LIQUID CLEANING AGENT CONTAINING LIQUID AND SOLID ENZYME FORMULAS

Description

[0001] The present application is directed to a liquid cleaning agent, preferably a dishwashing agent, preferably an automatic dishwashing agent, which contains at least one solid and at least one liquid enzyme formulation, and to the use of such a cleaning agent.

[0002] The most important criterion when cleaning hard surfaces, especially in automatic dishwashing, is the cleaning performance on a wide variety of soils, which are introduced primarily in the form of food residue. Even though the cleaning performance of the dishwashing detergents used today is generally high, the problem arises, partly due to the general trend in automatic dishwashing toward the increased use of low-temperature programs, that many conventional automatic dishwashing detergents have insufficient cleaning performance on stubborn soils. Such inadequate cleaning performance and the resulting inadequate cleaning of dishes lead to consumer dissatisfaction and the pre-treating of such soils by the consumer, which in turn increases water and energy consumption.Therefore, there is a general need for automatic dishwashing detergents that provide good cleaning performance even on stubborn soils.

[0003] Cleaning agents for hard surfaces, such as dishwashing detergents, are available to consumers in a wide variety of forms. In addition to traditional solid agents, free-flowing and, in particular, liquid to gel-like cleaning agents have recently become increasingly important. Consumers particularly value the rapid solubility and the associated rapid availability of the ingredients in the cleaning solution, particularly in short dishwashing programs and at low temperatures. Enzyme-containing washing and / or cleaning agents, in particular those containing protease and / or amylase, are known from, for example, GB 2392449 A, DE 19918457 A1, EP 2100949 A1 and WO 2010 / 090915 A1, WO 2011 / 036263A1, US 6287841 B1, US 2014 / 179585 A1 and EP 1921148 A2.

[0004] The importance of concentrated compositions, in particular those with a reduced water content compared to conventional compositions, is increasing. For consumers, compositions with the lowest possible water content, for example, less than 25% by weight, are therefore particularly desirable.

[0005] Furthermore, consumers have become accustomed to the convenient dosing of pre-portioned dishwasher detergents and have so far primarily used these products in tablet form. To package a liquid dishwashing detergent, which offers the aforementioned advantages over solid formulations, in a pre-portioned format, the use of cold-water-soluble films in the form of sachets is common. However, this places limits on formula development, as only a limited amount of water can be incorporated into the product. Exceeding the tolerable amount of water leads to premature dissolution of the enveloping water-soluble film. To ensure good storage stability of these water-soluble containers, water contents of less than 25% by weight are also desirable.

[0006] Furthermore, liquid formulations are particularly visually appealing to consumers when they contain stably suspended, solid, and possibly colored, components. If these solid components contain cleaning-active substances and are advertised as particularly effective, this gives the consumer the impression that such a product is more effective than one without these solid components.

[0007] The object of the present invention was therefore to provide a liquid cleaning agent, preferably a dishwashing agent, preferably an automatic dishwashing agent, which has an increased cleaning performance, has a low water content and is visually appealing.

[0008] Surprisingly, it has now been found that the use of a combination of liquid enzyme formulations and solid enzyme granules leads to improved performance in liquid dishwashing detergents compared to the use of either liquid or solid enzyme formulations alone. Furthermore, the use of solid enzyme formulations offers the advantage of further reducing the water content in low-water detergent formulations, as liquid enzyme formulations typically have a high water content.

[0009] In a first aspect, the present invention is therefore directed to a liquid cleaning agent, in particular automatic dishwashing agent according to claim 1, containing (1) at least one liquid enzyme formulation containing at least one amylase (A1) and optionally at least one protease (P1); and (2) at least one solid enzyme formulation, preferably in the form of granules, containing at least one protease (P2) and / or at least one amylase (A2), wherein the solid enzyme formulation is homogeneously suspended in the liquid dishwashing detergent, wherein the amylase (A1) is selected from a) an AA560 α-amylase from Bacillus sp. or a functional fragment thereof; and / or b) an amylase which comprises an amino acid sequence which 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 the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 320, 323, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and / or one of the deletions D183* and G184* in the numbering according to SEQ ID NO:2;and / or c) an amylase which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO:2 over its entire length and has the following amino acid substitutions and / or deletions in the numbering according to SEQ ID NO:2: (i) M9L + M323T; (ii) M9L + M202L / T / V / I + M323T; (iii) M9L + N195F + M202L / T / V / I + M323T; (iv) M9L + R118K + D183* + G184* + R320K + M323T + R458K; (v) M9L + R118K + D183* + G184* + M202L / T / V / I + R320K + M323T + R458K; (vi) M9L + G149A + G182T + G186A + M202L + T257I + Y295F + N299Y + M323T + A339S + E345R; (vii) M9L + G149A + G182T + G186A + M202I + T257I + Y295F + N299Y + M323T + A339S + E345R; (viii) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (ix) M9L + R118K + G149A + G182T + D183* + G184* + G186A + N195F + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K;(x) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202I + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (xi) M9L + R118K + D183* + D184* + N195F + M202L + R320K + M323T + R458K; (xii) M9L + R118K + D183* + D184* + N195F + M202T + R320K + M323T + R458K; (xiii) M9L + R118K + D183* + D184* + N195F + M202I + R320K + M323T + R458K; (xiv) M9L + R118K + D183* + D184* + N195F + M202V + R320K + M323T + R458K; (xv) M9L + R118K + N150H + D183* + D184* + N195F + M202L + V214T + R320K + M323T + R458K; or (xvi) M9L + R118K + D183* + D184* + N195F + M202L + V214T + R320K + M323T + E345N + R458K. ;

[0010] A further object of the present invention is the use of a cleaning agent described herein as a dishwashing detergent, preferably as an automatic dishwashing detergent.

[0011] Yet another aspect relates to a method for cleaning dishes in an automatic dishwasher, wherein a cleaning agent as described herein is used and is preferably dosed into the interior of the dishwasher during the running of a dishwashing program before the start of the main wash cycle or during the course of the main wash cycle.

[0012] In various embodiments of the invention, temperatures lower than those commonly used are used in the dishwashing process.

[0013] "Homogenously suspended," as used herein, refers to a suspension containing the solid enzyme preparation in the form of stably and uniformly dispersed particles. "Stably dispersed" means that the particles do not sediment or cream when stored at room temperature for a period of at least one week.

[0014] "Low temperatures" or "temperatures lower than conventionally used temperatures," as used herein in connection with dishwashing processes, preferably refers to temperatures below 60°C, especially below 55°C, more preferably 50°C or lower, particularly preferably 45°C or lower, and most preferably 40°C or lower. These temperature specifications refer to the target temperatures used in the cleaning steps.

[0015] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. It is understood that any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples. All percentages are by weight unless otherwise indicated. Numerical ranges given in the format "from x to y" include the stated values. Where multiple preferred numerical ranges are given in this format, it is understood that all ranges resulting from the combination of the various endpoints are also encompassed.

[0016] In various embodiments of the invention, the cleaning agent comprises at least one first (A2) and / or at least one second amylase (A1), wherein (A) the first amylase (A2) is contained in the solid enzyme formulation; and (B) the second amylase (A1) is contained in the liquid enzyme formulation.

[0017] The amylases used are primarily alkaline α-amylases. They act as hydrolases and cleave the α-(1-4) glycoside bond of polysaccharides, especially starches such as amylose, thereby breaking down starchy soils on the items being cleaned. Dextrins are formed as cleavage products, which then convert to maltose, glucose, and branched oligosaccharides. Their pH optimum is usually in the significantly alkaline range.

[0018] In various embodiments of the invention, the first amylase is an α-amylase from Bacillus sp.No. 707 or a functional fragment or variant thereof. In various further embodiments, the second amylase is an AA560 α-amylase from Bacillus sp. or a functional fragment or variant thereof.

[0019] The wild-type sequences of the mature α-amylase from Bacillus sp. No. 707 or the mature AA560 α-amylase from Bacillus sp. are given in SEQ ID NO:1 and SEQ ID NO:2, respectively.

[0020] "Different," as used herein with reference to enzymes, refers to enzymes that differ in their amino acid sequence. In various embodiments, different enzymes originate from different species of organisms or differ from each other through, for example, artificially induced mutations.

[0021] "Variant," as used herein in connection with enzymes, refers to natural or artificially produced variations of a native enzyme that have a modified amino acid sequence compared to the reference form. Such a variant may contain single or multiple point mutations, i.e., substitutions of a naturally occurring amino acid by another, insertions (insertion of one or more amino acids) and / or deletions (removal of one or more amino acids), in particular one or more point mutations. Such variants preferably have at least 50%, preferably 60% or more, more preferably 70%, 80%, 90%, 100% or more of the enzyme activity of the reference form.In various embodiments, such a variant has an amino acid sequence that is at least 70%, preferably 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% identical to the reference sequence over its entire length. The variants preferably have the same length as the reference sequence. Variants can be distinguished from the reference form by improved properties, such as higher enzyme activity, higher stability, altered substrate specificity, etc. Only those variants that exhibit enzymatic activity are used. "Enzymatic activity," as used in this context, means in particular that the corresponding enzymes exhibit at least 50%, preferably at least 90%, of the catalytic activity of their reference enzyme.

[0022] "Fragment," as used herein in connection with enzymes, refers to polypeptides shortened by one or more amino acids at the N-terminal and / or C-terminal levels compared to the reference enzyme. Only fragments exhibiting enzymatic activity are used. "Enzymatic activity," as used in this context, means in particular that the corresponding enzymes exhibit at least 50%, preferably at least 90%, of the catalytic activity of their reference enzyme.

[0023] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the state-of-the-art and commonly used BLAST algorithm (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215:403-410, and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp. 3389-3402) and is essentially performed by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences. A tabular assignment of the relevant positions is called alignment. Another state-of-the-art algorithm is the FASTA algorithm.

[0024] Such a comparison also allows a statement to be made about the similarity of the compared sequences. This is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same positions or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the protein. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes, or just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the total length of the respective nucleic acid or amino acid sequence.

[0025] As the first amylase within the meaning of the present invention, in various preferred embodiments an amylase is used which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length and optionally has at least one amino acid substitution at one of the positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:1, in particular selected from the group consisting of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N and R172Q.

[0026] In preferred embodiments of the invention, the first amylase is a variant of the α-amylase from Bacillus sp.No. 707 with the amino acid sequence given in SEQ ID NO:1, which is at least 80% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length and has at least one amino acid substitution at one of positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:1. Preference is given to using amylases which have an amino acid substitution at two, preferably three, of the aforementioned positions, in particular a substitution at position 202 selected from M202L, M202V, M202S, M202T, M202I, M202Q, M202W, a substitution at position 255, in particular S255N, and a substitution at position 172, in particular R172Q. The M202L and M202T mutants are very particularly preferred.

[0027] Further variants that can be used are those that have an amino acid sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:1, wherein positions 172, 202 and 255 are preferably substituted as described above. Such variants may, for example, include a shortening of the C-terminus, for example by 1-20 amino acids, or a deletion of one or more amino acids, in particular at positions 181, 182, 183, and 184 in the numbering according to SEQ ID NO:1, while retaining the enzymatic activity, i.e., the activity of the variant is at least 60% of the activity of the enzyme having the amino acid sequence of SEQ ID NO:1. Suitable amylases are also described in WO 2008 / 112459 A2, the entire disclosure of which is incorporated herein by reference.

[0028] The second amylase is different from the first amylase, ie an amylase that falls under the definition of both the first amylase and the second amylase cannot be counted as both the first and second amylase.

[0029] In various embodiments of the invention, the second amylase comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO:2 over its entire length and optionally has at least one amino acid substitution at one of the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 320, 323, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and / or one of the deletions D183* and G184* in the numbering according to SEQ ID NO:2

[0030] In particularly preferred embodiments, the second amylase has the following amino acid substitutions and / or deletions in the count according to SEQ ID NO:2: (i) M9L + M323T; (ii) M9L + M202L / T / V / I + M323T; (iii) M9L + N195F + M202L / T / V / I + M323T; (iv) M9L + R118K + D183* + G184* + R320K + M323T + R458K; (v) M9L + R118K + D183* + G184* + M202L / T / V / I + R320K + M323T + R458K; (vi) M9L + G149A + G182T + G186A + M202L + T257I + Y295F + N299Y + M323T + A339S + E345R; (vii) M9L + G149A + G182T + G186A + M202I + T257I + Y295F + N299Y + M323T + A339S + E345R; (viii) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (ix) M9L + R118K + G149A + G182T + D183* + G184* + G186A + N195F + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (x) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202I + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (xi) M9L + R118K + D183* + D184* + N195F + M202L + R320K + M323T + R458K; (xii) M9L + R118K + D183* + D184* + N195F + M202T + R320K + M323T + R458K;(xiii) M9L + R118K + D183* + D184* + N195F + M202I + R320K + M323T + R458K; (xiv) M9L + R118K + D183* + D184* + N195F + M202V + R320K + M323T + R458K; (xv) M9L + R118K + N150H + D183* + D184* + N195F + M202L + V214T + R320K + M323T + R458K; or (xvi) M9L + R118K + D183* + D184* + N195F + M202L + V214T + R320K + M323T + E345N + R458K. ;

[0031] A particularly preferred second amylase is the variant commercially available under the trade name Stainzyme Plus™< (Novozymes A / S, Bagsvaerd, Denmark).

[0032] In the context of the present invention, preference is given to combinations of a first amylase which is at least 80% identical to the amino acid sequence given in SEQ ID NO:1 over its entire length and has at least one amino acid substitution at one of positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:1, in particular a substitution at position 202 selected from M202L, M202V, M202S, M202T, M202I, M202Q, M202W, a substitution at position 255, in particular S255N, and a substitution at position 172, in particular R172Q, and a second amylase which is at least 80% identical to the amino acid sequence given in SEQ ID NO:2 over its entire length and has the following amino acid substitutions and / or deletions (i) M9L + M323T; (ii) M9L + M202L / T / V / I + M323T; (iii) M9L + N195F + M202L / T / V / I + M323T; (iv) M9L + R118K + D183* + G184* + R320K + M323T + R458K; (v) M9L + R118K + D183* + G184* + M202L / T / V / I + R320K + M323T + R458K; (vi) M9L + G149A + G182T + G186A + M202L + T257I + Y295F + N299Y + M323T + A339S + E345R; (vii) M9L + G149A + G182T + G186A + M202I + T257I + Y295F + N299Y + M323T + A339S + E345R; (viii) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (ix) M9L + R118K + G149A + G182T + D183* + G184* + G186A + N195F + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (x) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202I + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (xi) M9L + R118K + D183* + D184* + N195F + M202L + R320K + M323T + R458K; (xii) M9L + R118K + D183* + D184* + N195F + M202T + R320K + M323T + R458K;(xiii) M9L + R118K + D183* + D184* + N195F + M202I + R320K + M323T + R458K; (xiv) M9L + R118K + D183* + D184* + N195F + M202V + R320K + M323T + R458K; (xv) M9L + R118K + N150H + D183* + D184* + N195F + M202L + V214T + R320K + M323T + R458K; or (xvi) M9L + R118K + D183* + D184* + N195F + M202L + V214T + R320K + M323T + E345N + R458K. ;

[0033] In various embodiments, these combinations of amylases are used in a mass ratio based on active protein of 10:1 to 1:10, preferably 5:1 to 1:5, in particular 2:1 to 1:2, for example 2:3 to 3:2, particularly preferably in equal parts.

[0034] The cleaning agents described herein may, in preferred embodiments, contain at least one first (P2) and at least one second protease (P1), wherein (A) the first protease (P2) is contained in the solid enzyme formulation; and (B) the second protease (P1) is contained in the liquid enzyme formulation.

[0035] The cleaning agents may contain these proteases either alone or, preferably, in combination with the amylases described above. The various enzymes may be formulated separately in a liquid or solid formulation, or together in a solid or liquid formulation (i.e., the first amylase and first protease in a common solid formulation and / or the second amylase and second protease in a common liquid formulation).

[0036] It may be preferable to formulate the first protease in the solid enzyme formulation and the second amylase in the liquid enzyme formulation.

[0037] It may also be preferable to formulate the first amylase in the solid enzyme formulation and the second protease in the liquid enzyme formulation.

[0038] Preferred combinations contain a corresponding amylase in both the liquid phase and the solid phase, and in one of the two phases a corresponding protease in either the liquid or the solid phase.

[0039] It may also be preferred that both the liquid and the solid phase each contain one of the corresponding amylase and one of the corresponding protease.

[0040] The proteases are primarily alkaline serine proteases. They act as nonspecific endopeptidases, meaning they hydrolyze any acid amide bonds found within peptides or proteins, thereby breaking down protein-containing soils on the items being cleaned. Their pH optimum is usually in the significantly alkaline range.

[0041] In various embodiments of the invention, the at least one first protease comprises a protease from Bacillus alkalophilusPB92 or a functional fragment or variant thereof. The sequence of the mature protease from Bacillus alkalophilus PB92 (wild type) is given in SEQ ID NO:4. In preferred embodiments, this first protease can have an amino acid sequence that is at least 80%, preferably at least 90%, in particular 100% identical to the amino acid sequence given in SEQ ID NO:4 over its entire length and that optionally has at least one amino acid substitution at one of the following positions 32, 33, 48-54, 58-62, 94-107, 116, 123-133, 150, 152-156, 158-161, 164, 169, 175-186, 197, 198, 203-216 in the numbering according to SEQ ID NO:4.

[0042] Further variants that can be used are those that have an amino acid sequence that is at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 99% identical to the amino acid sequence given in SEQ ID NO:4 and in the numbering according to SEQ ID NO:4 at least one of the following positions 32, 33, 48-54, 58-62, 94-107, 116, 123-133, 150, 152-156, 158-161, 164, 169, 175-186, 197, 198, 203-216 carries an amino acid substitution.

[0043] Preferably, a variant of the protease having the amino acid sequence shown in SEQ ID NO:4 can be used, which is at least 80% identical to the amino acid sequence shown in SEQ ID NO:4 over its entire length and which has at least one amino acid substitution at one of the positions 116, 126, 127, 128, and 160 in the numbering according to SEQ ID NO:4. Preferably, proteases are used which have an amino acid substitution at two, preferably three or more, in particular four, of the aforementioned positions.

[0044] Further variants that can be used are those which have an amino acid sequence that is at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:4 and which have at least one amino acid substitution at one of the following positions 116, 126, 127, 128 and 160.

[0045] Particularly preferably, such a protease has an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO:4 over its entire length and which has one of the following combinations of amino acid substitutions in the numbering according to SEQ ID NO:4: (i) G116V + S126L + P127Q + S128A (ii) G116V + S126N + P127S + S128A + S160D (iii) G116V + S126L + P127Q + S128A + S160D (iv) G116V + S126V + P127E + S128K (v) G116V + S126V + P127M + A160D (vi) S128T (vii) G116V + S126F + P127L + S128T (viii) G116V + S126L + P127N + S128V (ix) G116V + S126F + P127Q (x) G116V + S126V+ P127E + S128K +S160D (xi) G116V + S126R + P127S + S128P (xii) S126R + P127Q + S128D (xiii) S126C + P127R + S128D; or (xiv) S126C + P127R + S128G.

[0046] Such a protease preferably has an amino acid sequence which, in the numbering according to SEQ ID NO:4, has at least one, preferably several, in particular each of the following amino acid substitutions G116V, S126L, P127Q and / or S128A and at all other positions corresponds to the amino acid sequence given in SEQ ID NO:4 over its entire length by at least 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 99%, in particular 100% identical. Particularly preferred is a protease which has an amino acid sequence obtainable starting from the amino acid sequence with SEQ ID NO:4 through the amino acid substitutions G116V, S126L, P127Q, and S128A, as numbered according to SEQ ID NO:4. Such a protease may have the amino acid sequence given in SEQ ID NO:8.

[0047] The at least one second protease is preferably selected from the group consisting of a subtilisin 309 from Bacillus lentus or a functional fragment or variant thereof and an alkaline protease from Bacillus lentus DSM 5483 or a functional fragment or variant thereof. Combinations of several of the aforementioned enzymes can also be used.

[0048] The sequences of the mature protease subtilisin 309 from Bacillus lentus or the mature alkaline protease from Bacillus lentus DSM 5483 are given in SEQ ID NO:3 and SEQ ID NO:5 respectively.

[0049] In various embodiments of the invention, the second protease comprises a subtilisin 309 from Bacillus lentusor a functional fragment or variant thereof, comprising an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100% identical to the amino acid sequence given in SEQ ID NO:3 over its entire length and has at least one amino acid substitution at one of positions 9, 15, 66, 212, and 239 in the numbering according to SEQ ID NO:3. Preference is given to those which have an amino acid substitution at two, preferably three, in particular four, and most preferably five of the aforementioned positions.

[0050] Further variants that can be used are those which have an amino acid sequence which is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:3, wherein one or more of positions 9, 15, 66, 212 and 239 are substituted, ie the amino acid at these positions does not correspond to the corresponding amino acid in SEQ ID NO:3.

[0051] Particularly preferably, a variant with at least one, preferably two, in particular three, particularly preferably four or very particularly preferably 5 of the amino acid substitutions selected from S9R, A15T, V66A, N212D and Q239R based on the numbering according to SEQ ID NO: 3 is used. The following combinations are preferred: S9R+V66A+N212D+Q239R, S9R+A15T+N212D+Q239R, S9R+A15T+V66A+Q239R, S9R+A15T+V66A+N212D, A15T+V66A+N212D+Q239R; S9R+A15T+V66A, S9R+A15T+N212D, S9R+A15T+Q239R, S9R+N212D+Q239R, S9R+V66A+N212D, S9R+V66A+Q239R, A15T+V66A+N212D, A15T+V66A+Q239R, A15T+N212D+Q239R, V66A+N212D+Q239R; S9R+A15T, S9R+V66A, S9R+N212D, S9R+Q239R, A15T+V66A, A15T+N212D, A15T+Q239R, V66A+N212D, V66A+Q239R, N212D+Q239R. A variant comprising all of the above-mentioned changes has the amino acid sequence given in SEQ ID NO:6 (S9R+A15T+V66A+N212D+Q239R).

[0052] Also particularly preferred are variants of the protease having the amino acid sequence given in SEQ ID NO:3, which have an amino acid substitution at position 99 and an insertion of one amino acid between the amino acids at positions 99 and 100 in the numbering according to SEQ ID NO:3, preferably selected from S99A and / or S99_G100InsD. Further variants that can be used are those that have an amino acid sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO: 3, wherein these variants have one or both of the above-mentioned mutations at positions 99 and 100. Preference is given to those that have both mutations. Such a variant has the amino acid sequence given in SEQ ID NO: 7.

[0053] In various still further embodiments of the invention, the second protease comprises an alkaline protease from Bacillus lentus DSM 5483 or a functional fragment or variant thereof which has an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100% identical to the amino acid sequence given in SEQ ID NO: 5 over its entire length and which optionally has at least one amino acid substitution at one, two, three or four of the following positions 3, 4, 99 and 199 in the numbering according to SEQ ID NO: 5. Preference is given to using proteases which have an amino acid substitution at two, preferably three or more, in particular four of the aforementioned positions.

[0054] Further variants that can be used are those that have an amino acid sequence that is at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence given in SEQ ID NO:5 and that have at least one amino acid substitution at one of the following positions 3, 4, 99 and 199.

[0055] Particularly preferably, such a protease has an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO:5 over its entire length and which, in the numbering according to SEQ ID NO:5, has the amino acid substitution R99E or R99D, and optionally additionally at least one or two, preferably all three, of the amino acid substitutions S3T, V4I and V199I.

[0056] Such a protease preferably has an amino acid sequence which, in the numbering according to SEQ ID NO:5, has at least one, preferably several, in particular each of the following amino acid substitutions R99E / R99D, S3T, V4I and / or V199I and at all other positions corresponds to the amino acid sequence given in SEQ ID NO:5 over its entire length by at least 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 99%, in particular 100% identical. Particularly preferred is a protease which has an amino acid sequence obtainable starting from the amino acid sequence with SEQ ID NO:5 by one or more of the amino acid substitutions R99E / R99D, S3T, V4I, and V199I, as numbered according to SEQ ID NO:5. Such a protease can have the amino acid sequence given in one of SEQ ID Nos:9-10.

[0057] According to the invention, it is particularly preferred to use a combination of a first and a second protease. A first protease is particularly preferred which has an amino acid sequence obtainable starting from the amino acid sequence with SEQ ID NO:4 through the amino acid substitutions G116V, S126L, P127Q, and S128A according to the numbering according to SEQ ID NO:4. Such a protease can have the amino acid sequence given in SEQ ID NO:8. In particular, a variant of the protease with the amino acid sequence according to SEQ ID NO:9 is used as the second protease.

[0058] In various embodiments, these combinations of two proteases are used in a mass ratio based on active protein of 10:1 to 1:10, preferably 5:1 to 1:5, in particular 2:1 to 1:2, for example 2:3 to 3:2, particularly preferably in equal parts.

[0059] The cleaning agents of the invention can contain the solid enzyme formulation in an amount of 0.01 to 5 wt.%, preferably 0.2 to 2 wt.%, based on the total weight of the cleaning agent. The solid enzyme formulation can in particular have an active enzyme content of 2 to 20 wt.%.

[0060] The liquid enzyme formulation can be present in the cleaning agents in an amount of 0.01 to 8 wt.%, preferably 0.3 to 6 wt.%, based on the total weight of the cleaning agent. The liquid enzyme formulation can in particular have an active enzyme content of 1 to 6 wt.%.

[0061] 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. The active protein concentration is determined by titrating the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)) and determining the residual activity (cf. M. Bender et al., J. Am. Chem. Soc. 88, 24 (1966), pp. 5890-5913).

[0062] In general, the cleaning agent may contain the liquid enzyme formulation and the solid enzyme formulation in a mass ratio of 10:1 to 1:10, preferably 1:1.

[0063] Surprisingly, the combinations of liquid and solid formulated amylases or proteases described herein exhibit the property of improving the performance of the cleaning agent, preferably the dishwashing detergent, by leading to improved cleaning performance on enzyme-sensitive soils.

[0064] In this case, the improvement in cleaning performance is generally understood to mean that when using the cleaning agents described herein, in particular the dishwashing agents, the removal of soiling on hard surfaces, in particular dishes, when cleaning them, preferably in an automatic dishwasher, is noticeably improved compared to the use of cleaning agents, preferably dishwashing agents, which do not contain the enzyme combinations described herein.

[0065] The enzymes to be used are also prepared in the respective formulations together with accompanying substances, for example from fermentation, or with stabilizers.

[0066] The enzymes can be protected, particularly during storage, against damage such as inactivation, denaturation, or degradation due to physical influences, oxidation, or proteolytic cleavage. In the case of microbial extraction, inhibition of proteolysis is particularly preferred. The described agents may contain stabilizers for this purpose. Cleaning-active enzymes are typically provided in the form of stabilized, storable, and transportable preparations. These prefabricated preparations include, for example, solid preparations obtained by granulation, extrusion, or lyophilization or, particularly in the case of liquid or gel-like agents, solutions of the enzymes, advantageously as concentrated as possible, with little water content, and / or mixed with stabilizers or other auxiliaries.

[0067] Alternatively, the enzymes can be encapsulated for both solid and liquid dosage forms, for example by spray-drying or extrusion of the enzyme solution together with a preferably natural polymer, or in the form of capsules, for example those in which the enzymes are enclosed as if in a solidified gel, or in those of the core-shell type, in which an enzyme-containing core is coated with a water-, air-, and / or chemical-impermeable protective layer. Additional active ingredients, such as stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be applied in superimposed layers. Such capsules are applied using methods known per se, for example by shake or roll granulation or in fluid-bed processes. Such granules, for example by applying polymeric film formers, are advantageously low in dust and, due to the coating, are stable during storage.

[0068] Furthermore, it is possible to package two or more enzymes together so that a single granulate has multiple enzyme activities.

[0069] As can be seen from the above, the enzyme protein constitutes only a fraction of the total weight of conventional enzyme preparations. Typically used enzyme preparations contain between 0.1 and 40 wt.%, preferably between 0.2 and 30 wt.%, particularly preferably between 0.4 and 20 wt.%, and especially between 0.8 and 15 wt.% of the enzyme protein.

[0070] In various embodiments of the invention, the solid enzyme preparation is a granulate. The granulate particles may be colored or have light-reflecting properties. The particles typically have an average particle size (sieve analysis) in the range of 1 µm to 700 µm.

[0071] Preferred liquid agents have densities of 0.5 to 2.0 g / cm 3 , in particular 0.7 to 1.7 g / cm 3 , in particular 1.0 to 1.5 g / cm 3 . The density difference between the granules and the liquid phase of the agent is preferably not more than 10% of the density of one of the two and is in particular so small that the granules according to the invention and preferably also any other solid particles contained in the agents float in the liquid phase.

[0072] In various embodiments, the liquid enzyme preparation is a solution, in particular an aqueous solution.

[0073] The cleaning agents described herein are (homogeneous) solutions in which the solid enzyme formulations are stably suspended and the liquid enzyme preparations are preferably dissolved.

[0074] In a preferred embodiment of the invention, the cleaning agent, in particular the automatic dishwashing detergent, is in a pre-portioned form. In one embodiment of the invention, the cleaning agent comprises several spatially separated compositions, making it possible to separate incompatible ingredients from one another or to offer combinations of compositions that are used at different times in the dishwasher. This is particularly advantageous when the automatic dishwashing detergent is in a pre-portioned form.

[0075] The cleaning agents of the invention are preferably liquid, low-water compositions. The cleaning agents according to the invention are preferably dishwashing detergents, in particular automatic dishwashing detergents.

[0076] The term "low-water," as used herein, means that the composition characterized in this way contains less than 25% water by weight, preferably less than 20% water by weight. In particular, this term includes compositions containing 1 to 20% water by weight, 1 to 15% water by weight, 5-15% water by weight, or 10 to less than 20% water by weight.

[0077] The water content as defined herein refers to the water content determined by Karl Fischer titration.

[0078] "Liquid" as used herein in relation to the cleaning agent according to the invention includes all flowable compositions and in particular also covers gels and pasty compositions.

[0079] "At least one" as used herein means 1 or more, for example 1, 2, 3, 4, 5, or more.

[0080] In various embodiments, the cleaning agent contains at least one polyhydric alcohol, in particular selected from glycerin and mixtures of glycerin and 1,2-propylene glycol. The polyhydric alcohols allow the incorporation of other components into the cleaning agent formulation even with a small amount of water, in particular when the amount of water is limited to 20 wt.%.

[0081] The total amount of polyhydric alcohol or alcohol mixtures used in cleaning agents according to the invention is preferably at least 20% by weight, in particular at least 25% by weight, particularly preferably at least 28% by weight, especially at least 30% by weight. Preferred ranges are 20 to 50% by weight, in particular 25 to 45% by weight, especially 28 to 40% by weight.

[0082] The polyhydric alcohol is preferably selected from glycerin, sorbitol, and mixtures of glycerin and / or sorbitol with 1,2-propylene glycol. Glycerin is preferably used in the inventive agents in an amount of 1 to 50 wt.%, in particular in an amount of 10 to 45 wt.%, particularly preferably in an amount of 20 to 40 wt.%. Sorbitol is preferably used in the inventive agents in an amount of 1 to 50 wt.%, in particular in an amount of 10 to 45 wt.%, particularly preferably in an amount of 20 to 40 wt.%.

[0083] Alternatively, a mixture of glycerin and 1,2-propylene glycol can be used. The glycerin is preferably used in an amount of 0.1 to 50 wt.%, in particular in an amount of 15 to 45 wt.%, particularly preferably in an amount of 20 to 40 wt.%. The 1,2-propylene glycol is preferably used in an amount of 1 to 20 wt.%, in particular in an amount of 5 to 15 wt.%, particularly preferably in an amount of 8 to 12 wt.%, in each case based on the total mass of the cleaning agent, wherein the total amount of glycerin and 1,2-propylene glycol is preferably at least 20 wt.%, in particular at least 25 wt.%, especially at least 30 wt.%, particularly preferably 25 to 45 wt.%, in particular 30 to 42 wt.%, especially 35 to 40 wt.%, in each case based on the total mass of the cleaning agent.

[0084] Alternatively, a mixture of sorbitol and 1,2-propylene glycol can be used. The sorbitol is preferably used in an amount of 0.1 to 50 wt.%, in particular in an amount of 15 to 45 wt.%, particularly preferably in an amount of 20 to 40 wt.%. The 1,2-propylene glycol is preferably used in an amount of 1 to 20 wt.%, in particular in an amount of 5 to 15 wt.%, particularly preferably in an amount of 8 to 12 wt.%, in each case based on the total mass of the cleaning agent, wherein the total amount of sorbitol and 1,2-propylene glycol is preferably at least 20 wt.%, in particular at least 25 wt.%, especially at least 30 wt.%, particularly preferably 25 to 45 wt.%, in particular 30 to 42 wt.%, especially 35 to 40 wt.%, in each case based on the total mass of the cleaning agent.

[0085] In various embodiments of the invention, the cleaning agents are characterized in that the mass ratio of glycerin to 1,2-propylene glycol is greater than 2:1.

[0086] The cleaning agent may also be a phosphate-containing cleaning agent, in particular a phosphate-containing automatic dishwashing detergent. The phosphates are preferably present in the form of polyphosphates. Polyphosphates that can be used according to the invention include, for example, tripolyphosphates, pyrophosphates, and metaphosphates, and in particular their sodium or potassium salts. Tripolyphosphates are preferably used.

[0087] The tripolyphosphates (or triphosphates) usable according to the invention are condensation products of orthophosphoric acid (H 3 PO 4 ) with the empirical formula P 3 O 10 5-<, which are usually used in the form of their salts, preferably the alkali metal or alkaline earth metal salts, more preferably in the form of their alkali metal salts. Tripolyphosphate salts are generally hygroscopic, white, odorless, non-flammable solids that are readily soluble in water. According to the invention, in particular the potassium salt of tripolyphosphate (K 5 P 3 O 10 ) or a mixture of the potassium salt of tripolyphosphate and the sodium salt of tripolyphosphate (Na 5 P 3 O 10 ) is used. Most preferably, exclusively the potassium salt of tripolyphosphate is used.

[0088] The weight proportion of the polyphosphates, in particular of the tripolyphosphate, in the total weight of the cleaning agent according to the invention is preferably from 0.1 to 30 wt.%, in particular from 1 to 28 wt.%, particularly preferably from 5 to 25 wt.%, even more preferably from 10 to 23 wt.%.

[0089] The cleaning agents can preferably contain one or more non-phosphate-containing builders (builders / co-builders) (optionally in addition to or instead of the at least one phosphate-containing builder component). The weight fraction of this at least one non-phosphate-containing builder component in addition to that of a phosphate-containing builder component in the total weight of the agents according to the invention is preferably 0.1 to 10 wt.% and in particular 2 to 7 wt.%. The weight fraction of these builders other than the at least one non-phosphate-containing builder component in the total weight of the agents according to the invention is preferably 0.1 to 60 wt.% and in particular 2 to 45 wt.%.These non-phosphate-containing builder components / builders include in particular carbonates, citrates, phosphonates, MGDA (methylglycinediacetic acid) or its salts, GLDA (glutamic acid-N,N-diacetic acid) or its salts, EDDS (ethylenediamine-N,N'-disuccinic acid) or its salts, organic cobuilders and silicates.

[0090] For example, it is possible to use carbonate(s) and / or hydrogen carbonate(s), preferably alkali carbonate(s), particularly preferably sodium carbonate.

[0091] Organic cobuilders include, in particular, polycarboxylates / polycarboxylic acids, polymeric carboxylates, aspartic acid, polyacetals, dextrins, and organic cobuilders. These substance classes are described below.

[0092] Useful organic builders include, for example, polycarboxylic acids, which can be used in the form of the free acid and / or their sodium salts. Polycarboxylic acids are understood to be carboxylic acids that carry more than one acid function. Examples include citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid,

[0093] Maleic acid, fumaric acid, sugar acids, aminocarboxylic acids, nitrilotriacetic acid (NTA), provided such use is acceptable for ecological reasons, and mixtures thereof. In addition to their builder effect, the free acids typically also have the property of an acidifying component and thus also serve to adjust a lower and milder pH value of cleaning agents. Citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof are particularly suitable.

[0094] Particularly preferred cleaning agents contain citrate builders, for example sodium or potassium citrate, as one of their essential non-phosphate-containing builder components. Cleaning agents containing 1 to 10 wt.%, preferably 2 to 5 wt.%, of citrate are preferred according to the invention.

[0095] 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.

[0096] Suitable polymers are, in particular, polyacrylates, which preferably have a molecular weight of 2000 to 20,000 g / mol. Due to their superior solubility, short-chain polyacrylates, which have molecular weights of 2000 to 10,000 g / mol, and particularly preferably of 3000 to 5000 g / mol, may be preferred from this group.

[0097] The cleaning agents can also contain phosphonates as builders. A hydroxyalkane and / or aminoalkanephosphonate is preferably used as the phosphonate compound. Among the hydroxyalkanephosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance. Ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues are preferred as aminoalkanephosphonates. Phosphonates are preferably present in the agents in amounts of 0.1 to 10 wt.%, in particular in amounts of 0.5 to 8 wt.%, based in each case on the total weight of the cleaning agent.

[0098] The cleaning agents can also contain, as a further builder component, crystalline layered silicates of the general formula NaMSi x O 2x+1 y H 2 O, in which M is sodium or hydrogen, x is a number from 1.9 to 22, preferably from 1.9 to 4, with particularly preferred values ​​for x being 2, 3 or 4, and y is a number from 0 to 33, preferably from 0 to 20. Amorphous sodium silicates with a modulus Na 2 O:SiO 2 of 1:2 to 1:3.3, preferably from 1:2 to 1:2.8 and in particular from 1:2 to 1:2.6, which are preferably delayed in dissolution and have secondary washing properties, can also be used.

[0099] In preferred cleaning agents, the silicate content, based on the total weight of the cleaning agent, is limited to amounts below 10 wt.%, preferably below 5 wt.%, and especially below 2 wt.%. Particularly preferred cleaning agents are silicate-free.

[0100] The cleaning agents according to the invention may further contain a sulfopolymer. The weight fraction of the sulfopolymer in the total weight of the cleaning agent according to the invention is preferably from 0.1 to 20 wt. %, in particular from 0.5 to 18 wt. %, particularly preferably from 1.0 to 15 wt. %, in particular from 4 to 14 wt. %, especially from 6 to 12 wt. %. The sulfopolymer is usually used in the form of an aqueous solution, with the aqueous solutions typically containing from 20 to 70 wt. %, in particular from 30 to 50 wt. %, preferably from about 35 to 40 wt. % of sulfopolymer(s).

[0101] The sulfopolymer used is preferably a copolymeric polysulfonate, preferably a hydrophobically modified copolymeric polysulfonate.

[0102] The copolymers can have two, three, four or more different monomer units.

[0103] Preferred copolymeric polysulfonates contain, in addition to monomer(s) containing sulfonic acid groups, at least one monomer from the group of unsaturated carboxylic acids.

[0104] As unsaturated carboxylic acid(s) it is / are particularly preferred to use unsaturated carboxylic acids of the formula R 1< (R 2< )C=C(R 3< )COOH, in which R 1< to R 3< independently of one another represent -H, -CH 3 , a straight-chain or branched saturated alkyl radical having 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical having 2 to 12 carbon atoms, alkyl or alkenyl radicals substituted by -NH 2 , -OH or -COOH as defined above or represents -COOH or -COOR 4<, where R 4< is a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms.

[0105] Particularly preferred unsaturated carboxylic acids are acrylic acid, methacrylic acid, ethacrylic acid, α-chloroacrylic acid, α-cyanoacrylic acid, crotonic acid, α-phenylacrylic acid, maleic acid, maleic anhydride, fumaric acid, itaconic acid, citraconic acid, methylenemalonic acid, sorbic acid, cinnamic acid, or mixtures thereof. Unsaturated dicarboxylic acids can, of course, also be used.

[0106] Among the sulfonic acid group-containing monomers, those of the formula R 5< (R 6< )C=C(R 7< )-X-SO 3 H are preferred, in which R 5< to R 7< independently of one another represent -H, -CH 3 , a straight-chain or branched saturated alkyl radical having 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical having 2 to 12 carbon atoms, alkyl or alkenyl radicals substituted by -NH 2 , -OH or -COOH or -COOH or -COOR 4<, where R 4< is a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms, and X represents an optionally present spacer group selected from -(CH 2 ) n - with n = 0 to 4, -COO-(CH 2 ) k - with k = 1 to 6, -C(O)-NH-C(CH 3 ) 2 -, -C(O)-NH-C(CH 3 ) 2 -CH 2 - and -C(O)-NH-CH(CH 3 )-CH 2 -.

[0107] Preferred among these monomers are those of the formulas H 2 C=CH-X-SO 3 H H 2 C=C(CH 3 )-X-SO 3 H HO 3 SX-(R 6< )C=C(R 7< )-X-SO 3 H, in which R 6< and R 7< are independently selected from -H, -CH 3 , -CH 2 CH 3 , -CH 2 CH 2 CH 3 and -CH(CH 3 ) 2 and X represents an optionally present spacer group selected from -(CH 2 ) n - with n = 0 to 4, -COO-(CH 2 ) k - with k = 1 to 6, -C(O)-NH-C(CH 3 ) 2 -, -C(O)-NH-C(CH 3 ) 2 -CH 2 - and -C(O)-NH-CH(CH 3 )-CH 2 -.

[0108] Particularly preferred monomers containing sulfonic acid groups are 1-acrylamido-1-propanesulfonic acid, 2-acrylamido-2-propanesulfonic acid, 2-acrylamido-2-methyl-1-propanesulfonic acid, 2-methacrylamido-2-methyl-1-propanesulfonic acid, 3-methacrylamido-2-hydroxypropanesulfonic acid, allylsulfonic acid, methallylsulfonic acid, allyloxybenzenesulfonic acid, methallyloxybenzenesulfonic acid, 2-hydroxy-3-(2-propenyloxy)propanesulfonic acid, 2-methyl-2-propen1-sulfonic acid, styrenesulfonic acid, vinylsulfonic acid, 3-sulfopropyl acrylate, 3-sulfopropyl methacrylate, sulfomethacrylamide, sulfomethylmethacrylamide and mixtures of the acids mentioned or their water-soluble salts.

[0109] In the polymers, the sulfonic acid groups may be present entirely or partially in neutralized form, i.e., the acidic hydrogen atom of the sulfonic acid group in some or all of the sulfonic acid groups may be exchanged for metal ions, preferably alkali metal ions and especially sodium ions. The use of partially or fully neutralized copolymers containing sulfonic acid groups is preferred according to the invention.

[0110] The monomer distribution of the copolymers preferably used according to the invention is, for copolymers which contain only monomers containing carboxylic acid groups and monomers containing sulfonic acid groups, preferably in each case 5 to 95 wt.%, particularly preferably the proportion of the monomer containing sulfonic acid groups is 50 to 90 wt.% and the proportion of the monomer containing carboxylic acid groups is 10 to 50 wt.%, the monomers are preferably selected from those mentioned above.

[0111] The molecular weight of the sulfo-copolymers preferably used according to the invention can be varied to adapt the properties of the polymers to the desired application. Preferred cleaning agents are characterized by the copolymers having molecular weights of 2,000 to 200,000 gmol -1 , preferably of 4,000 to 25,000 gmol -1 , and in particular of 5,000 to 15,000 gmol -1 .

[0112] In a further preferred embodiment, the copolymers comprise, in addition to the carboxyl-containing monomer and the sulfonic acid-containing monomer, at least one nonionic, preferably hydrophobic monomer. The use of these hydrophobically modified polymers has been shown to improve, in particular, the rinse performance of automatic dishwashing detergents according to the invention.

[0113] Anionic copolymers comprising carboxylic acid group-containing monomers, sulfonic acid group-containing monomers and nonionic monomers, in particular hydrophobic monomers, are therefore preferred according to the invention.

[0114] Monomers of the general formula R 1< (R 2< )C=C(R 3< )-XR 4< are preferably used as non-ionic monomers, in which R 1< to R 3< independently of one another represent -H, -CH 3 or -C 2 H 5, X represents an optionally present spacer group selected from -CH 2 -, -C(O)O- and -C(O)-NH-, and R 4< represents a straight-chain or branched saturated alkyl radical having 2 to 22 carbon atoms or an unsaturated, preferably aromatic radical having 6 to 22 carbon atoms.

[0115] Particularly preferred non-ionic monomers are butene, isobutene, pentene, 3-methylbutene, 2-methylbutene, cyclopentene, hexene, hexene-1, 2-methylpentene-1, 3-methylpentene-1, cyclohexene, methylcyclopentene, cycloheptene, methylcyclohexene, 2,4,4-trimethylpentene-1, 2,4,4-trimethylpentene-2, 2,3-dimethylhexene-1, 2,4-dimethylhexene-1, 2,5-dimethylhexene-1, 3,5-dimethylhexene-1, 4,4-dimehtylhexane-1, ethylcyclohexyne, 1-octene, α-olefins having 10 or more carbon atoms such as 1-decene, 1-dodecene, 1-hexadecene, 1-Octadecene and C 22 -α-olefin, 2-styrene, α-methylstyrene, 3-methylstyrene, 4-propylstyrene, 4-cyclohexylstyrene, 4-dodecylstyrene, 2-ethyl-4-benzylstyrene, 1-vinylnaphthalene, 2-vinylnaphthalene, methyl acrylate, ethyl acrylate, propyl acrylate, butyl acrylate, pentyl acrylate, hexyl acrylate, methyl methacrylate, N-(methyl)acrylamide, 2-ethylhexyl acrylate, 2-ethylhexyl methacrylate, N-(2-Ethylhexyl)acrylamide, octyl acrylate, octyl methacrylate, N -(Octyl)acrylamide, acrylic acid lauryl ester, methacrylic acid lauryl ester, N -(Lauryl)acrylamide, stearyl acrylate, stearyl methacrylate, N -(Stearyl)acrylamide, acrylic acid behenyl ester, methacrylic acid behenyl ester and N -(Behenyl)acrylamide or mixtures thereof.

[0116] The monomer distribution of the hydrophobically modified copolymers preferably used according to the invention is preferably 5 to 80 wt.% in relation to the sulfonic acid group-containing monomer, the hydrophobic monomer and the carboxylic acid group-containing monomer, particularly preferably the proportion of the sulfonic acid group-containing monomer and the hydrophobic monomer is 5 to 30 wt.% in each case and the proportion of the carboxylic acid group-containing monomer is 60 to 80 wt.%, the monomers are preferably selected from those mentioned above.

[0117] In addition to the aforementioned builders, the cleaning agents may contain alkali metal hydroxides. These alkali carriers are preferably used in the cleaning agents only in small amounts, preferably in amounts below 10 wt.%, preferably below 6 wt.%, preferably below 5 wt.%, each based on the total weight of the cleaning agent. Preferred cleaning agents according to the invention are free of alkali metal hydroxides.

[0118] The cleaning agents according to the invention preferably further contain at least one nonionic surfactant. All nonionic surfactants known to those skilled in the art can be used as nonionic surfactants. Low-foaming nonionic surfactants are preferred, in particular alkoxylated, especially ethoxylated, low-foaming nonionic surfactants. The automatic dishwashing detergents particularly preferably contain nonionic surfactants from the group of alkoxylated alcohols.

[0119] Particularly preferred are nonionic surfactants with a melting point above room temperature. Nonionic surfactant(s) with a melting point above 20°C, preferably above 25°C, particularly preferably between 25 and 60°C, and especially between 26.6 and 43.3°C, are particularly preferred.

[0120] Preferred surfactants come from the group of alkoxylated nonionic surfactants, especially ethoxylated primary alcohols and mixtures of these surfactants with structurally more complex surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants). Such (PO / EO / PO) nonionic surfactants are also characterized by good foam control.

[0121] Particularly preferred nonionic surfactants in the context of the present invention are low-foaming nonionic surfactants which have alternating ethylene oxide and alkylene oxide units. Among these, surfactants with EO-AO-EO-AO blocks are preferred, with one to ten EO or AO groups being bonded to one another before a block of the respective other groups follows. These are nonionic surfactants of the general formula preferred in which R 1< represents a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 alkyl or alkenyl radical; each group R 2< or R 3< is independently selected from -CH 3 , -CH 2 CH 3 , -CH 2 CH 2 -CH 3 , CH(CH 3 ) 2 and the indices w, x, y, z independently represent integers from 1 to 6.

[0122] Thus, nonionic surfactants which have a C 9-15 alkyl radical with 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units, followed by 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units are particularly preferred.

[0123] Preferred nonionic surfactants are those of the general formula R 1< -CH(OH)CH 2 O-(AO) w -(A'O) x -(A"O) y -(A‴O) z -R 2< , in which R 1< represents a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 alkyl or alkenyl radical; R 2< represents H or a linear or branched hydrocarbon radical having 2 to 26 carbon atoms; A, A', A" and A‴ independently of one another represent a radical from the group -CH 2 CH 2 , -CH 2 CH 2 -CH 2 , -CH 2 -CH(CH 3 ), -CH 2 -CH 2 -CH 2 -CH 2 , -CH 2 -CH(CH 3 )-CH 2 -, -CH 2 -CH(CH 2 -CH 3 ), w, x, y and z represent values ​​between 0.5 and 120, where x, y and / or z can also be 0.

[0124] By adding the above-mentioned non-ionic surfactants of the general formula R 1< -CH(OH)CH 2 O-(AO) w -(A'O) x -(A"O) y -(A‴O) z -R 2< , hereinafter also referred to as "hydroxy mixed ethers", the cleaning performance of the preparations according to the invention can be significantly improved, both in comparison to surfactant-free systems and in comparison to systems which contain alternative non-ionic surfactants, for example from the group of polyalkoxylated fatty alcohols.

[0125] Particularly preferred are those end-capped, poly(oxyalkylated) nonionic surfactants which, according to the formula R 1< O[CH 2 CH 2 O] x CH 2 CH(OH)R 2< , in addition to a radical R 1< which stands for linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 2 to 30 carbon atoms, preferably having 4 to 22 carbon atoms, furthermore have a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radical R 2< having 1 to 30 carbon atoms, where x stands for values ​​between 1 and 90, preferably for values ​​between 30 and 80 and in particular for values ​​between 30 and 60.

[0126] Particularly preferred surfactants are those of the formula R 1< O[CH 2 CH(CH 3 )O] x [CH 2 CH 2 O] y CH 2 CH(OH)R 2< , in which R 1< is a linear or branched aliphatic hydrocarbon radical having 4 to 18 carbon atoms or mixtures thereof, R 2< is a linear or branched hydrocarbon radical having 2 to 26 carbon atoms or mixtures thereof and x is between 0.5 and 1.5 and y is at least 15.

[0127] The group of these non-ionic surfactants includes, for example, the C 2-26 fatty alcohol (PO) 1 -(EO) 15-40 -2-hydroxyalkyl ethers, in particular the C 8-10 fatty alcohol (PO) 1 -(EO) 22 -2-hydroxydecyl ethers.

[0128] Particularly preferred are also those end-capped poly(oxyalkylated) nonionic surfactants of the formula R 1< O[CH 2 CH 2 O] x [CH 2 CH(R 3< )O] y CH 2 CH(OH)R 2< , in which R 1< and R 2< independently of one another represent a linear or branched, saturated or mono- or polyunsaturated hydrocarbon radical having 2 to 26 carbon atoms, R 3< independently of one another is selected from -CH 3 , -CH 2 CH 3 , -CH 2 CH 2 -CH 3 , -CH(CH 3 ) 2 , but preferably represents -CH 3 , and x and y independently of one another represent values ​​between 1 and 32, with nonionic surfactants with R 3< = -CH 3 and values ​​for x from 15 to 32 and y from 0.5 to 1.5 being very particularly preferred.

[0129] Further nonionic surfactants which can preferably be used are the end-group-capped poly(oxyalkylated) nonionic surfactants of the formula R 1< O[CH 2 CH(R 3< )O] x [CH 2 ] k CH(OH)[CH 2 ] j OR 2< , in which R 1< and R 2< are linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 1 to 30 carbon atoms, R 3< is H or a methyl, ethyl, n-propyl, isopropyl, n-butyl, 2-butyl or 2-methyl-2-butyl radical, x is between 1 and 30, k and j are between 1 and 12, preferably between 1 and 5. If the value x ≥ 2, each R 3< in the above formula R 1< O[CH 2 CH(R 3< )O] x [CH 2 ] k CH(OH)[CH 2 ] j OR 2< can be different. R 1< and R 2< are preferably linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 6 to 22 carbon atoms, with radicals having 8 to 18 carbon atoms being particularly preferred.For the radical R 3<, H, -CH 3 or -CH 2 CH 3 are particularly preferred. Particularly preferred values ​​for x are in the range from 1 to 20, in particular from 6 to 15.

[0130] As described above, each R 3< in the above formula can be different if x ≥ 2. This allows the alkylene oxide unit in the square brackets to be varied. For example, if x is 3, the radical R 3< can be selected to form ethylene oxide (R 3< = H) or propylene oxide (R 3< = CH 3 ) units, which can be joined together in any order, for example (EO)(PO)(EO), (EO)(EO)(PO), (EO)(EO)(EO), (PO)(EO)(PO), (PO)(PO)(EO) and (PO)(PO)(PO). The value 3 for x has been chosen here as an example and can certainly be larger, whereby the range of variation increases with increasing values ​​of x and includes, for example, a large number of (EO) groups combined with a small number of (PO) groups, or vice versa.

[0131] Particularly preferred end-capped poly(oxyalkylated) alcohols of the above formula have values ​​of k = 1 and j = 1, so that the above formula is simplified to R 1< O[CH 2 CH(R 3< )O] x CH 2 CH(OH)CH 2 OR 2<. In the latter formula, R 1<, R 2< and R 3< are as defined above and x stands for numbers from 1 to 30, preferably from 1 to 20 and in particular from 6 to 18. Particular preference is given to surfactants in which the radicals R 1< and R 2< have 9 to 14 C atoms, R 3< stands for H and x assumes values ​​from 6 to 15.

[0132] Finally, the non-ionic surfactants of the general formula R 1< -CH(OH)CH 2 O-(AO) w -R 2< have proven to be particularly effective, in which R 1< represents a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 alkyl or alkenyl radical; R 2< represents a linear or branched hydrocarbon radical having 2 to 26 carbon atoms; A represents a radical from the group CH 2 CH 2 , CH 2 CH 2 CH 2 , CH 2 CH(CH 3 ), preferably CH 2 CH 2 , and w represents values ​​between 1 and 120, preferably 10 to 80, in particular 20 to 40.

[0133] The group of these non-ionic surfactants includes, for example, the C 4-22 fatty alcohol (EO) 10-80 -2-hydroxyalkyl ethers, in particular the C 8-12 fatty alcohol (EO) 22 -2-hydroxydecyl ethers and the C 4 - 22 fatty alcohol (EO) 40-80 -2-hydroxyalkyl ethers.

[0134] In various embodiments of the invention, the corresponding non-end-capped hydroxy mixed ethers can also be used instead of the above-defined end-capped hydroxy mixed ethers. These can satisfy the above formulas, but where R 2< is hydrogen and R 1< , R 3< , A, A', A", A‴, w, x, y, and z are as defined above.

[0135] Preferred liquid cleaning agents are characterized in that the cleaning agent contains at least one non-ionic surfactant, preferably a non-ionic surfactant from the group of hydroxy mixed ethers, wherein the weight fraction of the non-ionic surfactant in the total weight of the cleaning agent is preferably 0.1 to 10 wt.%, preferably 0.5 to 8.0 wt.% and in particular 1.0 to 4.0 wt.%.

[0136] In general, the pH of the cleaning agent can be adjusted using conventional pH regulators, with the pH being selected depending on the desired application. In various embodiments, the pH is in a range from 5.5 to 10.5, preferably 5.5 to 9.5, more preferably 7 to 9, in particular greater than 7, especially in the range 7.5 to 8.5. Acids and / or alkalis, preferably alkalis, serve as pH adjusters. Suitable acids are, in particular, organic acids such as acetic acid, citric acid, glycolic acid, lactic acid, succinic acid, adipic acid, malic acid, tartaric acid, and gluconic acid, or even amidosulfonic acid. In addition, the mineral acids hydrochloric acid, sulfuric acid, and nitric acid, or mixtures thereof, can also be used. Suitable bases come from the group of alkali and alkaline earth metal hydroxides and carbonates, in particular alkali metal hydroxides, of which potassium hydroxide and especially sodium hydroxide are preferred.However, volatile alkali is particularly preferred, for example in the form of ammonia and / or alkanolamines, which can contain up to 9 carbon atoms per molecule. The alkanolamine is preferably selected from the group consisting of mono-, di-, triethanolamine, and propanolamine, and mixtures thereof. The alkanolamine is preferably present in the agents according to the invention in an amount of 0.5 to 10 wt.%, in particular in an amount of 1 to 6 wt.%.

[0137] To adjust and / or stabilize the pH, the agent according to the invention may contain one or more buffer substances (INCI buffering agents), typically in amounts of 0.001 to 5 wt.%. Buffer substances that are also complexing agents or even chelating agents (INCI chelating agents) are preferred. Particularly preferred buffer substances are citric acid or citrates, especially sodium and potassium citrates, for example trisodium citrate·2H2O and tripotassium citrate·H2O.

[0138] The agents according to the invention preferably contain at least one further component, preferably selected from the group consisting of anionic, cationic and amphoteric surfactants, bleaching agents, bleach activators, bleach catalysts, polymers, non-amylase and non-protease enzymes, thickeners, sequestering agents, electrolytes, corrosion inhibitors, in particular silver protectants, glass corrosion inhibitors, foam inhibitors, dyes, fragrances, bittering agents, and antimicrobial agents.

[0139] Preferred anionic surfactants are fatty alcohol sulfates, fatty alcohol ether sulfates, dialkyl ether sulfates, monoglyceride sulfates, alkylbenzenesulfonates, olefinsulfonates, alkanesulfonates, ethersulfonates, n-alkyl ether sulfonates, estersulfonates, and ligninsulfonates. Also usable within the scope of the present invention are fatty acid cyanamides, sulfosuccinates (sulfosuccinic acid esters), in particular sulfosuccinic acid mono- and di-C 8 -C 18 alkyl esters, sulfosuccinamates, sulfosuccinamides, fatty acid isethionates, acylaminoalkanesulfonates (fatty acid taurides), fatty acid sarcosinates, ethercarboxylic acids, and alkyl (ether) phosphates, as well as α-sulfofatty acid salts, acylglutamates, monoglyceride disulfates, and alkyl ethers of glycerol disulfate.

[0140] The anionic surfactants are preferably used as sodium salts, but can also be present as other alkali or alkaline earth metal salts, for example potassium or magnesium salts, as well as in the form of ammonium or mono-, di-, tri- or tetraalkylammonium salts, and in the case of sulfonates also in the form of their corresponding acid, e.g. dodecylbenzenesulfonic acid.

[0141] Suitable amphoteric surfactants are, for example, betaines of the formula (R iii< )(R iv< )(R v< )N +< CH 2 COO -< , in which R iii< is an alkyl radical optionally interrupted by heteroatoms or heteroatom groups having 8 to 25, preferably 10 to 21 carbon atoms and R iv< and R v< are identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C 10 -C 18 -alkyldimethylcarboxymethylbetaine and C 11 -C 17 -alkylamidopropyldimethylcarboxymethylbetaine.

[0142] Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R vi< )(R vii< )(R viii< )(R ix< )N +< X -< , in which R vi< to R ix< represent four identical or different, in particular two long-chain and two short-chain, alkyl radicals and X -< represents an anion, in particular a halide ion, for example didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride and mixtures thereof. 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. By using quaternary surface-active compounds with antimicrobial activity, the agent can be given an antimicrobial effect or its already existing antimicrobial effect due to other ingredients can be improved.

[0143] In addition to the above-mentioned proteases and amylases, the enzymes include, in particular, lipases, hemicellulases, cellulases, perhydrolases, and oxidoreductases, as well as preferably mixtures thereof. These enzymes are essentially of natural origin; based on the natural molecules, improved variants are available for use in cleaning agents and are therefore preferably used. Cleaning agents according to the invention preferably contain these enzymes in total amounts of 1 × 10 -6 to 5 wt.%, based on active protein.

[0144] Lipases or cutinases can be used according to the invention, in particular because of their triglyceride-cleaving activities, but also to produce from suitable precursors in situ These include, for example, the peracids originally from Humicola lanuginosa ( Thermomyces lanuginosus ) available or further developed lipases, especially those with the amino acid exchange D96L.

[0145] Enzymes collectively referred to as hemicellulases can also be used. These include, for example, mannanases, xanthan lyases, pectin lyases (=pectinases), pectinesterases, pectate lyases, xyloglucanases (=xylanases), pullulanases, and β-glucanases.

[0146] 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, organic compounds, particularly aromatic ones, that interact with the enzymes are also added to enhance the activity of the respective oxidoreductases (enhancers) or to ensure electron flow in the event of significantly different redox potentials between the oxidizing enzymes and the soils (mediators).

[0147] The enzymes can be packaged and formulated as described above for the proteases and amylases.

[0148] Zinc salts, especially zinc acetate, are preferably used as glass corrosion inhibitors. Glass corrosion inhibitors are preferably present in the compositions according to the invention in an amount of 0.05 to 5 wt.%, in particular in an amount of 0.1 to 2 wt.%.

[0149] In various embodiments, the cleaning agent has a viscosity above 2,000 mPas (Brookfield Viscometer DV-II+Pro, spindle 25, 30 rpm, 20°C) immediately after production, in particular between 2,000 and 10,000 mPas. After storage, the viscosity may be higher, for example, greater than 10,000 mPas, such as in the range 10,000-50,000 mPas, preferably around 35,000 mPas (Brookfield Viscometer DV-II+Pro, spindle 25, 5 rpm, 20°C).

[0150] The cleaning agent can be contained in a water-insoluble, water-soluble, or water-dispersible package. The invention therefore also relates to kits containing the cleaning agent together with such a package. The cleaning agent can be packaged in such a way that single-dose portions are each packaged separately.

[0151] The cleaning agent according to the invention is preferably contained in a water-soluble package. The water-soluble package allows the cleaning agent to be portioned. The amount of cleaning agent in the portion pack is preferably 5 to 50 g, particularly preferably 10 to 30 g, especially 15 to 25 g.

[0152] The water-soluble wrappings / packaging are preferably deep-drawn or injection-molded bodies.

[0153] The water-soluble containers / envelopes / packaging can also be produced by injection molding. Injection molding refers to the forming of a molding compound in such a way that the compound contained in a cylinder for more than one injection molding process softens plastically under the influence of heat and flows under pressure through a nozzle into the cavity of a previously closed mold. The process is mainly used for non-hardenable molding compounds, which solidify in the mold upon cooling. Injection molding is a very economical, modern process for the production of non-cutting molded objects and is particularly suitable for automated mass production. In practice, the thermoplastic molding compounds (powders, granules, cubes, pastes, etc.) are heated.) until liquefied (up to 180°C) and then injected under high pressure (up to 140 MPa) into closed, two-part, preferably water-cooled molds consisting of a die (formerly the female mold) and core (formerly the male mold), where they cool and solidify. Piston and screw injection molding machines are suitable.

[0154] Such molded bodies can also have one, two, three, or more chambers and be filled with liquid and / or solid compositions, one of which is one of the compositions according to the invention. For example, it is possible to close the chambers on the open side either with a second molded body or with one or more water-soluble films (in particular as described herein). Thus, the release of the compositions contained in the chambers can be controlled as desired according to the desired release time. The entire agent can be released either all at once (either directly at the beginning of the cleaning cycle or at a specific time during the cleaning cycle) or by varying the film composition at specific, mutually different times within the dishwasher cycle (for example, depending on the temperature of the rinse water).

[0155] The water-soluble wrapping is preferably formed from a water-soluble film material selected from the group consisting of polymers or polymer blends. The wrapping can be formed from one or two or more layers of the water-soluble film material. The water-soluble film material of the first layer and the additional layers, if present, can be the same or different. Films that can be glued and / or sealed, for example, to form packages such as tubes or pillows after being filled with an agent are particularly preferred.

[0156] It is preferred that the water-soluble coating contains polyvinyl alcohol or a polyvinyl alcohol copolymer. Water-soluble coatings containing polyvinyl alcohol or a polyvinyl alcohol copolymer exhibit good stability with sufficiently high water solubility, particularly cold water solubility.

[0157] Suitable water-soluble films for producing the water-soluble coating are preferably based on a polyvinyl alcohol or a polyvinyl alcohol copolymer whose molecular weight is in the range from 10,000 to 1,000,000 gmol -1< , preferably from 20,000 to 500,000 gmol -1< , particularly preferably from 30,000 to 100,000 gmol -1< and in particular from 40,000 to 80,000 gmol -1<.

[0158] Polyvinyl alcohol is typically produced by hydrolysis of polyvinyl acetate, since the direct synthesis route is not possible. The same applies to polyvinyl alcohol copolymers, which are produced from polyvinyl acetate copolymers. It is preferred if at least one layer of the water-soluble coating comprises a polyvinyl alcohol whose degree of hydrolysis is 70 to 100 mol%, preferably 80 to 90 mol%, particularly preferably 81 to 89 mol%, and especially 82 to 88 mol%.

[0159] A polymer selected from the group comprising (meth)acrylic acid-containing (co)polymers, polyacrylamides, oxazoline polymers, polystyrenesulfonates, polyurethanes, polyesters, polyethers, polylactic acid, or mixtures of the above polymers can additionally be added to a polyvinyl alcohol-containing film material suitable for producing the water-soluble wrapping. A preferred additional polymer is polylactic acid.

[0160] Preferred polyvinyl alcohol copolymers comprise, in addition to vinyl alcohol, dicarboxylic acids as further monomers. Suitable dicarboxylic acids are itaconic acid, malonic acid, succinic acid, and mixtures thereof, with itaconic acid being preferred.

[0161] Likewise preferred polyvinyl alcohol copolymers comprise, in addition to vinyl alcohol, an ethylenically unsaturated carboxylic acid, its salt, or its ester. Particularly preferably, such polyvinyl alcohol copolymers contain, in addition to vinyl alcohol, acrylic acid, methacrylic acid, acrylic acid esters, methacrylic acid esters, or mixtures thereof.

[0162] It may be preferred for the film material to contain further additives. The film material may contain, for example, plasticizers such as dipropylene glycol, ethylene glycol, diethylene glycol, propylene glycol, glycerin, sorbitol, mannitol, or mixtures thereof. Further additives include, for example, release aids, fillers, crosslinking agents, surfactants, antioxidants, UV absorbers, antiblocking agents, anti-adhesive agents, or mixtures thereof.

[0163] Suitable water-soluble films for use in the water-soluble wrappers of the water-soluble packages according to the invention are films sold by MonoSol LLC, for example, under the designation M8630, C8400, or M8900. Other suitable films include films designated Solublon®< PT, Solublon®< GA, Solublon®< KC, or Solublon®< KL by Aicello Chemical Europe GmbH, or VF-HP films by Kuraray.

[0164] The cleaning agents according to the invention can be used as dishwashing agents, in particular automatic dishwashing agents. The corresponding use is also the subject of the invention. The invention also relates to a dishwashing process, in particular an automatic dishwashing process, in which a cleaning agent according to the invention is used.

[0165] The present application therefore further relates to a method for cleaning dishes in a dishwasher, in which the agent is metered into the interior of a dishwasher during the course of a dishwashing program, before the start of the main wash cycle or during the main wash cycle. The metering or introduction of the agent into the interior of the dishwasher can be done manually, but preferably the agent is metered into the interior of the dishwasher by means of the metering chamber. In various embodiments of the invention, the (washing) temperature in such dishwashing methods is preferably 50°C or lower, particularly preferably 45°C or lower, even more preferably 40°C or lower.

[0166] All enzyme combinations described as particular embodiments in connection with the cleaning agents disclosed herein can also be used in the described methods and uses. Example 1: Liquid dishwashing detergent formulations containing proteases

[0167] Table 1: Composition of the automatic dishwashing detergent (data in wt.% active substance) Recipe 1 Recipe 2 Glycerin 26 26 1,2-propylene glycol 10,00 10,00 Sulfopolymer 8,5 8,5 Potassium tripolyphosphate 21 21 Na Citrate Dihydrate 4,00 4,00 HEDP 2,40 2,40 Nonionic surfactant 2,00 2,00 Ethanolamine 3,50 3,50 Polyacrylate 0,20 0,20 Protease 2 0,00 0,20 Amylase 2 0,015 0,015 Protease 1 0,3 0,1 Amylase 1 0,00 0,00 Zinc acetate 0,20 0,20 Bitter agent, preservative, colorant, perfume, water Ad 100 Ad 100

[0168] Information refers to the weight proportion of the respective active protein Protease1 = solid, SEQ ID NO:8 Protease 2 = liquid, SEQ ID NO:9 Amylase 1 = solid, variant of α-amylase from Bacillus sp. No. 707 Amylase 2 = liquid, Stainzyme ®< 12L (Novozymes, DK) Cleaning performance on protease-sensitive egg yolk soils

[0169] In a Miele GSL dishwasher, dishes soiled with egg yolk were washed at 50°C (normal program) and 21°dH using a liquid dishwashing detergent formulation (see Table 1 for composition: formulation 1 = comparison formulation, formulation 2 = invention). After each wash cycle, the cleaning performance was determined gravimetrically (evaluation from 1-10; the higher the value, the better the performance; differences of at least 1 are significant). The results for the tested formulations are listed in Table 2 as arithmetic means. Higher values ​​indicate better cleaning performance. Table 2: Cleaning performance on egg yolk egg yolk Recipe 1 2,6 Recipe 2 3,5

[0170] Table 2 clearly shows that the combination of the two different enzyme formulations leads to a significant improvement in cleaning performance, even though both formulations have the same active enzyme content. Example 2: Liquid dishwashing detergent formulations containing amylases

[0171] Table 3: Composition of the automatic dishwashing detergent (data in wt.% active substance) Recipe 3 Recipe 4 Recipe 5 Glycerin 26 26 26 1,2-propylene glycol 10,00 10,00 10,00 Sulfopolymer 8,5 8,5 8,5 Potassium tripolyphosphate 21 21 21 Na Citrate Dihydrate 4,00 4,00 4,00 HEDP 2,40 2,40 2,40 Nonionic surfactant 2,00 2,00 2,00 Ethanolamine 3,50 3,50 3,50 Polyacrylate 0,20 0,20 0,20 Protease 2 0,20 0,20 0,20 Amylase 2 0,075 0,00 0,015 Protease 1 0,00 0,00 0,00 Amylase 1 0,025 0,05 0,00 Zinc acetate 0,20 0,20 0,20 Bitter agent, preservative, colorant, perfume, water Ad 100 Ad 100 Ad 100 Protease1 = solid, SEQ ID NO:8 Protease 2 = liquid, SEQ ID NO:9 Amylase 1 = solid, variant of α-amylase from Bacillus sp. No. 707 Amylase 2 = liquid, Stainzyme ®< 12L (Novozymes, DK)

[0172] In a Miele GSL dishwasher, dishes soiled with porridge or spaghetti were washed at 50°C (Normal program) and 21°dH using a liquid dishwashing detergent formulation (see Table 3 for composition: formulations 4 / 5 = comparison formulation, formulation 3 = invention). After each wash cycle, the cleaning performance was visually determined according to the IKW (rating from 1-10; the higher the value, the better the performance; differences of at least 1 are significant). The results for the tested formulations are listed in Table 4 as arithmetic means. Higher values ​​indicate better cleaning performance. Table 4: Cleaning performance on porridge / spaghetti porridge spaghetti Recipe 3 7,8 3,9 Recipe 4 7,0 2,6 Recipe 5 7,3 3,6

[0173] Table 4 clearly shows that the combination according to the invention leads to an increase in cleaning performance.

Claims

1. A liquid cleaning agent, in particular an automatic dishwasher detergent, containing (1) at least one liquid enzyme formulation which contains at least one amylase (A1) and optionally at least one protease (P1); and (2) at least one solid enzyme formulation, preferably in the form of granular material, which contains at least one protease (P2) and / or at least one amylase (A2), the solid enzyme formulation being suspended homogeneously in the liquid dishwasher detergent, characterized in that a) the amylase (A1) is an AA560 α-amylase from Bacillus sp. or a functional fragment thereof; and / or b) the amylase (A1) has an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO:2 over the entire length thereof and optionally has at least one amino acid substitution at one of the positions 9, 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 195, 202, 203, 214, 231, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 320, 323, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 458, 461, 471, 482 and 484 and / or one of the deletions D183* and G184* in the numbering according to SEQ ID NO:2; and / or d) the amylase (A1) has an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO:2 over the entire length thereof and, in the numbering according to SEQ ID NO:2, has the following amino acid substitutions and / or deletions: (i) M9L + M323T; (ii) M9L + M202L / T / V / I + M323T; (iii) M9L + N195F + M202L / T / V / I + M323T; (iv) M9L + R118K + D183* + G184* + R320K + M323T + R458K; (v) M9L + R118K + D183* + G184* + M202L / T / V / I + R320K + M323T + R458K; (vi) M9L + G149A + G182T + G186A + M202L + T257I + Y295F + N299Y + M323T + A339S + E345R; (vii) M9L + G149A + G182T + G186A + M202I + T257I + Y295F + N299Y + M323T + A339S + E345R; (viii) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (ix) M9L + R118K + G149A + G182T + D183* + G184* + G186A + N195F + M202L + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (x) M9L + R118K + G149A + G182T + D183* + G184* + G186A + M202I + T257I + Y295F + N299Y + R320K + M323T + A339S + E345R + R458K; (xi) M9L + R118K + D183* + D184* + N195F + M202L + R320K + M323T + R458K; (xii) M9L + R118K + D183* + D184* + N195F + M202T + R320K + M323T + R458K; (xiii) M9L + R118K + D183* + D184* + N195F + M202I + R320K + M323T + R458K; (xiv) M9L + R118K + D183* + D184* + N195F + M202V + R320K + M323T + R458K; (xv) M9L + R118K + N150H + D183* + D184* + N195F + M202L + V214T + R320K + M323T + R458K; or (xvi) M9L + R118K + D183* + D184* + N195F + M202L + V214T + R320K + M323T + E345N + R458K.

2. The cleaning agent according to claim 1, characterized in that the cleaning agent comprises at least one first amylase (A2) and at least one second amylase (A1), (A) the first amylase (A2) being contained in the solid enzyme formulation; and (B) the second amylase (A1) being contained in the liquid enzyme formulation.

3. The cleaning agent according to claim 1 or 2, characterized in that a) the amylase (A2) is an α-amylase from Bacillus sp. No. 707 or a functional fragment or a variant thereof; and / or b) the amylase (A2) has an amino acid sequence which is at least 80% identical to the amino acid sequence specified in SEQ ID NO:1 over the entire length thereof, and optionally has at least one amino acid substitution at one of the positions 172, 202, 208, 255 and 261 in the numbering according to SEQ ID NO:1, in particular selected from the group consisting of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N and R172Q.

4. The cleaning agent according to one of claims 1 to 3, characterized in that the cleaning agent contains at least one first protease (P2) and at least one second protease (P1), (A) the first protease (P2) being contained in the solid enzyme formulation; and (B) the second protease (P1) being contained in the liquid enzyme formulation.

5. The cleaning agent according to one of claims 1 to 4, characterized in that the protease (P2) comprises a protease from Bacillus alkalophilus PB92 or a functional fragment or a variant thereof, in particular one which has an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100%, identical to the amino acid sequence specified in SEQ ID NO:4 over the entire length thereof and optionally has at least one amino acid substitution at one of the following positions 32, 33, 48-54, 58-62, 94-107, 116, 123-133, 150, 152-156, 158-161, 164, 169, 175-186, 197, 198, 203-216 in the numbering according to SEQ ID NO:4, in particular at least one amino acid substitution at one, two, three or four of the following positions 116, 126, 127, 128 and 160 in the numbering according to SEQ ID NO:4, preferably at least one, even more preferably a plurality, most preferably each, of the amino acid substitutions G116V, S126L, P127Q and / or S128A.

6. The cleaning agent according to one of claims 1 to 5, characterized in that the protease (P1) (a) comprises a subtilisin 309 from Bacillus lentus or a functional fragment or a variant thereof, in particular one which has an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100%, identical to the amino acid sequence specified in SEQ ID NO:3 over the entire length thereof and has at least one amino acid substitution at one of the positions 9, 15, 66, 212 and 239 in the numbering according to SEQ ID NO:3, preferably selected from the group consisting of S9R, A15T, V66A, N212D and Q239R; (b) comprises a subtilisin 309 from Bacillus lentus or a functional fragment or a variant thereof, in particular one which has an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100%, identical to the amino acid sequence specified in SEQ ID NO:3 over the entire length thereof and has an amino acid substitution at the position 99 and an insertion of an amino acid between the amino acids at positions 99 and 100 in the numbering according to SEQ ID NO:3, preferably selected from S99A and / or S99_G100InsD; (c) comprises an alkaline protease from Bacillus lentus DSM 5483 or a functional fragment or a variant thereof, in particular one which has an amino acid sequence which is at least 80%, preferably at least 90%, in particular 100%, identical to the amino acid sequence specified in SEQ ID NO:5 over the entire length thereof and optionally has at least one amino acid substitution at one, two, three or four of the following positions 3, 4, 99 and 199 in the numbering according to SEQ ID NO:5, in particular the amino acid substitution R99E or R99D, and optionally additionally at least one or two, preferably all three, of the amino acid substitutions S3T, V4I and V199I; or (d) has an amino acid sequence according to one of SEQ ID NOs: 6-10.

7. The cleaning agent according to one of claims 1 to 6, characterized in that (A) the solid enzyme formulation is contained in an amount of 0.01 to 5 wt.%, preferably from 0.2 to 2 wt.%, based on the total weight of the cleaning agent, the solid enzyme formulation having in particular an active enzyme content of 2 to 20 wt. %; and / or (B) the liquid enzyme formulation is contained in an amount of 0.01 to 8 wt.%, preferably from 0.3 to 6 wt.%, based on the total weight of the cleaning agent, the liquid enzyme formulation having in particular an active enzyme content of 1 to 6 wt.%.

8. The cleaning agent according to one of claims 1 to 7, characterized in that the cleaning agent contains the liquid enzyme formulation and the solid enzyme formulation in a weight ratio of 10:1 to 1:10, preferably 1:1.

9. The cleaning agent according to one of claims 1 to 8, characterized in that the cleaning agent (A) contains at least one phosphate-containing builder component, preferably a polyphosphate, in particular potassium and / or sodium triphosphate, and / or at least one non-phosphate-containing builder component or cobuilder, in particular citrate and / or phosphonate, preferably in the form of the sodium salt; (B) contains at least one polyhydric alcohol, in particular selected from glycerol and mixtures of glycerol and 1,2-propylene glycol; (C) has a water content of less than 50 wt.%, preferably less than 25 wt.%,10. The cleaning agent according to one of claims 1 to 9, characterized in that the cleaning agent contains at least one sulfopolymer.

11. The cleaning agent according to one of claims 1 to 10, characterized in that the cleaning agent further contains one or more of the substances selected from the group consisting of complexing agents, pH adjusters, nonionic, anionic, cationic and amphoteric surfactants, bleaching agents, bleach activators, bleach catalysts, polymers, non-protease and nonamylase enzymes, thickeners, sequestering agents, electrolytes, corrosion inhibitors, in particular silver protecting agents, glass corrosion inhibitors, foam inhibitors, dyes, fragrances, bitterns, and antimicrobial active ingredients.

12. The cleaning agent according to one of claims 1 to 11, characterized in that the cleaning agent is an automatic dishwasher detergent and (1) is in a pre-portioned form; and / or (2) has a plurality of compositions that are spatially separated from one another; and / or (3) is in a water-insoluble, water-soluble or water-dispersible packaging, in particular in a film containing polyvinyl alcohol.

13. A use of the cleaning agent according to one of claims 1 to 12 as a dishwasher detergent, in particular as an automatic dishwasher detergent.

14. A method for cleaning dishes in an automatic dishwasher, characterized in that a cleaning agent according to one of claims 1 to 12 is used and is dispensed into the interior of the dishwasher preferably while a dishwashing program is running, before the main washing cycle begins or during the main washing cycle.