Detergent composition, polymer and method for producing same

Abstract

The present invention provides an aqueous liquid detergent composition comprising: (A) at least one polymer having (a) a backbone derived from an aliphatic compound having at least four amino groups per molecule, at least one of which is a —(CH) a is a —NH group, and the variable a is selected from 2 to 4, and is the —(CH) a At least 40 mole percent of the —NH2 groups are (b) of the general formula —(CH2) a The present invention relates to a composition comprising a polymer comprising a backbone converted with sugars based on monosaccharides, disaccharides, or polysaccharides under the formation of a secondary amino group of -NH-CH2-.

Description

[Technical Field]

[0001] The present invention provides an aqueous liquid detergent composition comprising: (A) at least one polymer, (a) A main chain derived from an aliphatic compound having at least four amino groups per molecule, at least one of which is -(CH2) a is a —NH group, and the variable a is selected from 2 to 4, and is the —(CH) a At least 40 mole percent of the —NH groups are (b) General formula -(CH2) a The present invention relates to a composition comprising a polymer comprising a backbone converted with sugars based on monosaccharides, disaccharides, or polysaccharides under the formation of a secondary amino group of -NH-CH2-.

[0002] The present invention is further directed to a polymer (A) and a process for making such a polymer (A). [Background technology]

[0003] Laundry detergents must meet several requirements. They must remove all types of stains from laundry, including all types of pigments, clays, fatty stains, and dyes derived from foods and beverages such as red wine, tea, coffee, and fruits, including berry juices. Laundry detergents must also exhibit certain storage stability properties. In particular, laundry detergents that are liquid or contain moisture-absorbing ingredients often lack good storage stability, e.g., enzymes tend to become inactive.

[0004] Greasy soils remain a challenge in laundry. Many removal suggestions have been made (polymers, enzymes, surfactants), but finding a solution that works well is still challenging. The use of lipases has been suggested to aid in grease removal, but many builders do not work well with lipases, especially in liquid laundry detergents.

[0005] In addition, graying of laundry remains a significant problem. Graying is caused by the redeposition of soil during washing. To reduce soil redeposition, certain natural or modified polysaccharides, such as polysaccharides treated with gaseous or liquid SO2, have been developed. Many components with various structures have been suggested, see, for example, WO 2015 / 091160, EP 3266858 A1, and EP 3226858 A1. However, there is still room for improvement, and the graying prevention performance of such compounds remains insufficient. Therefore, there is a continuous need for improved graying inhibitors that can be used in the laundry process. In particular, it is desirable to provide an anti-graying agent that reduces graying of washed fabrics.

[0006] Several polymers have been suggested as additives, however many of them suffer from rapid degradation and therefore short shelf life. Summary of the Invention [Problem to be solved by the invention]

[0007] It was therefore an object to provide detergent compositions that meet the above needs. It was also an object to provide ingredients that meet the above needs, and to provide processes for making such ingredients and detergent compositions.

[0008] It was therefore an object to provide detergent compositions that meet the above needs. It was also an object to provide ingredients that meet the above needs, and to provide processes for making such ingredients and detergent compositions. [Means for solving the problem]

[0009] Accordingly, a detergent composition as defined above, hereinafter also referred to as the inventive composition or the composition according to the invention, has been found. The inventive composition contains at least one polymer (A) comprising a backbone (a) and an amount of monosaccharide, disaccharide, or polysaccharide groups (b) attached to the backbone. The polymer (A) and the detergent composition comprising the polymer (A) are described in more detail below. DETAILED DESCRIPTION OF THE INVENTION

[0010] The main chain (A) is derived from an aliphatic compound having at least four amino groups per molecule, preferably 4 or 20 to 70 amino groups per molecule, at least one of which is -(CH2) a is an —NH 2 group, and the variable a is selected from 2 to 4.

[0011] Examples of backbones (a) are polylysine, polyvinylamine and polyalkyleneimines such as polyethyleneimine and polypropyleneimine, and H2N-(CH2)3-NH-CH2CH2-N(CH2)3-NH2 ("N4 amine").

[0012] The polyalkyleneimine used as the backbone (a) may have a linear or preferably branched structure. The branch may be an alkyleneamino group such as, but not limited to, a -CH-CH-NH group or a (CH)-NH- group. Longer branches may be, for example, a -(CH)-N(CHCHCHNH) or -(CH)-N(CHCHNH) group.

[0013] The polyvinylamine preferably has an average molecular weight M in the range of 500 to 100,000 g / mol, as determined by GPC (gel permeation chromatography) using water as the eluent. w Polyvinylamines can be prepared by their polymerization of N-vinylformamide followed by saponification ( 1 The degree of hydrolysis may range from 20 to 100%, for example 80 to 100%, as determined by H NMR. Fully hydrolyzed polyvinylamine is preferred.

[0014] Polyvinylamine may have an average of 2 to 200, preferably 25 to 100, primary amino groups per molecule.

[0015] The term "polyethyleneimine" in the context of the present invention refers not only to polyethyleneimine homopolymers, but also to polyalkyleneimines containing an NH-CH-CH-NH structural element together with other alkyleneimine structural elements, such as an NH-CH-CH-CH-NH structural element, an NH-CH-CH(CH)-NH structural element, an NH-(CH)-NH structural element, an NH-(CH)-NH structural element, an NH-(CH)-NH structural element, or an (NH-(CH)-NH structural element), with the proviso that the NH-CH-CH-NH structural element predominates in terms of molar distribution. Preferred polyethyleneimines contain an NH-CH-CH-NH structural element that predominates in terms of molar distribution, for example, representing 60 mol % or more, more preferably at least 70 mol %, relative to all alkyleneimine structural elements. In a particular embodiment, the term polyethyleneimine refers to a polyalkyleneimine having only one or zero alkyleneimine structural element per molecule that is different from NH-CH-CH-NH.

[0016] In one embodiment of the present invention, the average molecular weight M of the branched polyethyleneimine w The average molecular weight M of the branched polyethyleneimine is in the range of 500 to 100,000 g / mol, preferably up to 50,000 g / mol, more preferably from 800 to up to 25,000 g / mol. w can be determined by gel permeation chromatography (GPC) using 1.5 wt % aqueous formic acid as the eluent and cross-linked polyhydroxyethyl methacrylate as the stationary phase.

[0017] In one embodiment of the present invention, the branched polyalkyleneimine has a polydispersity Q=M of at least 3.5, preferably in the range of 3.5 to 10, more preferably in the range of 4 to 9, even more preferably in the range of 4.0 to 5.5. w / M nIn another embodiment of the present invention, the branched polyalkyleneimine has a polydispersity Q=M of 3.4 or less, for example in the range of 1.1 to 3.0, more preferably 1.3 to 2.5, and even more preferably 1.5 to 2.0. w / M n Shows.

[0018] Branched polyethyleneimine is 13 The branching degree, as determined by C NMR spectroscopy, may range from 0.30 to 0.75, preferably from 0.5 to 0.7, and more preferably from 0.55 to 0.7. In the context of the present invention, the term "branched polyethyleneimine" includes polymers also known as highly branched polyethyleneimines. The branching degree is calculated as (D+T) / (D+T+L), where D refers to dendritic (or tertiary) amine groups, L (linear) refers to secondary amino groups, and L (linear) refers to primary amino groups. Branched polyethyleneimines may be obtained by polymerization of ethyleneimine (aziridine).

[0019] The term "polypropyleneimine" in the context of the present invention refers not only to polypropyleneimine homopolymers, but also to those containing the NH-CH-CH-CH-NH structural element or the NH-CH-CH(CH)-NH structural element together with other alkylenediamine structural elements, such as the NH-CH-CH-NH structural element, the NH-(CH)-NH structural element, the NH-(CH)-NH structural element, the NH-(CH)-NH structural element, or the (NH-(CH)-NH structural element, provided that the NH-CH-CH-CH-NH structural element or the NH-CH-CH(CH)-NH structural element is the majority in terms of molar distribution. , also refers to polyalkyleneimine. Preferred polypropyleneimine contains a majority of NH-CH-CH-CH-NH or NH-CH-CH(CH)-NH structural elements in terms of molar distribution, for example, representing 60 mol% or more, more preferably at least 70 mol%, of all alkyleneimine structural elements. In a special embodiment, polypropyleneimine refers to a polyalkyleneimine having one or zero alkyleneimine structural elements per molecule that are different from both NH-CH-CH-CH-NH and NH-CH-CH(CH)-NH.

[0020] Preferably, the branching degree of the branched polypropyleneimine is 13 It is in the range of 0.30 to 0.75, preferably 0.5 to 0.7, and more preferably 0.55 to 0.7, as determined by C NMR spectroscopy.

[0021] The branched polyethyleneimine and branched polypropyleneimine may have 2 to 200 primary amino groups per molecule, and preferably have 4 to 50 primary amino groups per molecule.

[0022] Polylysine is preferably a polypeptide having an average of 3 to 50, preferably 25 to 35, lysine units per molecule, for example, 3 to 9 or 25 to 35 lysine units. Polylysine may be selected from α-polylysine and ε-polylysine, with ε-polylysine being preferred. Polylysine may be based on D-lysine and L-lysine and mixtures thereof, with the L-enantiomer being preferred. Another embodiment of polylysine is so-called branched polylysine. In this context, branched polylysine contains lysine moieties, in which both amino groups form amide bonds with other lysine moieties.

[0023] During production, partial racemization may occur, but the L-enantiomer predominates.Furthermore, the term polylysine in the context of the present invention includes polypeptides containing lysine and at least one additional amino acid, such as alanine, glycine, valine, threonine, etc., and the majority of amino acids in the polylysine is lysine.However, polylysine containing lysine as the only amino acid building block is preferred.

[0024] In one embodiment of the present invention, the main chain (a) has an average molecular weight M in the range of 500 to 20,000 g / mol. w The branched polyethyleneimine is selected from the branched polyethyleneimine having the formula:

[0025] The N4 amine may be used in pure form or with 0.1 to 20% by weight of the N3-amine as an impurity.

[0026] In one embodiment of the present invention, the backbone (a) is selected from N4 amines, polyvinylamines, branched polyethyleneimines, and polylysines, in particular branched polylysines and ε-polylysines.

[0027] (CH2) of the main chain (a) a Of the -NH2 groups, (b) at least 40 mol % of the CH—(CH) a The -NH group is a monosaccharide, disaccharide, or polysaccharide-based sugar, hereinafter also referred to as moiety (b), of the general formula -(CH)a -NH-CH2 to a secondary amine. It is clear that the conversion is under reducing conditions.

[0028] Suitable sugars for the formation of part (b) are reducing sugars. During the conversion, a ring-opening reaction is observed.

[0029] Preferably, -(CH2) a At least 50 mol % of the -NH2 groups are converted.

[0030] Monosaccharides suitable for part (b) should be based on aldose sugars such as glyceraldehyde, erythrose, threose, ribose, arabinose, xylose, and lyxose, as well as hexoses such as glucose and galactose, preferably the D-enantiomers in each case. Preferred monosaccharides are arabinose, xylose, and glucose.

[0031] Examples of disaccharides suitable for moiety (b) are cellobiose, lactose, and maltose. Mixtures such as glucose syrup are also suitable.

[0032] Examples of polysaccharides are maltodextrin and dextrin, with maltodextrin being preferred. The dextrose equivalent is the ratio of the -(CH2) of the main chain (a) to the dextrose equivalent. a It can be used to calculate the amount of "aldehyde" groups that can react with -NH2 groups.

[0033] The percentage of converted amino groups in the backbone (a) is determined by measuring the secondary amine number, ASTM D2074. In one embodiment of the present invention, the polymer (A) has an amine number (measured according to DIN 53240 (2013)) ranging from 10 to 2000, preferably from 25 to 700 mg KOH / g polymer (A).

[0034] Details of the conversion reaction are further disclosed below.

[0035] The compositions of the present invention may contain impurities from the synthesis of polymer (A), such as unreacted sugars based on mono-, di-, or polysaccharides, respectively, or unreacted backbone (a), particularly in embodiments where backbone (a) has fewer than 5 primary amino groups per molecule, or reduced polyols based on mono-, di-, or polysaccharides.

[0036] In one embodiment of the present invention, the composition of the present invention contains polymer (A) in an amount ranging from 0.1 to 10% by weight based on the total solids content, which is determined by evaporating volatile materials in a vacuum at a maximum temperature of 100°C.

[0037] The detergent compositions of the present invention may be solid or liquid, but preferably they are liquid at ambient temperature. More preferably, the detergent compositions of the present invention are aqueous compositions. The term "aqueous composition" in the context of the present invention refers to a composition that is liquid at ambient temperature and whose continuous phase contains at least 75% by volume of water.

[0038] In one embodiment of the present invention, the composition of the present invention comprises at least one enzyme. The enzyme is identified by its polypeptide sequence (also referred to herein as its amino acid sequence). The polypeptide sequence specifies the three-dimensional structure of the enzyme, including the "active site," which therefore determines the catalytic activity of the enzyme. The polypeptide sequence can be identified by its SEQ ID NO:. In accordance with the World Intellectual Property Organization (WIPO) Standard ST.25 (1998), amino acids are represented herein using their three-letter code with the first letter capitalized or their single-letter equivalents.

[0039] Any enzyme according to the present invention refers to a parent enzyme and / or a variant enzyme, both of which have enzymatic activity. An enzyme with enzymatic activity is enzymatically active or effects an enzymatic conversion, meaning that the enzyme acts on a substrate and converts it into a product. As used herein, the term "enzyme" excludes inactive variants of an enzyme.

[0040] A "parent" sequence (of a parent protein or enzyme, also called a "parent enzyme") is a starting sequence for introducing changes into the sequence (e.g., by introducing one or more amino acid substitutions, insertions, deletions, or a combination thereof) to result in a "variant" of the parent sequence. The term parent enzyme (or parent sequence) includes wild-type enzymes (sequences) and synthetically produced sequences (enzymes) that are used as starting sequences for introducing (further) changes.

[0041] The terms "enzyme variant" or "sequence variant" or "variant enzyme" refer to an enzyme that differs to some extent in its amino acid sequence from its parent enzyme. Unless otherwise specified, a variant enzyme that is "enzymatically active" means that the variant enzyme has the same type of enzymatic activity as the corresponding parent enzyme.

[0042] In describing variants of the present invention, the following nomenclature is used: Amino acid substitutions are described by giving the original amino acid of the parent enzyme, followed by the position number in the amino acid sequence, followed by the substituted amino acid. Amino acid deletions are described by giving the original amino acid of the parent enzyme, followed by the position number in the amino acid sequence, followed by a *. Amino acid insertions are described by giving the original amino acid of the parent enzyme, followed by the position number in the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, the insertion of a lysine at position 180 next to a glycine would be designated as "Gly180GlyLys" or "G180GK." If the substitution and insertion occur at the same position, this can be designated as S99SD+S99A or, for short, S99AD. Degeneracy in nomenclature occurs when an amino acid residue identical to an existing amino acid residue is inserted. For example, if a glycine were inserted after the glycine in the above example, this would be designated as G180GG. Where different alterations can be introduced at a position, the different alterations are separated by commas, e.g., "Arg170Tyr,Glu" represents the substitution of arginine at position 170 with tyrosine or glutamic acid, respectively. Alternatively, the different alterations or optional substitutions may be indicated in parentheses, e.g., Arg170[Tyr,Gly] or Arg170{Tyr,Gly}; or simply R170[Y,G] or R170{Y,G}; or fully R170Y, R170G.

[0043] Enzyme variants can be defined by their sequence identity when compared with the parent enzyme. Sequence identity is usually expressed as "% sequence identity" or "% identity." To calculate sequence identity, a sequence alignment must be generated in the first step. According to the present invention, a pairwise global alignment must be generated, which means that two sequences must be aligned over their entire length, which is usually generated by using a mathematical method called an alignment algorithm. According to the present invention, the alignment is generated by using the Needleman and Wunsch algorithm (J. Mol. Biol. (1979) 48, pp. 443-453), which means that two sequences must be aligned over their entire length. Preferably, the program "NEEDLE" (European Molecular Biology Open Software Suite (EMBOSS)) is used in the present invention with the program's default parameters (gap open = 10.0, gap extension = 0.5, and matrix = EBLOSUM62).

[0044] According to the present invention, the following %-identity calculation is: % identity = (identical residues / length of the alignment region showing each sequence of the present invention over its full length) * 100.

[0045] According to the present invention, enzyme variants can be described as amino acid sequences that are at least n% identical to the amino acid sequence of their respective parent enzymes, where "n" is an integer between 10 and 100. In one embodiment, the variant enzyme is at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the full-length amino acid sequence of the parent enzyme, and the enzyme variant has enzymatic activity.

[0046] "Enzyme activity" refers to the catalytic effect exerted by an enzyme and is usually expressed in units per milligram of enzyme (specific activity) related to the molecules of substrate converted per minute per molecule of enzyme (molecular activity). A variant enzyme may possess enzymatic activity according to the present invention if the enzyme variant exhibits at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the enzymatic activity of the respective parent enzyme.

[0047] In one embodiment, the enzyme is selected from hydrolases, preferably from proteases, amylases, lipases, cellulases, mannanases.

[0048] In one embodiment of the present invention, the composition of the present invention comprises: (B) At least one hydrolase (hereinafter also referred to as hydrolase (B)), which is preferably selected from lipases (hereinafter also referred to as lipases (B)).

[0049] "Lipase," "lipolytic enzyme," and "lipid esterase" all refer to enzymes in EC class 3.1.1 ("carboxyl ester hydrolases"). Such lipases (B) may have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes with cutinase activity may be referred to herein as cutinases), sterol esterase activity (EC 3.1.1.13), and / or wax-ester hydrolase activity (EC 3.1.1.50). Lipases (B) include those of bacterial or fungal origin.

[0050] Commercially available lipases (B) include, but are not limited to, those sold under the trade names Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Preferenz™ L (DuPont), Lumafast (originally from Genencor), and Lipomax (Gist-Brocades / now DSM).

[0051] In one aspect of the invention, the lipase (B) is selected from the following: lipases from the genus Humicola (synonym Thermomyces), such as those from H. lanuginosa (T. lanuginosus) as described in EP 258068, EP 305216, WO 92 / 05249 and WO 2009 / 109500 or from H. insolens as described in WO 96 / 13580; lipases from Pseudomonas strains (some of which have now been renamed Burkholderia), such as P. alcaligenes or P. pseudoalcaligenes (EP 218272, WO 94 / 25578, WO 95 / 30744, WO 95 / 35381, WO 96 / 00292), P. cepacia (EP 331376), P. stutzeri (GB 1372034), P. fluorescens, Pseudomonas species sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (WO 96 / 12012), Pseudomonas mendocina (WO 95 / 14783), P. glumae (WO 95 / 35381, WO 96 / 00292); Streptomyces griseus (WO 2011 / 150157) and S.Lipases from S. pristinaespiralis (WO 2012 / 137147), GDSL-type Streptomyces lipases (WO 2010 / 065455); lipases from Thermobifida fusca disclosed in WO 2011 / 084412; lipases from Geobacillus stearothermophilus disclosed in WO 2011 / 084417; Bacillus lipases, such as those disclosed in WO 00 / 60063, Dartois et al. (1992), Biochemica et Biophysica Bacillus subtilis, B. stearothermophilus (B. stearothermophilus) (JP 64-074992 A) or B. pumilus (B.Lipases derived from Candida pumilus (WO 91 / 16422); and lipases derived from Candida antarctica disclosed in WO 94 / 01541. Suitable lipases (B) include variants of the above lipases that have lipolytic activity. Such suitable lipase variants are developed by the methods disclosed, for example, in WO 95 / 22615, WO 97 / 04079, WO 97 / 07202, WO 00 / 60063, WO 2007 / 087508, EP 407225, and EP 260105. Such suitable lipase variants are, for example, those developed by the methods as disclosed in WO 95 / 22615, WO 97 / 04079, WO 97 / 07202, WO 00 / 60063, WO 2007 / 087508, EP 407225 and EP 260105.

[0052] Suitable lipases (B) also include lipolytically active variants of the lipases described above. Suitable lipase variants include variants having at least 40-100% identity to the full-length polypeptide sequences of the parent enzymes described above. In one embodiment, the lipolytically active lipase variants may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the full-length polypeptide sequences of the parent enzymes disclosed above.

[0053] Lipase (B) has "lipolytic activity." Methods for determining lipolytic activity are well known in the literature (see, e.g., Gupta et al. (2003), Biotechnol. Appl. Biochem. 37:63-71). For example, lipase activity can be measured by ester bond hydrolysis of the substrate paranitrophenyl palmitate (pNP-Palmitate, C:16), releasing the yellow colored pNP, which can be detected at 405 nm.

[0054] In one embodiment, the lipase (B) is selected from fungal triacylglycerol lipases (EC class 3.1.1.3). The fungal triacylglycerol lipase may be selected from Thermomyces lanuginosa lipases. In one embodiment, the at least one Thermomyces lanuginosa lipase is selected from the triacylglycerol lipases according to amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438 and variants thereof having lipolytic activity.

[0055] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity that is at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the full-length polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 in U.S. Pat. No. 5,869,438.

[0056] The Thermomyces lanuginosa lipase can be selected from variants with lipolytic activity that contain only conservative mutations that do not belong to the functional domain of amino acids 1-269 of SEQ ID NO:2 of U.S. Patent No. 5,869,438. The lipase variant of this embodiment with lipolytic activity can be at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full-length polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 of U.S. Patent No. 5,869,438.

[0057] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity that contain at least the following amino acid substitutions: T231R and N233R when compared to amino acids 1-269 of SEQ ID NO:2 in U.S. Patent No. 5,869,438. The lipase variant can further contain one or more of the following amino acid exchanges: Q4V, V60S, A150G, L227G, and P256K when compared to amino acids 1-269 of SEQ ID NO:2 in U.S. Patent No. 5,869,438.

[0058] The Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising at least the amino acid substitutions T231R, N233R, Q4V, V60S, A150G, L227G, P256K within the polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 of U.S. Pat. No. 5,869,438, and which are at least 95%, at least 96%, or at least 97% similar when compared to the full-length polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 of U.S. Pat. No. 5,869,438.

[0059] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity comprising the amino acid substitutions T231R and N233R within amino acids 1-269 of SEQ ID NO:2 of U.S. Pat. No. 5,869,438, and which are at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full-length polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 of U.S. Pat. No. 5,869,438.

[0060] The Thermomyces lanuginosa lipase may be a variant of amino acids 1-269 of SEQ ID NO:2 of U.S. Patent No. 5,869,438 having lipolytic activity, characterized in that the variant of amino acids 1-269 of SEQ ID NO:2 of U.S. Patent No. 5,869,438 contains the amino acid substitutions T231R and N233R. Such a lipase may be referred to herein as Lipex.

[0061] In one embodiment of the present invention, a combination of at least two of the above lipases (B) may be used.

[0062] In one embodiment of the present invention, lipase (B) is included in the composition of the present invention in an amount such that the final composition of the present invention has a lipolytic enzymatic activity in the range of 100 to 0.005 LU / mg of the composition, preferably 25 to 0.05 LU / mg. A lipase unit (LU) is calculated as the lipase activity measured at a temperature of 30°C, pH = 9.0, and with a substrate of 13 mmol / L Ca in 5 mmol / L Tris buffer. 2+ and the amount of lipase that produces 1 μmol of titratable fatty acids per minute on a pH stat in an emulsion of 3.3 wt.% olive oil and 3.3% gum arabic in the presence of 20 mmol / l NaCl.

[0063] In one embodiment of the present invention, the composition of the invention comprises at least one protease (D), hereinafter also referred to as protease (D).

[0064] In one embodiment, at least one protease (D) is selected from the group of serine endopeptidases (EC 3.4.21), most preferably from the group of subtilisin-type proteases (EC 3.4.21.62). Serine proteases or serine peptidases are characterized by having a serine in the catalytic active site, which forms a covalent adduct with the substrate during the catalytic reaction. In the context of the present invention, the serine protease may be selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21.79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118 or EC 3.4.21.119), plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5), and subtilisin. Subtilisins are also known as subtilopeptidases, e.g., EC 3.4.21.62, the latter of which will also be referred to hereinafter as "subtilisins." The subtilisin-related class of serine proteases shares a common amino acid sequence that defines a catalytic triad that distinguishes them from the chymotrypsin-related class of serine proteases. Both subtilisins and chymotrypsin-related serine proteases have a catalytic triad containing aspartic acid, histidine, and serine.

[0065] Proteases are active proteins that exert "protease activity" or "proteolytic activity." Proteolytic activity relates to the rate of degradation of proteins by proteases or proteolytic enzymes in a defined period of time.

[0066] Methods for assaying proteolytic activity are well known in the literature (see, e.g., Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60:381-395). Proteolytic activity can be determined using Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, abbreviated AAPF; see, e.g., DelMar et al. (1979), Analytical Biochem 99, 316-320) as a substrate. pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in the release of free pNA, which is yellow in color, and is expressed as OD 0. 405 It can be quantified by measuring

[0067] Proteolytic activity can be provided in units per gram of enzyme. For example, 1 U of protease can correspond to the amount of protease that liberates 1 μmole of Folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37° C. (using casein as a substrate).

[0068] Subtilisin type proteases (EC 3.4.21.62) are proteases from the genera Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus or Streptomyces. The protease may be a bacterial protease derived from a microorganism selected from the group consisting of proteases derived from the genus Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

[0069] In one embodiment of the invention, the at least one protease (D) is selected from the group consisting of Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus The protease is selected from Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus thuringiensis.

[0070] In one embodiment of the present invention, the at least one protease (D) is selected from the group consisting of subtilisin from Bacillus amyloliquefaciens BPN' (described in Vasantha et al. (1984) J. Bacteriol. Volume 159, pp. 811-819 and J.A. Wells et al. (1983), Nucleic Acids Research, Volume 11, pp. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; E.L. Smith et al. (1968), J. Biol. Chem., Volume 243, pp. 2184-2191 and Jacobs et al. (1985), Nucleic Acids Research, Vol. 11, pp. 2184-2191); 13, pp. 8913-8926); subtilisin PB92 (the native sequence of alkaline protease PB92 is described in EP 283075 A2); subtilisins 147 and / or 309 (Esperase® and Savinase®, respectively) disclosed in WO 89 / 06279; subtilisins derived from Bacillus lentus, as disclosed in WO 91 / 02792, such as those derived from Bacillus lentus DSM 5483 or variants of Bacillus lentus DSM 5483 described in WO 95 / 23221; subtilisin B from Bacillus alkalophilus, as disclosed in DE 10064983 A1. subtilisins from Bacillus alcalophilus (DSM 11233); subtilisins from Bacillus gibsonii (DSM 14391) disclosed in WO 2003 / 054184; subtilisins from Bacillus sp. (DSM 14390) disclosed in WO 2003 / 056017; and subtilisins from Bacillus sp. disclosed in WO 2003 / 055974.) (DSM 14392); a subtilisin from Bacillus gibsonii (DSM 14393) disclosed in WO 2003 / 054184; a subtilisin having SEQ ID NO: 4 described in WO 2005 / 063974; a subtilisin having SEQ ID NO: 4 described in WO 2005 / 103244; a subtilisin having SEQ ID NO: 7 described in WO 2005 / 103244; and a subtilisin having SEQ ID NO: 2 described in German Patent Application Publication No. DE 102005028295.4.

[0071] Examples of proteases useful according to the present invention include variants described in WO 92 / 19729, WO 95 / 23221, WO 96 / 34946, WO 98 / 20115, WO 98 / 20116, WO 99 / 11768, WO 01 / 44452, WO 02 / 088340, WO 03 / 006602, WO 2004 / 03186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2011 / 036264 and WO 2011 / 072099. A suitable example is SEQ ID NO: 22 (Bacillus lentus) as described in EP 1921147, which has amino acid substitutions at one or more of the following positions, in particular having proteolytic activity: lentus) DSM5483) which is the sequence of the mature alkaline protease from DSM5483) at positions 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 131, 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252, and 274 (according to BPN numbering). In one embodiment, such proteases are not mutated at positions Asp32, His64, and Ser221 (according to BPN numbering).

[0072] In one embodiment, at least one protease (D) is a protease having the sequence SEQ ID NO: 22 described in EP 1921147 or at least 80% identical thereto and having proteolytic activity. In one embodiment, said protease is characterized by having the amino acid glutamic acid, or aspartic acid, or asparagine, or glutamine, or alanine, or glycine, or serine at position 101 (according to BPN numbering) and has proteolytic activity. In one embodiment, the protease comprises one or more additional substitutions: (a) threonine (3T) at position 3; (b) isoleucine (4I) at position 4; (c) alanine, threonine, or arginine (63A, 63T, or 63R) at position 63; (d) aspartic acid or glutamic acid (156D or 156E) at position 156; (e) proline (194P) at position 194; (f) methionine (199M) at position 199; (g) isoleucine (205I) at position 205; (h) aspartic acid, glutamic acid, or glycine (217D, 217E, or 217G) at position 217; or (i) a combination of two or more amino acids according to (a)-(h).

[0073] At least one protease (D) may be at least 80% identical to SEQ ID NO: 22 described in EP 1 921 147 B1 and is characterized in that it comprises one amino acid (according to (a) to (h)) or a combination according to (i) together with amino acids 101E, 101D, 101N, 101Q, 101A, 101G, or 101S (according to BPN numbering). In one embodiment, the protease comprises the mutations (according to BPN numbering) R101E, or S3T + V4I + V205I, or R101E and S3T, V4I, and V205I, or S3T + V4I + V199M + V205I + L217D, and is characterized in that it has proteolytic activity. A protease having the sequence of SEQ ID NO: 22 described in EP 1 921 147 B1 comprising 101E may be referred to herein as Lavergy.

[0074] In one embodiment, the protease of SEQ ID NO: 22 described in EP 1921147 is characterized in that it comprises the mutations (according to BPN numbering) S3T+V4I+S9R+A15T+V68A+D99S+R101S+A103S+I104V+N218D and has proteolytic activity.

[0075] The compositions of the present invention may comprise a combination of at least two proteases (D) (all as disclosed above), preferably selected from the group of serine endopeptidases (EC 3.4.21), more preferably selected from the group of subtilisin-type proteases (EC 3.4.21.62).

[0076] It is preferred to use a combination of lipase (B) and protease (D) in the composition, for example 1 to 2% by weight of protease (D) and 0.1 to 0.5% by weight of lipase (B), both relative to the total weight of the composition.

[0077] In the context of the present invention, a lipase (B) and / or a protease (D) is considered stable if its enzymatic activity "available for application" is at least 60% compared to the initial enzymatic activity before storage. An enzyme can be called stable in the present invention if its enzymatic activity available for application is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or at least 99.5% compared to the initial enzymatic activity before storage.

[0078] Subtracting a% from 100% gives the "loss of enzyme activity during storage" compared to the initial enzyme activity before storage. In one embodiment, an enzyme is stable according to the present invention if substantially no loss of enzyme activity occurs during storage, i.e., if the loss in enzyme activity is equal to 0% compared to the initial enzyme activity before storage. In the present invention, substantially no loss of enzyme activity can mean that the loss of enzyme activity is less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 9%, less than 8%, less than 7%, less than 6%, or less than 5%.

[0079] In one embodiment of the present invention, the composition of the present invention comprises at least one anionic surfactant, also referred to below as (C) anionic surfactant (C).

[0080] Examples of the anionic surfactant (C) include C8 to C 18 -Alkyl sulfates, C8-C 18 -Fatty alcohol polyether sulfate, ethoxylated C4-C 12 -sulfuric acid half esters of alkylphenols (ethoxylated: 1 to 50 mol ethylene oxide / mol), C 12 ~C 18 Sulfofatty acid alkyl esters, such as C 12 ~C 18 Sulfofatty acid methyl ester, further C 12 ~C 18 -Alkyl sulfonic acid and C 10 ~C 18 -Alkali metal and ammonium salts of alkylarylsulfonic acids. The alkali metal salts of the above compounds are preferred, in particular the sodium salts.

[0081] Further examples of anionic surfactants (C) are soaps, for example the sodium or potassium salts of stearic acid, oleic acid, palmitic acid, carboxylic acid ether and alkyl ether phosphates.

[0082] In a preferred embodiment of the present invention, the anionic surfactant (C) is represented by the general formula (I): R1 -O(CH2CH2O) x1 -SO3M (I) [In the formula, R 1 nC 10 ~C 18 - alkyl, especially those having an even number of carbon atoms, such as n-decyl, n-dodecyl, n-tetradecyl, n-hexadecyl or n-octadecyl, preferably C 10 ~C 14 -alkyl, more preferably nC 12 -alkyl, x1 is a number ranging from 1 to 5, preferably 2 to 4, and even more preferably 3; M is selected from alkali metals, preferably potassium, and even more preferably sodium. The compound is selected from the compounds according to the formula:

[0083] In the anionic surfactant (C), x1 may be an average number, and therefore x1 is not necessarily an integer, but in each molecule of formula (I), x1 represents an integer.

[0084] In one embodiment of the present invention, the composition of the present invention may contain 0.1 to 60% by weight of an anionic surfactant (C), preferably 5 to 50% by weight.

[0085] The compositions of the present invention may contain ingredients other than those listed above, such as nonionic surfactants, fragrances, dyes, biocides, preservatives, enzymes, hydrotropes, builders, viscosity modifiers, polymers, buffers, antifoam agents, and anticorrosion additives.

[0086] Preferred compositions of the present invention may contain one or more nonionic surfactants.

[0087] Preferred nonionic surfactants are alkoxylated alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or propylene oxide, alkyl polyglycosides (APGs), hydroxyalkyl mixed ethers and amine oxides.

[0088] Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds of the general formula (II): [ka] where the variables are defined as follows: R 2 are the same or different and are hydrogen and straight chain C1-C 10 alkyl, preferably identical in each case and ethyl, particularly preferably hydrogen or methyl, R 3 is C8~C 22 -Alkyl, branched or linear, e.g., n-CH 17 , nC 10 H 21 , nC 12 H 25 , nC 14 H 29 , nC 16 H 33 or nC 18 H 37 is selected from R 4 is C1~C 10 - alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl or isodecyl, The variables e and f are in the range of 0 to 300, and the sum of e and f is at least 1, preferably in the range of 3 to 50. Preferably, e is in the range of 1 to 100, and f is in the range of 0 to 30.

[0089] In one embodiment, the compound of general formula (II) may be a block copolymer or a random copolymer, with block copolymers being preferred.

[0090] Other preferred examples of alkoxylated alcohols include, for example, those represented by the general formula (III): [ka] where the variables are defined as follows: R 2 are identical or different and are selected from hydrogen and linear C1-C0 alkyl, preferably identical in each case and ethyl, particularly preferably hydrogen or methyl, R 5 C6~C 20 -Alkyl, branched or linear, especially n-CH 17 , nC 10 H 21 , nC 12 H 25 , nC 13 H 27 , nC 15 H 31 , nC 14 H 29 , nC 16 H 33 , nC 18 H 37 is selected from a is a number ranging from 0 to 10, preferably from 1 to 6; b is a number ranging from 1 to 80, preferably from 4 to 20; d is a number ranging from 0 to 50, preferably from 4 to 25. is a compound of

[0091] The sum of a+b+d is preferably in the range of 5-100, and even more preferably in the range of 9-50.

[0092] The compounds of general formulae (IIIa) and (IIIb) may be block copolymers or random copolymers, with block copolymers being preferred.

[0093] Further suitable nonionic surfactants are selected from di- and multi-block copolymers composed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, especially linear C4-C 16 -Alkyl polyglucosides and branched C8-C 14 Likewise suitable are alkyl polyglycosides, for example compounds of the general formula (IV) [ka] During the ceremony, R 6 is C1-C4 alkyl, in particular ethyl, n-propyl or isopropyl, R 7 is -(CH2)2-R 6 and G 1 is selected from monosaccharides having 4 to 6 carbon atoms, in particular glucose and xylose, y1 is in the range of 1.1 to 4, and y1 is an average number.

[0094] Further examples of nonionic surfactants include those represented by the general formulae (V) and (VI): [ka] is a compound of AO is selected from ethylene oxide, propylene oxide and butylene oxide; EO is ethylene oxide, CH2CH2-O, R 8 is a branched or straight chain C8-C 18 -alkyl, and R 5 is defined as above. A 3 O is selected from propylene oxide and butylene oxide; w is a number ranging from 15 to 70, preferably from 30 to 50; w1 and w3 are numbers ranging from 1 to 5, w2 is a number in the range of 13 to 35.

[0095] An overview of further suitable nonionic surfactants is given in EP-A 0 851 023 and DE-A 19 819 187.

[0096] Mixtures of two or more different nonionic surfactants selected from the aforementioned nonionic surfactants may also be present.

[0097] Other surfactants that may be present may be selected from amphoteric (zwitterionic) surfactants and anionic surfactants, and mixtures thereof.

[0098] An example of amphoteric surfactant is a surfactant that has positive and negative charges in the same molecule under the conditions of use.A preferred example of amphoteric surfactant is so-called betaine surfactant.Many examples of betaine surfactant have one quaternary nitrogen atom and one carboxylic acid group per molecule.A particularly preferred example of amphoteric surfactant is cocamidopropyl betaine (lauramidopropyl betaine).

[0099] Examples of amine oxide surfactants include those represented by the general formula (VII): R 9 R 10 R 11 N → O(VII) wherein R 9 , R 10 and R 11 are each independently an aliphatic, alicyclic or C2-C4-alkylene C 10 ~C 20 -alkylamide moieties. Preferably, R 9 is C8~C 20-Alkyl or C2-C4-alkylene C 10 ~C 20 -alkylamide, and R 10 and R 11 are both methyl.

[0100] A particularly preferred example is lauryl dimethylamine oxide, sometimes called lauramine oxide. A further particularly preferred example is cocamidyl propyl dimethylamine oxide, sometimes called cocamidopropyl amine oxide.

[0101] In one embodiment of the present invention, the composition of the present invention may contain 0.1 to 60% by weight of at least one surfactant selected from nonionic surfactants, amphoteric surfactants, and amine oxide surfactants.

[0102] In a preferred embodiment, the solid detergent compositions of the present invention for cleaning applications, particularly for automatic dishwashing applications, do not contain any anionic surfactants.

[0103] The composition of the present invention may contain at least one bleaching agent, also called a bleaching agent. The bleaching agent may be selected from chlorine bleaches and peroxide bleaches, and the peroxide bleaches may be selected from inorganic peroxide bleaches and organic peroxide bleaches. Inorganic peroxide bleaches selected from alkali metal percarbonates, alkali metal perborates, and alkali metal persulfates are preferred.

[0104] Examples of organic peroxide bleaching agents are organic percarboxylic acids, especially organic percarboxylic acids.

[0105] In the composition of the present invention, alkali metal percarbonates, especially sodium percarbonate, are preferably used in the form of coatings. Such coatings can be organic or inorganic. Examples include glycerol, sodium sulfate, silicates, sodium carbonate, and combinations of at least two of the above, such as a combination of sodium carbonate and sodium sulfate.

[0106] Suitable chlorine-containing bleaching agents are, for example, 1,3-dichloro-5,5-dimethylhydantoin, N-chlorosulfamide, chloramine T, chloramine B, sodium hypochlorite, calcium hypochlorite, magnesium hypochlorite, potassium hypochlorite, potassium dichloroisocyanurate and sodium dichloroisocyanurate.

[0107] The composition of the present invention may contain, for example, a chlorine-containing bleaching agent in the range of 3 to 10% by weight.

[0108] The compositions of the present invention may contain one or more bleaching catalysts. The bleaching catalysts may be selected from bleach-accelerating transition metal salts or transition metal complexes, such as manganese-, iron-, cobalt-, ruthenium-, or molybdenum-salen or -carbonyl complexes. Complexes of manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium, and copper with nitrogen-containing tripodal ligands, as well as cobalt-, iron-, copper-, and ruthenium-amine complexes, may also be used as bleaching catalysts.

[0109] The compositions of the present invention may include one or more bleach activators, such as N-methylmorpholinium-acetonitrile salts ("MMA salts"), trimethylammonium acetonitrile salts, N-acylimides such as N-nonanoylsuccinimide, 1,5-diacetyl-2,2-dioxohexahydro-1,3,5-triazine ("DADHT"), or nitrile quaternary ammonium (trimethylammonium acetonitrile salts).

[0110] Further examples of suitable bleach activators are tetraacetylethylenediamine (TAED) and tetraacetylhexylenediamine.

[0111] Examples of fragrances are benzyl salicylate, 2-(4-tert.-butylphenyl) 2-methylpropional, commercially available as Lilial®, and hexyl cinnamaldehyde.

[0112] Examples of dyes are Acid Blue 9, Acid Yellow 3, Acid Yellow 23, Acid Yellow 73, Pigment Yellow 101, Acid Green 1, Solvent Green 7 and Acid Green 25.

[0113] The compositions of the present invention may contain one or more preservatives or biocides. Biocides and preservatives prevent deterioration of the liquid detergent compositions of the present invention due to attack by microorganisms. Examples of biocides and preservatives include BTA (1,2,3-benzotriazole), benzalkonium chloride, 1,2-benzisothiazolin-3-one ("BIT"), 2-methyl-2H-isothiazol-3-one ("MIT"), 5-chloro-2-methyl-2H-isothiazol-3-one ("CIT"), benzoic acid, sorbic acid, iodopropynyl butylcarbamate ("IPBC"), dichlorodimethylhydantoin ("DCDMH"), bromochlorodimethylhydantoin ("BCDMH"), and dibromodimethylhydantoin ("DBDMH").

[0114] Examples of particularly interesting antimicrobial and / or antiseptic agents are: 4,4'-Dichloro-2-hydroxydiphenyl ether (CAS number 3380-30-1), also known as 5-chloro-2-(4-chlorophenoxy)phenol, Diclosan, DCPP (commercially available under the trade name Tinosan® HP100 as a 30% by weight solution of 4,4'-dichloro-2-hydroxydiphenyl ether in 1,2-propylene glycol): and 2-phenoxyethanol (CAS No. 122-99-6, also known as: phenoxyethanol, methylphenyl glycol, phenoxetol, ethylene glycol phenyl ether, ethylene glycol monophenyl ether, Protectol® PE); 2-Bromo-2-nitropropane-1,3-diol (CAS-number 52-51-7, further names: 2-bromo-2-nitro-1,3-propanediol, Bronopol®, Protectol® BN, Myacide AS); glutaraldehyde (CAS number 111-30-8, further names: 1-5-pentanedial, pentane-1,5-dial, glutaral, glutaric dialdehyde, Protectol® GA, Protectol® GA 50, Myacide® GA); glyoxal (CAS number 107-22-2; further names: ethanedial, oxylaldehyde, 1,2-ethanedial, Protectol® GL); 2-butyl-benzo[d]isothiazol-3-one (BBIT, CAS number 4299-07-4); 2-methyl-2H-isothiazol-3-one (MIT, 2-Octyl-2H-isothiazol-3-one (OIT, CAS No. 26530-20-1); 5-chloro-2-methyl-2H-isothiazol-3-one (CIT, CMIT, CAS No. 26172-55-4); 5-chloro-2-methyl-2H-isothiazol-3-one (CMIT, EINECS 247-500-7) and 2-methyl-2H-isothiazol-3-one (MIT, EINECS 220-239-6) mixture (CMIT / MIT mixture, CAS No. 55965-84-9); 1,2-Benzothiazol-3(2H)-one (BIT, CAS No. 2634-33-5); Hexa-2,4-dienoic acid (sorbic acid, CAS number 110-44-1) and its salts, such as calcium sorbate, sodium sorbate, potassium (E,E)-hexa-2,4-dienoate (potassium sorbate, CAS number 24634-61-5); lactic acid and its salts; in particular sodium lactate, L-(+)-lactic acid (CAS number 79-33-4); Benzoic acid (CAS No. 65-85-0, CAS No. 532-32-1) and its salts, such as sodium benzoate, ammonium benzoate, calcium benzoate, magnesium benzoate, MEA-benzoate, potassium benzoate; salicylic acid and its salts, such as calcium salicylate, magnesium salicylate, MEA-salicylate, sodium salicylate, potassium salicylate, TEA-salicylate; benzalkonium chloride, benzalkonium bromide, benzalkonium saccharinate (CAS Nos. 8001-54-5, 68989-29-4, 91080-41-2, 63449-01-5, 68424-85-1, 68391-01-5, 61789-y71-7, 85409-22-9); Didecyldimethylammonium chloride (DDAC, CAS No. 68424-95-3 and CAS No. 7173-51-5); N-(3-aminopropyl)-N-dodecylpropane-1,3-diamine (diamine, CAS No. 2372-82-9); peracetic acid (CAS No. 79-21-0); hydrogen peroxide (CAS No. 7722-84-1).

[0115] The biocide or preservative may be added to the composition of the present invention at a concentration of 0.001 to 10% by weight relative to the total weight of the composition. Preferably, the composition of the present invention contains 2-phenoxyethanol at a concentration of 0.1 to 2% or 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP) at a concentration of 0.005 to 0.6%.

[0116] Thus, the present invention further relates to a method for protecting the compositions of the present invention from bacterial contamination or growth, which method comprises the addition of 2-phenoxyethanol.

[0117] The present invention therefore further relates to a method for imparting antimicrobial activity to textiles after treatment with a composition of the present invention containing 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP).

[0118] Examples of viscosity modifiers are agar, carrageenan, tragacanth, gum arabic, alginate, pectin, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, crosslinked poly(meth)acrylates, such as polyacrylic acid crosslinked with bis(meth)acrylamide, as well as silicic acid, clays (including but not limited to montmorillonite, zeolite, dextrin, and the like), and casein.

[0119] In the context of the present invention, a hydrotrope is a compound that promotes the dissolution of compounds that have limited solubility in water. Examples of hydrotropes include, but are not limited to, organic solvents such as ethanol, isopropanol, ethylene glycol, 1,2-propylene glycol, and other organic solvents that are miscible with water under normal conditions. Further examples of suitable hydrotropes are the sodium salts of toluenesulfonic acid, xylenesulfonic acid, and cumenesulfonic acid.

[0120] Examples of polymers other than polymer (A) are in particular polyacrylic acids and their corresponding alkali metal salts, in particular their sodium salts. Suitable polymers are in particular polyacrylic acids, preferably having an average molecular weight M in the range of 2,000 to 40,000 g / mol, preferably 2,000 to 10,000 g / mol, in particular 3,000 to 8,000 g / mol. w Each of these is partially or completely neutralized with alkali, especially sodium. Polycarboxylate copolymers, especially copolymers of acrylic acid and methacrylic acid and copolymers of acrylic acid or methacrylic acid with maleic acid and / or fumaric acid, are also suitable. Polyacrylic acid and its corresponding alkali metal salts can function as soil redeposition inhibitors.

[0121] A further example of a polymer is polyvinylpyrrolidone (PVP), which can function as a dye transfer inhibitor.

[0122] Further examples of polymers are polyethylene terephthalate, polyoxyethylene terephthalate and polyethylene terephthalate end-capped with one or two hydrophilic groups per molecule, the hydrophilic groups being selected from CH2CH2CH2-SONa, CH2CH(CH2-SONa)2 and CH2CH(CH2SONa)CH2-SONa.

[0123] Examples of buffers are monoethanolamine and N,N,N-triethanolamine.

[0124] An example of a defoaming agent is silicone.

[0125] The composition of the present invention is not only good for cleaning dirty laundry stained with organic fats such as oils.The liquid detergent composition of the present invention is very useful for removing non-bleachable stains from laundry, including but not limited to stains from red wine, tea, coffee, vegetable juice, and various fruit juices such as berry juice.In addition, the composition of the present invention does not leave residue on fabrics.

[0126] A further aspect of the present invention is therefore the use of the compositions of the present invention for laundry care, which in this context includes laundry cleaning.

[0127] In another aspect, the compositions of the present invention are useful for cleaning hard surfaces. Thus, a further aspect of the present invention is the use of the compositions of the present invention in cleaning hard surfaces.

[0128] In the context of the present invention, the term "hard surface cleaning composition" includes home care and institutional cleaners. The term "hard surface cleaning composition" includes, but is not limited to, dishwashing compositions, especially hand dishwashing compositions, automatic dishwashing and porcelain washing compositions, as well as hard surface cleaning compositions such as bathroom cleaning compositions, kitchen cleaning compositions, floor cleaning compositions, plumbing descaling compositions, window cleaning compositions, automobile cleaning compositions, including truck washing, open plant cleaning compositions, yard cleaning compositions, metal cleaning compositions, disinfecting cleaning compositions, farm cleaning compositions, and pressure cleaning compositions, but does not include laundry detergent compositions. A special embodiment of a hard surface cleaning composition is an automatic dishwashing composition.

[0129] In the context of the present invention, the terms "hard surface cleaning composition" and "hard surface cleaner composition" are used interchangeably.

[0130] In the context of the present invention, unless otherwise specified, percentages in relation to ingredients of laundry detergent compositions are percent by weight and refer to the total solids of the respective laundry detergent composition. In the context of the present invention, and unless otherwise specified, percentages in the context of ingredients of detergent compositions for hard surface cleaners are percent by weight and are based on the total solids of the detergent composition for cleaning hard surfaces.

[0131] The compositions of the present invention when used in automatic dishwashing preferably comprise (E) At least one builder component selected from aminopolycarboxylic acids and preferably their alkali metal salts, which in the context of the present invention is also called a complexing agent (E) or a sequestering agent (E). In the context of the present invention, the terms "sequestering agent" and "chelating agent" are used interchangeably.

[0132] Examples of the sequestering agent (E) include alkali metal salts of MGDA (methylglycine diacetate), alkali metal salts of GLDA (glutamic acid diacetate), alkali metal salts of IDS (iminodisuccinic acid), alkali metal salts of EDTA, and alkali metal salts of iminodisuccinic acid (IMDS) in which 20 to 90 mol % of the N atom is CH2COO - Polymers having complexing groups, such as polyethyleneimine, and their respective alkali metal salts, especially their sodium salts, such as MGDA-Na3, GLDA-Na4, or IDS-Na4.

[0133] Preferred sequestering agents are those of the general formula (IXa) [CH3-CH(COO)-N(CH2-COO)2]M 3-x2 H x2 (IXa) wherein M is the same or different and is selected from ammonium and alkali metal cations, such as sodium cations, potassium cations, and combinations of at least two of the foregoing. Ammonium may be alkyl substituted, but is not limited to unsubstituted ammonium NH4 + Preferred examples of alkali metal cations are sodium and potassium and combinations of sodium and potassium, and even more preferred in compounds according to general formula (IIa) are that all M are the same and that they are all Na; In formula (IIa), x2 is in the range of 0 to 1.0. or (IXb) [OOC-CH2CH2-CH(COO)-N(CH2-COO)2]M 4-x3 H x3 (IXb) (wherein M is as defined above, and x3 in formula (IXb) is in the range of 0 to 2.0, preferably up to 1.0), or (IXc) [OOC-CH2-CH(COO)]-N-CH(COO)-CH2-COO]M 4-x4 H x4 (IXc) (wherein M is as defined above, and x4 in formula (IXc) is in the range of 0 to 2.0, preferably up to 1.0). This is due to the following.

[0134] In one embodiment of the invention, the composition of the invention comprises a combination of at least two of the foregoing, for example a combination of a chelating agent according to general formula (IXa) and a chelating agent according to general formula (IXb).

[0135] The chelating agents according to the general formulae (IXa) and (IXb) are preferred, and the chelating agents according to the general formula (IXa) are even more preferred.

[0136] In one embodiment of the present invention, the compound according to general formula (IXa) is selected from the ammonium or alkali metal salts of racemic MGDA and the ammonium and alkali metal salts of a mixture of L- and D-enantiomers according to formula (IXa), said mixture containing predominantly the respective L-isomer with an enantiomeric excess (ee) in the range of 5-99%, preferably 5-95%, more preferably 10-75%, and even more preferably 10-66%.

[0137] In one embodiment of the present invention, the compound according to general formula (IXb) is selected from at least one alkali metal salt of a mixture of the L-enantiomer and the D-enantiomer according to formula (IXb), said mixture containing a racemic mixture or preferably containing predominantly the respective L-isomer with an enantiomeric excess (ee) in the range of, for example, 5-99%, preferably 15-95%.

[0138] The enantiomeric excess of the compound of general formula (IXa) can be determined by measuring polarized light (polarimetry) or preferably by chromatography, for example by HPLC with a chiral column, for example using one or more cyclodextrins as stationary phase or using a chiral stationary phase of the ligand exchange (Pirkle-brush) concept. Determination of the ee (enantiomeric excess) by HPLC is preferred using immobilized optically active amines such as D-penicillamine in the presence of copper(II) salts. The enantiomeric excess of the compound of general formula (IXb) can be determined by measuring polarized light (polarimetry).

[0139] Due to environmental concerns associated with the use of phosphates, advantageous compositions are preferably phosphate-free. "Phosphate-free" in the context of the present invention should be understood to mean that the phosphate and polyphosphate content ranges from the gravimetrically determined detection level to 1% by weight in total, preferably from 10 ppm to 0.2% by weight.

[0140] In one embodiment of the present invention, the composition of the present invention contains a sequestering agent (E) in an amount of 0.5 to 50% by weight, preferably 1 to 35% by weight, based on the total solid content.

[0141] To be suitable as a liquid laundry composition, the compositions of the present invention may be in bulk form or in unit dose form, such as in the form of a sachet or pouch. Suitable materials for pouches are water-soluble polymers such as polyvinyl alcohol.

[0142] In a preferred embodiment of the present invention, the composition of the present invention is in liquid or gel form at ambient temperature. In another preferred embodiment of the present invention, the composition of the present invention is in solid form, such as a powder or tablet, at ambient temperature.

[0143] In one embodiment of the invention, the compositions of the invention are liquid or gel type and have a pH value in the range of 7 to 9, preferably 7.5 to 8.5. In embodiments in which the compositions of the invention are in solid form, these pH values ​​may be in the range of 7.5 to 11, determined at ambient temperature after dissolution in distilled water at 1 g / 100 ml. In embodiments in which the compositions of the invention are used on hard surfaces such as tiles, e.g. bathroom tiles, these pH values ​​may even be acidic, e.g. 3 to 6.

[0144] In one embodiment of the present invention, the composition of the present invention is liquid or gel type and has a total solids content in the range of 8 to 80%, preferably 10 to 50%, as determined by drying under vacuum at 80°C.

[0145] Another aspect of the present invention relates to polymer (A), which is also referred to hereinafter as inventive polymer (A) or simply polymer (A). Inventive polymer (A) is identical to polymer (A), which is described above.

[0146] In one embodiment of the present invention, the polymer (A) of the present invention has an average molecular weight M w in the range of 750 to 350,000 g / mol, preferably 3,000 to 50,000 g / mol. The molecular weight can be measured by GPC using water as an eluent.

[0147] In one embodiment of the present invention, the polymer (A) of the present invention has a Hazen color number in the range of 20 to 500 as determined in a 10% by weight aqueous solution.

[0148] The polymer (A) of the present invention may contain impurities derived from the synthesis of the polymer (A), such as unreacted saccharides based on monosaccharides, disaccharides, or polysaccharides (b), respectively, or unreacted backbone (a), particularly in embodiments where backbone (a) has fewer than five primary amino groups per molecule, or reduced polyols based on monosaccharides, disaccharides, or polysaccharides. The amount of impurities may be in the range of 0.5% to 10% by weight, more preferably in the range of 2% to 5% by weight.

[0149] In one aspect, the present invention relates to a method for improving the cleaning performance of a liquid detergent composition by adding the polymer (A) of the present invention to the detergent composition, preferably comprising at least one lipase and / or at least one protease.

[0150] The term "improved cleaning performance" herein may indicate that polymer (A) provides better, i.e., improved, stain removal under appropriate washing conditions compared to the cleaning performance of a detergent composition lacking polymer (A). In one embodiment, "improved cleaning performance" refers to improved cleaning performance of a detergent comprising polymer (A) and at least one enzyme, preferably at least one hydrolase (B), in particular at least one lipase (B) and / or at least one protease (D), compared to the cleaning performance of a detergent comprising polymer (A) but without enzymes. In one embodiment, "improved cleaning performance" refers to improved cleaning performance of a detergent comprising polymer (A) and an enzyme, preferably a hydrolase (B), more preferably a lipase (B) and / or a protease (D), compared to the cleaning performance of a detergent comprising at least one enzyme, preferably at least one hydrolase (B), preferably a lipase (B) and / or at least one protease (D), but without polymer (A).

[0151] The term "suitable washing conditions" in this specification refers to the conditions actually used in a washing machine, automatic dishwasher or manual washing process, in particular the washing temperature, time, washing mechanism, soap concentration, type of detergent and water hardness.

[0152] The polymer (A) of the invention is eminently suitable as a composition of the invention or for the preparation of a composition of the invention.The polymer (A) of the invention is biodegradable.

[0153] A further aspect of the present invention relates to a process for producing the inventive polymer (A), hereinafter also referred to as the inventive process, which comprises steps (α) and (β): (α) a main chain molecule (a) that is an aliphatic compound having at least four amino groups per molecule, at least one of which is -(CH2) a providing a backbone molecule (a) which is an —NH group and the variable is selected from 2 to 4; (β) reacting the backbone molecule with at least one sugar molecule based on a monosaccharide, disaccharide, or polysaccharide in the presence of hydrogen and a catalyst or in the presence of aminoborane.

[0154] Steps (α) and (β) are described in more detail below.

[0155] The backbone molecule (a) is described in more detail above.

[0156] The ratio of backbone molecules (a) to sugar molecules based on mono-, di- or polysaccharides is preferably selected so that the molar amount of "aldehyde" groups corresponds to at least 40 mol %, preferably 40-100 mol %, more preferably 45-90 mol % of the primary amino groups of backbone (a).

[0157] In one embodiment of the present invention, the backbone molecule (a) is provided in bulk. However, the reaction is preferably carried out in solution, and it is advantageous to provide the backbone molecule (a) in solution. Suitable solvents include water and mixtures of water with alcohols (such as methanol and ethanol), glycols such as ethylene glycol, propylene glycol, and diethylene glycol, and solvents with an average molecular weight M of, for example, up to 500 g / mol. n and the water content is preferably at least 70% by weight. The solubility of many sugars in organic solvents is limited, therefore water and combinations of water with methanol or ethanol are preferred.

[0158] Step (β) involves the reduction of the sugar molecule and coupling with the backbone molecule (a).

[0159] Step (β) can be carried out at a temperature ranging from ambient temperature to 120°C, preferably from 25 to 70°C. For solvents such as methanol and ethanol, the upper limit is the boiling temperature, even more preferably from 40 to 65°C.

[0160] In one embodiment of the invention, step (β) is carried out at a pressure in the range of 1 to 200 bar (absolute), especially when hydrogen is used in the presence of a catalyst. In another embodiment of the invention, step (β) is carried out at a pressure in the range of 1 to 5 bar (absolute), especially when aminoborane is used as the reducing agent, especially at ambient pressure.

[0161] In one embodiment of the invention, particularly when hydrogen is used in the presence of a catalyst, step (β) is carried out at a temperature in the range of 25 to 125° C. In another embodiment of the invention, particularly when aminoborane is used as the reducing agent, step (β) is carried out at a temperature in the range of 20 to 100° C.

[0162] Examples of suitable catalysts are, but are not limited to, hydrogenation catalysts such as Raney metals, such as Raney nickel, and supported metal catalysts such as Ru, Rh, or Pd on charcoal, silica, or ZrO2.

[0163] Examples of suitable aminoboranes are, in particular, aromatic aminoboranes such as aniline-BH3, picoline boranes such as α-picoline borane, pyridine borane, zinc pyridine tetrahydroborate and also other boron-based reducing agents such as sodium cyanoborohydride, sodium triacetoxyborohydride, sodium borohydride and titanium isopropoxide / sodium borohydride.

[0164] Each hydrogen and aminoborane is used in at least a stoichiometric amount relative to the reducible "aldehyde" group of the sugar molecule, and preferably in excess.

[0165] Step (β) is preferably carried out at a weakly acidic pH value, for example, 3 to 6.5, preferably 3.5 to 5.5. The pH value may be adjusted by the addition of a carboxylic acid, such as, but not limited to, formic acid or acetic acid.

[0166] Without wishing to be bound by theory, the inventors hypothesize that in a first reaction, the amino group reacts with the "aldehyde" group under ring-opening and formation of a hemiaminal, which is subsequently reduced to a secondary amino group.

[0167] In one embodiment of the present invention, the reaction time in step (β) generally ranges from 1 to 36 hours.

[0168] When methanol is used as a solvent, the polymer (A) of the present invention precipitates.

[0169] After completion of step (β), the polymer (A) of the present invention is typically obtained as a solution or precipitate. Post-treatment steps, such as, but not limited to, catalyst deactivation or precipitation, may be performed. Unreacted borane and borane reaction products can be removed with the supernatant solvent or by filtration—the polymer (A) of the present invention preferably remains as a precipitate, and the boron compound remains in solution.

[0170] By carrying out the process of the present invention, the polymers of the present invention are obtained in good yield and with sufficient purity.

[0171] The present invention is further illustrated by examples. [Example]

[0172] Overview The amount and type of amine substituted with residues such as those of the backbone (a) and polymer (A), and optionally the presence of hydrogen, can be determined as described for polyethyleneimine in Lukovkin GM et al.: Europ. Polymer Journal 1973, 9, 559-565 and St. Pierre T. et al., Geckle M.: ACS Polym. Prep. 1981, 22, 128-129. 13 This can be determined by identifying primary, secondary, and tertiary amino groups with C-NMR.

[0173] 13 C-NMR spectra were recorded in CDCl 3 on a Bruker AV-401 instrument at ambient temperature. 1 H-NMR spectra were recorded in CDCl3 or CD3OD on a Bruker AV-401 instrument at ambient temperature.

[0174] Percentages are by weight unless otherwise indicated.

[0175] The degree of modification (DM) of the polymer of the present invention is 1 It can be determined by H-NMR spectroscopy, which DM = (moles of reducing sugar reacted with amino groups) / (moles of primary amino groups available on the polyamine backbone) x 100%

[0176] The determination of dextrose equivalent ("DE") is described in "Analytical Methods of the Member Companies of the Corn Refiners Association, Inc. part Dextrose;" or in the Official Journal of the European Community 22.9.79 (First Commission Directive 79 / 796 / EEC of July 26, 1979) No. L239 / 44.

[0177] The following starting materials were used: (a.1): Linear ε-polylysine, K value 19.6, commercially available from JNC Corp., Japan, measured in a 1 wt% aqueous solution (a.2): Branched polylysine, K value 12.5, see synthesis below (a.3): N4 amine, commercially available from BASF SE (a.4): Branched polyethyleneimine, M w = 800 g / mol (GPC in water as eluent), commercially available from BASF SE (b.1): D-Maltose (b.2): Maltodextrin, DE 17.8, purchased from Cargill® Cpur Series (b.3): Maltodextrin, DE 28.0, purchased from Cargill® Cpur Series (b.4): Maltodextrin, DE 37.7, purchased from Cargill® Cpur Series (b.5): D-glucose

[0178] Production of (a.2): Step (α.2): 500 g of an aqueous solution of L-lysine (50 wt %) was placed in a 1000 mL four-neck flask equipped with a stirrer, internal thermometer, gas inlet tube, vacuum condenser, and Dean-Stark receiver. The solution was heated to an internal temperature of 160 °C with stirring, and water was continuously removed. After a reaction time of 4.5 h, water was distilled off under reduced pressure (670 mbar). 272 ​​g of water fraction was collected, and the highly viscous polymer was discharged into a silicone container as quickly as possible while still hot and fluid. The k value of the resulting main chain molecule (a.2) was determined to be 12.5 in a 1 wt % aqueous solution.

[0179] Step (α.5): 500 g of an aqueous solution of L-lysine (50 wt%) was placed in a 1000 mL four-neck flask equipped with a stirrer, internal thermometer, gas inlet tube, vacuum condenser, and Dean-Stark receiver. The solution was heated to an internal temperature of 160°C with stirring, and water was continuously removed. After a reaction time of 3.5 hours, further water was distilled off under reduced pressure (670 mbar). Finally, 255 g of water fraction was recovered, and a high-viscosity polymer was released into the silicone-forming backbone molecule (a.5), which was determined to have an OH of 9.8.

[0180] Steps (α.1), (α.3): The main chain molecules (a.1) and (a.3) were used as commercially available products. Step (α.4): The backbone molecule (4) was degassed in a rotary evaporator before step (β).

[0181] Step (β) using aminoborane: Step (β1). Step (β) using hydrogen / catalyst: Step (β2).

[0182] I. Synthesis of Polymer (A) of the Present Invention I.1 Synthesis of the copolymers of the present invention using α-picoline borane as a reducing agent I.1.1 Step (β ​​1.1) - Synthesis of Polymer (A.1) of the Invention

[0183] In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 20.0 g of (a.1) was added to 110 g of a 10:1 water:acetic acid mixture by weight while stirring. Then, 24.6 g of (b.1) as a powder was added to the solution, followed by the dropwise addition of 7.30 g of a solution of α-picoline borane in 50 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated.

[0184] Post-treatment: The pH value was adjusted to 4 by adding aqueous HCl (1M), and (A.1) was precipitated in excess methanol (1:10 by weight). The precipitate was collected by filtration and dried in a vacuum oven at 40°C to obtain the polymer (A.1) of the present invention, DM: 47%. n : 13,315 g / mol, M w :13,952 g / mol.

[0185] I.1.2 Step (β1.2)—Synthesis of Polymer (A.2) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 20 g of (a.1) was added to 110 g of a 10:1 water:acetic acid mixture by weight while stirring. Then, 57.2 g of (B.1) as a powder was added to the solution, followed by the dropwise addition of 17.0 g of a solution of α-picoline borane in 50 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.2) of the present invention was obtained, DM: 91%, M n : 20,071 g / mol, M w :21,031 g / mol.

[0186] I.1.3 Step (β1.3)—Synthesis of Polymer (A.3) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 10.0 g of (a.2) was added to 60 g of a 10:1 water:acetic acid mixture by weight while stirring. Then, 28.6 g of (b.1) as a powder was added to the solution, followed by the dropwise addition of 4.25 g of a solution of α-picoline borane in 25 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.3) of the present invention was obtained, DM: 81%, M n : 4,460 g / mol, M w :8,278 g / mol.

[0187] I.1.4 Step (β1.4)—Synthesis of Polymer (A.4) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 4.0 g of (a.1) was added to 70 g of a 10:1 mixture of water and acetic acid by weight while stirring. Then, 31.6 g of (b.2) was added to the solution as a powder, followed by the dropwise addition of 3.34 g of a solution of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.4) of the present invention was obtained, DM: 40%, M n : 26,762 g / mol and M w :31,905 g / mol.

[0188] Step I.1.5 (β 1.5)—Synthesis of Polymer (A.5) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 4.0 g of (a.2) was added to 70 g of a 10:1 water:acetic acid mixture by weight while stirring. Then, 31.6 g of (b.2) as a powder with a DE of 17.8 was added to the solution, followed by the dropwise addition of 3.34 g of a solution of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (a.5) of the present invention was obtained, DM: 58%, M n :8,704g / mol and M w :18,551 g / mol.

[0189] Step I.1.6 (β1.6)—Synthesis of Polymer (A.6) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 60.0 g of (b.1) was added to 110 g of a 10:1 mixture of water and acetic acid by weight while stirring. Then, 20.0 g of (a.4) was added to the solution, followed by the dropwise addition of 18.8 g of a solution of α-picoline borane in 50 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.6) of the present invention was obtained, DM: 48%, M n : 1,336 g / mol and M w :1,781 g / mol.

[0190] Step I.1.7 (β1.7)—Synthesis of Polymer (A.7) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 25.3 g of (b.1) was added to 70 g of a 10:1 water:acetic acid mixture by weight while stirring. Then, 3.0 g of (a.4) was added to the solution, followed by the dropwise addition of 2.67 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.7) of the present invention was obtained, DM: 48%, M n : 3,060 g / mol, M w :4,663 g / mol.

[0191] Step I.1.8 (β1.8)—Synthesis of Polymer (A.8) of the Invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 3.0 g of (a.5) was added to 70 g of a 10:1 water:acetic acid mixture by weight while stirring. 20.8 g of (b.2) was then added to the solution, followed by the dropwise addition of 2.20 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.8) of the present invention was obtained, DM: 97%, M n : 4,763 g / mol, M w :6,789 g / mol.

[0192] I.2 Synthesis of the Copolymers of the Invention by Catalytic Hydrogenation I.2.1 General Protocol In a magnetically coupled 300 mL autoclave (stainless steel V4A) equipped with a pitched blade stirrer, electrical heating, internal temperature cascade control, and H2 press-on with repeated differential pressure dosing, 45 g of each sugar (b) was dissolved in water to obtain 100 mL of a 50 wt. % solution. The resulting solution was mixed with the corresponding backbone (a) to obtain a 1:1 DE / amine molar ratio (see Table 2). A 2.25 g amount of catalyst—Ru on charcoal—was added. The autoclave was flushed with nitrogen and then with hydrogen. 10 bar of hydrogen was then pressed in at low temperature. The reactor was heated to 60 °C under 100 bar of hydrogen pressure for 12 hours and stirred at 500 rpm. The autoclave was then allowed to cool to ambient temperature, expanded, and degassed. The resulting reaction mixture was purified by a freeze-drying procedure. Freeze-drying conditions: freeze-drying at approximately 75 °C in the refrigerator and at -70 °C in the condenser (inside the chamber). The sample was rapidly cooled to approximately -50°C in the first chamber using a freeze-dryer sublimation apparatus EKS 100. A compressor then created a "vacuum" in the second chamber with a maximum pressure of 6.10 mbar. This strong negative pressure caused moisture to pass through a valve from the product chamber to the second chamber. The resulting polymer was then washed with 50 mL of methanol before drying.

[0193] I.2.2 Specific examples of tabular formats

[0194] [Table 1]

[0195] II. Cleaning test II.1 Tests using polymers (A.1) to (A.8) In the test procedure based on L.1, 10 g of dipalmitoyl ethyl hydroxyethyl monium methosulfate was mixed with 0.3 g of CaCl2 as a softener. Water was added to make up a total of 100 g. The pH value was 4.

[0196] [Table 2]

[0197] Test soil mixtures were prepared according to Table 5 by mixing 75% deionized water, 20% yellow clay (JIS soil), 3.75% peanut oil (Luhua oil, Shandong), and 1.25% mineral oil. Specifically, 20% clay dispersion was first added to water and homogenized by stirring at 6,500 rpm for 10 minutes. Then, the mixture of two oils was slowly added, and the whole mixture was homogenized for another 10 minutes.

[0198] According to GBT 13174-2008, a Terg-o-meter (RHLG-IV, Shanghai Bank Equipment Co. Ltd, China) containing 12 barrels with respective rotor blades was used as the washing unit to simulate the washing process in the laboratory.

[0199] Before washing, all fabrics were pre-treated with fabric softener. 7 g of the above fabric softener formulation was diluted with 10 L of tap water (25°C) and transferred to a Haier PQ28SW mini washing machine. 300 g of fabrics to be used were placed in the washing machine and agitated for 3 minutes. The treated fabrics were then transferred to another washing machine of the same model without rinsing, spun dry for 1 minute, and then dried at 40°C for 1 hour.

[0200] The wash units were operated at an agitation speed of 120 revolutions per minute (rpm) and each contained 1 L of hard water (100 ppm Ca:Mg = 3:2). Three white test cloths of each type (15 cloths total) were washed in the same barrel at 30°C with 10 g of the clay and oil mixture in 0.93 g of wash liquor containing the detergent formulation shown in Table 3. After washing, the cloths were removed from the wash unit, drained, and rinsed twice with 10 L of tap water for 30 seconds. The wash cycle was repeated two more times with fresh clay and oil mixture and fresh wash liquor. After rinsing in the third wash cycle, the test cloths were air-dried instead. Details of the wash cycle are summarized in Table 4.

[0201] Anti-graying performance was measured at 457 nm using a Datacolor Elrepho 2000 spectrophotometer and characterized by the difference between the remission values ​​of the fabric before washing (except for L.1, after fabric softener treatment) and after washing. The smaller the difference in remission (ΔR), the better the performance. The results are summarized in Table 6.

[0202] For test procedure L.2, a slightly modified process was followed using a yellow clay-oil mixture (WFK soil oil mixture).

[0203] The laboratory washing process was simulated using a Tergotometer (RHLQ-IV by RIDCI) in accordance with GBT 13174-2008, which contained individual barrels with their own rotor blades as washing units. The washing units were operated at the same agitation speed of 120 rpm and each contained 1 L of wash liquor. White test cloths were washed in the same barrel at 30°C along with 10 g of the test soil mixture in a wash liquor containing the detergent formulation shown in Table 3. After washing, the cloths were removed from the washing unit, drained, and rinsed twice with 10 L of tap water for 30 seconds. The wash cycle was repeated three times with a new yellow clay and oil mixture and new wash liquor. After rinsing in the third wash cycle, the test cloths were dried. Details of the wash cycle are summarized in Table 4.

[0204] Anti-graying performance was measured using a Datacolor Elrepho 2000 spectrophotometer at 457 nm and characterized by the difference in remission values ​​(ΔR). Clean fabrics before washing were compared with washed fabrics after washing. The smaller the difference in remission (ΔR), the better the performance. The results are summarized in Table 7.

[0205] [Table 3]

[0206] [Table 4]

[0207] [Table 5]

[0208] [Table 6]

[0209] II.2 Tests using polymers (A.10) to (A.14) of the present invention The following protocol was used: Device LOM (number: 040) Washing temperature: 30℃ Washing time: 60 minutes Base mixture: Commercially available "Persil Kraft-Gel / / Persil 3g / L" German water hardness 2.5mmol CaCO3 / L Polymerization 3% (referring to the base mixture) Test monitor 2xMON-BASF-57 or 94 Stain enhancer and base cloth 2.5g SBL 2004, 20g BW 283

[0210] Color measurements were used to evaluate the overall level of cleaning. The reflectance values ​​of the monitor stains were measured using a spherical reflectance spectrometer (Datacolor, USA, SF500 model, wavelength range 360-700 nm, optical geometry d / 8°) equipped with a 460 nm UV cutoff filter. Here, using the CIE-Lab color space classification, the lightness L*, a* value on the red-green axis, and b* value on the yellow-blue axis were measured for each monitor stain before and after cleaning and averaged. The values ​​were determined by a color evaluation tool and expressed as follows:

number

[0211] [Table 7]

[0212] III. Biodegradability test Summary: The test was conducted in accordance with the OECD guidelines. According to the OECD guidelines, the test is valid in the following cases: 1. The reference reaches 60% within 14 days. 2. The difference between the extreme values ​​of the replicate tests up to the end of the test is less than 20%. 3. The oxygen uptake of the inoculum blank should be 20-30 mg O2 / l and should not exceed 60 mg O2 / l. 4. The pH value measured at the end of the test must be between 6 and 8.5.

[0213] Description of test methods used in connection with the present invention: Biodegradation in wastewater was tested in triplicate using the manometric respirometry method of OECD 301F, an aerobic test that measures the biodegradation of wastewater samples by measuring oxygen consumption. A measured amount of wastewater was spiked with 100 mg / L of the test substance, nominally the sole carbon source, along with an inoculum (aerated sludge from a municipal wastewater treatment plant in Shanghai, PR China, polymers (A.1)-(A.8), or Mannheim, Germany). The sludge was stirred in a sealed flask at a constant temperature (25°C) for 28 days. Oxygen consumption was determined by measuring the pressure change in the sealed flask using an Oxi TopC. The evolved carbon dioxide was absorbed in a solution of sodium hydroxide. A nitrification inhibitor was added to the flask to prevent oxygen consumption by nitrification. The amount of oxygen taken up by the microbial population during biodegradation of the test substance (corrected for uptake by a parallel blank inoculum) is expressed as a percentage of ThOD (theoretical oxygen demand as determined by elemental analysis of the compound). A positive control, glucose / glutamic acid, is run as a reference alongside the test sample in each cabinet. Calculation: Theoretical oxygen demand: The amount of O2 required to oxidize a compound to its final oxidation product. This amount is calculated using elemental analysis data. %biodegradable Experimental O2 uptake x 100 and divide by theoretical oxygen demand.

[0214] The results of the biodegradability tests are summarized in Table 9.

[0215] [Table 8]

[0216] IV. Synthesis of Polymers (A.13) to (A.17) of the Invention The following starting materials were used: (a.1): Linear ε-polylysine, K value 19.6, commercially available from JNC Corp., Japan, measured in a 1 wt% aqueous solution (a.2): Branched polylysine, K value 12.5, see synthesis below (a.3): N4 amine, commercially available from BASF SE (a.4): Branched polyethyleneimine, M w = GPC / mol (800 g in water as eluent), commercially available from BASF SE (a.5): Branched polylysine, K value 9.8, see synthesis below (a.6): Branched polylysine, K value 10.7, see synthesis below (a.7): Branched polylysine, K value 11.0, see synthesis below (b.1): D-Maltose (b.2): Maltodextrin, DE 17.8, purchased from Cargill® Cpur Series (b.3): Maltodextrin, DE 28.0, purchased from Cargill® Cpur Series (b.4): Maltodextrin, DE 37.7, purchased from Cargill® Cpur Series (b.5): D-glucose (b.6): Maltodextrin, DE9.0, purchased from Rockete Glucidex Series (b.7): Cellulose, DE16.7 purchased from Sigma-Aldrich

[0217] Production of (a.2): Step (α.6): Branched polylysine K value 10.7 A 1000 ml four-neck flask equipped with a stirrer, internal thermometer, gas inlet tube, vacuum condenser, and Dean-Stark receiver was charged with 500 g of an aqueous solution of L-lysine (50 wt %). The solution was heated to an internal temperature of 160 °C with stirring, and water was continuously removed. After a reaction time of 4.0 hours, water was distilled off under reduced pressure (670 mbar). 260 g of water fraction was collected, and the highly viscous polymer was discharged into a silicone container as quickly as possible while still hot and fluid. The k value of the resulting main chain molecule (a.6) was determined to be 10.7 in a 1 wt % aqueous solution.

[0218] Step (α.7): Branched polylysine K value 11.0 A 1000 ml four-neck flask equipped with a stirrer, internal thermometer, gas inlet tube, vacuum condenser, and Dean-Stark receiver was charged with 500 g of an aqueous solution of L-lysine (50 wt %). The solution was heated to an internal temperature of 160°C with stirring, and water was continuously removed. After a reaction time of 4.0 hours, water was distilled off under reduced pressure (670 mbar). 262 g of water fraction was collected, and the highly viscous polymer was discharged into a silicone container as quickly as possible while still hot and fluid. The k value of the resulting main chain molecule (a.7) was determined to be 11.0 in a 1 wt % aqueous solution.

[0219] Synthesis of Polymer (A) of the Present Invention Synthesis of the copolymer of the present invention with α-picoline borane as the reducing agent

[0220] Polymers of the invention (A.13) In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 3.0 g of (a.6) was added to 70 g of a 10:1 water:acetic acid mixture by weight while stirring. 20.8 g of (b.2) was then added to the solution, followed by the dropwise addition of 2.20 g of a solution of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at 85 °C for 24 h. After workup as described above, the polymer (A.13) of the present invention was obtained, with a DM of 72%, Mn of 5,426 g / mol, and Mw of 6,974 g / mol.

[0221] Polymers (A.14) of the invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 3.0 g of (a.6) was added to 90 g of a 10:1 water:acetic acid mixture by weight while stirring. Next, 42.0 g of (b.6) was added to the solution, followed by the dropwise addition of 2.25 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at ambient temperature until the reaction mixture became clear and no visible bubbles were generated. After workup as described above, the polymer (A.14) of the present invention was obtained, DM: 48%, Mn: 6,913 g / mol, Mw: 17,322 g / mol.

[0222] Polymers (A.15) of the invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 2.7 g of (a.2) was added to 90 g of a 10:1 water:acetic acid mixture by weight while stirring. Next, 42.0 g of (b.6) was added to the solution, followed by the dropwise addition of 2.25 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at 85 °C for 24 h. After workup as described above, the polymer (A.15) of the present invention was obtained, with a DM of 44%, Mn of 12,252 g / mol, and Mw of 50,844 g / mol.

[0223] Polymers (A.16) of the invention In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 4.0 g of (a.1) was added to 90 g of a 10:1 water:acetic acid mixture by weight while stirring. Next, 47.4 g of (b.2) was added to the solution, followed by the dropwise addition of 3.34 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at 60 °C for 24 h. After workup as described above, the polymer (A.16) of the present invention was obtained, with a DM of 86%, Mn of 50,570 g / mol, and Mw of 61,292 g / mol.

[0224] Polymers of the invention (A.17) In a 250 mL round-bottom flask equipped with a magnetic stirrer, condenser, and gas bubbler, 3.0 g of (a.7) was added to 70 g of a 10:1 water:acetic acid mixture by weight while stirring. Next, 18.50 g of (b.7) was added to the solution, followed by the dropwise addition of 2.25 g of α-picoline borane in 5 mL of methanol. The pH measured at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was allowed to proceed at 60 °C for 24 h. After workup as described above, the polymer (A.17) of the present invention was obtained, with a DM of 66%, Mn of 5,166 g / mol, and Mw of 8,594 g / mol.

[0225] V. Biodegradability of the polymers (A.13) to (A.17) of the present invention

[0226] [Table 9]

[0227] VI. Cleaning performance of the polymers (A.13) to (A.17) of the present invention Anti-graying performance Test 1 Yellow Clay Asia Condition In accordance with GBT 13174-2008, a Terg-o-meter (RHLG-IV, Shanghai Bank Equipment Co. Ltd., China) containing 12 barrels with their own rotor blades was used as the washing unit to simulate the laundry process in the laboratory. The washing units were operated at the same agitation speed of 120 revolutions per minute (rpm) and each contained 1 L of wash liquor. White test cloths were washed in the same barrel at 30°C together with 10 g of yellow clay and oil mixture in a wash liquor containing the detergent formulation shown in Table xx. After washing, the cloths were removed from the washing unit, drained, rinsed twice with 10 L of tap water for 30 seconds, and air-dried. The details of the wash cycle are summarized in Table xx.

[0228] Anti-graying performance was characterized by the Remission R value of the soiled fabric after washing and was determined by measuring the fabric at 457 nm using a Datacolor Elrepho 2000 spectrophotometer. The higher the Remission R value, the better the performance. The results are summarized in Table xx.

[0229] [Table 10]

[0230] [Table 11]

[0231] [Table 12]

[0232] Compatibility with liquid laundry detergent formulations

[0233] [Table 13]

[0234] [Table 14]

Claims

1. 1. An aqueous detergent composition comprising: (A) at least one polymer, (a) A main chain derived from an aliphatic compound having at least four amino groups per molecule, at least one of which is a —(CH ２ ) ａ -NH ２ group, the variable a is selected from 2 to 4, and the -(CH ２ ) ａ -NH ２ At least 40 mole percent of the groups are (b) General formula -(CH ２ ) ａ -NH-CH ２ - A composition comprising a polymer comprising a backbone converted with a sugar based on a monosaccharide, disaccharide, or polysaccharide under the formation of a secondary amino group.

2. The main chain (a) is H ２ N-(CH ２ ) ３ -NH-CH ２ CH ２ -N(CH ２ ) ３ -NH ２ , polyethyleneimine, and (poly)peptides having an average of at least two lysine moieties as building blocks.

3. The main chain (a) has an average molecular weight M in the range of 500 to 20,000 g / mol. ｗ 3. The composition of claim 1, wherein the branched polyethyleneimine is selected from the group consisting of:

4. The main chain (a) has a molecular weight M in the range of 1,000 to 8,000 g / mol. ｗ 3. The composition according to claim 1, wherein the ε-polylysine is selected from ε-polylysine having the formula:

5. The polymer (A) has an average molecular weight M in the range of 750 to 350,000 g / mol. ｗ The composition according to any one of claims 1 to 4, wherein

6. The composition according to any one of claims 1 to 5, wherein the sugar (b) is maltodextrin.

7. The composition further comprises The composition according to any one of claims 1 to 6, comprising (B) at least one hydrolase.

8. Use of a composition according to any one of claims 1 to 7 for laundry care.

9. A polymer comprising: (a) A main chain derived from an aliphatic compound having at least four amino groups per molecule, at least one of which is a —(CH ２ ) ａ -NH ２ group, the variable a is selected from 2 to 4, -(CH ２ ) ａ -NH ２ At least 40 mole percent of the groups are (b) General formula -(CH ２ ) ａ -NH-CH ２ - Polymers comprising a backbone converted with sugars based on mono-, di- or polysaccharides under the formation of secondary amino groups.

10. Average molecular weight M in the range of 750 to 350,000 g / mol ｗ 10. The polymer of claim 9 having the formula:

11. The main chain (a) is H ２ N-(CH ２ ) ３ -NH-CH ２ CH ２ -N(CH ２ ) ３ -NH ２ 11. The polymer according to claim 9 or 10, which is selected from polyethyleneimine and (poly)peptides having an average of at least two lysine moieties as building blocks.

12. The main chain (a) has a molecular weight M in the range of 1,000 to 8,000 g / mol. ｗ The polymer according to any one of claims 9 to 11, selected from ε-polylysine having the formula:

13. The polymer according to any one of claims 9 to 12, wherein the sugar (b) is maltodextrin.

14. A process for making the polymer of any one of claims 9 to 12, comprising: (α) A main chain molecule (A) that is an aliphatic compound having at least four amino groups per molecule, at least one of which is a —(CH ２ ) ａ -NH ２ providing a backbone molecule (A) wherein the backbone molecule (A) is a group, and the variable a is selected from 2 to 4; (β) reacting said backbone molecule (a) with at least one sugar molecule based on a monosaccharide, disaccharide, or polysaccharide in the presence of hydrogen and a catalyst or in the presence of aminoborane.

15. A method for improving the cleaning performance of a liquid detergent composition by adding the polymer (A) according to any one of claims 9 to 13 to the detergent composition comprising at least one lipase (b) and / or at least one protease (D).

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