WO2023232193A1

WO2023232193A1 - Detergents and cleaning agents with an improved enzyme stability

Info

Publication number: WO2023232193A1
Application number: PCT/DE2023/100389
Authority: WO
Inventors: Shohana ISLAM; Christian DEGERING; Susanne Wieland; Ayhan AYDEMIR
Original assignee: Henkel Ag & Co. Kgaa
Priority date: 2022-06-01
Filing date: 2023-05-24
Publication date: 2023-12-07
Also published as: DE102022205591A1

Abstract

The invention relates to detergents and cleaning agents, in particular liquid detergents and cleaning agents, particularly preferably liquid textile detergents, comprising (A) at least one protease, said protease having a proteolytic activity and an amino acid sequence which comprises an amino acid sequence that is at least 70% identical to the amino acid sequence specified in SEQ ID NO:1 over the entire length thereof and has, with respect to the numbering according to SEQ ID NO:1 in each case, (i) the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T, and 271 E at the positions corresponding to the positions 9, 130, 133, 144, 217, 252, and 271 and (ii) at least one additional 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, at at least one position, preferably two positions, more preferably three positions, corresponding to the positions 6, 89, 131, 166, 187, 189, 211, or 224, preferably in a quantity of 0,0001 to 1 wt.%, based on the total weight of the detergent and cleaning agent, (B) at least one compound with the formula (I) or (II), in which R is selected from -COOH, C1-6-alkyl-substituted or unsubstituted C2-6- dicarboxylic acids, C1-6-alkyl-substituted or unsubstituted C2-6-carboxylic acids, and -OOC-NR2 2 in each case, wherein R2 are the same or different and are selected from C1-6-alkyl or H, and salts, esters, or derivatives thereof, preferably in a quantity of 0.1 to 2 wt.%, based on the total weight of the detergent and cleaning agent, (C) optionally at least one additional enzyme, said additional enzyme differing from the at least one protease and being selected from amylase, cellulase, and lipase, preferably cellulase, preferably in a quantity of 0.0001 to 1 wt.%, based on the total weight of the detergent and cleaning agent, and (D) at least one ingredient, preferably in a quantity of 0.01 to 99.9 wt.%, based on the total weight of the detergent and cleaning agent. The invention likewise relates to the corresponding washing and cleaning methods, to the use of the agents described herein, and to the use of an inhibitor according to the invention for improving the stability of a protease and/or optionally additional enzymes in detergents or cleaning agents.

Description

DETERGENT AND CLEANING AGENTS WITH IMPROVED ENZYME STABILITY

The invention lies in the field of enzyme technology. The invention relates to detergents or cleaning agents comprising at least one protease, at least one reversible protease inhibitor and optionally at least one further enzyme. Also part of the invention are the corresponding washing and cleaning processes, the use of the agents described herein and the use of reversible protease inhibitors according to the invention to improve the stability of a protease in washing or cleaning agents.

The use of enzymes in detergents has been established in the state of the art for decades. They serve to expand the range of services of the funds in question according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three mentioned hydrolyze proteins, starch and fats and thus contribute directly to removing dirt. Cellulases are used in particular because of their effect on tissue. Another group of detergent enzymes are oxidative enzymes, in particular oxidases, which, in combination with other components, preferably serve to bleach stains or to generate the bleaching agents in situ. In addition to these enzymes, which are subject to continuous optimization, other enzymes are constantly being made available for use in detergents in order to be able to optimally tackle specific soils, such as pectinases, ß-glucanases, mannanases or other hemicellulases (glycosidases) for the hydrolysis of particular ones plant polymers.

Proteases are among the most technically important enzymes. For detergents and cleaning agents, they are the longest established enzymes and are contained in practically all modern, high-performance detergents and cleaning agents. In detergents and cleaning agents, proteases are used to break down protein-containing dirt on the items to be cleaned. However, they also hydrolyze themselves (autoproteolysis) and all other proteins contained in the products in question, i.e. in particular other enzymes contained in the detergents and cleaning products. This happens particularly during the cleaning process, i.e. in the aqueous washing or cleaning liquor, when comparatively favorable reaction conditions exist. However, this also happens 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 other enzymes. Due to the loss of enzymatic activity, they no longer show optimal cleaning performance. This is particularly problematic in gel-like or liquid and especially in water-containing recipes, because the water contained in these recipes provides both the reaction medium and the hydrolysis reagent.

In general, only selected proteases are suitable for use in liquid surfactant-containing preparations. Many proteases do not show sufficient catalytic performance in such preparations or they are not sufficiently stable. The use of proteases in cleaning agents therefore requires high catalytic activity and stability Conditions such as those that arise during a washing process are particularly desirable. 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 can be assigned to the subtilases but no longer to the subtilisins in the narrower sense, as well as variants of the proteases mentioned which have an amino acid sequence that is changed compared to the original protease. Proteases are modified in a targeted or random manner using methods known from the prior 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 parts of proteins. Correspondingly optimized variants are known for most of the proteases known from the prior art. In the European patent application EP 2016175 A1, for example, a protease from Bacillus pumilus intended for detergents and cleaning agents is disclosed.

A goal in the development of detergent and cleaning agent formulations is therefore to stabilize the enzymes contained, particularly during storage, and also to protect them from denaturation and/or cleavage or degradation and/or, particularly during storage and/or use of the detergent or cleaning agent To protect against decay caused by physical influences or oxidation etc. One focus of these developments is the protection of the proteins and/or enzymes contained against (auto-)proteolytic cleavage. This can be done by building up 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 route often taken is to add chemical compounds that inhibit the proteases and thus act overall as stabilizers or inhibitors for proteases and the other proteins and enzymes they contain. However, these must be reversible protease inhibitors, since the protease activity should only be prevented temporarily, especially during storage, but no longer during the cleaning process.

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

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 requirement for those containing boric acid Compounds, ie in particular boron-containing protease inhibitors, should be avoided in detergents and cleaning agents.

Surprisingly, it has now been found that certain compounds with the formula (I) or

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, can advantageously stabilize and reversibly inhibit a protease and are therefore particularly suitable for use in detergents or cleaning agents. In particular, it was surprisingly found that a protease from Bacillus pumilus, which comprises an amino acid sequence that is at least 70% identical to the amino acid sequence specified 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 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 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, 187D, 189R, 189T, 211 N and 224A Group is selected, has, by certain compounds with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, can be advantageously stabilized and this combination is therefore particularly suitable for use in detergents or cleaning agents.

The subject of the invention is therefore, in a first aspect, a detergent and cleaning agent, in particular a liquid detergent and cleaning agent, particularly preferably a liquid textile detergent

(A) at least one protease, wherein the protease has proteolytic activity and comprises an amino acid sequence which comprises an amino acid sequence which is at least 70% identical to the amino acid sequence specified 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 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 from that 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, 187D, 189R, 189T, 211 N and 224A, selected from the existing group, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the detergent and cleaning agent,

(B) at least one compound with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, preferably in an amount of 0.1 to 2% by weight, based on the total weight of the detergent and cleaning agent,

(C) optionally at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the detergent and cleaning agent, and

(D) at least one ingredient, preferably in an amount of 0.01 to 99.9% by weight, based on the total weight of the detergent and cleaning agent.

A further subject of the invention is a detergent and cleaning agent, in particular a liquid detergent and cleaning agent, particularly preferably a liquid textile detergent

(A) at least one protease, wherein the protease has proteolytic activity and comprises an amino acid sequence which comprises an amino acid sequence which is at least 70% identical to the amino acid sequence specified 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 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 from that 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, is selected from the existing group, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the detergent and cleaning agent,

(B) at least one compound selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate, preferably in an amount of 0.1 to 2% by weight, based on the total weight of the detergent and cleaning agent,

(C) optionally at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase, preferably in an amount of 0.0001 to 1% by weight, based on the total weight of the detergent and cleaning agent, and (D) at least one ingredient, preferably in an amount of 0.01 to 99.9% by weight, based on the total weight of the detergent and cleaning agent.

Further aspects of the invention relate to methods for producing such a detergent or cleaning agent, methods for cleaning textiles and/or hard surfaces, in particular dishes, using an agent according to the invention.

A further subject of the invention relates to the use of a compound having the formula

(I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to improve the stability, in particular the storage stability, of enzymes, preferably proteases, cellulases and / or amylases, in a protease-containing detergent and cleaning agent , wherein the protease is the protease from Bacillus pumilus as defined herein, preferably in a temperature range from about 20 ° C to about 60 ° C, more preferably from about 20 ° C to about 40 ° C, most preferably at about 30 ° C, and the use of a compound with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease being the protease from Bacillus pumilus as defined herein and the use of a compound with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, by an im Protease contained in detergents and cleaning agents, the protease being the protease from Bacillus pumilus defined herein. Preferably the compound is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate. The detergent according to the invention is preferably a liquid textile detergent. More preferably, the textile detergent according to the invention in 1% by weight 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.

Textile detergents according to the invention also show performance advantages over other textile detergents in particular if the textile detergents contain at least one additional enzyme of the same or a different type, for example amylase, cellulase, lipase, mannanase or pectinase, although the list of other enzymes is not complete. It is therefore preferred that the textile detergents according to the invention contain at least one additional enzyme of the same type (i.e. another protease) or of a different type.

These and other aspects, features and advantages of the invention will become apparent to those skilled in the art from reading the following detailed description and claims. Any feature from one aspect of the invention can be used 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.

Unless otherwise stated, all percentages are percentages by weight (wt.%).

Numerical ranges specified in the format "from x to y" include the stated values. When multiple preferred numerical ranges are specified in this format, it is understood that any ranges resulting from the combination of the various endpoints will also be captured.

“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.

The term "detergent 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 in the description explained.

"About", "approx." or "approximately", as used herein in reference to a numerical value, refers to the corresponding numerical value ±10%, preferably ±5%.

“Substantially free of” 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 particularly preferably less than 0. 1% by weight of the corresponding substance, based on the total weight of the composition/agent.

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

"Variant" as used herein refers to natural or artificially created variations of a native protease that have an amino acid sequence modified from the reference form.

An “improvement in the stability of an enzyme” within the meaning of the invention occurs when the presence of a compound defined herein with the formula (I) or (II) causes a washing or cleaning agent comprising at least one protease defined herein and at least one compound defined herein with the formula (I) or (II) (detergent or cleaning agent according to the invention) after storage has a higher enzymatic activity of the protease and / or possibly other enzymes contained in the detergent or cleaning agent compared to a control preparation which is only differs from the detergent or cleaning agent according to the invention by the absence of the compound defined herein with the formula (I) or (II) (control). After storage, the detergent or cleaning agent according to the invention therefore has a higher residual activity of the protease contained and/or possibly other enzymes contained in it compared to the control, with the detergent or cleaning agent according to the invention and the control having the same initial enzymatic activity at the start of storage, both agents treated in the same way, particularly as regards storage conditions and determination of enzyme activity. Storage is increasingly preferred for at least 1 week, 2 weeks, 3 weeks or 4 weeks. Storage is further preferably carried out at a temperature of 20°C, 25°C, 30°C or 40°C.

The present invention is based on the surprising finding of the inventors that the compounds described herein have the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, bring about improved storage stability of proteases defined herein in detergents and cleaning agents. This is particularly surprising since the verb defined here

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, not yet in connection with a reversible protease inhibition were connected. In particular, they have not yet been associated with the proteases from Bacillus pumilus described herein and improved storage stability and/or reduced autoproteolysis. Furthermore, the compounds described herein have the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, are not associated with reversible inhibition of the Bacillus pumilus protease described herein.

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 that is at least 70% identical to the amino acid sequence specified 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 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 from that 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, existing group is selected, by compounds with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, can advantageously be stabilized or reversibly inhibited in detergents and cleaning agents. This is particularly surprising since none of these compounds defined herein have the formula (I) or (

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, have so far been associated with improved stability or reversible inhibition of such a Bacillus pumilus protease in detergents or cleaning agents. Furthermore, such compounds defined herein have the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, so far not with improved stability further in the washing or

Enzymes contained in cleaning agents are associated when they are present in the detergent or cleaning agent together with the Bacillus pumilus protease mentioned.

The present invention is further 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 specified 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 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, 21 1 or 224, at least one further amino acid substitution from that 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, by a compound selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate is selected, can be advantageously stabilized in detergents and cleaning agents. This is particularly surprising since none of these compounds have previously been associated with improved stability of such a Bacillus pumilus protease in detergents or cleaning agents. Furthermore, such compounds have not yet been associated with improved stability of other enzymes contained in the detergent or cleaning agent when they are present in the detergent or cleaning agent together with the Bacillus pumilus protease mentioned.

According to the invention, compounds with the formula (I) or (II)

(II), where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, used as reversible protease inhibitors. Preferably the compound is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate. The agents according to the invention may comprise one or more reversible protease inhibitor(s).

The agents according to the invention can contain the reversible protease inhibitor(s) in a concentration of 0.1 to 2% by weight, preferably 0.3 to 1.5% by weight. If several inhibitors are included, this information refers to the total concentration.

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 specified in SEQ ID NO:1 over its total 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% is identical, and each based on the numbering according to SEQ ID NO:1 (i). 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 preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution 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, existing group is selected , having.

In further preferred embodiments, the protease used according to the invention has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and points, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271, which correspond to amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271 E 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.

In further preferred embodiments, the protease used according to the invention has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and points, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271 corresponding to 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 correspond to at least two amino acid substitutions are selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A.

In further preferred embodiments, the protease used according to the invention has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and points, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271 corresponding to 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, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A.

In further preferred embodiments, the protease used according to the invention has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and points, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224 , the amino acid substitutions S89A, N187D, S189R and S224A.

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

(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-Q271 E, whereby the numbering is based on the numbering according to SEQ ID NO:1.

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 specified in SEQ ID NO:1 over its total 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% is 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 a further amino acid substitution 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, existing group is selected,

(B) at least one compound with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, and

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase.

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 specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T, S211N and S224A,

(B) at least one compound with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, and (C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase.

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least two amino acid substitutions selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A,

(B) at least one compound with the formula (I) or (II)

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E 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 Y6W, S89A, G131H, S166M, N187D, S189R, S189T,

S211 N and S224A existing group are selected,

(B) at least one compound with the formula (I) or (II)

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at the positions corresponding to positions 89, 187, 189 and 224, the amino acid substitutions S89A , N187D, S189R and S224A,

(B) at least one compound with the formula (I) or (II)

(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-Q271E; P9T-S89A-N130D-G131 H-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, whereby the numbering is based on the numbering according to SEQ ID NO:1,

(B) at least one compound with the formula (I) or (II)

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 specified in SEQ ID NO:1 over its total 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% are identical, and each 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 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, is selected from the existing group,

(B) a compound selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E 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 is selected, has,

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224 correspond to at least two amino acid substitutions consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,

S211 N and S224A existing group are selected,

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A, (B) a compound selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate, and

(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-Q271E; P9T-S89A-N130D-G131 H-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, whereby the numbering is based on the numbering according to SEQ ID NO:1,

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% are identical, and each 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 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, is selected from the existing group,

(B) benzoic acid, and

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 specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least one of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least one amino acid substitution selected from the group consisting of YQ\N, S89A, G131H, S166M, N187D, S189R, S189T, S211N and S224A,

(B) benzoic acid, and

S211 N and S224A existing group are selected,

(B) benzoic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224 correspond, at least three Has amino acid substitutions selected from the group consisting of YQ\I\I, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A,

(B) benzoic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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 is, and each 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 271 E, 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 from the 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, existing group is selected,

(B) phenylmalonic acid, and

S211 N and S224A existing group are selected,

(B) phenylmalonic acid, and (C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase.

S211 N and S224A existing group are selected,

(B) phenylmalonic acid, and

(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-Q271E; P9T-S89A-N130D-G131 H-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, whereby the numbering is based on the numbering according to SEQ ID NO:1,

(B) phenylmalonic acid, and

(B) benzylmalonic acid, and

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase. In further preferred embodiments, the agent according to the invention comprises

(B) benzylmalonic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A,

(B) benzylmalonic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224, which have amino acid substitutions S89A, N187D, S189R and S224A,

(B) benzylmalonic acid, and

(B) phenylsuccinic acid, and

(A) a protease that has proteolytic activity and comprises an amino acid sequence that corresponds to the amino acid sequence specified in SEQ ID NO:1 over its entire length 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% is identical, and each based on the numbering according to SEQ ID NO:1, (i) at positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271 E 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 YQ\N, S89A, G131H, S166M, N187D, S189R, S189T , S211 N and S224A existing group is selected,

(B) phenylsuccinic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A, (B) phenylsuccinic acid, and

(B) phenylsuccinic acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each based on the numbering according to SEQ ID NO:1 (i) at the positions that represent the Positions 9, 130, 133, 144, 217, 252 and 271 correspond to 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 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, is selected from the existing group,

(B) benzyl succinic acid, and

S211 N and S224A existing group are selected,

(B) benzyl succinic acid, and (C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase.

(B) benzyl succinic acid, and

(B) Methyl 3-benzoylpropionate, and

S211 N and S224A existing group are selected,

(B) Methyl 3-benzoylpropionate, and

S211 N and S224A existing group are selected,

(B) Methyl 3-benzoylpropionate, and

(B) (S)-3-phenylbutyric acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least two of the positions corresponding to positions 6, 89, 131, 166, 1187, 89, 211 or 224 correspond to at least two amino acid substitutions consisting of Y6W, S89A, G131H, S166M, N187D, S189R, S189T,

S211 N and S224A existing group are selected,

(B) (S)-3-phenylbutyric acid, and

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is identical, and each 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 Q271 E and (ii) at least three of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, has at least three amino acid substitutions selected from the group consisting of Y6W, S89A, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A, (B) (S)-3-phenylbutyric acid, and

(B) (S)-3-phenylbutyric acid, and

(B) benzyl carbamate, and

S211 N and S224A existing group are selected,

(B) benzyl carbamate, and (C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, preferably cellulase.

S211 N and S224A existing group are selected,

(B) benzyl carbamate, and

(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-Q271E; P9T-S89A-N130D-G131 H-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, whereby the numbering is based on the numbering according to SEQ ID NO:1, and

(B) benzyl carbamate, and

In detergents or cleaning agents according to the invention, the detergent or cleaning agent comprises, based on the total weight of the detergent or cleaning agent, the enzyme, i.e. the protease, in an amount of 0.005 to 5% by weight, preferably from 0.05 to 2 % by weight, more preferably from 0.01 to 0.5% by weight and even more preferably from 0.02 to 0.2% by weight, and the reversible inhibitor (i.e. the compound defined herein having the formula ( I) or (II)) in an amount of 0.01 to 15% by weight, preferably from 0.05 to 5% by weight, more preferably from 0.1 to 1% by weight, even more preferably from 0.3 to 1.5% by weight and particularly preferably from 0.2 to 0.75% by weight.

In various embodiments, the enzyme and the reversible inhibitor may be preformulated in an enzyme composition. As can be seen from the previous statements, the enzyme protein only forms a fraction of the total weight of common enzyme preparations. Protease preparations which are preferably used contain between 0.1 and 40% by weight, preferably between 0.2 and 30% by weight, particularly preferably between 0.4 and 20% by weight and in particular between 0.8 and 10% by weight .-% of enzyme protein. In such compositions, the reversible inhibitor may be present in an amount of from 0.05 to 35 wt.%, preferably from 0.05 to 10 wt.%, more preferably from 0.1 to 1 wt.%, even more preferably from 0.3 to 1.5% by weight and particularly preferably from 0.2 to 0.75% by weight, 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 detergents or cleaning agents according to the invention, in amounts which lead to the final concentrations in the detergent or cleaning agent specified herein.

The proteases used according to the invention have enzymatic activity, i.e. they are capable of hydrolyzing peptides and proteins, especially in detergents or cleaning agents. A protease used according to the invention is therefore an enzyme which catalyzes the hydrolysis of amide/peptide bonds in protein/peptide substrates and is therefore able to cleave 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 given also refer to mature (processed) enzymes.

In various embodiments of the invention, the protease is a free enzyme. This means that the protease can act directly with all components of an agent and, if the agent is a liquid agent, that the protease is in direct contact with the agent's solvent (e.g. water). In other embodiments, an agent may be proteases which form an interaction complex with other molecules or which contain a “coating”. Here, a single or several protease molecules can be separated from the other components of the agent by a structure surrounding them. Such a separating structure can arise from, but is not limited to, vesicles such as a micelle or a liposome. The surrounding structure can 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.

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, for example, by fragmentation of the protease , are deleted. In various preferred embodiments, the proteases described herein have the sequence of SEQ ID NO:1, with the exception of the explicitly mentioned substitutions, i.e. apart from the substituted positions, they are 100% identical to the sequence according to SEQ ID NO:1.

The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the BLAST algorithm established and commonly used in the prior art (cf. e.g. Altschul et al. (1990) Basic local alignment search tool, J. Mol. Biol., 215:403-410, and Altschul et al (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25:3389-3402) and is basically done by similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences be assigned. A tabular assignment of the relevant positions is called alignment. Another algorithm available in the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. For example, the Clustal series (see e.g. Chenna et al. (2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 31:3497-3500), T-Coffee (see e.g. Notredame et al. (2000) T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 302:205-217) or programs that are based on these programs or algorithms. Sequence comparisons (alignments) are also possible using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified 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.

Such a comparison also allows a statement to be made about the similarity of the compared sequences to one another. It is usually given in percent identity, i.e. the proportion of identical nucleotides or amino acid residues in the same positions or in positions corresponding to one another in an alignment. The broader concept of homology includes conserved amino acid exchanges in amino acid sequences, i.e. amino acids with similar ones chemical activity, as they usually have similar chemical activities within the protein. Therefore, the similarity of the compared sequences can also be indicated as percent homology or percent similarity. Identity and/or homology statements can be made about entire polypeptides or genes or just about individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences. Such areas often have identical functions. They can be small and contain only a few nucleotides or amino acids. Such small areas often perform essential functions for the overall activity of the protein. It can therefore make sense to relate sequence matches only to individual, possibly small areas. Unless otherwise stated, identity or homology information in the present application refers to the total length of the nucleic acid or amino acid sequence specified in each case.

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 depends on the mature protein. This assignment is particularly applicable 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 positions mentioned 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 these positions in an alignment.

For the description of substitutions that affect exactly one amino acid position (amino acid exchanges), the following convention is used here: first the naturally present amino acid is designated in the form of the internationally used single-letter code, then follows the associated sequence position and finally the inserted amino acid. Multiple or alternative substitutions within the same polypeptide chain are separated by slashes. "130D/V" means that position 130 has mutated to D or V. In insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, for example a star or a dash, or an A is indicated before the corresponding position. For example, P9T describes the substitution of proline at position 9 by threonine, P9TH describes the insertion of histidine after the amino acid threonine at position 9, and P9* or AP9 describes the deletion of proline at position 9. This nomenclature is known to those skilled in the art of enzyme technology.

Advantageous positions for sequence changes, in particular substitutions, of the protease from Bacillus pumilus, which are preferably of importance when transferred to homologous positions of the proteases according to the invention and give the protease advantageous functional properties, are therefore the positions which correspond in an alignment to the positions described herein, ie in the count according to SEQ ID NO:1. The following amino acid residues are located at the positions mentioned 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. 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 the stability during storage and/or use, for example during the washing process, results in the enzymatic activity lasting longer and thus the cleaning performance being improved. In principle, all stabilization options described and/or appropriate in the prior art can be considered. Those stabilizations that are achieved via mutations of the enzyme itself are preferred, since such stabilizations do not require any further work steps after the enzyme has been obtained. Examples of sequence changes suitable for this are mentioned above. Other suitable sequence changes are known from the prior art.

Other stabilization options include:

Changing the binding of metal ions, in particular the calcium binding sites, for example by replacing one or more of the amino acids involved in the calcium binding with one or more negatively charged amino acids and / or by introducing sequence changes in at least one of the sequences both amino acids arginine/glycine;

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

Exchange of amino acids that are close to the N-terminus with those that presumably come into contact with the rest of the molecule via non-covalent interactions and thus contribute to the maintenance of the globular structure.

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

In addition, at least one further inhibitor compound 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), can also be used. and combinations thereof existing group is selected, be included.

In the context of the present invention, “phenylboronic acid derivative” is understood to mean a compound with the formula (III). The compound of formula (III) 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. The radical R in the phenylboronic acid derivative is preferably a C1-6 alkyl group and, among these, is more preferably -CH3, -CH3CH2 or -CH3CH2CH2. More preferably, the radical R in the phenylboronic acid derivative is hydrogen. The phenylboronic acid derivative 4-formylphenylboronic acid (4-FPBA) is particularly preferred.

The further inhibitor compound used can be boric acid. The agent according to the invention is preferably essentially free of other inhibitor compounds. Very particularly preferably, the agent according to the invention comprises, in addition to the compounds according to the invention with the formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, none of the further inhibitor compounds mentioned.

In particularly preferred embodiments, the detergent and cleaning agent according to the invention is essentially free of boron-containing compounds. “Substantially 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 detergents and cleaning agents according to the invention are free of boron-containing compounds, i.e. in particular they do not contain any boric acid and/or phenylboronic acid derivatives.

It is possible for a person skilled in the art to use known DNA and/or amino acid sequences to generate the corresponding nucleic acids, including complete genes, using methods that are generally known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and/or protein chemical methods to produce. Such methods are, for example, from Sambrook, J., Fritsch, E.F. and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition Cold Spring Laboratory Press, known.

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 which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1, i.e. has at least 80% of the reference washing performance , preferably at least 100%, more preferably at least 110% or more.

Washing or cleaning performance is understood to mean the ability of a detergent or cleaning agent to partially or completely remove existing soiling, in particular the whitening performance of one or more soilings on textiles. Examples of such soiling 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 which comprises the protease, or the washing or cleaning liquor formed by this agent, as well as 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. Washing or cleaning liquor is understood to mean the working solution containing the detergent or cleaning agent which acts on the textiles or hard surfaces and thus comes into contact with the dirt present on the textiles or hard surfaces. The washing or cleaning liquor is usually created when the washing or cleaning process begins and the washing or cleaning agent is diluted with water, for example in a washing machine or dishwasher or in another suitable container.

The cleaning performance can be determined in a washing system that contains a detergent in a dosage of between 2.0 and 8.0 grams per liter of washing liquor and the enzyme. The enzymes to be compared are used in the same concentration (based on active protein). The use of the respective enzymes with the same activity ensures that even if there is a discrepancy in the ratio of active substance to total protein (the values of the specific activity), the respective enzymatic properties, i.e. the cleaning performance on certain types of soiling, can be compared. In general, low specific activity can be compensated for by adding a larger amount of protein. Furthermore, the enzymes to be examined can also be used in the same amount or weight if the enzymes to be examined have a different affinity for the test substrate in an activity test. The expression “same amount of substance” in this context refers to the same molar use of the enzymes to be examined. The expression “equal weight” refers to an equal weight use of the enzymes to be examined.

The concentration of the protease in the detergent intended for such a washing system is 0.001 to 0.1% by weight, preferably 0.01 to 0.06% by weight, based on active protein.

A liquid reference detergent for such a washing system can, for example, be composed as follows (all information in percent by weight (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, remainder demineralized water. The dosage of the liquid detergent is preferably between 4.5 and 6.0 grams per liter of washing liquor, for example 4.7, 4.9 or 5.9 grams per liter of washing liquor. Washing is preferred in a pH range between pH 7 and pH 10.5, preferably between pH 8 and pH 9.

The cleaning performance against soiling on cotton is determined by measuring the degree of cleaning of the washed textiles. For example, the washing process can take place for 60 minutes at a temperature of 40°C and the water can have a hardness of between 15.5°dH and 16.5°dH (German hardness).

The degree of whiteness, ie the lightening of the dirt, as a measure of the cleaning performance is determined using optical measuring methods, preferably photometrically. A suitable device for this is, for example, the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably a supplied white standard. Preferred embodiments of 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.

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). In this regard, the active protein concentration can be determined by titrating the active centers using a suitable irreversible inhibitor and determining the residual activity (Bender et al., 1966, J. Am. Chem. Soc. 88, 24:5890-5913).

According to the invention, a detergent or cleaning agent is understood to mean all conceivable types of detergent or cleaning agent, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or for hand washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term detergent is used. This also includes, for example, dishwashing detergents for dishwashers (automatic 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 In addition to manual and machine dishwashing detergents, for example also scouring agents, glass cleaners, toilet fresheners, etc. The detergents and cleaning agents in the context of the invention also include washing aids which are added to the actual detergent when washing textiles manually or by machine in order to achieve a further effect . Furthermore, detergents and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e. those agents with which the item of laundry is brought into contact before the actual laundry, for example to dissolve stubborn dirt, and also those agents that are in one of the actual The step after textile washing gives the laundry other desirable properties such as a pleasant feel, crease resistance or low static charge. The last-mentioned agents include fabric softeners.

The detergents or cleaning agents according to the invention, which can be present as powdery or granular solids, in compressed or post-compacted particle form, as homogeneous solutions or suspensions, can contain, in addition to a protease according to the invention, all known ingredients that are customary in such agents, with preferably at least one further ingredient in the means is available. The agents according to the invention can in particular contain surfactants, builders (builders), polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators or bleach catalysts. They can also contain water-miscible organic solvents, other enzymes, enzyme stabilizers, sequestering agents, electrolytes, pH regulators and/or other auxiliary substances such as optical brighteners, graying inhibitors, color transfer inhibitors, foam regulators as well as dyes and fragrances and combinations thereof. Advantageous ingredients of agents according to the invention are disclosed in the international patent application WO 2009/121725, starting on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. Reference is expressly made to this disclosure and the content of the disclosure therein is incorporated into the present patent application.

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

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

The embodiments of the present invention include all solid, powdery, liquid, gel or pasty dosage forms of agents according to the invention, which may also consist of several phases and may be in compressed or non-compressed form. The agent can 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. The solid dosage forms of the agent also include extrudates, granules, tablets or pouches. Alternatively, the agent can also be liquid, gel 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 assets are generally preferred. Furthermore, the agent can be present as a one-component system. Such means consist of one phase. Alternatively, a means can also consist of several phases. Such a product is therefore divided into several components.

If 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.

The agents according to the invention can contain one or more surfactants, with anionic surfactants, nonionic surfactants and mixtures thereof being particularly suitable, but cationic, zwitterionic and/or amphoteric surfactants can also be included. The agents preferably contain 5 to 70% by weight of surfactant, preferably 5 to 60% by weight and further preferably 5 to 50% by weight of surfactant.

Suitable anionic surfactants are in particular soaps and those which contain sulfate or sulfonate groups with preferably alkali metal ions as cations. Soaps that can be used are preferably the alkali salts of saturated or unsaturated Ci2-18 fatty acids. Such fatty acids can also be used in a form that is not completely neutralized. The useful surfactants of the sulfate type include the salts of the sulfuric acid half-esters of Ci2-18 fatty alcohols and the sulfation products of the nonionic surfactants mentioned with a low degree of ethoxylation. To The sulfonate-type surfactants that can be used include, for example, Cg-u-alkylbenzene sulfonates, alkane sulfonates, which are obtained from Ci2-is alkanes, for example by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization, and Ci2-18-olefin sulfonates, which are obtained from the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkane sulfonates, disulfonates, such as those obtained, for example, from Ci2-is monoolefins with terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acid 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, for example asulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

The agent preferably has 2 to 55% by weight, preferably 3 to 35% by weight, of anionic surfactant. Very particularly preferably, the agent contains 3 to 25% by weight of alkylbenzene sulfonate. In addition, the agent can preferably contain further anionic surfactants, in particular alkyl ether sulfates, as well as nonionic surfactants, in particular fatty alcohol alkoxylates. These can then make up the rest of the surfactants.

Suitable alkylbenzene sulfonates are preferably selected from linear or branched alkylbenzene sulfonates of the formula

in which R' and R" are independently H or alkyl and together contain 6 to 19, preferably 7 to 15 and in particular 9 to 13 carbon atoms. A very particularly preferred representative is sodium dodecyl benzyl sulfonate.

Alk(en)yl sulfates are the alkali and in particular the sodium salts of the sulfuric acid half esters of the Ci2-18 fatty alcohols, e.g. from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the Cw-20 oxo alcohols and those secondary half esters Alcohols of these chain lengths are preferred. Also preferred are alk(en)yl sulfates of the chain length mentioned, which contain a synthetic straight-chain alkyl radical produced on a petrochemical basis and which have a degradation behavior analogous to that of the adequate compounds based on fatty chemical raw materials. For washing technology reasons, the Ci2-16 alkyl sulfates and Ci2-15 alkyl sulfates as well as Cu-is alkyl sulfates are preferred.

Also the sulfuric acid monoesters of the straight-chain or branched Cy-2i alcohols ethoxylated with 1 to 6 moles of ethylene oxide, such as 2-methyl-branched Cg-n alcohols with an average of 3.5 moles of ethylene oxide (EO) or Ci2-18 fatty alcohols with 1 up to 4 EO are suitable.

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

R ¹ -O-(AO) _n -SO ₃ - X ⁺ .

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 with an even number of carbon atoms being preferred. Particularly preferred radicals R ¹ are derived from Ci2-is fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or from Cw-20 oxo alcohols. AO represents an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index n represents an integer from 1 to 50, preferably from 1 to 20 and in particular from 2 to 10. Very particularly preferably n represents the numbers 2, 3, 4, 5, 6, 7 or 8. X ⁺ stands for a monovalent cation or the nth part of an n-valent cation, preference being given to the alkali metal ions and among them Na ⁺ or K ⁺ , with Na ⁺ being extremely preferred. ^Further ^cations ^_ ^_ ^_

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

with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are Na-Ci2-14 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical average, which can be a whole or a fractional number for a specific product. The alkoxylation levels reported represent statistical averages, which may be a whole or a fractional number for a specific product. Preferred alkoxylates/ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE).

It has proven to be beneficial for cold washing performance if the detergents also contain soap(s). Preferred detergents are therefore characterized in that they contain soap(s). Saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid, and in particular soap mixtures derived from natural fatty acids, e.g. coconut, palm kernel or tallow fatty acids, are suitable.

Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and/or propoxylation products of alkyl glycosides or linear or branched alcohols, each with 8 to about 18 carbon atoms in the alkyl part and 3 to 20, preferably 4 to 10 alkyl ether groups. Corresponding ethoxylation and/or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters and fatty acid amides, which correspond to the long-chain alcohol derivatives mentioned in terms of the alkyl part, and of alkylphenols with 5 to 12 carbon atoms in the alkyl radical can also be used.

The nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular 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, in which the alcohol residue can be linear or preferably methyl-branched in the 2-position or linear and methyl-branched residues in the mixture, as are usually present in oxo alcohol residues. In particular, however, alcohol ethoxylates with linear residues from alcohols of native origin with 12 to 18 carbon atoms, for example from coconut, palm, tallow or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol is preferred. The preferred ethoxylated alcohols include, for example, Ci2-14 alcohols with 3 EO or 4 EO, Cg-n-alcohol with 7 EO, C -is alcohols with 3 EO, 5 EO, 7 EO or 8 EO, Ci2-is- Alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of Ci2-14 alcohol with 3 EO and C12-18 alcohol with 5 EO. The ethoxylation levels reported represent statistical averages, which may be a whole or a fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these non-ionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples of this are tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.

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 with 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

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

RO(G)z, in which R represents a linear or branched, in particular methyl-branched, saturated or unsaturated, aliphatic radical with 8 to 22, preferably 12 to 18 carbon atoms and G is the symbol for a Glucose unit with 5 or 6 carbon atoms, preferably glucose. The degree of glycosidation z is between 1 and 4, preferably between 1 and 2 and in particular between 1.1 and 1.4. Linear alkyl polyglycosides, i.e. alkyl polyglycosides, in which the polyglycosyl residue is a glucose residue and the alkyl residue is an n-alkyl residue are preferred.

Nonionic surfactants of the amine oxide type, for example N-cocoalkyl-N,N-dimethylamine oxide and N-tallow alkyl-N,N-dihydroxyethylamine oxide, and the fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, in particular not more than half of it.

Suitable amphotensides are, for example, betaines of the formula

(R ⁱⁱⁱ )(R ^iv )(R ^v )N ⁺ CH ₂ COO-, in which R'" is an alkyl radical, optionally interrupted by heteroatoms or heteroatom groups, with 8 to 25, preferably 10 to 21, carbon atoms and R ^iv and R ^v of the same type or various alkyl radicals with 1 to 3 carbon atoms, in particular C10-18-alkyldimethylcarboxymethylbetaine and Cn-17-alkylamidopropyldimethylcarboxymethylbetaine.

Suitable cationic surfactants include the quaternary ammonium compounds of the formula (Rvi)(Rvü)(Rvüi)(Ri ^x ) _N +X-, in which R ^vi to R ^ix represent four identical or different ones, in particular two long- and two short-chain Alkyl radicals and Other suitable cationic surfactants are the quaternary surface-active compounds, in particular with a sulfonium, phosphonium, iodonium or arsonium group, which are also known as antimicrobial agents are known. By using quaternary surface-active compounds with an antimicrobial effect, the agent can be designed with an antimicrobial effect or its antimicrobial effect, which may already be present due to other ingredients, can be improved.

Another 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 complex-forming phosphonates include a number of different compounds, such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP). Hydroxyalkane or aminoalkane phosphonates are particularly preferred in this application. Among the hydroxyalkane phosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as a sodium salt, with the disodium salt reacting neutrally and the tetrasodium salt reacting alkaline (pH 9). The preferred aminoalkane phosphonates are ethylenediaminetetramethylene phosphonate (EDTMP), diethylenetriaminepentamethylene phosphonate (DTPMP) and their higher homologues. They are preferably used in the form of the neutrally reacting sodium salts, for example as the hexasodium salt of EDTMP or as the hepta- and octa-sodium salt of DTPMP. HEDP from the phosphonate class is preferably used as the builder. The aminoalkane phosphonates also have a pronounced heavy metal binding capacity. Accordingly, particularly if the agents also contain bleach, it may be preferred to use aminoalkane phosphonates, in particular DTPMP, or to use mixtures of the phosphonates mentioned. A detergent preferred in this application contains one or more phosphonate(s) from the group aminotrimethylenephosphonic acid (ATMP) and/or salts thereof; Ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and/or their salts;

Diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and/or their salts; 1-Hydroxyethane-1,1-diphosphonic acid (HEDP) and/or its salts; 2-Phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and/or its salts; Hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and/or their salts; Nitrilotri(methylenephosphonic acid) (NTMP) and/or their salts. Detergents which contain 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates are particularly preferred. 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, the proportion by weight of the phosphonate in the total weight of the detergent preferably being 0.1 and 8.0 wt .-%, preferably 0.2 and 5.0% by weight, more preferably 0.3 and 3.0% by weight and particularly preferably 0.5-2.0% by weight.

The detergents according to the invention also preferably contain builders, preferably at least one water-soluble and/or water-insoluble, organic and/or inorganic builder. The builders include in particular silicates, carbonates and organic cobuilders. Examples of organic cobuilders include, in particular, polycarboxylates/polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders and phosphonates. These substance classes are described below. If desired, organic cobuilder substances can be contained in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1 to 8% by weight. Useful organic builders include, for example, the polycarboxylic acids that can be used in the form of the free acid and/or their sodium salts, whereby polycarboxylic acids are understood to mean those 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 carboxymethylinulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycinediacetic acid, methylglycinediacetic acid, glutamic diacetic acid, nitrilotriacetic acid (NTA), iminodisuccinate such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisucainate, ethylendiamintetra vinegar acid as well as polyas paragic acid, polyphosphonic acids, especially aminotris (methylene phosphonic acid), ethylendiamintetrakis (methylene phosphonic acid), lysintetra (methylene phosphosic acid) and 1-hydroxyetics 1, 1-1-di Phosphonic acid, polymers hydroxy compounds such as dextrin and polymers (poly) carboxylic acids, in particular through oxidation of Polycarboxylates accessible to polysaccharides or dextrins, and/or polymeric acrylic acids, methacrylic acids, maleic acids and mixed polymers made from these, which can also contain small amounts of polymerizable substances without carboxylic acid functionality in polymerized form. If desired, such organic builder substances can be contained 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 are therefore also used to set a lower and milder pH value of detergents. In particular, citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid and any mixtures of these should be mentioned. Citric acid or salts of citric acid are particularly preferably used as a building substance. Further particularly preferred building substances are selected from methyl glycine dieside acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), imino disuccinate (IDS) and ethylene diamine disuccinate (EDDS), carboxymethyl inulin and polyaspartate. In preferred embodiments, citric acid and/or citrate is used as the water-soluble, organic builder. It is particularly preferred to use 0.5 to 25% by weight, preferably 0.75 to 12.5% by weight, more preferably 1 to 4% by weight of citric acid and/or 0.5 to 25% by weight. %, preferably 0.75 to 12.5% by weight, more preferably 1 to 4% by weight of citrate, preferably alkali metal citrate, more preferably sodium citrate. Citric acid/citrate can each be used in the form of their hydrates, for example citric acid can be used in the form of the monohydrate and citrate can be used in the form of trisodium citrate dihydrate.

Polymeric polycarboxylates are also suitable as builders, for example the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example those with a relative molecular mass of 500 to 70,000 g/mol. For the purposes of this application, the molecular weights specified for polymeric polycarboxylates are weight-average molecular weights Mw of the respective acid form, which are generally determined using gel permeation chromatography (GPC). using a UV detector. The measurement was carried out against an external polyacrylic acid standard, which provides realistic molecular weight values due to its structural similarity to the polymers examined. This information differs significantly from the molecular weight information in which polystyrene sulfonic acids are used as the standard. The molar masses measured against polystyrene sulfonic acids are generally significantly higher than the molar masses specified 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, can be preferred from this group. Copolymeric polycarboxylates are also suitable, in particular those of acrylic acid with methacrylic acid and acrylic acid or methacrylic acid with maleic acid. Copolymers of acrylic acid with maleic acid which contain 50 to 90% by weight of acrylic acid and 50 to 10% by weight of maleic acid have proven to be particularly suitable. Their relative molecular mass, 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.

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

In addition to the water-soluble organic builders mentioned above, the compositions of 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 present in the form of their alkaline, neutral or acidic sodium or potassium salts. Small amounts of calcium carbonates may also be contained in solid textile detergents. For example, water-soluble crystalline and/or amorphous alkali metal silicates are suitable. The alkali metal silicates that can be used as builders in the agents according to the invention preferably have a molar ratio of alkali metal 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 metal silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio Na2O:SiO2 of 1:2 to 1:2.8. The crystalline silicates used, which can be present alone or in _a mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na2Si 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 assumes the values 2 or 3 in the general formula mentioned. In particular, both ß- and δ-sodium disilicates (Na2Si2Os • y H2O) are preferred. Practically anhydrous crystalline alkali metal silicates of the above-mentioned general formula, in which x is a number from 1.9 to 2.1, produced from amorphous alkali metal silicates, 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, as can be produced from sand and soda. Crystalline sodium silicates with a modulus in the range from 1.9 to 3.5 are used in a further embodiment Agents according to the invention are used. In agents that contain both amorphous and crystalline alkali metal silicates, the weight ratio of amorphous alkali metal silicate to crystalline alkali metal silicate is preferably 1:2 to 2:1 and in particular 1:1 to 2:1. Crystalline layered silicates of the formula (I) given above are sold by Clariant GmbH under the trade name Na-SKS, e.g. Na-SKS-1 (Na2Si22O45 • x H2O, Kenyaite), Na-SKS-2 (Na2Sii4O29 • x H2O , magadiite), Na-SKS-3 (Na2SisOi7 • x H2O) or Na-SKS-4 (Na2Si4Og • x H2O, makatite). Of these, Na-SKS-5 (a-Na ₂ Si ₂ O5), Na-SKS-7 (ß-Na ₂ Si ₂ O5, natrosilite), Na-SKS-9 (NaHSi ₂ O ₅ • 3) are particularly suitable H ₂ O), Na-SKS-10 (NaHSi ₂ O ₅ • 3 H2O, kanemite), Na-SKS-11 (t-Na ₂ Si ₂ O5) and Na-SKS-13 (NaHSi ₂ O ₅ ), in particular but Na-SKS-6 (ö-Na2Si2Os). In one embodiment of the agents according to the invention, a granular compound of crystalline layered silicate and citrate, of crystalline layered silicate and the above-mentioned (co-)polymeric polycarboxylic acid, or of alkali metal silicate and alkali metal carbonate is used, as is commercially available, for example, under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably contained in the agents according to the invention in amounts of 1 to 20% by weight, in particular 5 to 15% by weight. Furthermore, the carbonates (and hydrogen carbonates), in particular sodium carbonate, and the phosphonic acids/phosphonates are also important as water-soluble inorganic builder substances.

The agents according to the invention are preferably free of phosphate builders, i.e. contain less than 1% by weight, preferably no deliberately added phosphate builders.

The agents can also contain water-insoluble builder substances. Water-insoluble inorganic builder materials are in particular crystalline or amorphous water-dispersible alkali alumosilicates, 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. -%, used. Among these are the crystalline sodium aluminosilicates in detergent quality, in particular zeolite A, zeolite P, zeolite MAP and possibly zeolite Condea Augusta S.p.A.), preferred. Amounts close to the upper limit mentioned are preferably used in solid, particulate agents. Suitable aluminosilicates in particular have no particles with a grain size of over 30 pm and preferably consist of at least 80% by weight of particles with a size of under 10 pm. Their calcium binding capacity, which can be determined according to DE 2412837 A1, is usually in the range of 100 to 200 mg CaO per gram.

In addition to the builders described above, the detergent can contain cleaning-active polymers. The proportion by weight of the cleaning-active polymers in the total weight of detergents according to the invention is preferably 0.1 to 20% by weight, preferably 1.0 to 15% by weight and more preferably 2.0 to 12% by weight.

Peroxygen compounds suitable for use in agents according to the invention include, in particular, organic peracids or peracid salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and inorganic salts that release hydrogen peroxide under the washing conditions, including perborate, percarbonate, persilicate and/or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds such as H2G2-urea adducts. Hydrogen peroxide can also be produced using an enzymatic system, ie 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 common washing, cleaning or disinfectant components. Particular preference is given to using alkali metal percarbonate or alkali metal perborate monohydrate. If an agent according to the invention contains peroxygen compounds, these are present in amounts of preferably up to 50% by weight, in particular from 5 to 30% by weight, more preferably from 0.1 to 20% by weight.

Compounds which, under perhydrolysis conditions, produce 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 agents. Substances which carry O- and/or N-acyl groups of the stated number of carbon atoms and/or optionally substituted benzoyl groups are suitable. 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 phenol sulfonates or carboxylates or the sulfonic or carboxylic acids of these, in particular nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS or LOBS), 4- (2-decanoyloxyethoxycarbonyloxy )-benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters as well as acetylated sorbitol and mannitol or their described mixtures ( SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactose, acetylated, possibly N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimide acids are formed, in particular aminoacetonitrile derivatives quaternized nitrogen atom, and/or oxygen-transferring sulfonimines and/or acylhydrazones. The hydrophilically substituted acyl acetals and the acyllactams are also preferably used. Combinations of conventional bleach activators can also be used. Such bleach activators can, especially in the presence of the above-mentioned hydrogen peroxide-producing bleaching agents, be present in the usual amount range, preferably in amounts of 0.5 to 10% by weight, in particular 1 to 8% by weight, based on the total agent, are missing Use of percarboxylic acid as the sole bleaching agent, however, preferably entirely.

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

Suitable graying inhibitors or soil release active ingredients (soil release polymer) are cellulose ethers, such as carboxymethyl cellulose, methyl cellulose, hydroxyalkyl celluloses and Mixed cellulose ethers such as methyl hydroxyethyl cellulose, methyl hydroxypropyl cellulose and methyl carboxymethyl cellulose. Sodium carboxymethylcellulose, hydroxyporpylmethylcellulose and their mixtures and, if appropriate, their mixtures with methylcellulose are preferably used. Commonly used soil release active ingredients include copolyesters containing dicarboxylic acid units, alkylene glycol units and polyalkylene glycol units. The proportion of graying inhibitors and/or soil release active ingredients in agents according to the invention is generally not more than 2% by weight and is preferably 0.5 to 1.5% by weight, particularly preferably 0.5 to 2% by weight. %.

Derivatives of diaminostilbenedisulfonic acid or its alkali metal salts, for example, can be included as optical brighteners for textiles made of cellulose fibers (e.g. cotton). Salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-yl-amino)-stilbene-2,2'-disulfonic acid or compounds of similar structure which are suitable are, for example the morpholino group carries a diethanolamino group, a methylamino group or a 2-methoxyethylamino group. Furthermore, brighteners of the substituted 4,4'-distyryl-diphenyl type may be present, for example 4,4'-bis-(4-chloro-3-sulfostyryl)-diphenyl. Mixtures of brighteners can also be used. Brighteners of the 1,3-diaryl-2-pyrazoline type are particularly suitable for polyamide fibers, e.g. 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazoline and compounds of similar structure. The content of optical brighteners or brightener mixtures in the agent is generally not more than 1% by weight, preferably 0.05 to 0.5% by weight. In a preferred embodiment of the invention, the agent is free of such active ingredients.

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

To adjust the desired pH value, 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 hydrogen sulfates, or bases, in particular ammonium or alkali metal hydroxides, preferably sodium hydroxide. Such pH regulators are contained in the agents according to the invention preferably not more than 10% by weight, in particular from 0.5 to 6% by weight, particularly preferably from 0.3 to 2% by weight.

The detergents according to the invention can contain an organic solvent as a further component. The addition of organic solvents has a beneficial effect on the Enzyme stability and the cleaning performance of these agents. Preferred organic solvents come from the group of mono- or polyhydric alcohols, alkanolamines or glycol ethers. The solvents are preferably selected from ethanol, n or i-propanol, butanol, glycol, propandiol, bustiol, glycerin, diglykol, propyldiglykol, butyldiglykol, hexylene glycol, ethylene glycolmethyl ether, ethylene gly column Lether, ethylene glycolmono-n- butylether, diethylene glycolmethyl ether, di-ethylene glycolethyl 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 proportion by weight of these organic solvents in the total weight of detergents according to the invention is preferably 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight and more preferably 0.5 to 5.0% by weight. A particularly preferred organic solvent that is particularly effective in terms of stabilizing the detergents is glycerin and 1,2 propylene glycol. Liquid detergents preferably comprise at least one polyol, preferably from the group of glycerol and 1,2-propylene glycol, based on the total weight of the detergent, preferably 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 the organic amines and alkanolamines. The detergents according to the invention preferably contain these amines in amounts of 0.1 to 10% by weight, preferably from 0.2 to 8.0% by weight and more preferably from 0.5 to 5.0% by weight, respectively based on their total weight. A particularly preferred alkanolamine is ethanolamine.

Detergents or cleaning agents according to the invention can only contain a 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 therefore represents agents which further comprise one or more further enzymes. Other enzymes which can preferably be used are all enzymes which can develop a 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 - which can be distinguished from the proteases according to the invention - and mixtures thereof. Further enzymes are advantageously contained in the agent in an amount of 1 x 10 ^-8 to 5 percent by weight based on active protein. Increasingly preferred is each further enzyme in an amount of 1 x 10 ^-7 to 3% by weight, from 0.00001 to 1% by weight, from 0.00005 to 0.5% by weight, from 0.0001 up to 0.1% by weight and particularly preferably from 0.0001 to 0.05% by weight in agents according to the invention, based on active protein. The enzymes particularly preferably show synergistic cleaning performance against certain dirt or stains, ie the enzymes contained in the agent composition support each other in their cleaning performance. Very particularly preferably, such a synergism exists between the protease contained according to the invention and a further enzyme of an agent according to the invention, including in particular between the protease mentioned and an amylase and/or a lipase and/or a mannanase and/or a cellulase and/or a pectinase . Synergistic effects cannot only occur between different enzymes, but also between one or more enzymes and other ingredients of the agent according to the invention.

Textile detergents preferred according to the invention have at least one protease and at least one amylase. In a further preferred embodiment of the invention, textile detergents have at least one protease and at least one cellulase. In a further preferred embodiment, textile detergents have at least one protease and at least one lipase. In a further preferred embodiment, textile detergents have at least one protease, at least one amylase and at least one lipase. In a further preferred embodiment, textile detergents have at least one protease, at least one amylase and at least one cellulase. In a further preferred embodiment, textile detergents have at least one protease, at least one amylase, at least one cellulase and at least one lipase. Textile detergents which have 3 to 10 different enzymes are particularly preferred, with textile detergents which have 3 to 10 different types of enzymes being particularly preferred in terms of their cleaning performance against a very wide range of stains.

Examples of proteases 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, subtilisin DY and the enzymes that can be assigned to the subtilases, but no longer to the subtilisins in the narrower sense thermitase, proteinase K and the proteases TW3 and TW7. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from the company Novozymes. The subtilisins 147 and 309 are sold by the company Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants are derived from the protease from Bacillus lentus DSM 5483. Other usable proteases include those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101 L® and Ovozyme® from the company Novozymes, which under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® from the company Danisco/DuPont, sold under the trade name Lavergy pro 104 LS® from the company BASF, sold under the trade name Protosol® from the company Advanced Biochemicals Ltd., under the trade name Wuxi® by the company Wuxi Snyder Bioproducts Ltd., under the trade names Proleather® and Protease P® by the company Amano Pharmaceuticals Ltd., and under the trade name Proteinase K-16 by the company Kao Corp, available enzymes. Particular preference is also given to using 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. Further proteases that can be used advantageously 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 proteases that can be used are those that are naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus.

Examples of amylases are the a-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens or Bacillus stearothermophilus and, in particular, those for use in washing or washing products Cleaning agents improved further developments. The enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl® and from the company Danisco/DuPont under the name Purastar® ST. Further development products of this a-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco/DuPont) and Keistase® (Daiwa Seiko Inc.). The a-amylase from Bacillus amyloliquefaciens is sold by the Novozymes company under the name BAN®, and derived variants of the a-amylase from Bacillus stearothermophilus under the names BSG® and Novamyl®, also by the Novozymes company. Furthermore, the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) should be highlighted. Furthermore, the amylolytic enzymes can be used which are described in WO 95/26397, WO 96/23873, WO 99/23211, WO 00/60060, WO 2003/002711, WO 2003/054177, WO 2006/002643, WO 2007/079 938, WHERE 2011/100410 and WO 2013/003659 are disclosed. Fusion products of all the molecules mentioned can also be used. In addition, the further developments of a-amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from the company 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 the company Novozymes, as well as the PREFERENCE S® series from the company Danisco /DuPont, including, for example, PREFERENCE S100®, PREFERENCE S1000® or PREFERENCE S210®. Variants of these enzymes obtainable through point mutations can also be used according to the invention.

Preferred amylases include a) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 80% and increasingly preferably to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% is identical and optionally at least one Amino acid substitution at one of positions 172, 202, 208, 255 and 261 in the count according to SEQ ID NO:2, preferably selected from M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, R172Q and combinations thereof existing group; and/or b) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:3 over its total 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 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 one of positions 183 and 184 in the count according to SEQ ID NO:3, preferably at least one amino acid substitution at one of positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, and/or more preferably at least one amino acid substitution or deletion selected from the group consisting of R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof; and/or c) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:4 over its total length to at least 65% and increasingly preferably to 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% is identical 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:4, preferably amino acid deletions at positions 183 and 184; and/or d) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:5 over its total length to at least 89% and increasingly preferably to at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical and has at least one deletion at one of positions 180, 181, 182, 183 and 184 in the count according to SEQ ID NO:5, preferably deletions at least two positions selected from the positions

180+181, 181+182, 182+183 and 183+184 in the count according to SEQ ID NO:5, particularly preferably at positions 183+184 in the count according to SEQ ID NO:5, and/or at least one substitution one of positions 405, 421, 422 and 428 in the count, SEQ ID NO:5, which is selected from the group consisting of I405L, A421H, A422P, A428T and combinations thereof.

In various embodiments of the invention, the amylase comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 80% and increasingly preferably to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% is identical and optionally at least one amino acid substitution on one of positions 172, 202, 208, 255 and 261 in the count according to SEQ ID NO:2, 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 positions mentioned above, 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, particularly R172Q. The M202L and M202T mutants are particularly preferred.

In various embodiments of the invention, the amylase comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:3 over its total 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 ,269,270,272,283,295,296,298,299,303,304,305,311,314,315,318,319,320,323,339,345,361,378,383,41 9, 421 , 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and/or a deletion at one of positions 183 and 184 in the count according to SEQ ID NO:3, preferably at least one Amino acid substitution at one of positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, particularly preferably from R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof existing group is selected. In various preferred embodiments, the amylase in the count according to SEQ ID NO:3 has amino acid substitutions at three or more of positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345 and optionally one or several, 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 in the count according to SEQ ID NO:3 has 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.

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% of the amino acid sequence specified in SEQ ID NO:4 over its total length. 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% is identical 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:4. 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/T7Y, 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 , N151 R, Y152H, Q169E, N174R, A186R, Y243F, S244Q, G303V, R320N, R359I, N418D and A447V. In various embodiments of the invention, the amylase comprises an amino acid sequence which corresponds to the sequence specified in SEQ ID NO:5 over its total length to at least 89% and increasingly preferably to 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 and has a deletion at one or more of positions 180, 181, 182, 183 and 184 in the count according to SEQ ID NO:5. 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 count according to SEQ ID NO:5, particularly preferred Deletions H183*+G184*. Preferably, such an α-amylase in the count according to SEQ ID NO:5 further has an amino acid substitution at one or more of positions 405, 421, 422 and 428. One or more of the substitutions I405L, A421H, A422P and A428T are particularly preferred. In a particularly preferred embodiment, the a-amylase in the count according to SEQ ID NO:5 has the deletions H183*+G184* and additionally the substitutions I405L, A421 H, A422P and A428T.

The term "cellulase" as used herein refers to an enzyme that catalyzes the hydrolysis of 1,4-β-D-glucoside bonds in cellulose (cellobiose), and/or lichenin and/or β-D-glucans. They are often also able to hydrolyze the 1,4 bonds in ß-D-glucans, which have 1,3 bonds in addition to the 1,4 bonds. Cellulases are able to break down cellulose into ß-glucose. Consequently, cellulases act in particular on residues containing cellulose or cellulose derivatives 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-endoglucan hydrolase , celludextrinase or avicelase. The determining 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.

The term “cellulase activity” is defined herein 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. B. as follows: Cellulases release glucose from CMC (carboxymethylcellulose). The 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). The reaction with p-hydroxybenzoic acid hydrazide (PAHBAH) in the presence of bismuth produces a yellow dye that can be determined photometrically at 410 nm. The prerequisite is an alkaline pH value during the color reaction. The amount of sugar released corresponding to the coloring is a measure of enzyme activity (Lever, Anal. Biochem., 1972, 47 & 1977, 81).

Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. B. the fungal cellulases from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum, which are disclosed in US 4435307, US 5648263, US 5691178, US 5776757 and WO 89/09259. Particularly suitable cellulases are the alkaline or neutral cellulases color-caring 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 such as those 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 and WO 99/01544 and WO 2019/122520 are described.

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. A further example may include a GH44 xyloglucanase, e.g. a xyloglucanase enzyme with a sequence of at least 60% identity to positions 40 to 559 of SEQ ID NO:2 of WO 2001/062903.

Other examples of cellulases include the GH45 cellulases described in WO 96/29397 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), and Ecostone® and Biotouch® (AB Enzymes ).

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

Suitable lipases and cutinases are those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples are lipase from Thermomyces, for example from T. lanuginosus (formerly called Humicola lanuginosa), as described in EP 0258068 and EP 0305216, cutinase from Humicola, for example H. insolens (WO 96/13580), lipase from strains of Pseudomonas (some of them 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). Preferred lipases include, for example, the lipases originally available from Humicola lanuginosa (Thermomyces lanuginosus) or further developed therefrom, in particular those with one or more of the following amino acid exchanges starting from the lipase mentioned in the positions D96L, T213R and / or N233R, particularly preferably T213R and N233R. Lipases are sold, for example, by the company Novozymes under the trade names Lipolase®, Lipolase® Ultra, LipoPrime®, Lipozyme® and Lipex®. Another lipase that can be used advantageously is available from the company Novozymes under the trade name Lipoclean®.

Furthermore, for example, the cutinases that were originally isolated from Fusarium solani pisi and Humicola insolens can be used. Equally usable lipases are available from the company Amano 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® available. For example, the lipases or cutinases from the company Danisco/DuPont can be used, the starting enzymes of which were originally isolated from Pseudomonas mendocina and Fusarium solanii. Other important commercial products that should be mentioned are the preparations M1 Lipase® and Lipomax® sold by the company Danisco/DuPont and the enzymes sold by the company Meito Sangyo KK under the names Lipase MY-30®, Lipase OF® and Lipase PL® the product Lumafast® from the company Danisco/DuPont.

Further examples are lipases, which are 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 the 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 such as those 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 are described.

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

To increase the bleaching effect, oxidoreductases, for example 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, preferably organic, particularly preferably aromatic, compounds that interact with the enzymes are added in order to increase the activity of the relevant oxidoreductases (enhancers) or to ensure the flow of electrons in the case of very different redox potentials between the oxidizing enzymes and the soils (mediators).

In the cleaning agents described here, the enzymes to be used can also be formulated together with accompanying substances, for example from fermentation. In liquid formulations, the enzymes are preferably used as enzyme liquid formulation(s). 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, the solid preparations obtained by granulation, extrusion or lyophilization or, in particular in the case of liquid or gel-like agents, solutions of the enzymes, advantageously as concentrated as possible, with little water and/or mixed with stabilizers or other auxiliaries.

Alternatively, the enzymes can be encapsulated for both the 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 in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is covered with a water-, air- and/or chemical-impermeable protective layer. Additional active ingredients, such as stabilizers, emulsifiers, pigments, bleaches or dyes, can also be applied in superimposed layers. Such capsules are applied using methods known per se, for example by shaking or rolling granulation or in fluid bed processes. Such granules are advantageously low-dust, for example by applying polymeric film formers, and are storage-stable due to the coating.

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

The enzymes can also be incorporated into water-soluble films, such as those used, for example, in the packaging of detergents and cleaning agents in unit dosage form. Such a film allows the enzymes to be released after contact with water. As used herein, "water soluble" refers to a film structure that is preferably completely water soluble. Such a film preferably consists of (completely or partially hydrolyzed) polyvinyl alcohol (PVA).

A further subject of the invention is a process for cleaning textiles or hard surfaces, which is characterized in that an agent according to the invention is used in at least one process step. In various embodiments, the method described above is characterized in that the protease is 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 is used.

This includes both manual and mechanical processes, with mechanical processes being preferred due to their more precise controllability, for example in terms of the quantities used and exposure times. Methods for cleaning textiles are generally characterized by the fact that various cleaning-active substances are applied to the items to be cleaned in several process steps and washed off after the exposure time, or that the items to be cleaned are treated in some other way with a detergent or a solution or dilution of this agent. All facts, objects and embodiments that are described for proteases according to the invention and agents containing them are also applicable to this subject matter of the invention. Therefore, at this point, express reference is made to the disclosure in the appropriate place with the note that this disclosure also applies to the above methods according to the invention.

Another subject of the invention is the use of a compound with the formula (I) or

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-6-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to improve the stability, in particular the storage stability, of enzymes, preferably proteases, cellulases and / or amylases, in a protease-containing detergent and cleaning agent , wherein the protease comprises an amino acid sequence that is at least 70% identical to the amino acid sequence specified 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 that correspond to the Positions 9, 130, 133, 144, 217, 252 and 271 correspond to 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 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, is selected from the existing group.

(II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease comprising an amino acid sequence corresponding to that in SEQ ID NO:1 specified amino acid sequence over the total length of which is at least 70% 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 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, 131H, 166M, 189T, 211N and 224A, is selected from the existing group. Another subject of the invention is the use of a compound with the formula (I) or

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, particularly preferably cellulases , by a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence which corresponds to the amino acid sequence specified 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% are identical, and each 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 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, is selected from the existing group,

All facts, objects and embodiments that are described for proteases according to the invention and agents containing them are also applicable to this subject matter of the invention. Therefore, at this point, express reference is made to the disclosure in the appropriate place with the note that this disclosure also applies to the above use according to the invention.

PREFERRED EMBODIMENTS

1 . Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(A) at least one protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified 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% is identical, and each 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 correspond to 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, 21 1 or 224 correspond to at least one further amino acid substitution 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group,

(B) at least one compound with the formula (I) or (II)

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase.

2. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(B) at least one compound with the formula (I) or (II)

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, wherein the washing and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds .

3. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(A) at least one protease which has proteolytic activity and comprises an amino acid sequence which 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% is identical, and each 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 correspond to 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 correspond to at least one further amino acid substitution 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group,

(B) at least one compound with the formula (I) or (II)

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, the agent having a pH in 1% by weight solution in deionized water at 20 ° C -Value 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.

4. Detergents and cleaning agents, in particular liquid detergents 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 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% is identical, and each 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 correspond to 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 correspond to at least one further amino acid substitution 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group,

(B) at least one compound with the formula (I) or (II)

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, wherein the washing and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds , and wherein the agent in 1% by weight 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.

5. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(B) at least one compound with the formula (I) or (II)

6. Detergents and cleaning agents, in particular liquid detergents and cleaning agents, particularly preferably liquid textile detergents, comprising

(B) at least one compound with the formula (I) or (II)

7. Detergents and cleaning agents, in particular liquid detergents and cleaning agents, particularly preferably liquid textile detergents, comprising

(A) a protease which has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% is 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 Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224 having the amino acid substitutions S89A, N187D, S189R and S224A,

(B) at least one compound with the formula (I) or (II)

8. Detergents and cleaning agents, in particular liquid detergents and cleaning agents, particularly preferably liquid textile detergents, comprising

(B) at least one compound with the formula (I) or (II)

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, and

(C) at least one further enzyme, wherein the further enzyme is different from the at least one protease and is preferably selected from amylase, cellulase and lipase, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the agent in 1% by weight solution in deionized water at 20 ° C has a pH in a range of approximately 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.

9. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(A) at least one protease that has proteolytic activity and one of the following amino acid substitution variants, each based on 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-Q271 E, and

(B) at least one compound with the formula (I) or (II)

10. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(B) at least one compound with the formula (I) or (II)

11. Detergent and cleaning agent, in particular liquid detergent and cleaning agent, particularly preferably liquid textile detergent, comprising

(A) at least one protease that has proteolytic activity and one of the following amino acid substitution variants, each 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-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-Q271 E, and

(B) at least one compound with the formula (I) or (II)

12. Detergents and cleaning agents, in particular liquid detergents and cleaning agents, particularly preferably liquid textile detergents, comprising

(A) at least one protease that has proteolytic activity and one of the following amino acid substitution variants, each 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-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-Q271 E, and

(B) at least one compound with the formula (I) or (II)

13. Detergents and cleaning agents according to one of the points to 12, wherein the at least one further from 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 and/or at least one lipase.

14. Detergents and cleaning agents according to one of points 1 to 12, wherein the at least one further enzyme is a cellulase.

15. Detergent and cleaning agent according to one of points 1 to 12, wherein the at least one further enzyme is an amylase, the amylase having amylolytic activity and being selected from a) an a-amylase which comprises an amino acid sequence corresponding to that in SEQ ID NO:2 specified amino acid sequence over its total length to at least 80% and increasingly preferably to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% is identical and optionally at least one amino acid substitution at one of positions 172, 202, 208, 255 and 261 in the count according to SEQ ID NO:2, 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 which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:3 over its total 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 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 one of positions 183 and 184 in the count according to SEQ ID NO:3, preferably at least one amino acid substitution at one of positions 9, 26, 149, 182, 186, 202, 257, 295, 299, 323, 339 and 345, and / or more preferably at least one amino acid substitution or deletion selected from the group consisting of R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof; and/or c) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:4 over its total length to at least 65% and increasingly preferably to 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% is identical 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:4, preferably amino acid deletions at positions 183 and 184; and/or d) an a-amylase which comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:5 over its total length to at least 89% and increasingly preferably to at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical and has at least one deletion at one of positions 180, 181, 182, 183 and 184 in the count according to SEQ ID NO:5, preferably deletions at least two positions selected from positions 180+181, 181+182, 182+183 and 183+184 in the count according to SEQ ID NO:5, particularly preferably at positions 183+184 in the count according to SEQ ID NO:5, and/or has at least one substitution at one of positions 405, 421, 422 and 428 in the count SEQ ID NO:5 selected from the group consisting of I405L, A421H, A422P, A428T and combinations thereof.

16. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to improve the stability, in particular the storage stability, of enzymes, preferably proteases, cellulases and / or amylases, in a protease-containing detergent and cleaning agent , wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified 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 correspond to at least one further amino acid substitution consisting of 6W/F, 89A/G, 131 H/Y/F, 166M/L/I, 187, 189T/L/I/R, 211 N/Q and 224A/ G, preferably 6W, 89A, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds , and wherein the detergent and cleaning agent in a 1% by weight 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 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.

17. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to improve the stability, in particular the storage stability, of enzymes, preferably proteases, cellulases and / or amylases, in a protease-containing detergent and cleaning agent , wherein the protease has proteolytic activity and comprises an amino acid sequence which corresponds to the amino acid sequence specified 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% are identical, and each based on the numbering according to SEQ ID NO:1 (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271, which correspond to 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, 21 1 or 224, at least one further amino acid substitution 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, which is Detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, 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 preferred at around 30°C.

18. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, for preventing and/or reducing the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% and 98% is identical, and each based on the numbering according to SEQ ID NO:1 (i) at the positions, which correspond 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, 21 1 or 224, at least one further amino acid substitution 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, is selected from the existing group , wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, wherein the detergent and cleaning agent in a 1% by weight solution in deionized water at 20 ° C has a pH value 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.

19. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence, which 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% is identical, and each based on the numbering according to SEQ ID NO:1 (i) at positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271 E, and (ii) at 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 from the 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, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the detergent and cleaning agent is in 1 weight. -% 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.

20. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence, which 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% is identical, and each based on the numbering according to SEQ ID NO:1 (i) at positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions 9T, 130D, 133A, 144K, 217M, 252T and 271 E, and (ii) on at least one, preferably two, more preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 21 1 or 224, at least one further amino acid substitution 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, is selected from the existing group , wherein the washing and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, 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 around 30°C.

21. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, for preventing and/or reducing the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:1 over its total 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% and 98% is identical, and each based on the numbering according to SEQ ID NO:1 (i) at the positions, which correspond 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, 21 1 or 224, at least one further amino acid substitution 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, is selected from the existing group , wherein the washing and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the washing and cleaning agent has a pH value in a 1% by weight solution in deionized water at 20 ° C 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.

22. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the autoproteolysis of a protease contained in the detergent and cleaning agent, the protease 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% are 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 a further amino acid substitution 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, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds.

23. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, by an im Protease contained in detergents and cleaning agents, the protease having proteolytic activity and comprising an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73% of the amino acid sequence specified in SEQ ID NO: 1 over its entire length, 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% is identical, and each 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 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, is preferably free of boron-containing compounds, and wherein the detergent and cleaning agent in 1% by weight 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.

24. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, by an im Protease contained in detergents and cleaning agents, the protease having proteolytic activity and comprising an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73% of the amino acid sequence specified in SEQ ID NO: 1 over its entire length, 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% is identical, and each 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 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, is preferably free of boron-containing compounds, 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.

25. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of further im Enzymes contained in detergents and cleaning agents, preferably amylases and / or cellulases, by a protease contained in the detergent and cleaning agent, the protease having proteolytic activity and comprising an amino acid sequence that corresponds to the amino acid sequence specified in SEQ ID NO: 1 over its entire length 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% are identical, and each based on the numbering according to SEQ ID NO:1 (i). 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 preferably three, of the positions corresponding to positions 6, 89, 131, 166, 187, 189, 211 or 224, at least one further amino acid substitution 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, existing group is selected , wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds, and wherein the detergent and cleaning agent has a pH value in 1% by weight solution in deionized water at 20 ° C 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.

26. Use of a compound of formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, by an im Protease contained in detergents and cleaning agents, the protease having proteolytic activity and comprising an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73% of the amino acid sequence specified in SEQ ID NO: 1 over its entire length, 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% is identical, and each 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 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, 131H, 166M, 187D, 189R, 189T, 211N and 224A, is selected from the existing group, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds.

27. Use according to one of points 16 to 26, where the further enzyme is cellulase.

28. Use according to one of points 16 to 26, wherein the protease has proteolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72% of the amino acid sequence specified in SEQ ID NO: 1 over its entire length. 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% is identical, and each 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 Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224, which has amino acid substitutions S89A, N187D, S189R and S224A.

29. Use according to one of points 16 to 28, wherein the compound is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzylcarbamate, preferably benzylmalonic acid.

30. Use according to one of points 16 to 29, wherein the protease has proteolytic activity and comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72% of the amino acid sequence specified in SEQ ID NO: 1 over its entire length. 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% is identical, and each 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 Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224 having amino acid substitutions S89A, N187D, S189R and S224A, and the compound is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl-3-benzoylpropionate, (S)-3-phenylbutyric acid and benzylcarbamate is, preferably benzylmalonic acid. EXAMPLES

Detergent matrix used

Table 1 shows a commercially available liquid detergent matrix that was used for the following experiments:

Protease activity assay

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 the pNA causes an increase in the absorbance at 410 nm, the time course of which is a measure of the enzymatic activity.

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.

Measurement approach:

10 pL AAPF solution (70 mg/mL) 1000 pL Tris/HCl (0.1 M; pH 8.6 with 0.1% Brij 35)

10 pL diluted protease solution

Kinetics created over 5 min at 25°C (410 nm)

Cellulase activity assay

The activity of cellulase is determined by the PAHBAH (para-hydrobenzoic acid hydrazide) method. Cellulases release glucose from carboxymethylcellulose (CMC), which reacts with PAHBAH to form a yellow dye that can be detected colorimetrically at 410 nm.

Measurement approach:

250 pL CMC solution (2.5%)

250 pL diluted cellulase solution

1.5 mL PAHBAH solution (1% with 1 mM bismuth and in 0.5 NaOH)

250 pL of CMC solution and 250 pL of diluted cellulase solution were combined and incubated in a water bath at 40°C for 15 minutes. After incubation, 1.5 mL of PAHBAH solution was added and the sample was incubated for 10 minutes at 70°C in the heating block for staining. After heating, the entire sample was cooled in an ice bath for 1–2 min. The cooled sample was then transferred to a disposable cuvette and the measurement was carried out at 410 nm.

Proteases used:

Protease 1 (P1): SEQ ID NO:1-P9T-N130D-Q271 E-N144K-N252T-Y217M-T133A-S224A-S189T-S89A

Protease 2 (P2): SEQ ID NO:1-P9T-N130D-Q271 E-N144K-N252T-Y217M-T133A-S224A-N187D-S189R-S89A

Example 1: Determination of the storage stability of protease

The following protease variants were stored at the same level of active protein (20 mg/job of active enzyme protein each) at 30°C in the formula A, B, C and D for 1, 2 and 4 weeks and their residual activity was determined using AAPF-pNA measurement.

The activity of the protease before storage was normalized to 100%. The difference values of the residual activity (RA) of the proteases P1 and P2 of the respective approach with inhibitor (formula B, C or D) compared to the approach without inhibitor (formula A) are given below. A difference >5 is considered significant.

The results show that both benzylmalonic acid and boric acid lead to a significantly higher residual activity of the proteases P1 and P2, especially of protease P2, after storage, ie improve the storage stability of the protease. It is particularly encouraging that benzylmalonic acid appears to be suitable for replacing boric acid as a protease inhibitor in detergents.

Example 2: Determination of the storage stability of cellulase

A commercially available cellulase (ex. AB Enzymes) was stored at the same level of active protein (2 mg/job of active enzyme protein) at 30 ° C in the formula A, B, C and D for 1, 2 and 4 weeks (together with protease 1 or 2 as stated in Example 1) and their residual activity determined using PAHBAH measurement.

The activity of cellulase before storage was normalized to 100%. The difference values of the residual activity (RA) of the cellulase of the respective approach with inhibitor (formula B, C or D) compared to the approach without inhibitor (formula A) are given below. A difference >5 is considered significant.

The results show that both benzylmalonic acid and boric acid lead to a significantly higher residual activity of cellulase after storage in the presence of protease P2, i.e. improve storage stability. It is particularly encouraging that benzylmalonic acid appears to be suitable for replacing boric acid as an inhibitor in detergents.

Claims

PATENT CLAIMS

(B) at least one compound with the formula (I) or (II)

2. Detergent and cleaning agent according to claim 1, wherein the protease comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO: 1 over its total 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% is identical, and points, in each case based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271 corresponding to 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, G131 H, S166M, N187D, S189R, S189T, S211 N and S224A.

3. Detergent and cleaning agent according to claim 1 or 2, wherein the protease comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO: 1 over its total 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% is identical, and each based on the numbering according to SEQ ID NO:1, (i) at the positions corresponding to the positions 9, 130, 133, 144, 217, 252 and 271, the amino acid substitutions P9T, N130D, T133A, N144K, Y217M, N252T and Q271 E and (ii) at positions corresponding to positions 89, 187, 189 and 224 , which has amino acid substitutions S89A, N187D, S189R and S224A.

4. Detergent and cleaning agent according to one of the preceding claims, wherein the protease has one of the following amino acid substitution variants, each based on 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.

5. Detergent and cleaning agent according to one of the preceding claims, wherein the compound (B) is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl-3-benzoylpropionate, (S)-3-phenylbutyric acid and benzylcarbamate .

6. Detergent and cleaning agent according to one of the preceding claims, wherein the at least one further enzyme from 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 and/or at least one lipase and/or at least one mannanase.

7. Detergent and cleaning agent according to one of the preceding claims, wherein the at least one further enzyme is an amylase and wherein the amylase is selected from

(a) an α-amylase which comprises an amino acid sequence that is at least 80% identical to the amino acid sequence given in SEQ ID NO:2 over its entire length and optionally at least one amino acid substitution at one of positions 172, 202, 208, 255 and 261 in the count according to SEQ ID NO:2, preferably selected from M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, R172Q and combinations thereof existing group; and or

(b) an a-amylase which comprises an amino acid sequence which is at least 60% identical to the amino acid sequence given in SEQ ID NO:3 over its entire length and optionally at least one amino acid substitution at one of 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 positions 183 and 184 in the count according to SEQ ID NO:3 has, preferably at least one amino acid substitution at one of 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 from R118K, D183*, G184*, N195F, R320K, R458K and combinations thereof existing group is selected; and or

(c) an a-amylase which comprises an amino acid sequence which is at least 65% identical to the amino acid sequence given in SEQ ID NO:4 over its entire length and optionally at least one substitution and/or deletion at one of 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 SE Q ID NO:4, preferably has amino acid deletions at positions 183 and 184; and or

(d) an a-amylase which comprises an amino acid sequence which is at least 89%, 90%, 91%, 92%, 93%, 94%, 95% of the amino acid sequence specified in SEQ ID NO:5 over its total length, 96%, 97%, 98%, 99% and 100% identical and has at least one deletion at one of positions 180, 181, 182, 183 and 184 in the count according to SEQ ID NO:5, preferably deletions at at least two positions selected from positions 180+181, 181+182,

182+183 and 183+184 in the count according to SEQ ID NO:5, particularly preferably at positions 183+184 in the count according to SEQ ID NO:5, and / or at least one substitution at one of the positions 405, 421, 422 and 428 having SEQ ID NO:5 selected from the group consisting of I405L, A421H, A422P, A428T and combinations thereof.

8. Detergent and cleaning agent according to one of the preceding claims, wherein the at least one further enzyme is a cellulase.

9. Detergent and cleaning agent according to one of the preceding claims, wherein a) the at least one protease is a protease according to one of claims 2 to 4, b) the at least one further enzyme is an amylase according to claim 7 and / or a cellulase.

10. Detergent and cleaning agent according to one of the preceding claims, wherein the detergent ingredient consists 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, sequestering agents, electrolytes, pH regulators and / or other auxiliaries such as optical brighteners, graying inhibitors, color transfer inhibitors, foam regulators as well as dyes and fragrances and combinations thereof is selected from the existing group.

11. Detergent and cleaning agent according to one of the preceding claims, wherein the detergent and cleaning agent is essentially free of boron-containing compounds, preferably free of boron-containing compounds.

12. Detergent and cleaning agent according to one of the preceding claims, wherein in 1% by weight solution in deionized water at 20 ° C there is a pH value 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.

13. A process for cleaning textiles and/or hard surfaces, characterized in that in at least one process step a detergent or cleaning agent according to one of claims 1 to 12 is used, the process preferably being carried out in a temperature range of about 20 ° C to about 60 ° C, particularly preferably from about 20 ° C to about 40 ° C, very particularly preferably from about 30 ° C.

14. Use of a detergent or cleaning agent according to one of claims 1 to 12 for cleaning textiles and / or hard surfaces, 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 about 30°C.

15. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-6-carboxylic acids and -OOC-NR ² 2, where R ² is the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to improve the stability, in particular the storage stability, of enzymes, preferably proteases, cellulases and/or amylases, in a detergent and cleaning agent, preferably in a washing or cleaning agent according to one of claims 1 to 12.

16. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, to prevent and/or reduce the proteolysis of other enzymes contained in the detergent and cleaning agent, preferably amylases and/or cellulases, preferably cellulases, by a protease contained in the detergent and cleaning agent, the detergent and cleaning agent preferably being a detergent and cleaning agent according to one of claims 1 to 12.

17. Use of a compound with formula (I) or (II)

where R is each selected from -COOH, Ci-e-alkyl-substituted or unsubstituted

C2-6-dicarboxylic acids, Ci-e-alkyl-substituted or unsubstituted C2-e-carboxylic acids and -OOC- NR ² 2, where R ² are the same or different and selected from Ci-e-alkyl or H, as well as salts, esters or derivatives thereof, for preventing and/or reducing the autoproteolysis of a protease contained in the detergent and cleaning agent, the detergent and cleaning agent preferably being a detergent and cleaning agent according to one of claims 1 to 12.

18. Use according to any one of the preceding claims 15 to 17, wherein the compound is selected from the group consisting of benzoic acid, phenylmalonic acid, benzylmalonic acid, phenylsuccinic acid, benzylsuccinic acid, methyl 3-benzoylpropionate, (S)-3-phenylbutyric acid and benzyl carbamate.

19. Use according to one of the preceding claims 15 to 18, wherein a) the one protease is a protease according to one of claims 2 to 4, b) the at least one further enzyme is an amylase according to claim 7 and / or a

cellulase is.