Solid washing or cleaning agent with amylase and soluble builder

Abstract

Containing solid washing or cleaning agent: a) 5 to 70 wt% surfactant; b) at least one α-amylase, wherein the α-amylase is characterized in that it comprises an amino acid sequence which is identical to the amino acid sequence specified in SEQ ID NO:1 over its total length to at least 97%; c) 5 to 70 wt% of a water-soluble builder system.

Description

[0001] The invention relates to a solid washing or cleaning agent containing an amylase, preferably in combination with a protease, wherein the amino acid sequences have been modified, particularly with regard to use in washing and cleaning agents. The invention further relates to methods for cleaning textiles and uses of this solid washing or cleaning agent.

[0002] Proteases are among the most technically important enzymes. They are the longest-established enzymes in detergents and cleaning agents and are found in virtually all modern, high-performance detergents and cleaning products. They break down protein-based soils on the items being cleaned. Of particular importance are subtilisin-type proteases (subtilases, subtilopeptidases, EC 3.4.21.62), which are serine proteases due to their catalytically active amino acids. They act as non-specific endopeptidases and hydrolyze any amide bonds located within peptides or proteins. Their optimum pH is usually in the strongly alkaline range. An overview of this family is provided, for example, by the article “Subtilases: subtilisin-like proteases” by R. Siezen, pages 75-95 in “Subtilisin enzymes”, edited by R. Bott and C. Betzel, New York, 1996. subtilases are naturally produced by microorganisms.Among these, the subtilisins produced and secreted by Bacillus species are particularly noteworthy as the most important group within the subtilases.

[0003] Proteases are modified using methods known from the prior art, either selectively or randomly, and thus optimized for use in detergents and cleaning agents, for example. These methods include point mutagenesis, deletion or insertion mutagenesis, or fusion with other proteins or protein fragments. Accordingly, optimized variants are known for most proteases known from the prior art.

[0004] Other enzymes used in detergents and cleaning agents are amylases. Alpha-amylases, in particular, are among the most technically important enzymes. Their use in detergents and cleaning agents is industrially established, and they are included in many modern, high-performance detergents and cleaning agents. An alpha-amylase is an enzyme that catalyzes the hydrolysis of the internal α(1-4) glycoside bonds of amylose, but not the cleavage of terminal or α(1-6) glycoside bonds. Alpha-amylases therefore represent a group of esterases (EC 3.2.1.1). Alpha-amylases catalyze the breakdown of starch, glycogen, and other oligo- and polysaccharides that possess an α(1-4) glycoside bond. In this respect, alpha-amylases are effective against starch residues in laundry and catalyze their hydrolysis (endohydrolysis).Broad-spectrum alpha-amylases are used particularly where inhomogeneous raw materials or substrate mixtures need to be processed, for example in detergents and cleaning agents, since soils can consist of differently structured starch molecules and oligosaccharides. The alpha-amylases used in detergents and cleaning agents known from the prior art are usually of microbial origin and generally come from bacteria or fungi, such as those of the genera Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma, or Trichosporon, especially Bacillus. Alpha-amylases are typically produced by suitable microorganisms using known biotechnological methods, for example, by transgenic expression hosts of the genus Bacillus or by filamentous fungi.

[0005] Surprisingly, it has now been found that an α-amylase according to the invention, in combination with a soluble builder system and optionally a protease according to the invention, exhibits significantly improved activity on starch-containing soils in solid detergents compared to known agents. In particular, the washability of starch-containing soils, such as rice or cereal starch, as well as the washability of bleach-sensitive soils, is increased.

[0006] The subject matter of the present invention is therefore, in a first aspect, a solid washing or cleaning agent according to claim 1, comprising (a) 5 to 70 wt% surfactant; (b) at least one α-amylase, wherein the α-amylase is characterized in that it comprises an amino acid sequence which is identical to the amino acid sequence specified in SEQ ID NO:1 over its total length to at least 97%; (c) 5 to 70 wt% of a water-soluble builder system.

[0007] In another aspect, the present invention relates to the use of a solid washing or cleaning agent according to the invention for washing textiles or cleaning hard surfaces, in particular for removing starch-containing soiling from textiles or hard surfaces.

[0008] In another aspect, the present invention relates to a method for cleaning textiles or hard surfaces, characterized in that a solid washing or cleaning agent according to the invention is used in at least one process step.

[0009] These and other aspects, features, and advantages of the invention will become apparent to the person skilled in the art upon studying the following detailed description and claims. Each feature from one aspect of the invention can be incorporated into any other aspect of the invention. Furthermore, it is understood that the examples contained herein are intended to describe and illustrate the invention, but do not limit it, and in particular, the invention is not limited to these examples. Unless otherwise stated, all percentages are weight percentages based on the total weight of the agent / composition. Numerical ranges specified in the format "from x to y" include the stated values. If several preferred numerical ranges are specified in this format, it is understood that all ranges resulting from the combination of the different endpoints are also included.

[0010] “At least one,” as used herein, refers to 1, 2, 3, 4, 5, 6, 7, 8, 9, or more. In the context of components of the compositions described herein, this term refers not to the absolute quantity of molecules but to the type of component. “At least one anionic surfactant,” for example, means one or more different anionic surfactants, i.e., one or more different types of anionic surfactants. When used in conjunction with quantity specifications, these quantities refer to the total amount of the respective type of component.

[0011] “Approximately”, “about” or “about”, as used herein in reference to a numerical value, refer to the corresponding numerical value ±10%, preferably ±5%.

[0012] Unless otherwise stated, where reference is made to the pH value of a product, this refers to the pH value of the washing or cleaning solution obtained with the product when dissolved in distilled water (in a weight ratio of 1:100) at 20°C.

[0013] A substance, e.g. a composition or an agent, is “solid” according to the invention if it is in the solid state at 25°C and 1013 mbar.

[0014] The amylases and proteases according to the invention are preferably the mature amylase / protease, i.e., the catalytically active molecule without signal and / or propeptide(s). Unless otherwise specified, the sequences given also refer to mature enzymes.

[0015] In various embodiments, the α-amylase used according to the invention is characterized in that it comprises an amino acid sequence which is identical to the amino acid sequence specified in SEQ ID NO:1 over its total length to at least 97% and increasingly preferably to at least 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4%, 99.6%, 99.8% or 100.0%.

[0016] In preferred embodiments, a composition according to the invention comprises at least one protease. The protease according to the invention comprises an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 80% and increasingly preferably to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, or to 100%.

[0017] A protease is preferred that has an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 80% and increasingly preferably to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 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% and is identical in the counting according to SEQ ID NO:2 at at least one of positions 3, 4, 99 and 199, preferably at two, three or four positions. exhibits amino acid substitution. Particularly preferred are proteases comprising (i) the amino acid glutamic acid (E) at position 99; and / or (ii) the amino acid threonine (T) at position 3, the amino acid isoleucine (I) at position 4 and the amino acid isoleucine (I) at position 199.

[0018] Amino acid positions specified within the scope of the present invention with the phrase "counting according to SEQ ID NO:X" are understood as follows: The further amino acid positions are defined by an alignment of the amino acid sequence of an amylase or protease according to the invention with the amino acid sequence as specified in SEQ ID NO:X. Furthermore, the assignment of the positions is based on the mature protein. This assignment is particularly relevant if the amino acid sequence of a protein according to the invention comprises a higher number of amino acid residues than the amylase or protease in SEQ ID NO:X. Starting from the aforementioned positions in the amino acid sequence, the modification positions in an amylase or protease according to the invention are those that are assigned to these positions in an alignment.

[0019] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the established 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 achieved 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 algorithm available in the prior art is the FASTA algorithm.Sequence alignments, especially multiple sequence alignments, are performed using computer programs. Commonly used programs include the Clustal series (see, for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500), T-Coffee (see, for example, Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217), or programs based on these programs or algorithms. Sequence alignments can also be performed using the Vector NTI® Suite 10.3 computer program (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with its predefined standard parameters, whose AlignX module for sequence alignments is based on ClustalW.

[0020] Such a comparison also allows for a statement about the similarity of the compared sequences to one another. This is usually expressed as percent identity, meaning the proportion of identical nucleotides or amino acid residues at the same positions or positions corresponding to each other in an alignment. The broader concept of homology, in the case of amino acid sequences, includes conserved amino acid substitutions in the analysis, i.e., amino acids with similar chemical activity, since these usually exert similar chemical activities within the protein. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes, or only for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are thus defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Often, such small regions perform essential functions for the overall activity of the protein. It can therefore be useful to refer to sequence similarities only for 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.

[0021] In the context of the present invention, the statement that an amino acid position corresponds to a numerically designated position in SEQ ID NO:1 or SEQ ID NO:2 therefore means that the corresponding position is assigned to the numerically designated position in SEQ ID NO:1 or SEQ ID NO:2 in an alignment as defined above.

[0022] In addition to the amino acid modifications described above, amylases and proteases according to the invention can exhibit further amino acid modifications, in particular amino acid substitutions, insertions, or deletions. Such amylases and proteases are further developed, for example, by targeted genetic modification, i.e., by mutagenesis techniques, and optimized for specific applications or with regard to special properties (e.g., their catalytic activity, stability, etc.). Furthermore, nucleic acids according to the invention can be introduced into recombination reactions and thus used to generate entirely novel amylases and proteases or other polypeptides.

[0023] The aim is to introduce targeted mutations, such as substitutions, insertions, or deletions, into known molecules in order to improve, for example, the cleaning performance of enzymes according to the invention. For this purpose, the surface charges and / or the isoelectric point of the molecules, and thus their interactions with the substrate, can be altered. For example, the net charge of the enzymes can be changed to influence substrate binding, particularly for use in detergents and cleaning agents. Alternatively or additionally, one or more corresponding mutations can increase the stability of the amylase or protease, thereby improving its cleaning performance. Advantageous properties of individual mutations, such as individual substitutions, can be complementary.An amylase or protease that is already optimized with regard to certain properties, for example with regard to its stability against surfactants and / or bleaching agents and / or other components, can therefore be further developed within the scope of the invention.

[0024] The following convention is used to describe substitutions affecting exactly one amino acid position (amino acid exchanges): first, the naturally occurring amino acid is designated using the internationally accepted one-letter code, followed by the corresponding sequence position, and finally the inserted amino acid. Multiple exchanges within the same polypeptide chain are separated by slashes. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, such as an asterisk or a dash. For example, A95G describes the substitution of alanine at position 95 by glycine, A95AG the insertion of glycine after the amino acid alanine at position 95, and A95* the deletion of alanine at position 95. This nomenclature is familiar to those skilled in the art of enzyme technology.

[0025] Another object of the present invention is therefore a washing and cleaning agent containing a combination of an α-amylase and a protease, wherein the α-amylase or protease is characterized in that it is obtainable from an amylase or protease according to the invention as a starting molecule by one or more conservative amino acid substitutions. The term "conservative amino acid substitution" means the exchange (substitution) of one amino acid residue for another amino acid residue, wherein this exchange does not lead to a change in polarity or charge at the position of the exchanged amino acid, e.g., the exchange of one nonpolar amino acid residue for another nonpolar amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G=A=S, I=V=L=M, D=E, N=Q, K=R, Y=F, S=T, G=A=I=V=L=M=Y=F=W=P=S=T.

[0026] A further object of the present invention is therefore a washing and cleaning agent containing an α-amylase, optionally in combination with a protease, wherein the α-amylase is characterized in that it is obtainable from an amylase according to the invention as a starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 475, 476, 477, 478, 479, 480 or 481 linked amino acids match the original molecule.Similarly, the protease can also be characterized in that it is obtainable from a protease according to the invention as a starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence that corresponds to the starting molecule over a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 262, 264, 265, 266, 267 or 268 contiguous amino acids.

[0027] For example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme without losing or reducing its enzymatic activity. Furthermore, such fragmentation, deletion, insertion, or substitution mutagenesis can, for instance, reduce the allergenicity of the enzymes in question and thus improve their overall usability. Advantageously, the enzymes retain their enzymatic activity even after mutagenesis; that is, their enzymatic activity is at least equivalent to that of the original enzyme. Substitutions can also have beneficial effects. Both single and multiple linked amino acids can be exchanged for other amino acids.

[0028] An enzyme according to the invention can be further stabilized, in particular by one or more mutations, for example substitutions, or by coupling to a polymer. Increased stability during storage and / or use, for example during the washing process, results in longer-lasting enzymatic activity and thus improved cleaning performance. In principle, all stabilization methods described in the prior art and / or deemed suitable are eligible. Stabilization achieved through mutations of the enzyme itself is preferred, as such stabilization does not require any further processing steps after enzyme production. Suitable sequence modifications for this purpose are known from the prior art.

[0029] Other stabilization options include, for example: - Alteration of the binding of metal ions, in particular the calcium binding sites, for example by exchanging one or more of the amino acid(s) involved in the calcium bond for one or more negatively charged amino acids and / or by introducing sequence changes in at least one of the sequences of the two amino acids arginine / glycine; - Protection against the effects of denaturing agents such as surfactants through mutations that cause a change in the amino acid sequence on or at the surface of the protein; - Exchange of amino acids located near the N-terminus for those that presumably interact with the rest of the molecule via non-covalent interactions and thus contribute to maintaining the globular structure.

[0030] Preferred embodiments are those in which the enzyme is stabilized in several ways, since multiple stabilizing mutations act additively or synergistically.

[0031] Another object of the invention is an enzyme as described above, characterized in that it has at least one chemical modification. An enzyme with such a modification is called a derivative, i.e., the enzyme is derivatized.

[0032] For the purposes of this application, derivatives are understood to be proteins whose pure amino acid chain has been chemically modified. Such derivatizations can, for example, occur in vivo by the host cell that expresses the protein. In this regard, couplings of low-molecular-weight compounds such as lipids or oligosaccharides are particularly noteworthy. Derivatizations can also be carried out in vitro, for example, by the chemical modification of a side chain of an amino acid or by covalently binding another compound to the protein. For example, the coupling of amines to carboxyl groups of an enzyme to alter the isoelectric point is possible. Such another compound can also be a further protein, which is, for example, linked to a protein according to the invention via bifunctional chemical bonds.Derivatization also refers to the covalent binding to a macromolecular support, or the non-covalent inclusion in suitable macromolecular cage structures. Derivatizations can, for example, influence substrate specificity or binding strength to the substrate, or temporarily block enzymatic activity if the attached substance is an inhibitor. This can be useful, for instance, during storage. Such modifications can also affect stability or enzymatic activity. Furthermore, they can reduce the allergenicity and / or immunogenicity of the protein, thereby increasing its skin tolerance, for example. For instance, coupling with macromolecular compounds, such as polyethylene glycol, can improve the protein's stability and / or skin tolerance.

[0033] Derivatives of a protein according to the invention can, in the broadest sense, also include preparations of these proteins. Depending on the method of extraction, processing, or preparation, a protein may be associated with various other substances, for example, from the culture of the producing microorganisms. A protein may also have been deliberately combined with other substances, for example, to increase its storage stability. Therefore, all preparations of a protein according to the invention are also considered to be in accordance with the invention. This is also independent of whether or not it actually exhibits this enzymatic activity in a particular preparation. It may be desirable for it to have no or only slight activity during storage and to only develop its enzymatic function at the time of use. This can be controlled, for example, by means of appropriate accompanying substances.

[0034] The combination of an α-amylase and a protease according to the invention in solid detergents and cleaning agents results in improved cleaning performance of the solid detergent and cleaning agent on starch-containing soils and also on protease-sensitive soils. In particular, α-amylases according to the invention can have a performance-enhancing effect on the protease also contained in the detergent and cleaning agent and consequently enable, among other things, improved removal of at least one, preferably several, protease-sensitive soils on textiles and / or hard surfaces, for example, dishes, due to their protease-stabilizing effect. Preferred embodiments of the detergent and cleaning agents according to the invention show particularly advantageous cleaning performance on blood-containing soils, for example, on the Blood / Milk / Ink soil: Product No.CFT C-05 available from CFT (Center for Testmaterials) BV Vlaardingen, Netherlands.

[0035] The combination of amylase and soluble builder, optionally in combination with a protease and / or at a comparatively low pH, also results in improved cleaning performance on starch-containing soils, in particular improved washability compared to the same enzyme combinations with less or no soluble builder and possibly a higher pH value.

[0036] Preferred embodiments of the inventive means achieve such advantageous cleaning performance even at low temperatures, particularly in the temperature ranges between 10°C and 60°C, preferably between 15°C and 50°C, and most preferably between 20°C and 40°C. Further preferred embodiments of the inventive combinations achieve such advantageous cleaning performance over a wide temperature range, for example between 15°C and 90°C, preferably between 20°C and 60°C.

[0037] In preferred embodiments of the present invention, solid washing or cleaning agents with improved cleaning performance are produced specifically with regard to starch-containing and optionally also protease-sensitive soiling.

[0038] Within the scope of the invention, cleaning performance is understood to mean the brightening performance of one or more soiled areas, particularly on laundry or dishes. Within the scope of the invention, both the washing or cleaning agent, which comprises the amylase, optionally in combination with a protease, and the washing or cleaning solution formed by this agent, as well as the amylase itself, possess a respective cleaning performance. The cleaning performance of the enzymes thus contributes to the cleaning performance of the agent and the washing or cleaning solution formed by the agent. The cleaning performance is preferably determined as described below.

[0039] Cleaning performance is determined in a washing system containing a detergent at a dosage of 3.5 to 6.5 grams per liter of wash liquor, as well as amylase and protease. The amylases being compared are used at identical concentrations (based on active protein). The cleaning performance of the enzymes against corresponding enzyme-sensitive soils is determined by measuring the whiteness of the washed textiles. The washing process lasts 70 minutes at a temperature of 40°C, with water having a hardness between 13.5 and 16.5° dH (German hardness).

[0040] The concentration of amylase in the detergent intended for this washing system is 0.001–0.15 wt%, preferably 0.005–0.012 wt%, based on active protein. The concentration of protease in the detergent intended for this washing system, if present, is 0.001–0.1 wt%, preferably 0.01–0.06 wt%, based on active protein.

[0041] Preferably, the dosage of the solid detergent is between 3.5 and 6.0 grams per liter of wash liquor, for example 4.7, 4.9, or 5.9 grams per liter of wash liquor. Washing is preferably carried out at a pH value ≥7.5, preferably between 7.5 and 11, more preferably between pH 7.5 and pH 9.5, and even more preferably between pH 8 and pH 9, most preferably at approximately pH 8.5.

[0042] A preferred powdered detergent for such a washing system is composed as follows (all values ​​in weight percent): 10% linear alkylbenzenesulfonate (sodium salt), 1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxyhydrate, 4.0% TAED, 3.0% polyacrylate, 1.0% carboxymethylcellulose, 1.0% phosphonate, 27% sodium sulfate, remainder: foam inhibitors, optical brightener, perfumes.

[0043] An alternative preferred powdered detergent for such a washing system is composed as follows (all values ​​in weight percent): 10-15% linear alkylbenzenesulfonate (sodium salt), 0-1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2-5% C12-C18 fatty alcohol with 7 EO, 0-2% soaps, 5-15% sodium carbonate, 4-10% amorphous sodium disilicate, 0.5-2% phosphonate (e.g., HEDP-Na4), 1-4% polyacrylate, 1-2% carboxymethylcellulose, remainder: sodium sulfate, foam inhibitors, optical brightener, perfumes, etc. Preferably, the dosage of the powdered detergent is between 4.5 and 7.0 grams per liter of wash liquor, for example, and particularly preferably, 4.7 grams per liter of wash liquor, or 5.5, 5.9, or 6.7 grams per liter of wash liquor, or approximately 65g / job.

[0044] The degree of whiteness, i.e., the lightening of the soiling, as a measure of cleaning performance, is preferably determined using optical measurement methods, preferably photometrically. A suitable device for this purpose is, for example, the Minolta CM508d spectrometer. Typically, the devices used for the measurement are calibrated beforehand with a white standard, preferably a supplied white standard.

[0045] Protein concentration can be determined using known methods, for example, the BCA method (bicinchoninic acid; 2,2'-bicinolyl-4,4'-dicarboxylic acid) or the biuret method (AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766). The determination of the active protein concentration can be carried out by titration of the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonylfluoride (PMSF)) and determination of the residual activity (cf. M. Bender et al., J. Am. Chem. Soc. 88, 24 (1966), pp. 5890-5913).

[0046] In various embodiments of the invention, the concentration of amylase in the washing or cleaning agent is 0.0005–0.2 wt.%, preferably 0.001–0.12 wt.%, based on active protein. The concentration of protease in the solid washing or cleaning agent can be 0.001–0.5 wt.%, preferably 0.01–0.1 wt.%, based on active protein.

[0047] The solid washing or cleaning agent further contains a soluble builder system. 'Soluble' or 'water-soluble', as used interchangeably in this context, means that under application conditions, the builder dissolves completely in the washing liquor at the concentration resulting from the amount of the agent containing it used under normal conditions; that is, the residue of the builder remaining as a solid is less than 1% of the total amount of the builder.

[0048] The composition according to the invention contains at least 5 wt.% and up to 70 wt.%, in particular 5 wt.% to 60 wt.% of water-soluble builder system.

[0049] In various embodiments of the invention, this builder system preferably comprises the components a) 5 wt.% to 70 wt.%, preferably 5 wt.%, more preferably 5 wt.% to 55 wt.% organic water-soluble builder and / or carbonate, which may also be at least partially replaced by hydrogen carbonate, b) up to 20 wt.% alkali silicate, preferably 3 to 10 wt.% alkali silicate, and c) up to 10 wt.%, preferably up to 5 wt.%, phosphate builders, The quantities given refer to the entire amount of washing or cleaning agent. This also applies to all subsequent quantities, unless explicitly stated otherwise.

[0050] In preferred embodiments of the invention, this builder system preferably comprises the components a) 5 wt.% to 60 wt.%, preferably 5 wt.%, more preferably 5 wt.% to 35 wt.% citrate and / or carbonate, which may also be at least partially replaced by hydrogen carbonate, b) up to 20 wt.% alkali silicate, preferably 3 to 10 wt.% alkali silicate, c) up to 10 wt.%, preferably up to 5 wt.%, phosphate builders, d) up to 10 wt.%, preferably 0 to 10 wt.%, more preferably 0.5 to 5 wt.% polymeric polycarboxylate, and e) up to 10 wt.%, preferably 0.05 to 3 wt.%, phosphonic acid and / or alkali phosphonate, The quantities given refer to the entire amount of washing or cleaning agent. This also applies to all subsequent quantities, unless explicitly stated otherwise.

[0051] The term carbonate, as used in the present invention, includes in particular alkali carbonate and alkali bicarbonate. Preferably, it refers to sodium carbonate and sodium bicarbonate. In various embodiments, the composition comprises 5-55 wt.%, preferably 5-40 wt.%, more preferably 5-35 wt.%, and even more preferably 5-25 wt.% carbonate. In various embodiments, the composition comprises 5-55 wt.%, preferably 5-40 wt.%, more preferably 5-35 wt.%, and even more preferably 5-25 wt.% alkali carbonate. In preferred embodiments, the composition comprises 5-55 wt.%, preferably 5-40 wt.%, more preferably 5-35 wt.%, and even more preferably 5-25 wt.% sodium carbonate.

[0052] Water-soluble organic builder substances include polycarboxylic acids, in particular citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycine diacetic acid, glutamic diacetic acid, nitrilotriacetic acid and ethylenediaminetetraacetic acid, as well as polyaspartic acid, polyphosphonic acids, in particular aminotris-(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid), diethylenetriaminepenta(methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acid, polymeric hydroxy compounds such as dextrin, as well as polymeric (poly)carboxylic acids, in particular polycarboxylates accessible by oxidation of polysaccharides or dextrins, and / or polymeric acrylic acids, methacrylic acids, maleic acids and copolymers of these, which may also contain small amounts of polymerizable substances without carboxylic acid functionality.The relative molecular mass of homopolymers of unsaturated carboxylic acids generally ranges from 5,000 to 200,000, and that of copolymers from 2,000 to 200,000, preferably from 50,000 to 120,000, in each case based on free acid. A particularly preferred acrylic acid-maleic acid copolymer has a relative molecular mass of 50,000 to 100,000. Suitable, though less preferred, compounds of this class are copolymers of acrylic acid or methacrylic acid with vinyl ethers, such as vinyl methyl ethers, vinyl esters, ethylene, propylene, and styrene, in which the acid content is at least 50% by weight. Terpolymers containing two unsaturated acids and / or their salts as monomers, and vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate as a third monomer, can also be used as water-soluble organic builder substances.The first acidic monomer or its salt is derived from a monoethylene-unsaturated C3-C8 carboxylic acid, preferably from a C3-C4 monocarboxylic acid, particularly (meth)acrylic acid. The second acidic monomer or its salt can be a derivative of a C4-C8 dicarboxylic acid, with maleic acid being particularly preferred, and / or a derivative of an allylsulfonic acid substituted at the 2-position with an alkyl or aryl group. Such polymers generally have a relative molecular mass between 1,000 and 200,000. Other preferred copolymers are those comprising acrolein and acrylic acid / acrylic acid salts or vinyl acetate as monomers. All of the aforementioned acids can be used in the form of their water-soluble salts, particularly their alkali salts.

[0053] Such organic builder substances can, if desired, be present in amounts up to 50 wt.%, preferably up to 25 wt.%, more preferably from 5 wt.% to 25 wt.% and most preferably from 10 wt.% to 20 wt.%.

[0054] With regard to component a), in a preferred embodiment, 15 wt.% to 25 wt.% alkali carbonate, which may be at least partially replaced by alkali bicarbonate, and up to 5 wt.%, in particular 0.5 wt.% to 2.5 wt.% citric acid and / or alkali citrate are contained. In an alternative embodiment, component a) contains 5 wt.% to 25 wt.%, in particular 5 wt.% to 15 wt.% citric acid and / or alkali citrate and up to 5 wt.%, in particular 1 wt.% to 5 wt.% alkali carbonate, which may be at least partially replaced by alkali bicarbonate. If both alkali carbonate and alkali bicarbonate are present, component a) preferably comprises alkali carbonate and alkali bicarbonate in a weight ratio of 10:1 to 1:1.

[0055] In various embodiments, citric acid and / or citrate are used as water-soluble, organic builders. The use of 5 wt.% to 25 wt.%, preferably 7.5 wt. to 12.5 wt.% citric acid and / or 5 wt.% to 25 wt.%, preferably 7.5 wt. to 12.5 wt.% citrate, preferably alkali citrate, even more preferably sodium citrate, is particularly preferred. Citric acid / citrate can each be used in the form of their hydrates; for example, citric acid can be used in the form of the monohydrate, and citrate in the form of trisodium citrate dihydrate. In certain embodiments of the invention, where the compound is intended to have a comparatively low pH value, the citrate is partially replaced by citric acid. In the embodiments described above, carbonate, in particular alkali carbonate or alkali bicarbonate, can additionally be used in amounts up to 15 wt.%, preferably 5 wt.% to 15 wt.%.

[0056] In various embodiments of the invention, in addition to the aforementioned components a), which are selected from carbonates, in particular alkali carbonates, and citrates, in particular alkali citrates, the builder system also contains up to 10 wt.%, preferably 0.05 to 3 wt.%, phosphonic acid and / or alkali phosphonate. Phosphonic acids are also understood to include, optionally, substituted alkylphosphonic acids, which may also have several phosphonic acid groups (so-called polyphosphonic acids).Preferably, they are selected from the hydroxy and / or aminoalkylphosphonic acids and / or their alkali salts, such as dimethylaminomethanediphosphonic acid, 3-aminopropane-1-hydroxy-1,1-diphosphonic acid, 1-amino-1-phenylmethanediphosphonic acid, 1-hydroxyethane-1,1-diphosphonic acid (HEDP), amino-tris(methylenephosphonic acid), N,N,N',N'-ethylenediaminetetrakis(methylenephosphonic acid), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and acylated derivatives of phosphorous acid, which can also be used in any mixtures.

[0057] Regarding component b), in a preferred embodiment alkali silicates with a modulus in the range of 1.8 to 2.5 are included, preferably in an amount of 1 wt.% to 5 wt.% alkali silicate with a modulus in the range of 1.8 to 2.5.

[0058] The term alkali silicate generally refers to both crystalline and amorphous alkali silicates. Crystalline alkali silicates include layered sodium silicates with the general formula NaMSi. x O 2x+1· yH z O, where M represents sodium or hydrogen, x is a number from 1.9 to 4, and y is a number from 0 to 20, with preferred values ​​for x being 2, 3, or 4. Such crystalline layered silicates are described, for example, in European patent application EP-A-0 164 514. Preferred crystalline layered silicates of the given formula are those in which M represents sodium and x takes the values ​​2 or 3. In particular, both β- and δ-sodium disilicates Na₂Si₂O₅·yH₂O are preferred.

[0059] Preferred amorphous alkali silicates are amorphous sodium silicates with a Na₂O : SiO₂ modulus of 1:1.8 to 1:3.3, preferably 1:1.8 to 1:2.8, and particularly 1:1.8 to 1:2.6, which exhibit delayed dissolution and secondary washing properties. The delayed dissolution compared to conventional amorphous sodium silicates can be achieved in various ways, for example, by surface treatment, compounding, compaction / densification, or superdrying. Within the scope of this invention, the term "amorphous" is also understood to mean "X-ray amorphous." This means that the silicates do not produce sharp X-ray reflections in X-ray diffraction experiments, as is typical for crystalline substances, but at most one or more maxima of the scattered X-rays, which have a width of several units of the diffraction angle.However, particularly good builder properties can indeed result if the silicate particles exhibit diffuse or even sharp diffraction maxima in electron diffraction experiments. This is to be interpreted as the products possessing microcrystalline regions ranging in size from 10 to several hundred nm, with values ​​up to a maximum of 50 nm and especially up to a maximum of 20 nm being preferred. Such so-called X-ray amorphous silicates, which also exhibit a dissolution delay compared to conventional water glasses, are described, for example, in German patent application DE-A-44 00 024. Particularly preferred are densified / compacted amorphous silicates, compounded amorphous silicates, and superdried X-ray amorphous silicates, with the superdried silicates being especially preferred as carriers in the granules according to the invention or used as carriers in the process according to the invention.

[0060] The composition contains 0-20 wt.%, preferably 0 to 15 wt.%, more preferably 3 to 10 wt.% alkali silicate builder, preferably sodium silicate builder.

[0061] The compositions according to the invention comprise 0-10 wt.%, preferably 0-5 wt.%, even more preferably 0-1 wt.% phosphate builders as component c). Among the multitude of commercially available phosphate builders, the alkali metal phosphates are particularly preferred, with pentasodium triphosphate, Na₅P₃O₄, being especially favored. 10 (Sodium tripolyphosphate) or pentapotassium triphosphate, K5P3O 10(Potassium tripolyphosphate) is of the greatest importance for the compositions according to the invention. If phosphates are used as cleaning-active substances in the washing or cleaning agent within the scope of the present application, preferred compositions contain these phosphates, preferably pentapotassium triphosphate. Preferably, however, the compositions are free of these phosphates, i.e., they contain <1 wt% to no phosphate, or no intentionally added phosphate.

[0062] Regarding polymeric polycarboxylates, suitable examples include the alkali metal salts of polyacrylic acid or polymethacrylic acid, such as those with a relative molecular mass of 500 to 70,000 g / mol. This class of substances has already been described in detail above. The (co-)polymeric polycarboxylates can be used either as a powder or as an aqueous solution. The (co-)polymeric polycarboxylate content of the agents is preferably 0 to 10 wt.%, and particularly 0.5 to 5 wt.%.

[0063] In addition to the aforementioned water-soluble builders, the composition of the invention may also contain inorganic, water-insoluble builders. Particularly suitable water-insoluble builders are aluminosilicates, especially zeolites. The term "zeolite builder," as used herein, refers not only to zeolite in the strict sense, but also to both crystalline and amorphous alkali aluminosilicate. Zeolite is present in the composition in amounts of 0 to 10 wt.%, preferably not exceeding 5 wt.%. Among these, crystalline sodium aluminosilicates of detergent quality, particularly zeolite A, P, and optionally X, are preferred. Amounts close to the aforementioned upper limit are preferably used in solid, particulate compositions. Suitable aluminosilicates, in particular, do not contain particles with a grain size greater than 30 µm and preferably consist of at least 80 wt.% of particles with a size less than 10 µm.Their calcium binding capacity, which can be determined according to the German patent DE 24 12 837, is generally in the range of 100 to 200 mg CaO per gram.

[0064] The product preferably contains 0-10 wt.%, preferably 0-5 wt.%, zeolite builder.

[0065] In various embodiments, the builder system preferably consists of the following components, each based on the total mass of the means: a) 5 wt.% to 25 wt.%, preferably 7.5 wt.% citric acid; b) 5 wt.% to 25 wt.%, preferably 7.5 wt.% citrate, preferably alkali citrate; c) 0 to 40 wt.%, preferably 0 to 15 wt.% alkali carbonate, which may also be replaced at least partially by alkali hydrogen carbonate, in particular sodium carbonate; d) 0 to 20 wt.%, preferably 3 to 10 wt.% alkali silicate; e) 0.005 to 10 wt.%, preferably 0.02 to 2 wt.% phosphonic acid and / or alkali phosphonate, in particular HEDP or DTPMP; and f) 0 to 10 wt.%, preferably 0.5 to 3 wt.% polymeric polycarboxylate, in particular polyacrylate.

[0066] The subject matter of the invention includes all conceivable types of solid washing or cleaning agents, both concentrates and undiluted agents, for use on a commercial scale, in washing machines, or for hand washing or cleaning. This includes, for example, detergents for textiles, carpets, or natural fibers, for which the term "detergent" is used. It also includes, for example, dishwashing liquids for dishwashers or manual dishwashing liquids, or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood, or leather, for which the term "cleaning agent" is used; thus, in addition to manual and machine dishwashing liquids, for example, scouring agents, glass cleaners, toilet fresheners, etc.Solid washing and cleaning agents within the scope of the invention also include washing aids that are added to the actual detergent during manual or machine washing of textiles to achieve an additional effect. Furthermore, washing and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e., agents with which the garment is brought into contact before the actual washing, for example, to loosen stubborn stains, and also agents that, in a step following the actual washing process, impart further desirable properties to the laundry, such as a pleasant feel, wrinkle resistance, or low static charge. Fabric softeners are among the latter types of agents.

[0067] The solid washing or cleaning agents according to the invention can contain, in addition to amylase and the optional protease, further enzymes. Lipases or cutinases, for example, can be used as further enzymes, particularly because of their triglyceride-cleaving activities, but also to generate peracids in situ from suitable precursors. These include, for example, the lipases originally obtained from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, especially those with the amino acid substitution D96L. These include, for example, the lipases originally obtained from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, especially those with one or more of the following amino acid substitutions starting from the aforementioned lipase at positions D96L, T213R and / or N233R, particularly preferably T213R and N233R.Furthermore, cutinases originally isolated from Fusarium solani pisi and Humicola insolens can be used, for example. Lipases, or cutinases, whose parent enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii can also be used.

[0068] The agents according to the invention may also contain cellulases or hemicellulases such as mannanases, xanthan lyases, pectin lyases (=pectinases), pectinesterases, pectate lyases, xyloglucanases (=xylanases), pullulanases or β-glucanases.

[0069] To enhance the bleaching effect, oxidoreductases, for example oxidases, oxygenases, catalases, peroxidases such as halo-, chloro-, bromo-, lignin-, glucose- or manganese-peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases), can be used according to the invention. Advantageously, preferably organic, and especially aromatic, compounds that interact with the enzymes are added to enhance the activity of the respective oxidoreductases (enhancers) or to ensure electron flow in cases of significantly different redox potentials between the oxidizing enzymes and the contaminants (mediators).

[0070] The products contain 5-70 wt% surfactant, which refers to one or more surfactants. Preferably, the products contain 5-55 wt%, and even more preferably 5-35 wt% surfactant. Anionic surfactants, non-ionic surfactants, and mixtures thereof are particularly suitable, but cationic, zwitterionic, and / or amphoteric surfactants may also be included.

[0071] Anionic surfactants used include, for example, those of the sulfonate and sulfate type. Sulfonate-type surfactants preferably include C9-13 alkylbenzenesulfonates, olefin sulfonates (i.e., mixtures of alkene and hydroxyalkane sulfonates), and disulfonates, such as those obtained from C12-18 monoolefins with terminal or central double bonds by sulfonation with gaseous sulfur trioxide followed by alkaline or acidic hydrolysis of the sulfonation products. Alkane sulfonates obtained from C12-18 alkanes, for example, by sulfochlorination or sulfoxidation followed by hydrolysis or neutralization, are also suitable. Esters of α-sulfofaticial acids (ester sulfonates), such as the α-sulfonated methyl esters of hydrogenated coconut, palm kernel, or tallow fatty acids, are also suitable.

[0072] Preferably, the composition contains 5-55 wt%, preferably 5-35 wt%, of anionic surfactant. Most preferably, the composition contains 5-35 wt% alkylbenzenesulfonate. Furthermore, the composition may preferably contain other anionic surfactants, in particular alkyl ether sulfates, as well as non-ionic surfactants, in particular fatty alcohol alkoxylates. These may then constitute the remainder of the surfactants.

[0073] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of formula in which R' and R'' are independent of H or alkyl and together contain 6 to 19, preferably 7 to 15, and particularly 9 to 13 carbon atoms. Sodium dodecylbenzylsulfonate is a particularly preferred representative.

[0074] The alkali and, in particular, the sodium salts of the sulfuric acid half-esters of C12-C18 fatty alcohols, for example, from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or of C10-C20 oxo alcohols, and those half-esters of secondary alcohols of these chain lengths are preferred as alk(en)yl sulfates. Also preferred are alk(en)yl sulfates of the aforementioned chain lengths which contain a synthetic, petrochemically produced, straight-chain alkyl group and which exhibit analogous degradation behavior to the corresponding compounds based on fatty chemical raw materials. For detergent applications, C12-C16 alkyl sulfates, C12-C15 alkyl sulfates, and C14-C15 alkyl sulfates are preferred.

[0075] Sulfuric acid monoesters of straight-chain or branched C7-21 alcohols ethoxylated with 1 to 6 moles of ethylene oxide, such as 2-methyl-branched C9-11 alcohols with an average of 3.5 moles of ethylene oxide (EO) or C12-18 fatty alcohols with 1 to 4 EO, are also suitable. Suitable alkyl ether sulfates include, for example, compounds of the formula R1-O-(AO) n -SO3 - X +

[0076] In this formula, R1 represents a linear or branched, substituted or unsubstituted alkyl group, preferably a linear, unsubstituted alkyl group, and particularly preferably a fatty alcohol group. Preferred R1 groups are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and eicosyl groups and mixtures thereof, with those having an even number of carbon atoms being preferred. Particularly preferred R1 groups are derived from C12-C18 fatty alcohols, for example, coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C10-C20 oxo alcohols. AO represents an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index n represents an integer from 1 to 50, preferably from 1 to 20 and particularly from 2 to 10. Most preferably, n represents the numbers 2, 3, 4, 5, 6, 7 or 8.X represents a monovalent cation or the nth part of an n-valent cation, preferably alkali metal ions, including Na+ or K+, with Na+ being highly preferred. Further cations X+ can be selected from NH4+, ½ Zn2+, ½ Mg2+, ½ Ca2+, ½ Mn2+, and mixtures thereof.

[0077] In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula with k = 11 to 19, n = 2, 3, 4, 5, 6, 7, or 8. Particularly preferred representatives are Na-C12-14 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical average, which may be a whole number or a fraction for a specific product. The stated degrees of alkoxylation represent statistical averages, which may be a whole number or a fraction for a specific product. Preferred alkoxylates / ethoxylates exhibit a narrow range of homologs (narrow range ethoxylates, NRE).

[0078] For cold washing performance, it has proven advantageous for detergents to contain additional soap(s). Preferred detergents are therefore characterized by the fact that they contain soap(s). Suitable soaps include saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, as well as, in particular, soap mixtures derived from natural fatty acids, e.g., coconut, palm kernel, or tallow fatty acids.

[0079] Preferably, alkoxylated, advantageously ethoxylated, and especially primary alcohols with preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol are used as nonionic surfactants. The alcohol residue in these alcohols may be linear or, preferably, methyl-branched at the 2-position, or the mixture may contain both linear and methyl-branched residues, as is commonly found in oxo alcohol residues. However, alcohol ethoxylates with linear residues derived from native alcohols with 12 to 18 carbon atoms, e.g., from coconut, palm, tallow, or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol, are particularly preferred. Preferred ethoxylated alcohols include, for example, C12-14 alcohols with 3 EO or 4 EO, C9-11 alcohol with 7 EO, C13-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C12-18 alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C12-14 alcohol with 3 EO and C12-18 alcohol with 5 EO.The stated degrees of ethoxylation represent statistical averages, which may be whole numbers or fractions for a specific product. Preferred alcohol ethoxylates exhibit a narrow range of homologs (NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohols with 14 EO, 25 EO, 30 EO, or 40 EO.

[0080] Another class of preferably used non-ionic surfactants, which are used either as the sole non-ionic surfactant or in combination with other non-ionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably with 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

[0081] Another class of nonionic surfactants that can be used advantageously are the alkyl polyglycosides (APGs). Suitable alkyl polyglycosides conform to the general formula RO(G)z, where R represents a linear or branched, particularly 2-methyl-branched, saturated or unsaturated, aliphatic residue with 8 to 22, preferably 12 to 18, carbon atoms, and G is the symbol representing a glucose unit with 5 or 6 carbon atoms, preferably glucose. The degree of glycosylation z is between 1.0 and 4.0, preferably between 1.0 and 2.0, and particularly between 1.1 and 1.4. Linear alkyl polyglycosides are preferred, i.e., alkyl polyglycosides in which the polyglycosyl residue is a glucose residue and the alkyl residue is an n-alkyl residue.

[0082] Non-ionic surfactants of the amine oxide type, for example N-cocosalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides, may also be suitable. The amount of these non-ionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, and in particular not more than half of it.

[0083] Suitable amphoteric surfactants include, for example, betaines of the formula (R iii )(R iv )(R v )N + CH2COO - , in the R iii an alkyl group, optionally interrupted by heteroatoms or heteroatom groups, with 8 to 25, preferably 10 to 21 carbon atoms and R iv as well as R v Alkyl groups of the same or different types with 1 to 3 carbon atoms, in particular C 10 -C 18 -Alkyldimethylcarboxymethyl betaine and C 11 -C 17 -Alkylamidopropyl dimethylcarboxymethyl betaine.

[0084] Suitable cationic surfactants include, among others, the quaternary ammonium compounds of the formula (R vi )(R vii )(R viii )(R ix )N + X - , in the R vi to R ix for four identical or different, in particular two long-chain and two short-chain, alkyl groups and X -Examples of suitable cationic surfactants include those with an anion, particularly a halide ion, such as didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary surfactants, especially those with a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. The use of quaternary surfactants with antimicrobial properties allows the product to be formulated with antimicrobial activity or to enhance any existing antimicrobial effect resulting from other ingredients.

[0085] In addition to the components mentioned above, the compositions according to the invention can, in principle, contain all known ingredients commonly used in such compositions. These include, but are not limited to, bleaching agents based on organic and / or inorganic peroxygen compounds, bleaching activators, bleaching catalysts, water-miscible organic solvents, sequestrants, electrolytes, pH regulators, and other auxiliary substances such as optical brighteners, graying inhibitors, foam regulators, as well as colorants and fragrances, and combinations thereof.

[0086] The solid washing or cleaning agents according to the invention can be provided in forms known to those skilled in the art. A substance, e.g., a composition or an agent, is, according to the definition of the invention, solid if it exists in the solid state at 25 °C and 1013 mbar. The solid dosage forms according to the invention include extrudates, granules, tablets, or pouches containing solid agents, which can be supplied in bulk containers or pre-packaged in individual portions. Alternatively, the agent is available as a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, and especially 500 g / l to 900 g / l or 600 g / l to 850 g / l.

[0087] The production of solid compositions according to the invention presents no difficulties and can be carried out in a known manner, for example by spray drying or granulation, whereby enzymes and any other thermally sensitive ingredients, such as bleaching agents, may optionally be added separately at a later date. For the production of compositions according to the invention with an increased bulk density, particularly in the range of 650 g / l to 950 g / l, a process comprising an extrusion step is preferred.

[0088] The solid washing or cleaning agents according to the invention preferably contain less than 10 wt.%, preferably less than 5 wt.% water based on their total weight.

[0089] The solid washing or cleaning agents according to the invention have a pH value of 7.5 to 9.5, preferably 8.0 to 9.0, and more preferably about 8.5 in various embodiments.

[0090] Another object of the invention is a method for cleaning textiles or hard surfaces, characterized in that an agent according to the invention is used in at least one process step, as well as the use of a solid washing or cleaning agent according to the invention for washing textiles or cleaning hard surfaces, in particular for removing starch-containing soiling from textiles or hard surfaces.

[0091] This includes both manual and machine-based methods, with machine-based methods being preferred. Methods for cleaning textiles are generally characterized by the fact that, in several process steps, various cleaning agents are applied to the item being cleaned and rinsed off after the contact time, or that the item being cleaned is otherwise treated with a detergent or a solution or dilution thereof. The same applies to methods for cleaning all materials other than textiles, in particular hard surfaces. All conceivable washing or cleaning methods can be enhanced in at least one of the process steps by the application of a detergent or cleaning agent according to the invention and then represent embodiments of the present invention.All circumstances, objects, and embodiments described for means according to the invention are also applicable to this subject matter of the invention. Therefore, explicit reference is made here to the disclosure at the relevant point, with the note that this disclosure also applies to the aforementioned methods according to the invention. Examples

[0092] The following examples illustrate the invention without limiting it: Example 1:

[0093] Table 1 shows a powder detergent B according to the invention with a soluble builder in comparison with non-inventive powder detergent A based on a zeolite / tripolyphosphate builder. Table 1: Detergent formulations: A% AS B% AS LAS-Na 3,4 12,5 FA 7EO 1,0 3,0 HEDP-Na4 0,3 1,1 Polyacrylate 0,7 2,7 Sodium silicate 2.1 22,0 7,0 Sodium carbonate 2,0 20,1 Zeolite A 12,0 0,3 Sodium tripolyphosphate 12,0 - Sodium sulfate / other Per 100 Per 100 Sodium carbonate peroxohydrate 17,0 10,0 TAED 5,0 3,5 Carboxymethylcellulose 0,6 1,3 Defoamer 0,036 0,052 Protease * (as%) 0,01485 0,01485 Amylase * (as%) 0,01470 0,01470 Dosage: 1 ladle 65 g 65 g All figures in % of weight Protease * (Protease which has the amino acid sequence according to SEQ ID NO:2 with the following substitutions: at position 3 the amino acid threonine (T), at position 4 the amino acid isoleucine (I) and at position 199 the amino acid isoleucine (I)) Amylase *: Amylase according to the invention (SEQ ID NO:1)

Claims

[1] Containing solid washing or cleaning agent: a) 5 to 70 wt% surfactant; b) at least one α-amylase, wherein the α-amylase characterized by is that it comprises an amino acid sequence that is at least 97% identical to the amino acid sequence specified in SEQ ID NO:1 over its entire length; c) 5 to 70 wt% of a water-soluble builder system. [2] Solid washing or cleaning agent according to claim 1, characterized by that it comprises at least one protease, wherein the protease comprises an amino acid sequence that is at least 80% identical to that in SEQ ID NO:2 over its total length. [3] Solid washing or cleaning agent according to claim 2, characterized by , that (1) the at least one protease comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 90%; and (2) the at least one protease having an amino acid substitution at at least one of positions 3, 4, 99 and 199, preferably at two, three or four positions, particularly preferably (i) at position 99 the amino acid glutamic acid (E) and / or (ii) at position 3 the amino acid threonine (T), at position 4 the amino acid isoleucine (I) and at position 199 the amino acid isoleucine (I). [4] Solid washing or cleaning agent according to any one of claims 1 to 3, characterized by , that the concentration of amylase in the washing or cleaning agent is 0.0005-0.2 wt% based on active protein and / or the concentration of protease in the solid washing or cleaning agent is 0.001-0.5 wt% based on active protein. [5] Solid washing or cleaning agent according to any one of claims 1 to 4, characterized by , that the water-soluble builder system includes, each based on the total mass of the product: a) 5 wt.% to 70 wt.% organic water-soluble builders and / or carbonate, which may also be at least partially replaced by hydrogen carbonate, b) up to 20 wt.% alkali silicate and c) up to 10 wt% phosphate builder. [6] Solid washing or cleaning agent according to any one of claims 1 to 5, characterized by , that the water-soluble organic builder system contains, each based on the total mass of the product: a) 5 wt.% to 60 wt.% citrate and / or carbonate, which may also be at least partially replaced by hydrogen carbonate, b) up to 20 wt.% alkali silicate, c) up to 10 wt% phosphate builders, d) up to 10 wt% polymeric polycarboxylate, and e) up to 10 wt% phosphonic acid and / or alkali phosphonate. [7] Solid washing or cleaning agent according to any one of claims 1 to 6, characterized by, that the water-soluble organic builder system contains, each based on the total mass of the product: a) 5% to 25% by weight citric acid; b) 5 wt.% to 25 wt.% citrate, preferably alkali citrate; c) 0 to 40 wt.% alkali carbonate, which may also be replaced at least partially by alkali hydrogen carbonate, in particular sodium carbonate; d) 0 to 20 wt.% alkali silicate; e) 0.005 to 10 wt% phosphonic acid and / or alkali phosphonate, in particular HEDP or DTPMP; and f) 0 to 10 wt% polymeric polycarboxylate, in particular polyacrylate. [8] Solid washing or cleaning agent according to any one of claims 1 to 7, characterized by that the product contains 5-55 wt% surfactant, in particular anionic surfactants, non-ionic surfactants and mixtures thereof. [9] Use of a solid washing or cleaning agent according to any one of claims 1-8 for washing textiles or cleaning hard surfaces, in particular for removing starch-containing soils from textiles or hard surfaces. [10] Methods for cleaning textiles or hard surfaces, characterized by , that in at least one process step a solid washing or cleaning agent according to one of claims 1-8 is used.