Detergent and cleaning agent with improved enzyme stability

Abstract

The invention relates to detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising: a) at least one protease, preferably in an amount of 0.0001 to 1 wt.% in relation to the total weight of the detergent and cleaning agent; b) at least one peptide (peptidic inhibitor), preferably with a 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5, 5.0, 10, 15, 18, 20, 25, 27 or 30 times molar excess in relation to the molarity of the protease used, particularly preferably a 15, 18, 20, 25 or 27 times molar excess, wherein the peptide preferably has a length from 50 to 200, particularly preferably 55 to 190, further preferably 60 to 180 of amino acid residues; and c) at least one detergent and cleaning agent constituent, preferably in an amount of 0.01 to 99.9 wt.% in relation to the total weight of the detergent and cleaning agent. The invention likewise relates to the corresponding washing and cleaning methods, the use of the agent described herein, and the use of a peptidic inhibitor for improving the stability of a protease in detergent or cleaning agent.

Description

[0001] DETERGENT AND CLEANING AGENTS WITH IMPROVED ENZYME STABILITY

[0002] The invention lies in the field of enzyme technology. The invention relates to washing or cleaning agents comprising at least one protease and at least one peptide inhibitor. Also included in the invention are the corresponding washing and cleaning processes, the use of the agents described herein, and the use of a peptide inhibitor to improve the stability of a protease in washing or cleaning agents.

[0003] The use of enzymes in detergents has been established in the state of the art for decades. They serve to expand the performance spectrum of the respective agents according to their special activities. These include, in particular, hydrolytic enzymes such as proteases, amylases, lipases, and cellulases. The first three hydrolyze proteins, starch, and fats and thus contribute directly to soil removal. Cellulases are used in particular for their effect on fabrics. Another group of detergent enzymes are oxidative enzymes, particularly oxidases, which, if necessary in conjunction with other components, preferably serve to bleach soils or generate the bleaching agents in situ. In addition to these enzymes, which are subject to continuous optimization, further enzymes are constantly being made available for use in detergents in order to optimally address special types of soiling, such as:Pectinases, ß-glucanases, mannanases or other hemicellulases (glycosidases) for the hydrolysis of special plant polymers in particular.

[0004] Proteases are among the most technically important enzymes. They are the longest-established enzymes in detergents and cleaning agents and are contained in virtually all modern, high-performance detergents and cleaning agents. In detergents and cleaning agents, proteases serve to break down protein-containing soiling on the items being cleaned. However, they also hydrolyze themselves (autoproteolysis) and all other proteins contained in the agents in question, i.e. in particular other enzymes contained in the detergents and cleaning agents. This occurs particularly during the cleaning process, i.e. in the aqueous washing or cleaning liquor, when comparatively favorable reaction conditions exist. This also occurs to a lesser extent during storage of the agents in question, which is why long storage is always accompanied by a certain loss of protease activity and the activity of the other enzymes.Due to the loss of enzymatic activity, they no longer perform optimally. This is particularly problematic in gel or liquid formulations, and especially in water-based formulations, because the water contained in these formulations provides both the reaction medium and the hydrolysis reagent.

[0005] In general, only selected proteases are suitable for use in liquid surfactant-containing preparations. Many proteases either do not exhibit sufficient catalytic performance in such preparations or are not sufficiently stable. Therefore, high catalytic activity and stability under conditions such as those encountered during a washing process are particularly desirable for the use of proteases in detergents.Examples of the subtilisin-type proteases preferably used in detergents and cleaning agents are the subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483, subtilisin DY, and the enzymes thermitase, proteinase K, and the proteases TW3 and TW7, which are classified as subtilases but no longer as subtilisins in the narrower sense, as well as variants of the aforementioned proteases that have an amino acid sequence that is altered compared to the parent protease. Proteases are modified in a targeted or random manner using methods known from the state of the art and are thus optimized, for example, for use in detergents and cleaning agents. These include point, deletion or insertion mutagenesis or fusion with other proteins or protein parts.For most of the proteases known from the state of the art, optimized variants are known. For example, European patent application EP 2016175 A1 discloses a protease from Bacillus pumilus intended for use in detergents and cleaning agents.

[0006] One goal in the development of detergent and cleaning agent formulations is therefore to stabilize the enzymes they contain, particularly during storage, and also to protect them from denaturation and / or cleavage or degradation and / or decomposition due to physical influences or oxidation, etc., particularly during storage and / or use of the detergent or cleaning agent. One focus of these developments is the protection of the proteins and / or enzymes they contain against (auto-)proteolytic cleavage. This can be achieved by creating physical barriers, for example by encapsulating the enzymes in special enzyme granules or by packaging the agents in two- or multi-chamber systems. The other frequently used approach is to add chemical compounds that inhibit the proteases and thus act as stabilizers for proteases and the other proteins and enzymes they contain.However, these must be reversible protease inhibitors, since the protease activity should only be inhibited temporarily, especially during storage, but not during the purification process.

[0007] Various reversible protease inhibitors are described in the prior art, e.g., polyols, particularly glycerol and 1,2-propylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids, or their salts or esters. The use of boric acid derivatives together with polyols is also known. 4-Formylphenylboronic acid (4-FPBA) is also a protease inhibitor known from the prior art. Peptide aldehydes, i.e., oligopeptides with a reduced C-terminus, particularly those consisting of 2 to 50 monomers, have also been described for this purpose. Peptide reversible protease inhibitors include, among others, ovomucoid and leupeptin. Specific, reversible peptide inhibitors and fusion proteins composed of proteases and specific peptide inhibitors are also used for this purpose.

[0008] However, there is still a need to improve the cleaning performance of enzyme-containing detergents and cleaning agents and to better stabilize the enzymes contained in the detergents and cleaning agents. In particular, there is an increasing demand to avoid boric acid-containing compounds, i.e. in particular boron-containing protease inhibitors, in detergents and cleaning agents. Surprisingly, it has now been found that certain peptide inhibitors can advantageously stabilize and reversibly inhibit a protease and are therefore particularly suitable for use in detergents or cleaning agents. In particular, it has surprisingly been found that a protease from Bacillus pumilus which comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217,252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, can be advantageously stabilized by certain peptide inhibitors and this combination is therefore particularly suitable for use in washing or cleaning agents.

[0009] The invention therefore relates, in a first aspect, to a washing and cleaning agent, in particular a liquid washing and cleaning agent, particularly preferably a liquid textile washing agent, comprising a) at least one protease, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the washing and cleaning agent, b) at least one peptide, preferably in a 0.5-, 1.0-, 1.5-, 2.0-, 2.5-, 3.0-, 3.5-, 4.0-, 4.5-, 5.0-, 10-, 15-, 18-, 20-, 25-, 27- or 30-fold molar excess based on the molarity of the protease used, wherein the peptide preferably has a length of 50 to 200, preferably 55 to 190, more preferably 60 to 180, amino acid residues and c) at least one washing and cleaning agent ingredient, preferably in an amount of 0.01 to 99.9% by weight, based on the total weight of the washing and cleaning agent.

[0010] The invention further relates to a washing and cleaning agent, in particular a liquid washing and cleaning agent, particularly preferably a liquid textile washing agent, comprising a) at least one protease, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G,131 H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide, preferably in a 0.5-, 1.0-, 1.5-, 2.0-, 2.5-, 3.0-, 3.5-, 4.0-, 4.5-, 5.0-, 10-, 15-, 18-, 20-, 25-, 27- or 30-fold molar excess based on the molarity of the protease used, wherein the peptide preferably has a length of 50 to 200, preferably 55 to 190, more preferably 60 to 180, amino acid residues, wherein the peptide has an amino acid sequence which is at least 90% identical over its entire length to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11,and c) at least one washing and cleaning agent ingredient, preferably in an amount of 0.01 to 99.9% by weight, based on the total weight of the washing and cleaning agent.

[0011] Further aspects of the invention relate to processes for producing such a washing or cleaning agent, processes for cleaning textiles and / or hard surfaces, in particular dishes, using an agent according to the invention.

[0012] A further subject matter of the invention relates to the use of a peptide (peptidic inhibitor) as defined herein for improving the stability, in particular the storage stability, of proteases, in particular of proteases from Bacillus pumilus as defined herein, in a washing and cleaning agent, preferably in a temperature range from about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, very particularly preferably at about 30°C, and to the use of a peptide as defined herein for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, in particular a protease from Bacillus pumilus as defined herein.

[0013] The detergent according to the invention is preferably a liquid textile detergent. Further preferably, the detergent according to the invention, in a 1 wt. % solution in deionized water at 20°C, has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, further preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0014] Textile detergents according to the invention exhibit performance advantages over other textile detergents, in particular, when the textile detergents contain at least one additional enzyme of the same or a different type, e.g., amylase, cellulase, lipase, mannanase, or pectinase, although the list of additional enzymes is not exhaustive. Therefore, it is preferred that the textile detergents according to the invention contain at least one additional enzyme of the same type (i.e., another protease) or a different type.

[0015] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples.

[0016] All percentages are by weight (wt%) unless otherwise stated. Numerical ranges expressed in the format "from x to y" include the stated values. Where multiple preferred numerical ranges are specified in this format, it is understood that all ranges resulting from the combination of the various endpoints are also included.

[0017] "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.

[0018] The term "washing and cleaning agent" or "washing or cleaning agent" as used herein is synonymous with the term "agent" and refers to a composition for cleaning textiles and / or hard surfaces, in particular dishes, as explained in the description.

[0019] "Approximately," "approximately," or "approximately," as used herein with reference to a numerical value, refers to the corresponding numerical value ±10%, preferably ±5%.

[0020] "Substantially free from" means that the composition or agent contains less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight and most preferably less than 0.1% by weight of the corresponding substance, based on the total weight of the composition / agent.

[0021] "Liquid," as used herein, includes liquids and gels, as well as pasty compositions. It is preferred that the liquid compositions be flowable and pourable at room temperature, but it is also possible for them to have a yield point. A substance, e.g., a composition or an agent, is solid according to the definition of the invention if it is in the solid state at 25°C and 1013 mbar. A substance, e.g., a composition or an agent, is liquid according to the definition of the invention if it is in the liquid state at 25°C and 1013 mbar. Liquid also includes gel.

[0022] "Variant", as used herein, refers to natural or artificially produced variations of a native protease that have a modified amino acid sequence compared to the reference form.

[0023] The statement "in a 0.5-fold molar excess of a raw material relative to the molarity of the protease used" means that the number of raw material particles present in the composition or agent corresponds exactly to half the number of protease particles present in the composition or agent. Accordingly, the statement "in a 2.0-fold molar excess of a raw material relative to the molarity of the protease used" means that twice the number of raw material particles compared to protease particles are present.

[0024] An "improvement in the stability of an enzyme" within the meaning of the invention exists if the presence of a peptide inhibitor causes a washing or cleaning agent comprising at least one protease and at least one peptide inhibitor (washing or cleaning agent according to the invention) to have, after storage, a higher enzymatic activity of the protease and / or, if appropriate, other enzymes contained in the washing or cleaning agent compared to a control preparation which differs from the washing or cleaning agent according to the invention only by the absence of the peptide inhibitor (control). After storage, the washing or cleaning agent according to the invention therefore has a higher residual activity of the protease and / or, if appropriate, other enzymes contained in the washing or cleaning agent.of other enzymes contained compared to the control, wherein the washing or cleaning agent according to the invention and the control have the same initial enzymatic activity at the start of storage, both agents are treated in the same way, in particular with regard to the storage conditions and the determination of enzyme activity. Storage is increasingly preferably for at least 1 week, 2 weeks, 3 weeks, or 4 weeks. Storage is further preferably at a temperature of 20°C, 25°C, 30°C, or 40°C.

[0025] The present invention is based on the inventors' surprising discovery that the peptide inhibitors described herein improve the storage stability of proteases in detergents and cleaning agents. This is particularly surprising since these peptide inhibitors have not previously been associated with reversible protease inhibition. In particular, they have not previously been associated with the proteases from Bacillus pumilus described herein and with improved storage stability and / or reduced autoproteolysis. Furthermore, the peptide inhibitors described herein have not been associated with reversible inhibition of the Bacillus pumilus protease described herein.

[0026] The present invention is based in particular on the surprising finding of the inventors that a Bacillus pumilus protease which comprises an amino acid sequence which is at least 70% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution which is selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A,can be advantageously stabilized in washing and cleaning agents by a peptide inhibitor defined herein. This is particularly surprising insofar as none of these peptide inhibitors defined herein has previously been associated with improved stability of such a Bacillus pumilus protease in washing or cleaning agents. Furthermore, such a peptide inhibitor has not previously been associated with improved stability of other enzymes contained in the washing or cleaning agent when they are present in the washing or cleaning agent together with the aforementioned Bacillus pumilus protease.

[0027] According to the invention, peptides having a length of 50 to 200, preferably 55 to 190, more preferably 60 to 180, amino acid residues are used as peptide inhibitors. Suitable peptide inhibitors can be isolated, for example, from Streptomyces albogriseolus, Hordeum vulgare, Brachypodium distachyon, Populus trichocarpa, Triticum urartu, Setaria italica, and Oryza sativa. Preferred peptide inhibitors are selected from peptides having an amino acid sequence which is at least 90%, and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical over its entire length to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12.Particularly preferred are peptide inhibitors having an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, SEQ ID NO:11, and SEQ ID NO:12. Very particularly preferred are peptide inhibitors having an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8, or SEQ ID NO:11.

[0028] The agents according to the invention may comprise one or more peptide inhibitor(s).

[0029] The agents according to the invention can contain the peptide inhibitor(s) in a 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5, 5.0, 10, 15, 18, 20, 25, 27 or 30-fold molar excess based on the molarity of the protease used. This means that if a composition according to the invention contains 1 pmol of protease, it can contain 0.5 pmol, 1 pmol, 1.5 pmol, 2.0 pmol, 2.5 pmol, 3.0 pmol, 3.5 pmol, 4.0 pmol, 4.5 pmol, 5.0 pmol, 10 pmol, 15 pmol, 18 pmol, 20 pmol, 25 pmol, 27 pmol, or 30 pmol of a corresponding peptide inhibitor. If multiple peptide inhibitors are present, these figures refer to the total concentration.

[0030] In a preferred embodiment, a peptide inhibitor according to the invention increases the residual activity of a protease after storage (as described in Example 2) by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide compared to storage without peptide.

[0031] In a further preferred embodiment, a peptide inhibitor according to the invention has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20.

[0032] In preferred embodiments, the protease contained in the agents according to the invention is a protease from Bacillus pumilus, which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution,which is selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A. In further preferred embodiments, the protease used according to the invention has proteolytic activity, comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and has, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions,corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A.

[0033] In further preferred embodiments, the protease used according to the invention has proteolytic activity, comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and has, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211 N and S224A existing group are selected.,

[0034] In further preferred embodiments, the protease used according to the invention has proteolytic activity, comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and has, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211 N and S224A existing group are selected.,

[0035] In further preferred embodiments, the protease used according to the invention has proteolytic activity, comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and has, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A.

[0036] In particularly preferred embodiments, the detergent according to the invention contains a protease with one of the following amino acid substitution variants:

[0037] (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271E;

[0038] (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271E;

[0039] (iii) P9T-S89A-N130D-G131 H-T133A-N144K-S189T-Y217M-S224A-N252T-Q271 E;

[0040] (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E;

[0041] (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E;

[0042] (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E;

[0043] (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E;

[0044] (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;

[0045] (ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering refers in each case to the numbering according to SEQ ID NO:1 .

[0046] In preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 189T, 211 N and 224A, and b) a peptide inhibitor having an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, via whose total length is at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.

[0047] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence which is at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over their entire length.

[0048] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence which is at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over their entire length.

[0049] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence which is at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over their entire length.

[0050] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor having an amino acid sequence which corresponds to an amino acid sequence,which is selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% are identical.

[0051] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;P9T-S89A-N130D-T133A-N144K- N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.;

[0052] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:2.

[0053] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:2.

[0054] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:2.

[0055] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:2.

[0056] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:2.

[0057] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:2.

[0058] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:3.

[0059] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:3.

[0060] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:3.

[0061] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:3.

[0062] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:3.

[0063] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:3.

[0064] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:4.

[0065] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:4.

[0066] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:4.

[0067] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:4.

[0068] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:4.

[0069] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:4.

[0070] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:5.

[0071] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:5.

[0072] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:5.

[0073] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:5.

[0074] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:5.

[0075] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:5.

[0076] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:6.

[0077] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:6.

[0078] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:6.

[0079] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of YQ\I\I, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:6.

[0080] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:6.

[0081] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:6.

[0082] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:7.

[0083] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:7.

[0084] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:7.

[0085] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:7.

[0086] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:7.

[0087] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:7.

[0088] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:8.

[0089] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:8.

[0090] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:8.

[0091] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:8.

[0092] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:8.

[0093] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:8.

[0094] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:9.

[0095] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\I\I, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:9.

[0096] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:9.

[0097] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:9.

[0098] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:9.In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:9.

[0099] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NQ:10.

[0100] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NQ:10.

[0101] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NQ:10.

[0102] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NQ:10.

[0103] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:10.

[0104] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:10.

[0105] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:11.

[0106] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:11.

[0107] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:11.

[0108] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:11.

[0109] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:11.

[0110] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor which has an amino acid sequence according to SEQ ID NO:11.

[0111] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F,166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0112] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0113] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least two amino acid substitutions selected from the group consisting of YQ\I\I, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0114] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,S211N and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0115] In further preferred embodiments, the agent according to the invention comprises a) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to 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%, 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% and 98.8% identical, and in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271E and (ii) at the positions corresponding to positions 89, 189 and 224, the amino acid substitutions S89A, S189T and S224A, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0116] In further preferred embodiments, the agent according to the invention comprises a) a protease with one of the following amino acid substitution variants: P9T-N130D-T133A- N144K-G166M-S189T-Y217M-N252T-Q271 E; P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-G131H-T133A-N144K-S189T-Y217M-S224A-N252T- Q271 E; Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-N130D-T133A- N144K-G166M-S211 N-Y217M-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, wherein the numbering is in each case based on the numbering according to SEQ ID NO:1, and b) a peptide inhibitor having an amino acid sequence according to SEQ ID NO:12.

[0117] In washing or cleaning agents according to the invention, the washing or cleaning agent comprises, in each case based on the total weight of the washing or cleaning agent, the enzyme, ie the protease, in an amount of 0.005 to 5 wt.%, preferably from 0.05 to 2 wt.%, more preferably from 0.01 to 0.5 wt.% and even more preferably from 0.02 to 0.2 wt.%, and the peptide inhibitor in an amount of 0.01 to 15 wt.%, preferably from 0.05 to 5 wt.%, more preferably from 0.1 to 1 wt.% and even more preferably from 0.2 to 0.75 wt.%.

[0118] In various embodiments, the enzyme and the peptide inhibitor can be preformulated in an enzyme composition. As can be seen from the previous explanations, the enzyme protein constitutes 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 peptide inhibitor can be present in an amount of 0.05 to 35 wt.%, preferably 0.05 to 10 wt.%, based on the total weight in the enzyme composition. This enzyme composition, which is also a component of the present invention, can then be used in washing or cleaning agents according to the invention, in amounts that lead to the final concentrations in the washing or cleaning agent specified herein.

[0119] The proteases used according to the invention exhibit enzymatic activity, i.e., they are capable of hydrolyzing peptides and proteins, particularly in detergents or cleaning agents. A protease used according to the invention is therefore an enzyme that catalyzes the hydrolysis of amide / peptide bonds in protein / peptide substrates and is thus capable of cleaving proteins or peptides. Furthermore, a protease used according to the invention is preferably a mature protease, i.e., the catalytically active molecule without signal and / or propeptide(s). Unless otherwise stated, the sequences indicated also refer to mature (processed) enzymes.

[0120] In various embodiments of the invention, the protease is a free enzyme. This means that the protease can interact directly with all components of a composition and, if the composition is a liquid composition, that the protease is in direct contact with the composition's solvent (e.g., water). In other embodiments, a composition may contain proteases that form an interaction complex with other molecules or that contain a "coat." In this case, a single or multiple protease molecules may be separated from the other components of the composition by a surrounding structure. Such a separating structure may be formed by, but is not limited to, vesicles, such as a micelle or a liposome. However, the surrounding structure may also be a virus particle, a bacterial cell, or a eukaryotic cell.In various embodiments, an agent may contain cells of Bacillus pumilus or Bacillus subtilis expressing the proteases of the invention, or cell culture supernatants of such cells.

[0121] In the context of the present invention, the feature that a protease has the specified substitutions means that it contains one (of the specified) substitution(s) at the respective position, i.e., at least the specified positions are not otherwise mutated or deleted, for example, by fragmentation of the protease. In various preferred embodiments, the proteases described herein, with the exception of the explicitly mentioned substitutions, have the sequence of SEQ ID NO:1, i.e., apart from the substituted positions, they are 100% identical to the sequence according to SEQ ID NO:1.

[0122] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the BLAST algorithm, which is established and commonly used in the state of the art (see, for example, 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) and is essentially achieved by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences to one another. A tabular assignment of the relevant positions is referred to as an alignment. Another algorithm available in the state of the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. Frequently used, for example, are 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 (cf. 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. Furthermore, sequence comparisons (alignments) are possible with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the given standard parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (use of the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise stated, sequence identity reported herein is determined using the BLAST algorithm.

[0123] Such a comparison also allows a statement to be made about the similarity of the compared sequences. This is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same positions or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the 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 just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the entire length of the respective nucleic acid or amino acid sequence.

[0124] In the context of the present invention, the statement that an amino acid position corresponds to a numerically designated position in SEQ ID NO:1 therefore means that the corresponding position is assigned to the numerically designated position in SEQ ID NO:1 in an alignment as defined above. Furthermore, the assignment of the positions is based on the mature protein. This assignment is also to be applied in particular if the amino acid sequence of a protease according to the invention comprises a higher number of amino acid residues than the protease from Bacillus pumilus according to SEQ ID NO:1. Starting from the stated positions in the amino acid sequence of the protease from Bacillus pumilus, the change positions in a protease according to the invention are those that are assigned to precisely these positions in an alignment.

[0125] The following convention is used to describe substitutions that affect exactly one amino acid position (amino acid exchanges): first, the naturally occurring amino acid is named using the internationally accepted one-letter code, followed by the corresponding sequence position, and finally, the inserted amino acid. Multiple or alternative exchanges within the same polypeptide chain are separated by slashes. "130DA / " thus means that position 130 is mutated to D or V. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, such as an asterisk or a dash, or an A is indicated in front of the corresponding position.For example, P9T describes the substitution of proline at position 9 by threonine, P9TH the insertion of histidine after the amino acid threonine at position 9, and P9* or AP9 the deletion of proline at position 9. This nomenclature is known to those skilled in the art of enzyme technology.

[0126] Advantageous positions for sequence changes, in particular substitutions, of the protease from Bacillus pumilus, which, when transferred to homologous positions of the proteases according to the invention, are preferably of importance and impart advantageous functional properties to the protease, are accordingly the positions which, in an alignment, correspond to the positions described herein, ie, in the numbering according to SEQ ID NO:1. The following amino acid residues are located at the stated positions in the wild-type molecule of the protease from Bacillus pumilus: P9, N130, T133, N144, Y217, N252 and Q271 as well as Y6, S89, G131, G166, N187, S189, S211 and S224.

[0127] In a further embodiment of the invention, a previously described protease is additionally stabilized, in particular by one or more mutations, for example substitutions, or by coupling to a polymer. Increasing stability during storage and / or use, for example during the washing process, results in longer-lasting enzymatic activity and thus improved cleaning performance. In principle, all stabilization options described and / or expedient in the prior art are contemplated. Preference is given to stabilizations achieved via mutations of the enzyme itself, since such stabilizations do not require any further steps following the isolation of the enzyme. Examples of suitable sequence modifications are mentioned above. Other suitable sequence modifications are known from the prior art.

[0128] Other options for stabilization include:

[0129] Altering the binding of metal ions, in particular the calcium binding sites, for example by exchanging one or more of the amino acid(s) involved in calcium binding for one or more negatively charged amino acids and / or by introducing sequence changes in at least one of the sequences of the two amino acids arginine / glycine;

[0130] Protection against the influence of denaturing agents such as surfactants through mutations that cause a change in the amino acid sequence on or at the surface of the protein;

[0131] Exchange of amino acids located near the N-terminus for those that presumably come into contact with the rest of the molecule via non-covalent interactions and thus contribute to maintaining the globular structure.

[0132] Preferred embodiments are those in which the enzyme is stabilized in several ways, since several stabilizing mutations act additively or synergistically.

[0133] In addition, at least one further stabilizer compound selected from the group consisting of polyols, in particular glycerol and 1,2-propylene 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), and combinations thereof, may also be present.

[0134] For the purposes of the present invention, "phenylboronic acid derivative" refers to a compound of formula (I). The compound of formula (I) has the following structural formula: where R is hydrogen, a hydroxyl, a C1-6 alkyl, a substituted C1-6 alkyl, a C1-6 alkenyl, or a substituted C1-6 alkenyl group. Preferably, the R radical in the phenylboronic acid derivative is a C1-6 alkyl group, and among these, it is more preferably -CH3, -CH3CH2, or -CH3CH2CH2. More preferably, the R radical in the phenylboronic acid derivative is hydrogen. The phenylboronic acid derivative is particularly preferred as 4-formylphenylboronic acid (4-FPBA).

[0135] The additional stabilizer compound used can be boric acid.

[0136] Preferably, the agent according to the invention is substantially free of other stabilizer compounds. Most preferably, the agent according to the invention does not comprise any of the aforementioned other stabilizer compounds in addition to the peptide inhibitors according to the invention.

[0137] In particularly preferred embodiments, the washing and cleaning agent according to the invention is essentially free of boron-containing compounds. "Essentially free of boron-containing compounds" in this context means that the agents according to the invention contain less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight, and particularly preferably less than 0.1% by weight, of boron-containing compounds, based on the total weight of the agent. In very particularly preferred embodiments, the washing and cleaning agents according to the invention are free of boron-containing compounds, i.e., they contain, in particular, no boric acid and / or phenylboronic acid derivatives.Using methods commonly known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, it is possible for the skilled person to produce the corresponding nucleic acids, including complete genes, based on known DNA and / or amino acid sequences. Such methods are known, for example, from Sambrook, J., Fritsch, EF, and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition, Cold Spring Laboratory Press.

[0138] In a further embodiment of the invention, the protease used according to the invention is characterized in that its cleaning performance is not significantly reduced compared to that of a protease comprising an amino acid sequence corresponding to the amino acid sequence given in SEQ ID NO:1, ie it has at least 80% of the reference washing performance, preferably at least 100%, more preferably at least 110% or more.

[0139] Washing or cleaning performance is understood to mean the ability of a washing or cleaning agent to partially or completely remove an existing soiling, in particular the lightening performance of one or more soils on textiles. Examples of such soils are blood on cotton or chocolate milk / soot on cotton, cocoa on cotton or porridge on cotton. Within the scope of the invention, both the washing or cleaning agent comprising the protease, or the washing or cleaning liquor formed by this agent, and the protease itself have a respective cleaning performance. The cleaning performance of the protease thus contributes to the cleaning performance of the agent or the washing or cleaning liquor formed by the agent.

[0140] The term "washing or cleaning liquor" refers to the working solution containing the washing or cleaning agent that acts on the textiles or hard surfaces and thus comes into contact with the soiling present on the textiles or hard surfaces. The washing or cleaning liquor is typically created when the washing or cleaning process begins and the washing or cleaning agent is diluted with water, for example, in a washing machine, dishwasher, or other suitable container.

[0141] The cleaning performance can be determined in a washing system that contains a detergent at a dosage of between 2.0 and 8.0 grams per liter of wash liquor and the enzyme. The enzymes to be compared are used at the same concentration (based on active protein). By using the same activity of the respective enzymes, it is ensured that even if there is a possible discrepancy in the ratio of active substance to total protein (the specific activity values), the respective enzymatic properties, for example the cleaning performance on specific soils, can be compared. In general, a low specific activity can be compensated for by adding a larger amount of protein. Furthermore, the enzymes to be tested can also be used in the same amount of substance or weight if the enzymes to be tested have a different affinity for the test substrate in an activity test.In this context, the term "equal amount of substance" refers to the same mole of the enzymes being tested. The term "equal amount by weight" refers to the same weight of the enzymes being tested. The concentration of protease in the detergent intended for such a washing system is 0.001 to 0.1 wt.%, preferably 0.01 to 0.06 wt.%, based on active protein.

[0142] A liquid reference detergent for such a washing system can, for example, be composed as follows (all data in weight percent (wt%)): 4.4% alkylbenzenesulfonic acid, 5.6% other anionic surfactants, 2.4% C12-18 Na salts of fatty acids (soaps), 4.4% non-ionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% NaOH, 0.01% defoamer, 2% glycerin, 0.08% preservatives, 1% ethanol, and the remainder demineralized water. The preferred dosage of the liquid detergent is between 4.5 and 6.0 grams per liter of wash liquor, for example 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.

[0143] The cleaning performance is determined by measuring the degree of cleanliness of the washed textiles compared to soiling on cotton. For example, the wash cycle can be carried out for 60 minutes at a temperature of 40°C and the water hardness can be between 15.5°dH and 16.5°dH (German hardness).

[0144] The degree of whiteness, i.e., the lightening of soils, as a measure of cleaning performance, is determined using optical measurement methods, preferably photometrically. A suitable device for this purpose is the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably one supplied with the product.

[0145] Preferred embodiments of proteases according to the invention achieve such advantageous cleaning performance even at low temperatures, in particular in the temperature ranges between 10°C and 60°C, preferably between 15°C and 50°C and particularly preferably between 20°C and 40°C.

[0146] The protein concentration can be determined using known methods, for example, the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall et al., 1948, J. Biol. Chem., 177:751-766). The active protein concentration can be determined by titrating the active sites using a suitable irreversible inhibitor and determining the residual activity (Bender et al., 1966, J. Am. Chem. Soc. 88, 24:5890-5913).

[0147] According to the invention, a washing or cleaning agent is understood to mean all conceivable types of washing or cleaning agents, both concentrated and undiluted, for use on a commercial scale, in washing machines or for hand washing or cleaning. These include, for example, washing agents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. This also includes, for example, dishwashing detergents for dishwashers (machine dishwashing detergents) or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood, or leather, for which the term "cleaning agent" is used. Thus, in addition to manual and machine dishwashing detergents, this also includes, for example, scouring agents, glass cleaners, toilet air fresheners, etc.The washing and cleaning agents within the scope of the invention also include washing aids that are added to the actual washing agent during manual or machine washing to achieve an additional effect. Furthermore, the washing and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e. agents with which the laundry is brought into contact before the actual washing, for example, to dissolve stubborn soils, and also agents that impart further desirable properties to the laundry, such as a pleasant feel, resistance to creasing, or low static charge, in a step following the actual textile washing. Fabric softeners, among others, are counted among the latter agents.

[0148] The detergents or cleaning agents according to the invention, which may be in the form of powdered or granular solids, in compacted or recompacted particle form, as homogeneous solutions or suspensions, may contain, in addition to a protease according to the invention, all known ingredients customary in such agents, with at least one further ingredient preferably being present in the agent. The agents according to the invention may contain, in particular, surfactants, builders, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators, or bleach catalysts. They may also contain water-miscible organic solvents, other enzymes, enzyme stabilizers, sequestering agents, electrolytes, pH regulators, and / or other auxiliaries such as optical brighteners, graying inhibitors, dye transfer inhibitors, foam regulators, as well as dyes and fragrances, and combinations thereof.

[0149] Advantageous ingredients of the compositions according to the invention are disclosed in the international patent application WO 2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly incorporated by reference, and the disclosure content therein is incorporated into the present patent application.

[0150] An agent according to the invention advantageously contains the protease according to the invention in an amount of 2 pg to 20 mg, preferably 5 pg to 17.5 mg, particularly preferably 20 pg to 15 mg, and most particularly preferably 50 pg to 10 mg per g of the agent. In various embodiments, the concentration of the protease described herein (active enzyme) in the agent is >0 to 1 wt.%, preferably 0.0001 or 0.001 to 0.1 wt.%, based on the total weight of the agent or composition.

[0151] An agent according to the invention contains the protease increasingly preferably in an amount of 1 x 10 -8 up to 5 wt.%, from 0.0001 to 1 wt.%, from 0.0005 to 0.5 wt.%, from 0.001 to 0.1 wt.%, each based on active protein and based on the total weight of the detergent.

[0152] An agent according to the invention increasingly preferably contains the protease in an amount of 0.1 pmol to 2 pmol, preferably 0.2 pmol to 1.5 pmol, more preferably 0.5 pmol to 1 pmol.

[0153] The embodiments of the present invention encompass all solid, powdered, liquid, gel-like, or pasty dosage forms of agents according to the invention, which may optionally also consist of multiple phases and may be present in compressed or uncompressed form. The agent may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the agent also include extrudates, granules, tablets, or pouches. Alternatively, the agent may also be liquid, gel-like, or pasty, for example in the form of a non-aqueous liquid detergent or a non-aqueous paste, or in the form of an aqueous liquid detergent or a water-containing paste. Liquid agents are generally preferred. Furthermore, the agent may be in the form of a one-component system. Such agents consist of one phase.Alternatively, a remedy can also consist of multiple phases. Such a remedy is therefore divided into several components.

[0154] When the detergents according to the invention are in liquid form, they preferably contain, based on their total weight, more than 40% by weight, preferably 50 to 90% by weight and particularly preferably 60 to 80% by weight of water.

[0155] The agents according to the invention may contain one or more surfactants, with particular preference being given to anionic surfactants, nonionic surfactants, and mixtures thereof, but cationic, zwitterionic, and / or amphoteric surfactants may also be present. The agents preferably contain 5 to 70% by weight of surfactant, more preferably 5 to 60% by weight, and more preferably 5 to 50% by weight of surfactant.

[0156] Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups, preferably with alkali ions as cations. Suitable soaps are preferably the alkali salts of saturated or unsaturated C12-C18 fatty acids. Such fatty acids can also be used in a non-neutralized form. Suitable sulfate-type surfactants include the salts of the sulfuric acid monoesters of C12-C18 fatty alcohols and the sulfation products of the aforementioned nonionic surfactants with a low degree of ethoxylation. The usable surfactants of the sulfonate type include, for example, Cg-u-alkylbenzenesulfonates, alkanesulfonates obtained from Ci2-is-alkanes, for example by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization, Ci2-18-olefinsulfonates, which are formed by the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkanesulfonates, disulfonates, as can be found, for example, infrom Ci2-18 monoolefins with terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation products, as well as a-sulfofatty acid esters (ester sulfonates) which are formed during the sulfonation of fatty acid methyl or ethyl esters, e.g. a-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

[0157] The agent preferably contains 2 to 55 wt.%, preferably 3 to 35 wt.%, of anionic surfactant. Most preferably, the agent contains 3 to 25 wt.% alkylbenzenesulfonate. Furthermore, the agent may preferably contain other anionic surfactants, especially alkyl ether sulfates, as well as nonionic surfactants, especially fatty alcohol alkoxylates. These can then make up the remainder of the surfactants.

[0158] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula in which R' and R" are independently H or alkyl and together contain 6 to 19, preferably 7 to 15 and in particular 9 to 13 C atoms. A particularly preferred representative is sodium dodecylbenzylsulfonate.

[0159] Preferred alk(en)yl sulfates are the alkali metal salts, especially the sodium salts, of the sulfuric acid half-esters of C12-18 fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or C18-20 oxo alcohols, and those half-esters of secondary alcohols of these chain lengths. Also preferred are alk(en)yl sulfates of the stated chain length that contain a synthetic, petrochemically produced straight-chain alkyl radical, which exhibit degradation behavior similar to that of equivalent compounds based on oleochemical raw materials. For washing purposes, C12-18 alkyl sulfates and C12-15 alkyl sulfates, as well as C11-15 alkyl sulfates, are preferred.

[0160] Also suitable are the sulfuric acid monoesters of straight-chain or branched C1-2i alcohols ethoxylated with 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C5-n alcohols with an average of 3.5 mol of ethylene oxide (EO) or C12-18 fatty alcohols with 1 to 4 EO.

[0161] Suitable alkyl ether sulfates are, for example, compounds of the formula

[0162] R 1 -O-(AO) n -SO3- X + .

[0163] In this formula, R 1 represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred radicals R 1 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, with the representatives having an even number of carbon atoms being preferred. Particularly preferred radicals R 1are derived from C12-18 fatty alcohols, e.g., from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C12-20 oxo alcohols. AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20, and in particular from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7, or 8. X + stands for a monovalent cation or the n-th part of an n-valent cation, preferably the alkali metal ions and among them Na + or K + , where Na + is highly preferred. Other cations X + can be selected from NH4 + , % Zn 2+ , % Mg 2+ , % Ca 2+ , % Mn 2+ and their mixtures.

[0164] In various embodiments, the alkyl ether sulfate may be selected from fatty alcohol ether sulfates of the formula so; Na with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are Na-Ci2-Ci4 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical mean, which can be a whole or fractional number for a specific product. The stated degrees of alkoxylation represent statistical mean, which can be a whole or fractional number for a specific product. Preferred alkoxylates / ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE).

[0165] It has proven beneficial for cold-wash performance if detergents also contain soap(s). Preferred detergents are therefore characterized by the presence of soap(s). Suitable soaps include saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, as well as, in particular, soap mixtures derived from natural fatty acids, e.g., coconut, palm kernel, or tallow fatty acids.

[0166] Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols, each containing 8 to about 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10, alkyl ether groups. Furthermore, corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters, and fatty acid amides, which correspond to the aforementioned long-chain alcohol derivatives with regard to the alkyl moiety, as well as of alkylphenols with 5 to 12 carbon atoms in the alkyl radical, are also suitable.

[0167] Nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, 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. The alcohol radical can be linear or, preferably, methyl-branched in the 2-position, or can contain linear and methyl-branched radicals in a mixture, as is usually the case in oxo alcohol radicals. However, alcohol ethoxylates with linear radicals from alcohols of native origin 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, C12-14 alcohols with 3 EO or 4 EO, C12-18 alcohols with 7 EO, C18-19 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C12-19 alcohols with 3 EO, 5 EO or 7 EO and mixtures thereof, such as mixtures of C12-14 alcohol with 3 EO and C12-18 alcohol with 5 EO.The stated degrees of ethoxylation represent statistical averages, which can be a whole or fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohol with 14 EO, 25 EO, 30 EO, or 40 EO.

[0168] Another class of preferably used nonionic surfactants, which are used either as the sole nonionic surfactant or in combination with other nonionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

[0169] Another class of nonionic surfactants that can be used advantageously are alkyl polyglycosides (APG). Suitable alkyl polyglycosides satisfy the general formula

[0170] RO(G)z, in which R is a linear or branched, in particular 2-methyl-branched, saturated or unsaturated, aliphatic radical having 8 to 22, preferably 12 to 18, carbon atoms, and G is the symbol representing a glycose unit having 5 or 6 carbon atoms, preferably glucose. The degree of glycosidation z is between 1 and 4, preferably between 1 and 2, and in particular between 1.1 and 1.4. Preference is given to using linear alkyl polyglycosides, i.e. alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical.

[0171] Nonionic surfactants of the amine oxide type, e.g., N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half that amount.

[0172] Suitable amphoteric surfactants are, for example, betaines of the formula

[0173] (R iii )(R iv )(R v )N + CH2COO-, in which R'" is an alkyl radical having 8 to 25, preferably 10 to 21 carbon atoms, optionally interrupted by heteroatoms or heteroatom groups, and R iv and R v identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C10-18-alkyldimethylcarboxymethylbetaine and Cn-17-alkylamidopropyldimethylcarboxymethylbetaine.

[0174] Suitable cationic surfactants include the quaternary ammonium compounds of the formula (Rvi )(R vii )(R viii )(R ix )N + X-, in the R vi to R ix represents four identical or different, in particular two long- and two short-chain, alkyl radicals, and X- represents an anion, in particular a halide ion, e.g., didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary surface-active compounds, in particular those containing a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. By using quaternary surface-active compounds with antimicrobial activity, the agent can be given an antimicrobial effect or its existing antimicrobial effect, possibly due to other ingredients, can be improved.

[0175] A further preferred component of detergents according to the invention are complexing agents. Particularly preferred complexing agents are phosphonates, provided their use is permitted by regulations. In addition to 1-hydroxyethane-1,1-diphosphonic acid, the complexing phosphonates include a number of different compounds, such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP). In this application, particular preference is given to hydroxyalkane and aminoalkanephosphonates. Among the hydroxyalkanephosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as the sodium salt, with the disodium salt being neutral and the tetrasodium salt being alkaline (pH 9). Preferred aminoalkanephosphonates are ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues. They are preferably used in the form of neutral sodium salts, e.g.as the hexasodium salt of EDTMP or as the hepta- and octasodium salt of DTPMP. HEDP is the preferred builder from the phosphonate class. Aminoalkanephosphonates also possess a pronounced heavy metal binding capacity. Accordingly, it may be preferable, especially if the products also contain bleach, to use aminoalkanephosphonates, especially DTPMP, or mixtures of the aforementioned phosphonates.A preferred detergent within the scope of this application contains one or more phosphonate(s) from the group aminotrimethylenephosphonic acid (ATMP) and / or salts thereof; ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or salts thereof; diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and / or salts thereof; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or salts thereof; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or salts thereof; hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and / or salts thereof; nitrilotri(methylenephosphonic acid) (NTMP) and / or salts thereof. Particularly preferred detergents are those containing 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates. Of course, the detergents according to the invention can contain two or more different phosphonates.Preferred detergents according to the invention are characterized in that the detergent contains at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, wherein the weight fraction of the phosphonate in the total weight of the detergent is preferably 0.1 and 8.0 wt.%, preferably 0.2 and 5.0 wt.%, more preferably 0.3 and 3.0 wt.% and particularly preferably 0.5-2.0 wt.%.

[0176] The detergents according to the invention preferably further contain builders, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. Builders include, in particular, silicates, carbonates, and organic cobuilders.

[0177] Organic cobuilders include, in particular, polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders, and phosphonates. These classes of substances are described below. Organic cobuilder substances can, if desired, be present in amounts of up to 40 wt.%, in particular up to 25 wt.%, and preferably from 1 to 8 wt.%. Suitable organic builders include, for example, polycarboxylic acids, which can be used in the form of the free acid and / or their sodium salts. Polycarboxylic acids are understood to be carboxylic acids that carry more than one acid function.For example, these are citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethyl inulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycinediacetic acid, methylglycinediacetic acid, glutaminediacetic acid, nitrilotriacetic acid (NTA), iminodisuccinate 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 orDextrin-accessible polycarboxylates, and / or polymeric acrylic acids, methacrylic acids, maleic acids, and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. Such organic builder substances can, if desired, be present in amounts of up to 50% by weight, in particular up to 25% by weight, preferably from 10 to 20% by weight, and particularly preferably from 1 to 5% by weight. In addition to their builder effect, the free acids typically also have the property of an acidifying component and thus also serve to adjust a lower and milder pH value of detergents. Particular mention should be made of citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof. Citric acid or salts of citric acid are particularly preferably used as the builder substance.Further particularly preferred builders are selected from methylglycinediside acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS), ethylenediamine disuccinate (EDDS), carboxymethylinulin, and polyaspartate. In preferred embodiments, citric acid and / or citrate are used as the water-soluble, organic builder. Particular preference is given to using 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% of citric acid and / or 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% of citrate, preferably alkali metal citrate, even more preferably sodium citrate. Citric acid / citrate can each be used in the form of their hydrates, for example citric acid can be used in the form of the monohydrate, citrate in the form of trisodium citrate dihydrate.

[0178] Other suitable builders include polymeric polycarboxylates, for example the alkali metal salts of polyacrylic acid or polymethacrylic acid, e.g. those with a relative molecular mass of 500 to 70,000 g / mol. For the purposes of this application, the molecular masses stated for polymeric polycarboxylates are weight-average molecular masses Mw of the respective acid form, which were generally determined by gel permeation chromatography (GPC) using a UV detector. The measurement was carried out against an external polyacrylic acid standard, which, due to its structural similarity to the polymers investigated, provides realistic molecular weight values. These figures differ significantly from the molecular weight figures used when polystyrenesulfonic acids are used as the standard. The molecular masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular masses stated in this application.Suitable polymers are, in particular, polyacrylates, which preferably have a molecular weight of 2000 to 20,000 g / mol. Due to their superior solubility, the short-chain polyacrylates, which have molecular weights of 2000 to 10,000 g / mol, and particularly preferably of 3000 to 5000 g / mol, may be preferred from this group. Also suitable are copolymers of polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid. Copolymers of acrylic acid with maleic acid, which contain 50 to 90 wt.% acrylic acid and 50 to 10 wt.% maleic acid, have proven particularly suitable. Their relative molecular weight, based on free acids, is generally 2000 to 70,000 g / mol, preferably 20,000 to 50,000 g / mol, and in particular 30,000 to 40,000 g / mol.

[0179] A solid detergent according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include the above-mentioned organic framework substances. In addition to the above-mentioned water-soluble organic builders, the detergents according to the invention can also contain inorganic water-soluble builders. Suitable water-soluble inorganic builder materials are, in particular, alkali metal silicates, alkali metal carbonates, alkali metal hydrogen carbonates, alkali metal phosphates, and / or sesquicarbonates, which can be in the form of their alkaline, neutral, or acidic sodium or potassium salts. Small amounts of calcium carbonates can also be present in solid textile detergents if desired. Suitable examples are water-soluble crystalline and / or amorphous alkali metal silicates.The alkali silicates usable as builders in the agents according to the invention preferably have a molar ratio of alkali oxide to SiO2 of less than 0.95, in particular from 1:1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are sodium silicates, in particular amorphous sodium silicates, with a molar ratio Na2O:SiO2 of 1:2 to 1:2.8. Crystalline silicates, which can be present alone or in a mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na2Si. xO2x+i • y H2O is used, in which x, the so-called modulus, is a number from 1.9 to 22, in particular 1.9 to 4 and y is a number from 0 to 33 and preferred values ​​for x are 2, 3 or 4. Preferred crystalline layered silicates are those in which x in the general formula mentioned takes on the values ​​2 or 3. In particular, both β- and δ-sodium disilicates (Na2Si2Os • y H2O) are preferred. Practically anhydrous crystalline alkali silicates produced from amorphous alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, can also be used in agents according to the invention. In a further embodiment of agents according to the invention, a crystalline sodium layered silicate with a modulus of 2 to 3 is used, such as can be produced from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further embodiment of the compositions according to the invention.In agents containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and in particular 1:1 to 2:1. Crystalline layered silicates of the above-mentioned formula (I) are marketed by Clariant GmbH under the trade name Na-SKS, e.g. Na-SKS-1 (Na2Si2O45 • x H2O, Kenyaite), Na-SKS-2 (Na2SiI4O29 • x H2O, Magadiite), Na-SKS-3 (Na2SiI7O17 • x H2O) or Na-SKS-4 (Na2SiI4Og • x H2O, Makatite). Of these, Na-SKS-5 (α-Na2Si2O5), Na-SKS-7 (β-Na2Si2O5, Natrosilite), Na-SKS-9 (NaHSi2O5• 3 H2O), Na-SKS-10 (NaHSi2O5• 3 H2O, Kanemite), Na-SKS-11 (β-Na2Si2O5) and Na-SKS-13 (NaHSi2O5), but especially Na-SKS-6 (δ-Na2Si2O5) are particularly suitable.In one embodiment of the inventive compositions, a granular compound of crystalline phyllosilicate and citrate, of crystalline phyllosilicate and the above-mentioned (co)polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate is used, as is commercially available, for example, under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably present in the compositions according to the invention in amounts of 1 to 20 wt.%, in particular 5 to 15 wt. Other important water-soluble inorganic builder substances are carbonates (and hydrocarbonates), in particular sodium carbonate, and phosphonic acids / phosphonates.

[0180] The agents according to the invention are preferably free of phosphate builders, i.e., they contain less than 1% by weight, preferably no deliberately added phosphate builder. The agents may also contain water-insoluble builders. Crystalline or amorphous, water-dispersible alkali aluminosilicates are used as water-insoluble inorganic builder materials, in particular in amounts of up to 50% by weight, preferably not more than 40% by weight, in particular from 3 to 20% by weight, and particularly preferably from 1 to 15% by weight. Among these, crystalline sodium aluminosilicates of detergent quality are preferred, in particular zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, alone or in mixtures, e.g., in the form of a co-crystallizate of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA). Amounts close to the stated upper limit are preferably used in solid, particulate agents.Suitable aluminosilicates, in particular, do not contain any particles with a grain size larger than 30 pm and preferably consist of at least 80 wt.% particles with a size smaller 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.

[0181] In addition to the builders described above, the detergent may contain cleaning-active polymers. The weight fraction of the cleaning-active polymers in the total weight of detergents according to the invention is preferably 0.1 to 20 wt.%, preferably 1.0 to 15 wt.%, and more preferably 2.0 to 12 wt.%.

[0182] Peroxygen compounds suitable for use in agents according to the invention include, in particular, organic peracids or peracidic salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid, or salts of diperdodecanedioic acid, hydrogen peroxide, and inorganic salts that release hydrogen peroxide under washing conditions, including perborate, percarbonate, persilicate, and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds, such as H2G2-urea adducts. Hydrogen peroxide can also be produced with the aid of an enzymatic system, i.e., an oxidase and its substrate. If solid peroxygen compounds are to be used, they can be used in the form of powders or granules, which can also be coated in a manner known in principle.The peroxygen compounds can be added to the wash liquor as such or in the form of agents containing them, which in principle can contain all conventional washing, cleaning, or disinfectant ingredients. Particular preference is given to using alkali metal percarbonate or alkali metal perborate monohydrate. If an agent according to the invention contains peroxygen compounds, they are present in amounts of preferably up to 50 wt.%, in particular from 5 to 30 wt.%, more preferably from 0.1 to 20 wt.%.

[0183] Compounds that, 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 can be used as bleach activators in the detergents. Suitable substances are those that carry O- and / or N-acyl groups with the stated number of carbon atoms and / or optionally substituted benzoyl groups. Preferred are multiply acylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N-acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates or carboxylates or the sulfonic or carboxylic acids thereof, in particular nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS orLOBS), 4-(2-decanoyloxyethoxycarbonyloxy)-benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic acid anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters as well as acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactose, acetylated, optionally N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimidic acids are formed, in particular aminoacetonitrile derivatives with a quaternized nitrogen atom, and / or Oxygen-transferring sulfonimines and / or acylhydrazones. Hydrophilically substituted acyl acetals and acyl lactams are also preferred. Combinations of conventional bleach activators can also be used.Such bleach activators can be present, particularly in the presence of the above-mentioned hydrogen peroxide-providing bleaching agents, in the usual amount range, preferably in amounts of 0.5 to 10 wt.%, in particular 1 to 8 wt.%, based on the total agent, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent.

[0184] In addition to the conventional bleach activators or instead of them, solid agents may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0185] Suitable graying inhibitors or soil-release agents (soil-release polymers) are cellulose ethers, such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, and cellulose mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, and methylcarboxymethylcellulose. Preference is given to using sodium carboxymethylcellulose, hydroxypropylmethylcellulose, and mixtures thereof, and optionally mixtures thereof with methylcellulose. Commonly used soil-release agents include copolyesters containing dicarboxylic acid units, alkylene glycol units, and polyalkylene glycol units. The proportion of graying inhibitors and / or soil-release agents in agents according to the invention generally does not exceed 2% by weight and is preferably 0.5 to 1.5% by weight, particularly preferably 0.5 to 2% by weight.

[0186] Optical brighteners, particularly for textiles made from cellulose fibers (e.g., cotton), may include derivatives of diaminostilbene disulfonic acid or its alkali metal salts. Suitable brighteners include, for example, salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-ylamino)stilbene-2,2'-disulfonic acid or similarly structured compounds that carry a diethanolamino group, a methylamino group, or a 2-methoxyethylamino group instead of the morpholino group. Furthermore, brighteners of the substituted 4,4'-distyryl-diphenyl type may be present, e.g., 4,4'-bis(4-chloro-3-sulfostyryl)-diphenyl. Mixtures of brighteners can also be used. Brighteners of the 1,3-diaryl-2-pyrazoline type, e.g., 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazoline, and similarly structured compounds, are particularly suitable for polyamide fibers. The optical brightener or brightener mixture content of the agent generally does not exceed 1 wt.-%, preferably 0.05 to 0.5 wt.%. In a preferred embodiment of the invention, the agent is free of such active ingredients.

[0187] The conventional foam regulators that can be used in the agents according to the invention include, for example, polysiloxane-silica mixtures, the finely divided silica contained therein preferably being silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as cross-linked polysiloxane resins and mixtures thereof. Other defoamers are paraffin hydrocarbons, in particular microparaffins and paraffin waxes, whose melting point is above 40°C, saturated fatty acids or soaps with, in particular, 20 to 22 C atoms, e.g., sodium behenate, and alkali metal salts of phosphoric acid mono- and / or dialkyl esters in which the alkyl chains each have 12 to 22 C atoms. Among these, sodium monoalkyl phosphate and / or dialkyl phosphate with cis-cis-alkyl groups is preferably used. The proportion of foam regulators can preferably be 0.2 to 2 wt.%, particularly preferably not more than 1 wt.%.

[0188] To adjust the desired pH, the agents according to the invention can contain system- and environmentally compatible acids, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid, and / or adipic acid, but also mineral acids, in particular sulfuric acid or alkali metal hydrogen sulfates, or bases, in particular ammonium or alkali metal hydroxides, preferably sodium hydroxide. Such pH regulators are preferably present in the agents according to the invention in amounts of no more than 10% by weight, in particular from 0.5 to 6% by weight, particularly preferably from 0.3 to 2% by weight.

[0189] The detergents according to the invention may contain an organic solvent as a further component. The addition of organic solvents has a beneficial effect on the enzyme stability and cleaning performance of these detergents. Preferred organic solvents are selected from the group consisting of mono- or polyhydric alcohols, alkanolamines, or glycol ethers.The solvents are preferably selected from ethanol, n- or i-propanol, butanol, glycol, propanediol, butanediol, glycerin, diglycol, propyl diglycol, butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, dipropylene glycol ethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and mixtures of these solvents. The weight proportion of these organic solvents in the total weight of detergents according to the invention is preferably 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.% and more preferably 0.5 to 5.0 wt.%.A particularly preferred organic solvent that is particularly effective with regard to stabilizing the detergents is glycerol and 1,2-propylene glycol. Liquid detergents preferably comprise at least one polyol, preferably from the group consisting of glycerol and 1,2-propylene glycol, based on the total weight of the detergent, preferably in an amount of 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight, and more preferably 0.5 to 5.0% by weight. Further preferred organic solvents are organic amines and alkanolamines. The detergents according to the invention preferably contain these amines in amounts of 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight, and more preferably 0.5 to 5.0% by weight, in each case based on their total weight. A particularly preferred alkanolamine is ethanolamine.

[0190] Detergents or cleaning agents according to the invention can contain only one protease. Alternatively, they can also contain further hydrolytic enzymes or other enzymes in a concentration appropriate for the effectiveness of the agent. A further embodiment of the invention thus represents agents which further comprise one or more further enzymes. Preferably used further enzymes are all enzymes which can exhibit catalytic activity in the agent according to the invention, in particular a lipase, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, ß-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase or other proteases distinguishable from the proteases according to the invention, as well as mixtures thereof. Further enzymes are advantageously present in the agent in an amount of 1 x 10 -8to 5 percent by weight based on active protein. Increasingly preferably, each additional enzyme is present in an amount of 1 x 10 -7to 3 wt.%, from 0.00001 to 1 wt.%, from 0.00005 to 0.5 wt.%, from 0.0001 to 0.1 wt.% and particularly preferably from 0.0001 to 0.05 wt.% in agents according to the invention, based on active protein. The enzymes particularly preferably display synergistic cleaning performance against certain soilings or stains, i.e. the enzymes contained in the agent composition support one another in their cleaning performance. Such synergism very particularly preferably exists between the protease contained according to the invention and another enzyme of an agent according to the invention, including in particular between the said protease and an amylase and / or a lipase and / or a mannanase and / or a cellulase and / or a pectinase. Synergistic effects can occur not only between different enzymes, but also between one or more enzymes and other ingredients of the agent according to the invention.

[0191] Textile detergents preferred according to the invention comprise at least one protease and at least one amylase. In a further preferred embodiment of the invention, textile detergents comprise at least one protease and at least one cellulase. In a further preferred embodiment, textile detergents comprise at least one protease and at least one lipase. In a further preferred embodiment, textile detergents comprise at least one protease, at least one amylase, and at least one lipase. In a further preferred embodiment, textile detergents comprise at least one protease, at least one amylase, and at least one cellulase. In a further preferred embodiment, textile detergents comprise at least one protease, at least one amylase, at least one cellulase, and at least one lipase.Particularly preferred are textile detergents which contain 3 to 10 different enzymes, whereby textile detergents which contain 3 to 10 different enzyme types may be particularly preferred with regard to cleaning performance against a very wide range of stains.

[0192] Examples of proteases are the subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus lentus formis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY, and the enzymes Thermitase, Proteinase K, and the proteases TW3 and TW7, which are classified as subtilases but no longer as subtilisins in the narrower sense. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes. Subtilisins 147 and 309 are marketed under the trade names Esperase® and Savinase®, respectively, by Novozymes. Protease variants are derived from the protease from Bacillus lentus DSM 5483. Other useful proteases include:the enzymes available under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101 L® and Ovozyme® from Novozymes, the enzymes available under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® from Danisco / DuPont, the enzyme available under the trade name Lavergy pro 104 LS® from BASF, the enzyme available under the trade name Protosol® from Advanced Biochemicals Ltd., the enzyme available under the trade name Wuxi® from Wuxi Snyder Bioproducts Ltd., the enzyme available under the trade names Proleather® and Protease P® from Amano Pharmaceuticals Ltd. and the enzyme available under the name Proteinase K-16 from Kao Corp. The proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in WO 2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697, are also particularly preferably used.Further advantageously usable proteases are disclosed in, for example, WO 91 / 02792, WO 2008 / 007319, WO 93 / 18140, WO 01 / 44452, GB 1243784 A, WO 96 / 34946, WO 02 / 029024 and WO 03 / 057246. Other usable proteases are those naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus.

[0193] Examples of amylases are the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus stearothermophilus, as well as their further developments that have been improved for use in detergents and cleaning agents. The enzyme from Bacillus licheniformis is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. Further developments of this α-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). The α-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derivatives of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also from Novozymes. Furthermore, the a-amylase from Bacillus sp. is used for this purpose.A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are particularly suitable. Furthermore, the amylolytic enzymes disclosed in WO 95 / 26397, WO 96 / 23873, WO 99 / 23211, WO 00 / 60060, WO 2003 / 002711, WO 2003 / 054177, WO 2006 / 002643, WO 2007 / 079938, WO 2011 / 100410, and WO 2013 / 003659 can be used. Fusion products of all of the above-mentioned molecules can also be used. In addition, the further developments of α-amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from Novozymes are suitable. Other commercial products that can be used advantageously include Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, as well as Amplify™ 12L or Amplify Prime™ 100L, the latter also from Novozymes, and the PREFERENZ S® series from Danisco / DuPont, including PREFERENZ S100®, PREFERENZ S1000®, and PREFERENZ S210®.Variants of these enzymes obtainable by point mutations can also be used according to the invention.

[0194] Preferred amylases comprise a) an α-amylase which comprises an amino acid sequence which is 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% or 99% identical to the amino acid sequence given in SEQ ID NO:13 over its entire length and optionally has at least one amino acid substitution at one of the positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:13, preferably selected from the group consisting of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, R172Q and combinations thereof; and / or b) an α-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:14 over its entire length to at least 60% and increasingly preferably to at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 92%, 93%, 94%,95%, 96%, 97%, 98% or 99% identical and optionally at least one amino acid substitution at one of the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 320, 323, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and / or a deletion at one of the positions 183 and 184 in the numbering according to SEQ ID NO:14, preferably at least one amino acid substitution at one of the positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, and / or particularly preferably at least one amino acid substitution or deletion which is selected from the group consisting of R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof; and / or c) an a-amylase comprising an amino acid sequence,which is at least 65%, and increasingly preferably at least 66%, 67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:15 and optionally at least one substitution and / or deletion at one of the positions 93, 116, 118, 129, 133, 134, 140, 142, 146, 147, 149, 151, 152, 169, 174, 183, 184, 186, 189, 193, 195, 197, 198, 200, 203, 206, 210, 212, 213, 235, 243, 244, 260, 262, 284, 303, 304, 320, 338, 347, 359, 418, 431, 434, 439, 447, 458, 469, 476 and 477 in the numbering according to SEQ ID NO:15, preferably Amino acid deletions at positions 183 and 184; and / or d) an a-amylase comprising an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:16 over its entire length by at least 89% and increasingly preferably by at least 90%, 91%, 92%, 93%, 94%, 95%,96%, 97%, 98% or 99% identical and has at least one deletion at one of the positions 180, 181, 182, 183 and 184 in the numbering according to SEQ ID NO:16, preferably deletions at at least two positions selected from the positions 180+181, 181+182, 182+183 and 183+184 in the numbering according to SEQ ID NO:16, particularly preferably at the positions 183+184 in the numbering according to SEQ ID NO:16, and / or has at least one substitution at one of the positions 405, 421, 422 and 428 in the numbering according to SEQ ID NO:16, which is selected from the group consisting of I405L, A421H, A422P, A428T and combinations thereof is.,

[0195] In various embodiments of the invention, the amylase comprises an amino acid sequence which is 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% or 99% identical to the amino acid sequence given in SEQ ID NO:13 over its entire length and optionally has at least one amino acid substitution at one of the positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:13, preferably selected from the group consisting of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, R172Q and combinations thereof.Amylases are preferably used which have an amino acid substitution at two, preferably three, of the aforementioned positions, in particular a substitution at position 202 selected from M202L, M202V, M202S, M202T, M202I, M202Q, M202W, a substitution at position 255, in particular S255N, and a substitution at position 172, in particular R172Q. The M202L and M202T mutants are particularly preferred.

[0196] In various embodiments of the invention, the amylase comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:14 over its entire length by at least 60% and increasingly preferably by at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical and optionally at least one amino acid substitution at one of the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 320, 323, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and / or a deletion at one of the positions 183 and 184 in the numbering according to SEQ ID NO:14, preferably at least one amino acid substitution at aof positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, particularly preferably selected from the group consisting of R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof. In various preferred embodiments, the amylase has, in the numbering according to SEQ ID NO:14, amino acid substitutions at three or more of the positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345 and optionally one or more, preferably all, of the substitutions and / or deletions at positions: 118, 183, 184, 195, 320 and 458, particularly preferably R118K, D183*, G184*, N195F, R320K and / or R458K. In particularly preferred embodiments, the amylase has, in the numbering according to SEQ ID NO:14, the following amino acid substitutions and / or deletions: M9L-M323T; M9L-M202L / T / V / I-M323T; M9L-N195F-M202L / T / V / I-M323T; M9L-R118K-D183*-G184*-R320K-M323T-R458K; M9L-R118K-D183*- G184*-M202L / T / V / l-R320K-M323T-R458K; M9L-G149A-G182T-G186A-M202L-T257I-Y295F-N299Y-M323T-A339S-E345R; M9L-G149A-G182T-G186A-M202I-T257I-Y295F-N299Y-M323T-A339S-E345R; M9L-R118K-G149A-G182T-D183*-G184*-G186A-M202L-T257I-Y295F-N299Y-R320K- M323T-A339S-E345R-R458K; M9L-R118K-G149A-G182T-D183*-G184*-G186A-N195F-M202L- T257I-Y295F-N299Y-R320K-M323T-A339S-E345R-R458K; M9L-R118K-G149A-G182T-D183*- G184*-G186A-M202I-T257I-Y295F-N299Y-R320K-M323T-A339S-E345R-R458K; M9L-R118K-D183*- D184*-N195F-M202L-R320K-M323T-R458K; M9L-R118K-D183*-D184*-N195F-M202T-R320K- M323T-R458K; M9L-R118K-D183*-D184*-N195F-M202I-R320K-M323T-R458K; M9L-R118K-D183*- D184*-N195F-M202V-R320K-M323T-R458K; M9L-R118K-N150H-D183*-D184*-N195F-M202L- V214T-R320K-M323T-R458K; or M9L-R118K-D183*-D184*-N195F-M202L-V214T-R320K-M323T- E345N-R458K.

[0197] In various embodiments of the invention, the amylase comprises an amino acid sequence which is at least 65%, and increasingly preferably at least 66%, 67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:15 over its entire length and optionally at least one substitution and / or deletion at one of the positions 93, 116, 118, 129, 133, 134, 140, 142, 146, 147, 149, 151, 152, 169, 174, 183, 184, 186, 189, 193, 195, 197, 198, 200, 203, 206, 210, 212, 213, 235, 243, 244, 260, 262, 284, 303, 304, 320, 338, 347, 359, 418, 431, 434, 439, 447, 458, 469, 476 and 477 in the count according to SEQ ID NO:15.Preferred amino acid substitutions in this regard include: E260A / D / C / Q / L / M / F / P / S / W / V / G / H / I / K / N / R / T / Y, G304R / K / E / Q, W140Y / F, W189E / G / T, D134E, F262G / P, W284D / H / F / Y / R, W347H / F / Y, W439R / G, G476E / Q / R / K, G477E / Q / K / M / R, N195F / Y, N197F / L, Y198N, Y200F, Y203F, I206H / L / N / F / Y, H210Y, E212V / G, V213A, M116T, Q129L, G133E, E134Y, K142R, P146S, G147E, G149R, N151R, Y152H, Q169E, N174R, A186R, Y243F, S244Q, G303V, R320N, R359I, N418D and A447V.

[0198] In various embodiments of the invention, the amylase comprises an amino acid sequence which is at least 89% and increasingly preferably at least 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% or 99% identical to the sequence given in SEQ ID NO:16 over its entire length and has a deletion in one or more of positions 180, 181, 182, 183 and 184 in the numbering according to SEQ ID NO:16. Particularly preferred is a deletion of two positions selected from 180+181, 181+182, 182+183, and 183+184. Very particularly preferred are deletions at positions 183+184 in the numbering according to SEQ ID NO:16, particularly preferably the deletions H183*+G184*. Preferably, such an α-amylase further comprises an amino acid substitution at one or more of positions 405, 421, 422, and 428 in the numbering according to SEQ ID NO:16.Particularly preferred are one or more of the substitutions I405L, A421H, A422P, and A428T. In a particularly preferred embodiment, the α-amylase has the deletions H183*+G184* in the numbering according to SEQ ID NO:16 and additionally the substitutions I405L, A421H, A422P, and A428T.

[0199] The term "cellulase," as used herein, refers to an enzyme that catalyzes the hydrolysis of 1,4-ß-D-glucoside bonds in cellulose (cellobiose), and / or lichenin and / or ß-D-glucans. They are often also capable of hydrolyzing the 1,4-bonds in ß-D-glucans, which possess 1,3-bonds in addition to the 1,4-bonds. Cellulases are capable of cleaving cellulose to ß-glucose. Consequently, cellulases act in particular on cellulose-containing or cellulose-derivative-containing residues and catalyze their hydrolysis. In a preferred embodiment of the invention, the cellulase is an endoglucanase (EC 3.2.1.4). Synonymous names can be used for cellulases, in particular endoglucanase, endo-1,4-ß-glucanase, carboxymethylcellulase, endo-1,4-ß-D-glucanase, ß-1,4-glucanase, ß-1,4-endoglucanhydrolase, celludextrinase or avicelase.The decisive factor as to whether an enzyme is a cellulase within the scope of the invention is its ability to hydrolyze 1,4-ß-D-glucoside bonds in cellulose.

[0200] The term "cellulase activity" is defined here as an enzyme that catalyzes the hydrolysis of 1,4-ß-D-glucoside bonds in ß-1,4-glucan (cellulose). Cellulose activity is measured using a standard method, e.g., as follows: Cellulases release glucose from CMC (carboxymethylcellulose). Samples are incubated with a substrate (1.25% CMC) under defined reaction conditions (100 mM sodium phosphate buffer pH 7.5, 40°C, 15 min). Reaction with p-hydroxybenzoic acid hydrazide (PAHBAH) in the presence of bismuth produces a yellow dye that can be determined photometrically at 410 nm. An alkaline pH value is required during the color reaction. The amount of sugar released corresponding to the color is a measure of enzyme activity (Lever, Anal. Biochem., 1972, 47 & 1977, 81).

[0201] Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are also included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum, disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, and WO 89 / 09259. Particularly suitable cellulases are alkaline or neutral cellulases with color-care properties. Examples of such cellulases are cellulases described in EP 0495257, EP 0531372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940. Other examples are cellulase variants as described in WO 94 / 07998, EP 0531315, EP 3212777, EP 3502243, EP 3653705, EP 3653706, US 5457046, US 5686593, US 5763254, WO 95 / 24471, WO 98 / 12307, WO 99 / 01544, and WO 2019 / 122520.

[0202] Examples of cellulases with endo-1,4-glucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, e.g., those with a sequence of at least 97% identity to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091. Another example may comprise a GH44 xyloglucanase, e.g., a xyloglucanase enzyme with a sequence of at least 60% identity to positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903.

[0203] Other examples of cellulases include the GH45 cellulases described in WO 96 / 29397 and in particular variants thereof with substitution, insertion and / or deletion at one or more of the positions corresponding to the following positions in SEQ ID NO:8 of WO 2002 / 099091: 2, 4, 7, 8, 10, 13, 15, 19, 20, 21, 25, 26, 29, 32, 33, 34, 35, 37, 40, 42, 42a, 43, 44, 48, 53, 54, 55, 58, 59, 63, 64, 65, 66, 67, 70, 72, 76, 79, 80, 82, 84, 86, 88, 90, 91, 93, 95, 95d, 95h, 95j, 97, 100, 101, 102, 103, 113, 114, 117, 119, 121, 133, 136, 137, 138, 139, 140a, 141, 143a, 145, 146, 147, 150e, 150j, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160c, 160e, 160k, 161 , 162, 164, 165, 168, 170, 171, 172, 173, 175, 176, 178, 181, 183, 184, 185, 186, 188, 191, 192, 195, 196, 200, and / or 20, preferably selected from P19A, G20K, Q44K, N48E, Q119H or Q146R. 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).

[0204] Other enzymes that can be used include lipases or cutinases, particularly because of their triglyceride-cleaving activities, but also to produce peracids in situ from suitable precursors.

[0205] Suitable lipases and cutinases are those of bacterial or fungal origin. Chemically modified or mutated enzymes produced by protein engineering are included. Examples are lipase from Thermomyces, e.g. from T. lanuginosus (formerly called Humicola lanuginosa), as described in EP 0258068 and EP 0305216, cutinase from Humicola, e.g. H. insolens (WO 96 / 13580), lipase from strains of Pseudomonas (some of which are now renamed Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP 0218272), P. cepacia (EP 0331376), P. sp. Strain SD705 (WO 95 / 06720 & WO 96 / 27002), P. wisconsinensis (WO 96 / 12012), Streptomyces lipases of the GDSL type (WO 2010 / 065455), cutinase from Magnaporthe grisea (WO 2010 / 107560), cutinase from Pseudomonas mendocina (US 5389536), lipase from Thermobifida fusca (WO 2011 / 084412), lipase from Geobacillus stearothermophilus (WO 2011 / 084417), lipase from Bacillus subtilis (WO 2011 / 084599), and lipase from Streptomyces griseus (WO 2011 / 150157) and S.pristinaespiralis (WO 2012 / 137147).

[0206] Preferred lipases include, for example, those originally obtained from Humicola lanuginosa (Thermomyces lanuginosus) or those developed from it, particularly those with one or more of the following amino acid substitutions starting from the aforementioned lipase at positions D96L, T213R, and / or N233R, particularly preferably T213R and N233R. Lipases are marketed, for example, by Novozymes under the trade names Lipolase®, Lipolase® Ultra, LipoPrime®, Lipozyme®, and Lipex®. Another advantageously usable lipase is available from Novozymes under the trade name Lipoclean®.

[0207] Cutinases originally isolated from Fusarium solani pisi and Humicola insolens can also be used. Equally useful lipases are available from the Amano company under the names Lipase CE®, Lipase P®, Lipase B® or Lipase CES®, Lipase AKG®, Bacillus sp. Lipase®, Lipase AP®, Lipase M-AP®, and Lipase AML®. Lipases and cutinases from the Danisco / DuPont company, for example, are available whose starting enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Other important commercial products include the preparations M1 Lipase® and Lipomax® marketed by Danisco / DuPont and the enzymes marketed by Meito Sangyo KK under the names Lipase MY-30®, Lipase OF® and Lipase PL®, as well as the product Lumafast® from Danisco / DuPont.

[0208] Further examples are lipases, also referred to as acyltransferases or perhydrolases, e.g., acyltransferases with homology to Candida antarctica lipase A (WO 2010 / 111143), acyltransferase from Mycobacterium smegmatis (WO 2005 / 056782), perhydrolases from the CE 7 family (WO 2009 / 067279) and variants of M. smegmatis perhydrolase, in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 2010 / 100028). Further examples are lipase variants as described in EP 0407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO 97 / 07202, WO 2000 / 034450, WO 2000 / 060063, WO 2001 / 092502, WO 2007 / 087508 and WO 2009 / 109500.

[0209] Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0210] To increase the bleaching effect, oxidoreductases, e.g., oxidases, oxygenases, catalases, peroxidases such as halo-, chloro-, bromo-, lignin-, glucose-, or manganese peroxidases, dioxygenases, or laccases (phenol oxidases, polyphenol oxidases) can be used according to the invention. Advantageously, organic compounds, particularly aromatic ones, that interact with the enzymes are also added to enhance the activity of the respective oxidoreductases (enhancers) or to ensure electron flow in the event of significantly different redox potentials between the oxidizing enzymes and the soils (mediators).

[0211] In the cleaning agents described herein, the enzymes to be used can also be formulated together with accompanying substances, such as those from fermentation. In liquid formulations, the enzymes are preferably used as liquid enzyme formulation(s).

[0212] The enzymes are generally not provided in the form of pure protein, but rather in the form of stabilized, storable, and transportable preparations. These prefabricated preparations include, for example, solid preparations obtained by granulation, extrusion, or lyophilization or, particularly in the case of liquid or gel-like products, solutions of the enzymes, preferably as concentrated as possible, with little water content, and / or containing stabilizers or other additives.

[0213] Alternatively, the enzymes can be encapsulated for both solid and liquid dosage forms, for example by spray-drying or extrusion of the enzyme solution together with a preferably natural polymer, or in the form of capsules, for example those in which the enzymes are enclosed as if 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. Additional active ingredients, such as stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be applied in superimposed layers. Such capsules are applied using methods known per se, for example by shake or roll granulation or in fluid-bed processes. Such granules, for example by applying polymeric film formers, are advantageously low in dust and, due to the coating, are stable during storage.

[0214] Furthermore, it is possible to package two or more enzymes together so that a single granule exhibits multiple enzyme activities. The enzymes can also be incorporated into water-soluble films, such as those used, for example, in the packaging of unit-dose detergents and cleaning agents. Such a film allows the enzymes to be released 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).

[0215] The invention further relates to a method for cleaning textiles or hard surfaces, characterized in that an agent according to the invention is used in at least one method step. In various embodiments, the method described above is characterized in that the protease is used at a temperature of 0°C to 100°C, preferably 20°C to 60°C, more preferably 20°C to 40°C, and most preferably at 30°C.

[0216] This includes both manual and mechanical processes, with mechanical processes being preferred due to their more precise controllability, for example, regarding the quantities used and contact times. Processes for cleaning textiles are generally characterized by the application of various cleaning agents to the items to be cleaned in several steps and their subsequent washing off after the contact time, or by the cleaning items being treated in some other way with a detergent or a solution or dilution of this agent.

[0217] All facts, objects, and embodiments described for the protease according to the invention and agents containing it are also applicable to this subject matter of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above-mentioned methods according to the invention.

[0218] A further subject of the invention is the use of a peptide (peptidic inhibitor) for improving the stability, in particular the storage stability, of proteases in a washing and cleaning agent, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably from SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 8 or SEQ ID NO: 11, over the entire length thereof to at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.

[0219] A further subject of the invention is the use of a peptide (peptidic inhibitor) for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably from SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 8 or SEQ ID NO: 11, over the entire length thereof to at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.

[0220] All facts, objects, and embodiments described for the protease according to the invention and agents containing it are also applicable to this subject matter of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above-mentioned use according to the invention.

[0221] PREFERRED EMBODIMENTS

[0222] 1. Washing and cleaning agent, in particular liquid washing and cleaning agent, particularly preferably liquid textile washing agent, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0223] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.

[0224] 2. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, b) at least one peptide having an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12 group, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% is identical, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds.

[0225] 3. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0226] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical, wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, most preferably from about 8 to about 9.

[0227] 4. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0228] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent is present in 1 wt.-% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0229] 5. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;(ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide having an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 8 or SEQ ID NO: 11, over the entire length thereof to at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.;

[0230] 6. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S21 1 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;(ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide having an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 8 or SEQ ID NO: 11, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds.;

[0231] 7. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S21 1 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271 E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271 E; (ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide having an amino acid sequence,which is selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9. 8. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO:1,comprises: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A- N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A- N252T-Q271 E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E; (ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide having an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 8 or SEQ ID NO: 11,wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent in a 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0232] 9. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0233] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide.

[0234] 10. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0235] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide,wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds.

[0236] 11. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, b) at least one peptide having an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12 group, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% are identical, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9,when the protease is stored together with the peptide, the agent in a 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0237] 12. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0238] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide which has an amino acid sequence which belongs to an amino acid sequence which belongs to the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide,wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent in a 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0239] 13. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0240] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20.

[0241] 14. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, b) at least one peptide inhibitor having an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds.

[0242] 15. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0243] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20, wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0244] 16. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 189T, 211N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0245] 17. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;(ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide inhibitor having an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20;

[0246] 18. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;(ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds. 19. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E;(iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E; (ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20, wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9;

[0247] 20. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile detergent, comprising a) at least one protease which has proteolytic activity and has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271 E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271 E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K- S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E;(ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271 E, and b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.;

[0248] 21. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0249] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide.

[0250] 22. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0251] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds. 23. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile detergents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence,which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical to the amino acid sequence given in SEQ ID NO:1, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D,

[0252] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide, wherein the agent is in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0253] 24. Washing and cleaning agents, in particular liquid washing and cleaning agents, particularly preferably liquid textile washing agents, comprising a) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D,

[0254] 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211 N and 224A, b) at least one peptide inhibitor which has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the protease after storage (as described in Example 2) has a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent is in 1 wt.-% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0255] 25. Washing and cleaning agent according to one of points 1 to 24, wherein the washing and cleaning agent comprises at least one further enzyme, wherein the enzyme is selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, ß-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipases, proteases and combinations thereof, preferably at least one amylase and / or at least one cellulase.

[0256] 26. Washing and cleaning agents according to item 25, wherein the at least one further enzyme is an amylase, wherein the amylase has amylolytic activity and is selected from a) an α-amylase which comprises an amino acid sequence which is 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% or 99% identical to the amino acid sequence given in SEQ ID NO:13 over its entire length and optionally has at least one amino acid substitution at one of the positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:13, preferably selected from the group consisting of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, R172Q and combinations thereof; and / or b) an a-amylase comprising an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:14 over its entire length to at least 60% and increasingly preferably to at least 61%, 62%, 63%, 64%, 65%, 66%,67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% is identical and optionally at least one amino acid substitution at one of the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231 , 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311 , 314, 315, 318, 319, 320, 323, 339, 345, 361 , 378, 383, 419, 421 , 437, 441 , 444, 445, 446, 447, 450, 458, 461 , 471 , 482 and 484 and / or a deletion at one of the positions 183 and 184 in the numbering according to SEQ ID NO:14, preferably at least one amino acid substitution at one of the positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, and / or particularly preferably at least one amino acid substitution or deletion which is selected from the group consisting of R118K, D183*, G184*, N195F, R320K,R458K and combinations thereof; and / or c) an α-amylase which comprises an amino acid sequence which is at least 65%, and increasingly preferably at least 66%, 67%, 68%, 69%, 79%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:15 over its entire length and optionally at least one substitution and / or deletion at one of the positions 93, 116, 118, 129, 133, 134, 140, 142, 146, 147, 149, 151, 152, 169, 174, 183, 184, 186, 189, 193, 195, 197, 198, 200, 203, 206, 210, 212, 213, 235, 243, 244, 260, 262, 284, 303, 304, 320, 338, 347, 359, 418, 431, 434, 439, 447, 458, 469, 476 and 477 in the numbering according to SEQ ID NO:15, preferably amino acid deletions at positions 183 and 184; and / or d) an a-amylase comprising an amino acid sequence,which is at least 89% and increasingly preferably at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:16 over its entire length and has at least one deletion at one of the positions 180, 181, 182, 183 and 184 in the numbering according to SEQ ID NO:16, preferably deletions at at least two positions selected from the positions 180+181, 181+182, 182+183 and 183+184 in the numbering according to SEQ ID NO:16, particularly preferably at the positions 183+184 in the numbering according to SEQ ID NO:16, and / or at least one substitution at one of the positions 405, 421, 422 and 428 in the enumeration according to SEQ ID NO:16, which is selected from the group consisting of I405L, A421H, A422P, A428T and combinations thereof.,

[0257] 27. Use of a peptide for improving the stability, in particular the storage stability, of proteases in a washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% is identical, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds,and wherein the washing and cleaning agent in a 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9, preferably in a temperature range from about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably at about 30°C.

[0258] 28. Use of a peptide for improving the stability, in particular the storage stability, of proteases in a washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% are identical, and wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, preferably in a temperature range of about 20°C to about 60°C,particularly preferably from about 20°C to about 40°C, most preferably at about 30°C.,

[0259] 29. Use of a peptide for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11 and SEQ ID NO: 12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% are identical, and wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds,wherein the washing and cleaning agent in a 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.

[0260] 30. Use of a peptide for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide has an amino acid sequence which corresponds to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the entire length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% are identical, and wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds,and wherein the washing and cleaning agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9, preferably in a temperature range from about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably at about 30°C. 31. Use of a peptide inhibitor for improving the stability, in particular the storage stability, of proteases in a washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95,5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide inhibitor has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, more preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds,is preferably free of boron-containing compounds, and wherein the washing and cleaning agent in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9, preferably in a temperature range from about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably at about 30°C.

[0261] 32. Use of a peptide for improving the stability, in particular the storage stability, of proteases in a washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide inhibitor has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, and wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, preferably in a temperature range of about 20°C to about 60°C, especially preferably from about 20°C to about 40°C, most preferably at about 30°C.,

[0262] 33. Use of a peptide for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide inhibitor has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, wherein the washing and cleaning agent is in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9.,

[0263] 34. Use of a peptide for preventing and / or reducing the autoproteolysis of a protease contained in the washing and cleaning agent, wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224,at least one further amino acid substitution selected from the group consisting of 6W / F, 89A / G, 131H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211N / Q and 224A / G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, wherein the peptide inhibitor has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the washing and cleaning agent is in 1 wt.% solution in deionized water at 20°C has a pH in a range from about 6 to about 11, in particular from about 6.5 to about 10.5, more preferably from about 7 to about 10, particularly preferably from about 8 to about 9, preferably in a temperature range from about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C,most preferably at about 30°C.,

[0264] 35. Use according to any one of items 27 to 34, wherein the peptide leads to an increased residual activity of the protease by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9 (as described in Example 2).

[0265] EXAMPLES

[0266] Example 1: Determination of the activity of proteases in the presence of peptide inhibitors

[0267] The activity of a protease according to the invention in the presence of peptide inhibitors (PI) was determined in a commercially available detergent matrix (Table 1) using a common protease activity assay.

[0268] Table 1 : Detergent matrices used:

[0269] Table 2: Peptide inhibitors

[0270] The activity of the protease is determined by the release of the chromophore para-nitroaniline from the substrate succinyl alanine-alanine-proline-phenylalanine-para-nitroanilide (AAPF-pNA; Bachem L-1400). The release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of enzymatic activity.

[0271] The measurement was carried out at a temperature of 25°C, at pH 8.6 and a wavelength of 410 nm. The measurement time was 15 h with a measurement interval of 3 minutes.

[0272] Measurement approach:

[0273] 10 pl inhibitor (final concentration: 0.2 pg)

[0274] 10 pL AAPF solution (final concentration: 1.25 pg)

[0275] 10 pL diluted protease solution (final concentration: 0.014 U)

[0276] 170 pL Tris / HCl (0.1 M; pH 8.6)

[0277] Protease used:

[0278] SEQ ID NO:1 -P9T-N130D-Q271 E-N144K-N252T-Y217M-T133A-S224A-S189T-S89A

[0279] The activity of the protease without inhibitor, determined as described above, was normalized to 100% and the activity of the protease in the presence of the peptide inhibitors was determined in relation to this.

[0280] Table 3: Results of the activity measurement (determination of the initial inhibitory performance of the peptide inhibitors) Example 2: Determination of the storage stability of a protease according to the invention:

[0281] The residual activity (ie activity after storage) of a protease according to the invention in the presence of peptide inhibitors (PI) was determined in a commercially available detergent matrix (Table 1) using a common protease activity assay.

[0282] The protease variant was stored in the detergent matrix according to Table 1 at 30°C for 4 weeks and at 40°C for 1 week. The residual activity of the protease after storage was determined using the AAPF-pNA method.

[0283] The measurement was carried out at a temperature of 25°C, at pH 8.6 and a wavelength of 410 nm. The measurement time was 5 minutes with a measurement interval of 20 to 60 seconds.

[0284] Measurement approach:

[0285] 10 pL AAPF solution (70 mg / mL)

[0286] 1000 pL Tris / HCl (0.1 M; pH 8.6 with 0.1% Brij 35)

[0287] 10 pL diluted protease solution from detergent matrix

[0288] Kinetics generated over 5 min at 25°C (410 nm)

[0289] The protease activity before storage (t = 0) determined as described above was normalized to 100% and the protease activity after storage was determined in relation to this.

[0290] Table 4: Results of residual activity:

Claims

PATENT CLAIMS 1. Washing and cleaning agents, in particular liquid washing and cleaning agents, especially preferably liquid textile detergents, comprising a) at least one protease, preferably in an amount of 0.0001 to 1 wt.%, based on the total weight of the washing and cleaning agent, b) at least one peptide, preferably in a 0.5-, 1.0-, 1.5-, 2.0-, 2.5-, 3.0-, 3.5-, 4.0-, 4.5-, 5.0-, 10-, 15-, 18-, 20-, 25-, 27- or 30-fold molar excess based on the molarity of the protease used, preferably in a 15-, 18-, 20-, 25- or 27-fold molar excess, wherein the peptide preferably has a length of 50 to 200, more preferably 55 to 190, more preferably 60 to 180, amino acid residues, and c) at least one washing and cleaning agent ingredient, preferably in an amount of 0.01 to 99.9 wt.%, based on the total weight of the washing and cleaning agent.

2. Washing and cleaning agent according to claim 1, wherein the protease, after storage (as described in example 2), exhibits a residual activity increased by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9, when the protease is stored together with the peptide.

3. Washing and cleaning agent according to claim 1, wherein the peptide has an initial inhibitory power of at least 2.5 to 50, preferably 5 to 40, preferably 10 to 30, more preferably 12.5 to 20.

4. Washing and cleaning agent according to any of the preceding claims, wherein the peptide has an amino acid sequence that is identical over its total length to at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NQ:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:

11.

5. Washing and cleaning agent according to any one of the preceding claims, wherein the protease has proteolytic activity and comprises an amino acid sequence that corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total length to at least 70% and increasingly preferably to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5% and 98% identical, and in each case, with reference to the numbering according to SEQ ID NO:1, (i) at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D / V, 133A, 144K, 217M, 252T and 271E, and (ii) at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further Amino acid substitutions selected from the group consisting of 6W / F, 89A / G, 131 H / Y / F, 166M / L / I, 187D, 189T / L / I / R, 211 N / Q and 224A / G, preferably 6W, 89A, 131 H, 166M, 187D, 189R, 189T, 211N and 224A.

6. Washing and cleaning agent according to any of the preceding claims, wherein the protease has one of the following amino acid substitution variants, each with reference to the numbering according to SEQ ID NO:1: (i) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-N252T-Q271E; (ii) P9T-N130D-T133A-N144K-G166M-S189T-Y217M-S224A-N252T-Q271E; (iii) P9T-S89A-N130D-G131 H-T133A-N144K-S189T-Y217M-S224A-N252T-Q271 E; (iv) Y6W-P9T-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (v) P9T-N130D-T133A-N144K-G166M-S211 N-Y217M-N252T-Q271 E; (vi) P9T-S89A-N130D-T133A-N144K-S189T-Y217M-S224A-N252T-Q271E; (vii) P9T-S89A-N130D-T133A-N144K-N187D-Y217M-S224A-N252T-Q271E; (viii) P9T-S89A-N130D-T133A-N144K-S189R-Y217M-S224A-N252T-Q271E; (ix) P9T-S89A-N130D-T133A-N144K-N187D-S189R-Y217M-S224A-N252T-Q271E.

7. Washing and cleaning agent according to any of the preceding claims, wherein the washing and cleaning agent comprises at least one further enzyme, wherein the enzyme is selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipases, proteases and combinations thereof, preferably at least one amylase and / or at least one cellulase and / or at least one lipase and / or at least one mannanase.

8. Washing and cleaning agents according to any of the preceding claims, wherein the washing and cleaning agent ingredient is selected from the group consisting of 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 further auxiliary substances such as optical brighteners, graying inhibitors, color transfer inhibitors, foam regulators, as well as dyes and perfumes and combinations thereof.

9. Washing and cleaning agent according to one of the preceding claims, wherein the washing and cleaning agent is substantially free of boron-containing compounds, preferably free of boron-containing compounds.

10. Washing and cleaning agent according to any of the preceding claims, wherein in a 1 wt% solution in deionized water at 20°C it has a pH value in the range of about 6 to approximately 11, in particular from approximately 6.5 to approximately 10.5, more preferably from approximately 7 to approximately 10, and most preferably from approximately 8 to approximately 9.

11. Method for cleaning textiles and / or hard surfaces, characterized in that in at least one process step a washing or cleaning agent according to one of claims 1 to 9 is used, wherein the process is preferably carried out in a temperature range of about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably from about 30°C.

12. Use of a washing or cleaning agent according to any one of claims 1 to 10 for cleaning textiles and / or hard surfaces, preferably in a temperature range of about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably from about 30°C.

13. Use of a peptide to improve the stability, in particular the storage stability, of proteases in a washing and cleaning agent, preferably in a washing or cleaning agent according to any one of claims 1 to 10, wherein the peptide has an amino acid sequence comprising an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the total length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, is 98%, 99% or 100% identical, preferably in a temperature range of about 20°C to about 60°C, particularly preferably from about 20°C to about 40°C, most preferably at about 30°C.

14. Use according to claim 13, wherein the peptide leads to an increase in the residual activity of the protease by a factor of at least 1.1 to 2.5, preferably 1.2 to 2.0, more preferably 1.3 to 1.9 (as described in Example 2).

15. Use of a peptide to prevent and / or reduce the autoproteolysis of a protease contained in a detergent and cleaning agent, wherein the detergent and cleaning agent is preferably a detergent and cleaning agent according to any one of claims 1 to 10, wherein the peptide has an amino acid sequence comprising an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NQ:10, and SEQ ID NO:11 and SEQ ID NO:12, preferably from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:8 or SEQ ID NO:11, over the total length of which at least 90% and increasingly preferably at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical.

16. Use according to any one of claims 11 to 15, wherein the protease is a protease as defined in any one of claims 5 to 6.

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