic Acids Res., 25, pp. 3389-3402 [0045]
• Surfactants, Vol. 7 (1970), pp. 125-132 [0048]
• Del Mar et al., 1979 [0048]
• Del Mar et al., 1979 [0064]

Claims (11)

Washing or cleaning agent, preferably a liquid detergent containing (A) at least one protease; (B) at least one enzyme stabilizer, wherein the at least one enzyme stabilizer is selected from compounds (I) of the general structural formula (I) ZA-NH-CH (R) -C (O) -X (I), wherein A is an amino acid residue; X is hydrogen; Z is an N-capping moiety selected from phosphoramidate [(R'O) ₂ (O) P-], sulfenamide [(SR ') ₂ -], sulfonamide [(R' (O) ₂ S-], sulfonic acid [SO ₃ H ], Phosphinamide [(R ') ₂ (O) P-], sulfamoyl derivatives [R'O (O) ₂ S-], thiourea [(R') ₂ N (O) C-], thiocarbamate [R'O (S) C-], phosphonate [R'-P (O) OH], amidophosphate [R'O (OH) (O) P-], carbamate (R'O (O) C-) and urea (R ') NH (O) C-), wherein each R 'is independently selected from C1 -C6 straight or branched unsubstituted alkyl, phenyl, C7-C9 alkylaryl and cycloalkyl radicals wherein the cycloalkyl ring may be a C4-C8 cycloalkyl ring and one or more heteroatoms selected from O, N, and S; and R is selected from C1 to C6 straight or branched unsubstituted alkyl, phenyl and C7 to C9 alkylaryl radicals, and stereoisomers, tautomers and salts thereof; (II) the general structural formula (II) YB ₁ -B ₀ -X (II), wherein X is hydrogen; B _{1 is} a single D or L amino acid residue; B _{0 is} an amino acid residue and Y consists of one or more, preferably one or two, amino acid residues and optionally an N-capping residue, wherein the N-capping residue is as defined under (I); and (C) at least one salt of the general structural formula (III) (C ^{E +} ) _p (D ^F- ) _q (III) where C is a cation selected from the group consisting of Al ³⁺ , Ca ²⁺ , Li ⁺ , Mg ²⁺ , Mn ²⁺ , Ni ²⁺ , K ⁺ , NR''4 ⁺ and Na ⁺ , each R '' is independently H or a linear or branched, substituted or unsubstituted alkyl, aryl or alkenyl group, all of which may optionally contain one or more heteroatom (s); E is an integer from 1 to 3 and corresponds to the valency of the cation; p is the number of cations in the salt; D represents an anion selected from the group consisting of CH ₃ COO ^-, Br ^-, CO ₃ ^2-, Cl ^-, C ₃ H ₅ O (COO) ₃ ^3-, HCOO ^-, HCO ₃ ^-, HSO ₄ ^-, C ₂ O _{4 is} ^2- , SO _{4 is} ^2- and SO _{3 is} ^2- ; F is an integer from 1 to 3 and corresponds to the valence of the anion; q corresponds to the number of anions in the salt; wherein the net charge of the salt is 0. Detergents or cleaners according to claim 1, wherein (A) the washing or cleaning agent contains the salt according to structural formula (III) in a concentration of 50-2000 mM, preferably in a concentration of 200 mM; (B) the washing or cleaning agent contains the enzyme stabilizer according to structural formula (I) and / or (II) in a concentration of 0.01-50 mM, preferably in a concentration of 0.1-0.5 mM; and / or (C) the salt according to structural formula (III) is Na ₂ SO ₄ . Detergent or cleaner according to claim 1 or 2, characterized in that (A) A is selected from Ala, Gly, Val, Ile, Leu, Phe and Lys; (B) R is selected from methyl, iso -propyl, sec -butyl, iso -butyl, -C ₆ H ₅ , -CH ₂ -C ₆ H ₅ , and -CH ₂ -CH ₂ -C ₆ H ₅ ; and / or (C) Z is selected from methyl, ethyl or benzyl carbamate groups [CH ₃ O- (O) C-; CH ₃ CH ₂ O- (O) C-; or C ₆ H ₅ CH ₂ O- (O) C-], methyl, ethyl or benzyl urea groups [CH ₃ NH- (O) C-; CH ₃ CH ₂ NH- (O) C-; or C ₆ H ₅ CH ₂ NH- (O) C-], methyl, ethyl or benzylsulfonamide groups [CH ₃ SO ₂ -; CH ₃ CH ₂ SO ₂ -; or C ₆ H ₅ CH ₂ SO ₂ -], and a methyl, ethyl or benzylamidophosphate groups [CH ₃ O (OH) (O) P-; CH ₃ CH ₂ O (OH) (O) P-; or C ₆ H ₅ CH ₂ O (OH) (O) P-]. Washing or cleaning agent according to one of claims 1-3, characterized in that (A) B _{0 is} a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile and Nle; (B) B _{1 is} an amino acid residue having an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. Washing or cleaning agent according to one of claims 1-4, characterized in that YB ₂ , B ₃ -B ₂ , ZB ₂ , ZB ₃ -B ₂ , wherein B ₂ and B _{3 are} each independently an amino acid residue and Z a N-capping moiety, wherein the N-capping moiety is as defined in claim 1 under (I). Detergent or cleaner according to claim 5, characterized in that (A) B _{2 is} selected from Val, Gly, Ala, Arg, Leu, Phe and Thr, and / or (B) B _{3 is} selected from Phe, Tyr, Trp , Phe-nylglycine, Leu, Val, Nva, Nle and Iie. Washing or cleaning agent according to any one of claims 1-6, characterized in that the at least one enzyme stabilizer is selected from Cbz-Arg-Ala-Tyr-H, Ac-Gly-Ala-Tyr-H, Cbz-Gly-Ala Tb-H, Cbz-Gly-Ala-Tyr-H, Cbz-Val-Ala-Tyr-H, Cbz-Gly-Ala-Phe-H, Cbz-Gly-Ala-Val-H, Cbz-Gly-Gly Tyr-H, Cbz-Gly-Gly-Phe-H, Cbz-Arg-Val-Tyr-H, Cbz-Leu-Val-Tyr-H, Ac-Leu-Gly-Ala-Tyr-H, Ac-Phe- Gly-Ala-Tyr-H, Ac-Tyr-Gly-Ala-Tyr-H, Ac-Phe-Gly-Ala-Leu-H, Ac-Phe-Gly-Ala-Phe-H, Ac-Phe-Gly Val-Tyr-H, Ac-Phe-Gly-Ala-Met-H, Ac-Trp-Leu-Val-Tyr-H, MeO-CO-Val-Ala-Leu-H, MeNCO-Val-Ala-Leu H, MeO-CO-Phe-Gly-Ala-Leu-H, MeO-CO-Phe-Gly-Ala-Phe-H, MeSO ₂ -Phe-Gly-Ala-Leu-H, Me-SO ₂ -Val. Ala-Leu-H, PhCH ₂ O (OH) (O) P-Val-Ala-Leu-H, EtSO ₂ -Phe-Gly-Ala-Leu-H, PhCH ₂ SO ₂ -Val-Ala-Leu-H , PhCH ₂ O (OH) (O) P-Leu-Ala-Leu-H, PhCH ₂ O (OH) (O) P-Phe-Ala-Leu-H, MeO (OH) (O) P-Leu Gly-Ala-Leu-H, α-MAPI, β-MAPI, Phe-urea-Arg-Val-Tyr-H, Phe-urea-Gly-Gly-Tyr-H, Phe-urea-Gly-Ala-Phe- H, Phe-urea-Gly-Ala-Tyr-H, Phe-urea-Gly-Ala-Leu-H, Phe-urea-Gly-Ala-Nva-H, Phe-urea-Gly-Ala-Nle-H, Tyr-urea-Arg-Val-Tyr-H, Tyr-urea-Gly-Ala-Tyr-H, Phe- urea Cys-Ser-Arg-Val-Phe-H, Phe-Cys-Ser-Arg-Val-Tyr-H, Phe-Cys-Ser-Gly-Ala-Tyr-H, Antipain, GE20372A, GE20372B, Chymostatin A, Chymostatin B and chymostatin C. Washing or cleaning agent according to any one of claims 1-7, characterized in that the at least one protease in an amount of 0.05-5 wt .-%, preferably 0.05-2 wt .-%, and the at least one enzyme stabilizer in an amount of 0.05-15 wt .-%, preferably to 0.05-5 wt .-%, based on the total weight of the detergent or cleaning agent in this are included.  Use of a washing or cleaning agent according to any one of claims 1-8 for washing textiles or cleaning solid surfaces. A process for cleaning textiles or hard surfaces, characterized in that in at least one process step, a washing or cleaning agent according to any one of claims 1-8 is applied. Use of a salt for increasing the effect of a peptide stabilizer in a protease-containing washing or cleaning agent, wherein the salt of the general structural formula (III) (C ^{E +} ) _p (D ^F- ) _q (III) where C is a cation selected from the group consisting of Al ³⁺ , Ca ²⁺ , Li ⁺ , Mg ²⁺ , Mn ²⁺ , Ni ²⁺ , K ⁺ , NR''4 ⁺ and Na ⁺ , each R '' is independently H or a linear or branched, substituted or unsubstituted alkyl, aryl or alkenyl group, all of which may optionally contain one or more heteroatom (s); E is an integer from 1 to 3 and corresponds to the valency of the cation; p is the number of cations in the salt; D represents an anion selected from the group consisting of CH ₃ COO ^-, Br ^-, CO ₃ ^2-, Cl ^-, C ₃ H ₅ O (COO) ₃ ^3-, HCOO ^-, HCO ₃ ^-, HSO ₄ ^-, C ₂ O _{4 is} ^2- , SO _{4 is} ^2- and SO _{3 is} ^2- ; F is an integer from 1 to 3 and corresponds to the valence of the anion; q corresponds to the number of anions in the salt; wherein the net charge of the salt is 0.