Detergent composition, polymer and manufacturing method thereof

Abstract

The present invention relates to an aqueous detergent composition comprising (A) at least one polymer comprising (a) a backbone derived from an aliphatic compound having at least 4 amino groups per molecule, at least one of the amino groups being a-(CH2) a-NH2 group, the variable a being selected from 2 to 4, and the variable b being selected from 2 to 4; wherein at least 40 mol-% of the-(CH2) a-NH2 group is converted with (b) a saccharide based on a monosaccharide, disaccharide or polysaccharide under the formation of a secondary amino group having the general formula-(CH2) a-NH-CH2-.

Description

[0001] The present invention relates to an aqueous detergent composition, which comprises

[0002] (A) at least one polymer, which polymer comprises

[0003] (a) a main chain which is derived from an aliphatic compound having at least 4 amino groups per molecule, at least one of said amino groups being a -(CH 2 ) a -NH 2 group, the variable a being selected from 2 to 4, wherein at least 40 mol-% of said -(CH 2 ) a -NH 2 groups are converted with

[0004] (b) sugars based on monosaccharides, disaccharides or polysaccharides are converted in the formation of a secondary amino group having the general formula -(CH 2 ) a -NH-CH 2 -.

[0005] Furthermore, the present invention relates to the polymer (A) and a method for preparing such polymer (A).

[0006] Laundry detergents have to meet several requirements. They need to remove all kinds of dirt on clothes, such as all kinds of pigments, clays, fatty dirt and dyes, including dyes from food and beverages such as red wine, tea, coffee and fruits (including fruit juices). Laundry detergents also need to exhibit a certain storage stability. In particular, liquid laundry detergents or those containing hygroscopic components often lack good storage stability. For example, enzymes tend to become inactivated.

[0007] Fatty dirt remains a challenge in washing. Although many suggestions have been made for its removal - polymers, enzymes, surfactants - solutions with good effects are still of interest. The use of lipases has been proposed to help remove fat, but many builders (especially in liquid laundry detergents) do not work well with lipases.

[0008] In addition, laundry graying is still a significant problem. Graying is attributed to the redeposition of dirt during washing. To reduce the redeposition of dirt, specific natural or modified polysaccharides have been developed, such as with gaseous or liquid SO 2Processed polysaccharides. A variety of components with different structures have been proposed, see, for example, WO 2015 / 091160, EP 3 266 858 A1 and EP 3 226 858 A1, but there is still room for improvement, and the anti-greying performance of such compounds is still insufficient. Therefore, there is a continuous need for improved anti-greying agents that can be used in the laundry process. In particular, it is desirable to provide an anti-greying agent that reduces the greying of washed fabrics.

[0009] Several polymers have been proposed as additives. However, many of these polymers degrade rapidly and thus have a shortened shelf life.

[0010] Accordingly, an object is to provide a detergent composition that meets the above requirements. Another object is to provide a component that meets the above requirements, and an object is to provide a method for preparing such a component and a detergent composition.

[0011] Accordingly, an object is to provide a detergent composition that meets the above requirements. Another object is to provide a component that meets the above requirements, and an object is to provide a method for preparing such a component and a detergent composition.

[0012] Accordingly, a detergent composition as defined at the beginning has been found, which is also referred to hereinafter as the composition of the present invention or the composition according to the present invention. The composition of the present invention contains at least one polymer (A), which polymer comprises a main chain (a) and a certain amount of monosaccharide, disaccharide or polysaccharide groups (b) attached to said main chain. The polymer (A) and the detergent composition containing the polymer (A) will be described in more detail below.

[0013] The main chain (A) is derived from an aliphatic compound having at least 4 amino groups per molecule, preferably 4 or 20 to 70 amino groups per molecule, at least one of these amino groups being a - (CH 2 ) a -NH 2 group, and the variable a is selected from 2 to 4.

[0014] Examples of the main chain (a) are polylysine, polyvinylamine and polyalkyleneimine (such as polyethyleneimine and polypropyleneimine) and H 2 N-(CH 2 ) 3 -NH-CH 2 CH 2 -N(CH 2 ) 3 -NH 2 ("N4-amine").

[0015] The polyalkyleneimine used as the main chain (a) may have a linear or preferably branched structure. The branches may be alkyleneamino groups such as, but not limited to, -CH 2 -CH 2 -NH 2 groups or (CH 2 ) 3 -NH 2 - groups. Longer branches may be, for example, -(CH 2 ) 3 -N(CH 2 CH 2 CH 2 NH 2 ) 2 or -(CH 2 ) 2 -N(CH 2 CH 2 NH 2 ) 2 groups.

[0016] The polyvinylamine may have an average molecular weight M in the range of 500 to 100,000 g / mol, preferably determined by GPC (gel permeation chromatography) with water as the eluent. w . Due to their manufacture, i.e., saponification after the polymerization of N-vinylformamide, the polyvinylamine may have a degree of hydrolysis in the range of 20% to 100%, for example 80% to 100%, determined by ( 1 H NMR). Preferred is fully hydrolyzed polyvinylamine.

[0017] Each molecule of polyvinylamine may have an average of 2 to 200, preferably 25 to 100, primary amino groups.

[0018] In the context of the present invention, the term "polyethyleneimine" refers not only to polyethyleneimine homopolymers but also to polyalkyleneimines containing NH-CH 2 -CH 2 -NH structural units and other alkylene diamine structural units such as NH-CH 2 -CH 2 -CH 2 -NH structural units, NH-CH 2 -CH(CH 3 )-NH structural units, NH-(CH 2 ) 4 -NH structural units, NH-(CH 2 ) 6 -NH structural units or (NH-(CH 2 ) 8 -NH structural units, but in terms of molar fraction, NH-CH2 -CH 2 -NH structural units are in the majority. Preferred polyethyleneimines contain NH-CH 2 -CH 2 -NH structural units in the majority in terms of molar fraction, for example 60 mol-% or more, more preferably at least 70 mol-% relative to all alkyleneimine structural units. In particular embodiments, the term polyethyleneimine refers to those polyalkyleneimines that carry only one or zero alkyleneimine structural units per molecule that are different from NH-CH 2 -CH 2 -NH.

[0019] In one embodiment of the present invention, the average molecular weight M w of the branched polyethyleneimine is in the range from 500 to 100,000 g / mol, preferably up to 50,000 g / mol and more preferably from 800 to 25,000 g / mol. The average molecular weight M w of the branched polyethyleneimine can be determined by gel permeation chromatography (GPC) using an aqueous 1.5% formic acid solution as eluent and crosslinked polyhydroxyethyl methacrylate as stationary phase.

[0020] In one embodiment of the present invention, the branched polyethyleneimine exhibits a polydispersity Q = M w / M n of at least 3.5, preferably in the range from 3.5 to 10, more preferably in the range from 4 to 9 and even more preferably from 4.0 to 5.5. In other embodiments of the present invention, the branched polyalkyleneimine exhibits a polydispersity Q = M w / M n of at most 3.4, for example in the range from 1.1 to 3.0, more preferably in the range from 1.3 to 2.5 and even more preferably from 1.5 to 2.0.

[0021] The branched polyethyleneimine can have a degree of branching in the range from 0.30 to 0.75, preferably from 0.5 to 0.7, more preferably from 0.55 to 0.7, determined by 13 13C NMR spectroscopy in D 2 2O. In the context of the present invention, the term "branched polyethyleneimine" includes polymers also known as highly branched polyethyleneimines. The degree of branching is calculated as (D + T) / (D + T + L). In this formula, D refers to dendritic (or tertiary) amine groups, L (linear) refers to secondary amine groups, and L (linear) refers to primary amine groups. The branched polyethyleneimine can be obtained by polymerization of ethyleneimine (aziridine).

[0022] In the context of the present invention, the term "polypropyleneimine" refers not only to polypropyleneimine homopolymers, but also to polyalkyleneimines containing NH-CH 2 -CH 2 -CH 2 -NH structural units or NH-CH 2 -CH(CH 3 )-NH structural units and other alkylene diamine structural units such as NH-CH 2 -CH 2 -NH structural units, NH-(CH 2 ) 4 -NH structural units, NH-(CH 2 ) 6 -NH structural units or (NH-(CH 2 ) 8 -NH structural units, but in terms of molar fraction, the NH-CH 2 -CH 2 -CH 2 -NH structural units or NH-CH 2 -CH(CH 3 )-NH structural units are in the majority. Preferred polypropyleneimines contain, in terms of molar fraction, a majority of NH-CH 2 -CH 2 -CH 2 -NH or NH-CH 2 -CH(CH 3 )-NH structural units, for example 60 mol-% or more, more preferably at least 70 mol-%, relative to all alkyleneimine structural units. In particular embodiments, polypropyleneimine refers to those polyalkyleneimines having one or zero alkyleneimine structural units per molecule different from both NH-CH 2 -CH 2 -CH 2 -NH and NH-CH 2 -CH(CH 3 )-NH.

[0023] Preferably, the degree of branching of branched polypropyleneimine is determined by 13 C NMR spectroscopy in D 2 O to be in the range of 0.30 to 0.75, preferably 0.5 to 0.7, more preferably 0.55 to 0.7.

[0024] Branched polyethyleneimine and branched polypropyleneimine can each carry 2 to 200 primary amino groups per molecule, preferably 4 to 50 primary amino groups.

[0025] Polylysine is a polypeptide that preferably has an average of 3 to 50, preferably 25 to 35, lysine units per molecule, such as 3 to 9 or 25 to 35 lysine units. Polylysine can be selected from α-polylysine and ε-polylysine, with ε-polylysine being preferred. Polylysine can be based on D-lysine and L-lysine and their mixtures, with the L-enantiomer being preferred. Another embodiment of polylysine is the so-called branched polylysine. In this context, branched polylysine contains lysine moieties where two amino groups form amide bonds with another lysine moiety.

[0026] During the manufacturing process, partial racemization may occur, but the L-enantiomer is the major one. Additionally, in the context of the present invention, the term polylysine includes polypeptides containing lysine and at least one additional amino acid such as alanine, glycine, valine, threonine, etc., where most of the amino acids in the polylysine are lysine. However, polylysine containing lysine as the sole amino acid structural unit is preferred.

[0027] In one embodiment of the present invention, the main chain (a) is selected from branched polyethyleneimine with an average molecular weight M w in the range of 500 to 20,000 g / mol.

[0028] The N4-amine can be used in pure form or together with 0.1% to 20% by weight of N3-amine as an impurity.

[0029] In one embodiment of the present invention, the main chain (a) is selected from N4-amine, polyvinylamine, branched polyethyleneimine, and polylysine, especially branched polylysine and ε-polylysine.

[0030] Regarding the (CH 2 ) a -NH 2 group,

[0031] (b) At least 40 mol-% of the CH 2 -(CH 2 ) a -NH 2 groups are converted into secondary amines with the general formula -(CH 2 ) a -NH-CH 2 using a sugar based on monosaccharides, disaccharides, or polysaccharides (hereinafter also referred to as part (b)). It is evident that the conversion is carried out under reducing conditions.

[0032] Sugars suitable for forming part (b) are reducing sugars. During the conversion process, a ring-opening reaction is observed.

[0033] Preferably, at least 50 mol-% of the -(CH 2 ) a -NH 2 groups are converted.

[0034] Monosaccharides suitable as part (b) are based on aldoses (such as glyceraldehyde), erythrose, threose, ribose, arabinose, xylose and lyxose, and hexoses such as glucose, galactose, preferably in each case the D-enantiomer. Preferred monosaccharides are arabinose, xylose and glucose.

[0035] Examples of disaccharides suitable as part (b) are cellobiose, lactose and maltose. Mixtures such as glucose syrup are also suitable.

[0036] Examples of polysaccharides are maltodextrin and dextrin, with maltodextrin being preferred. The dextrose equivalent can be used to calculate the amount of "aldehyde" groups that can react with the -(CH 2 ) a -NH 2 groups of the main chain (a).

[0037] The proportion of converted amino groups in the main chain (a) is determined by measuring the secondary amine value (ASTM D2074). In one embodiment of the invention, the polymer (A) has an amine value in the range of 10 to 2000, preferably 25 to 700 mg KOH / g of polymer (A) measured according to DIN 53240 (2013).

[0038] Details of the conversion reaction are further disclosed below.

[0039] The compositions of the present invention may contain impurities resulting from the synthesis of polymer (A), such as unreacted sugars based on monosaccharides, disaccharides or polysaccharides respectively, or unreacted main chain (a) (especially in embodiments where the main chain (a) bears less than 5 primary amino groups per molecule), or reduced polyols based on monosaccharides, disaccharides or polysaccharides.

[0040] In one embodiment of the invention, the compositions of the present invention contain polymer (A) in the range of 0.1% to 10% by weight based on the total solids content. The total solids content is determined by evaporating the volatile matter in vacuo at a maximum temperature of 100 °C.

[0041] The detergent compositions of the present invention can be solid or liquid, but preferably they are liquid at ambient temperature. More preferably, the detergent compositions of the present invention are aqueous compositions. In the context of the present invention, the term "aqueous composition" refers to a composition that is liquid at ambient temperature and in which the continuous phase contains at least 75% by volume of water.

[0042] In one embodiment of the present invention, the composition of the present invention comprises at least one enzyme. Enzymes are identified by a polypeptide sequence (also referred to herein as an amino acid sequence). The polypeptide sequence specifies the three-dimensional structure including the "active site" of the enzyme, which in turn determines the catalytic activity of the enzyme. The polypeptide sequence can be identified by SEQ ID NO. In this document, amino acids are represented using the three-letter code with the first letter in uppercase or the corresponding single-letter representation in accordance with the World Intellectual Property Organization (WIPO) Standard ST.25 (1998).

[0043] Any enzyme according to the present invention relates to a parent enzyme and / or a variant enzyme, both of which have enzyme activity. An enzyme having enzyme activity is enzymatically active or exerts an enzyme conversion effect, meaning that the enzyme acts on a substrate and converts it into a product. In this document, the term "enzyme" does not include inactive variants of the enzyme.

[0044] The "parent" sequence (of a parent protein or enzyme, also referred to as the "parent enzyme") is the starting sequence for introducing changes into the sequence (e.g., by introducing one or more amino acid substitutions, insertions, deletions, or combinations thereof), resulting in a "variant" of the parent sequence. The term parent enzyme (or parent sequence) includes wild-type enzymes (sequences) and synthetically generated sequences (enzymes), which are used as starting sequences to introduce (further) changes.

[0045] The term "enzyme variant" or "sequence variant" or "variant enzyme" refers to an enzyme whose amino acid sequence differs to some extent from its parent enzyme. If not otherwise specified, "having enzyme activity" for a variant enzyme means that such a variant enzyme has the same type of enzyme activity as the corresponding parent enzyme.

[0046] In describing the variants of the present invention, the nomenclature described below is used:

[0047] Amino acid substitutions are described by providing the original amino acid of the parental enzyme, followed by the position number within the amino acid sequence, followed by the substituted amino acid. Amino acid deletions are described by providing the original amino acid of the parental enzyme, followed by the position number within the amino acid sequence, followed by an asterisk. Amino acid insertions are described by providing the original amino acid of the parental enzyme, followed by the position number within the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, insertion of lysine at position 180 near glycine is named "Gly180GlyLys" or "G180GK". In the case where a substitution and an insertion occur at the same position, this can be represented as S99SD+S99A or, in short, S99AD. Naming degeneracy occurs in the case of inserting an amino acid residue identical to an existing amino acid residue. If, for example, in the above example, glycine is inserted after glycine, this would be represented as G180GG. When different alterations can be introduced at one position, these different alterations are separated by commas, for example, "Arg170Tyr,Glu" represents substitution of arginine at position 170 by tyrosine or glutamic acid. Alternatively, different alterations or alternative substitutions can be indicated in parentheses, for example, Arg170[Tyr,Gly] or Arg170{Tyr,Gly}; or, in short, R170[Y,G] or R170{Y,G}; or in detail, R170Y, R170G.

[0048] Enzyme variants can be defined by their sequence identity when compared to the parental enzyme. Sequence identity is usually provided in the form of "sequence identity %" or "identity %". To calculate sequence identity, in the first step, a sequence alignment must be generated. According to the present invention, a pairwise global alignment must be generated, which means that the 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 algorithm of Needleman and Wunsch (J. Mol. Biol. [Journal of Molecular Biology] (1979) 48, pp. 443-453). Preferably, the program "NEEDLE" (European Molecular Biology Open Software Suite (EMBOSS)) is used for the purposes of the present invention, where the program default parameters are used (gap open = 10.0, gap extend = 0.5, and matrix = EBLOSUM62).

[0049] According to the present invention, the following calculation of % identity is applied: Identity % = (number of identical residues / length of the alignment region of the corresponding sequence of the present invention showing the full length) * 100.

[0050] According to the present invention, an enzyme variant can be described as an amino acid sequence that is at least n% identical to the amino acid sequence of the corresponding parental enzyme, where "n" is an integer between 10 and 100. In one embodiment, when compared to the full-length amino acid sequence of the parental enzyme, 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, and the enzyme variant has enzyme activity.

[0051] "Enzyme activity" means the catalytic effect exerted by an enzyme, which is usually expressed in units / mg of enzyme (specific activity), and is related to the number of substrate molecules converted per minute by each enzyme molecule (molecular activity). When an 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 enzyme activity of the corresponding parental enzyme, the variant enzyme can have enzyme activity according to the present invention.

[0052] In one embodiment, the enzyme is selected from hydrolases, preferably selected from proteases, amylases, lipases, cellulases and mannanases.

[0053] In one embodiment of the present invention, the composition of the present invention comprises

[0054] (B) at least one hydrolase, hereinafter also referred to as hydrolase (B), preferably selected from lipases, hereinafter also referred to as lipase (B).

[0055] "Lipase", "lipolytic enzyme", "lipid esterase" all refer to enzymes of EC class 3.1.1 ("carboxylic ester hydrolases"). Such lipase (B) can have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; an enzyme with cutinase activity can be referred to as cutinase herein), sterol esterase activity (EC 3.1.1.13) and / or wax ester hydrolase activity (EC 3.1.1.50). Lipase (B) includes those from bacterial or fungal sources.

[0056] Commercially available lipases (B) include, but are not limited to, those sold under the trade names Lipolase TM , Lipex TM , Lipolex TM and Lipoclean TM(Novozymes A / S), Preferenz TM those sold by L (DuPont), Lumafast (originally from Genencor), and Lipomax (Gist-Brocades / now DSM).

[0057] In one aspect of the present invention, the lipase (B) is selected from the following: lipases from Humicola (synonym: Thermomyces), such as the lipase from Humicola lanuginosa (Thermomyces lanuginosus) as described in EP 258068, EP 305216, WO 92 / 05249 and WO 2009 / 109500 or the lipase from Humicola insolens as described in WO 96 / 13580; the lipase derived from Rhizomucor miehei as described in WO 92 / 05249; lipases from Pseudomonas strains (some of which are now renamed Burkholderia), such as the lipase from Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP 218272, WO 94 / 25578, WO 95 / 30744, WO 95 / 35381, WO 96 / 00292), Pseudomonas cepacia (EP 331376), Pseudomonas stutzeri (GB 1372034), Pseudomonas fluorescens, Pseudomonas sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), Pseudomonas wisconsinensis (WO 96 / 12012), Pseudomonas mendocina (WO 95 / 14783), Pseudomonas glumae (WO 95 / 35381, WO96 / 00292); the lipase from Streptomyces griseus (WO 2011 / 150157) and Streptomyces pristinaespiralis (S.Lipases from Aspergillus oryzae (WO 2012 / 137147), GDSL-type Streptomyces lipases (WO 2010 / 065455); lipases from Thermobifida fusca as disclosed in WO 2011 / 084412; lipases from Geobacillus stearothermophilus as disclosed in WO 2011 / 084417; Bacillus lipases, such as those disclosed in WO00 / 60063, as in Dartois et al. (1992), Biochemica et Biophysica Acta [Acta Biochimica et Biophysica], 1131, 253-360 or lipases from Bacillus subtilis, Bacillus stearothermophilus (JP S64-074992) or Bacillus pumilus (WO 91 / 16422) as disclosed in WO 2011 / 084599; lipases from Candida antarctica as disclosed in WO 94 / 01541. Suitable lipases (B) also include those that are variants of the above lipases having lipolytic activity. Such suitable lipase variants are, for example, those developed by the methods disclosed in WO 95 / 22615, WO 97 / 04079, WO 97 / 07202, WO 00 / 60063, WO 2007 / 087508, EP 407225 and EP 260105. Suitable lipase variants are, for example, those developed by the methods disclosed in WO 95 / 22615, WO 97 / 04079, WO 97 / 07202, WO 00 / 60063, WO 2007 / 087508, EP 407225 and EP 260105..

[0058] Suitable lipases (B) also include those that are variants of the above lipases having lipolytic activity. Suitable lipase variants include variants having at least 40% to 100% identity when compared to the full-length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment, a lipase variant having lipolytic activity can 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 when compared to the full-length polypeptide sequence of the parent enzyme as disclosed above.

[0059] Lipase (B) has "lipolytic activity". Methods for determining lipolytic activity are well known in the literature (see, for example, Gupta et al. (2003), Biotechnol. Appl. Biochem. [Biotechnology and Applied Biochemistry] 37, pp. 63-71). For example, lipase activity can be measured by hydrolysis of the ester bond in the substrate p-nitrophenyl palmitate (pNP-Palmitate, C:16), releasing yellow pNP that can be detected at 405 nm.

[0060] In one embodiment, lipase (B) is selected from fungal triacylglycerol lipases (EC class 3.1.1.3). The fungal triacylglycerol lipase can be selected from the lipase of Thermomyces lanuginosa. In one embodiment, at least one Thermomyces lanuginosa lipase is selected from the triacylglycerol lipase of amino acids 1-269 of SEQ ID NO:2 according to US5869438 and its variants having lipolytic activity.

[0061] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity that are 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 when compared to the full-length polypeptide sequence of amino acids 1-269 of SEQ ID NO:2 of US 5,869,438.

[0062] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity that contain only conservative mutations and do not involve the functional domains of amino acids 1-269 of SEQ ID NO:2 of US 5,869,438. The lipase variant of this embodiment having 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 US 5,869,438.

[0063] The Thermomyces lanuginosa lipase can be selected from variants having lipolytic activity that contain at least the following amino acid substitutions when compared to amino acids 1-269 of SEQ ID NO:2 of US 5,869,438: T231R and N233R. When compared to amino acids 1-269 of SEQ ID NO:2 of US 5,869,438, the lipase variant can further contain one or more of the following amino acid exchanges: Q4V, V60S, A150G, L227G, P256K.

[0064] The Thermomyces lanuginosus lipase may be a variant having lipolytic activity that comprises within the polypeptide sequence of amino acids 1 - 269 of SEQ ID NO:2 of US 5,869,438 at least the amino acid substitutions T231R, N233R, Q4V, V60S, A150G, L227G, P256K and is 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 US 5,869,438.

[0065] The Thermomyces lanuginosus lipase may be a variant having lipolytic activity that comprises within amino acids 1 - 269 of SEQ ID NO:2 of US5869438 the amino acid substitutions T231R and N233R and is 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 US 5,869,438.

[0066] The Thermomyces lanuginosus lipase may be a variant having lipolytic activity of amino acids 1 - 269 of SEQ ID NO:2 of US5869438, wherein the variant of amino acids 1 - 269 of SEQ ID NO:2 of US 5,869,438 is characterized by containing the amino acid substitutions T231R and N233R. The lipase may be referred to herein as Lipex.

[0067] In one embodiment of the present invention, a combination of at least two of the aforementioned lipases (B) may be used.

[0068] In one embodiment of the present invention, the 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 enzyme activity in the range of 100 to 0.005 LU / mg, preferably 25 to 0.05 LU / mg of the composition. A lipase unit (LU) is the amount of lipase that produces 1 μmol of titratable fatty acid per minute under the following conditions in pH - stat: temperature 30°C; pH = 9.0; the substrate is an emulsion of 3.3 wt.% olive oil and 3.3% gum arabic in 5 mmol / l Tris buffer in the presence of 13 mmol / l Ca 2+ and 20 mmol / l NaCl.

[0069] In one embodiment of the present invention, the composition of the present invention comprises

[0070] (D) at least one protease (D), also referred to hereinafter as protease (D).

[0071] 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 proteases of the subtilisin type (EC 3.4.21.62). Serine proteases or serine peptidases are characterized by having serine at the catalytic active site, which forms a covalent adduct with the substrate during the catalytic reaction. Serine proteases in the context of the present invention can 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. Subtilisin is also known as subtilopeptidase, e.g., EC 3.4.21.62, which is also referred to as "subtilisin" hereinafter. Serine proteases of the subtilisin-related class share a common amino acid sequence defining a catalytic triad that differentiates them from serine proteases of the chymotrypsin-related class. Both subtilisin and chymotrypsin-related serine proteases have a catalytic triad comprising aspartic acid, histidine and serine.

[0072] A protease is an active protein that exerts "protease activity" or "proteolytic activity". Proteolytic activity is related to the rate of degradation of proteins by a protease or proteolytic enzyme over a defined time course.

[0073] Methods for analyzing proteolytic activity are well known in the literature (see, for example, Gupta et al. (2002), Appl. Microbiol. Biotechnol. [Applied Microbiology and Biotechnology] 60: 381 - 395). Proteolytic activity can be determined by using succinyl - alanyl - alanyl - prolyl - phenylalanine - p - nitroanilide (Suc - AAPF - pNA, abbreviated as AAPF; see, for example, DelMar et al. (1979), Analytical Biochem [Analytical Biochemistry] 99, 316 - 320) as a substrate. Proteolytic cleavage cleaves pNA from the substrate molecule, resulting in the release of free yellow pNA, which can be quantified by measuring OD 405 for quantification.

[0074] Proteolytic activity can be provided in units / gram of enzyme. For example, 1 U of protease can correspond to the amount of protease that releases 1 μmol of Folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37 °C (using casein as the substrate).

[0075] A protease of the subtilisin type (EC 3.4.21.62) can be a bacterial protease derived from a microorganism selected from the group consisting of Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces proteases, or Gram-negative bacterial polypeptides such as Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

[0076] In one aspect of the present invention, at least one protease (D) is selected from proteases 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 pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis or Bacillus thuringiensis.

[0077] In one embodiment of the present invention, at least one protease (D) is selected from the following: subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Vol. 159, pp. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Vol. 11, pp. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) J. Biol Chem, Vol. 243, pp. 2184-2191 and Jacobs et al. (1985) Nucl. Acids Res, Vol. 13, pp. 8913-8926); subtilisin PB92 (the original sequence of alkaline protease PB92 is described in EP 283075A2); subtilisin 147 and / or 309 as disclosed in WO89 / 06279 (respectively ) proteases from Bacillus lentus as disclosed in WO 91 / 02792, such as proteases from Bacillus lentus DSM 5483 or variants of Bacillus lentus DSM 5483 as described in WO 95 / 23221; proteases from Bacillus alkalophilus (DSM 11233) as disclosed in DE 10064983; proteases from Bacillus gibsonii (DSM 14391) as disclosed in WO 2003 / 054184; proteases from Bacillus sp. (DSM14390) as disclosed in WO 2003 / 056017; proteases from Bacillus sp. (DSM 14392) as disclosed in WO 2003 / 055974; proteases from Bacillus gibsonii (DSM 14393) as disclosed in WO 2003 / 054184; proteases having SEQ ID NO:4 as described in WO 2005 / 063974; proteases having SEQ ID NO:4 as described in WO 2005 / 103244; proteases having SEQ ID NO:7 as described in WO 2005 / 103244; and proteases having SEQ ID NO:2 as described in application DE 102005028295.4.

[0078] Examples of proteases useful according to the present invention include variants described in the following: WO 92 / 19729, WO95 / 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. Suitable examples include in particular variants of subtilisin which are derived from SEQ ID NO:22 as described in EP 1921147 (which is the sequence of the mature alkaline protease from Bacillus lentus DSM 5483) and which have amino acid substitutions at one or more of the following 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) and which have proteolytic activity. In one embodiment, such a protease has no mutations at positions Asp32, His64 and Ser221 (according to BPN' numbering).

[0079] In one embodiment, at least one protease (D) has a sequence according to SEQ ID NO:22 as described in EP 1921147, or a protease that is at least 80% identical thereto and has proteolytic activity. In one embodiment, the protease is characterized by having the amino acid glutamate, 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 at position 3 (3T), (b) isoleucine at position 4 (4I), (c) alanine, threonine or arginine at position 63 (63A, 63T or 63R), (d) aspartic acid or glutamic acid at position 156 (156D or 156E), (e) proline at position 194 (194P), (f) methionine at position 199 (199M), (g) isoleucine at position 205 (205I), (h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or 217G), (i) a combination of two or more of the amino acids according to (a) to (h).

[0080] At least one protease (D) can be at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising one amino acid (according to (a)-(h)) or a combination with amino acids 101E, 101D, 101N, 101Q, 101A, 101G or 101S (according to BPN’ numbering) according to (i). In one embodiment, the protease is characterized by comprising a mutation (according to BPN’ numbering) R101E, or S3T+V4I+V205I, or R101E and S3T, V4I and V205I, or S3T+V4I+V199M+V205I+L217D, and has proteolytic activity. A protease having the sequence according to SEQ ID NO:22 as described in EP 1921147 and 101E can be referred to herein as Lavergy.

[0081] In one embodiment, the protease according to SEQ ID NO:22 as described in EP 1921147 is characterized by comprising a mutation (according to BPN’ numbering) S3T+V4I+S9R+A15T+V68A+D99S+R101S+A103S+I104V+N218D, and has proteolytic activity.

[0082] The composition of the present invention may comprise a combination of at least two proteases (D), preferably selected from the group of serine endopeptidases (EC 3.4.21), more preferably selected from the group of proteases of the subtilisin type (EC 3.4.21.62), all as disclosed above.

[0083] Preferably, a combination of lipase (B) and protease (D) is used 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.

[0084] In the context of the present invention, when compared to the initial enzyme activity before storage, the enzyme activity of lipase (B) and / or protease (D) that is "available in the application" is considered stable when it is equal to at least 60%. If the enzyme activity available in the 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% when compared to the initial enzyme activity before storage, the enzyme can be referred to as stable in the present invention.

[0085] Subtracting a% from 100% gives the "enzyme activity loss during storage" when compared to the initial enzyme activity before storage. In one embodiment, when there is substantially no loss of enzyme activity during storage, i.e., when the enzyme activity loss is equal to 0% when compared to the initial enzyme activity before storage, the enzyme according to the present invention is stable. Substantially no loss of enzyme activity in the present invention can mean that the enzyme activity loss 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%, less than 5%.

[0086] In one embodiment of the present invention, the composition of the present invention comprises

[0087] (C) at least one anionic surfactant, also referred to hereinafter as anionic surfactant (C).

[0088] Examples of anionic surfactant (C) are C 8 -C 18 -alkali metal and ammonium salts of alkyl sulfates, C 8 -C 18 -alkali metal and ammonium salts of fatty alcohol polyether sulfates, ethoxylated C 4 -C 12 -alkali metal and ammonium salts of half esters of sulfuric acid of alkylphenols (ethoxylated: 1 to 50 mol ethylene oxide / mol), C 12 -C 18 -alkyl sulfofatty acid esters (e.g., C 12 -C 18Alkali metal and ammonium salts of sulfofatty acid methyl esters), and also C 12 -C 18 -alkanesulfonic acid alkali metal and ammonium salts and C 10 -C 18 -alkylarylsulfonic acid alkali metal and ammonium salts. The alkali metal salts of the above compounds are preferred, and the sodium salts are particularly preferred.

[0089] Further examples of the anionic surfactant (C) are soaps, such as sodium or potassium salts of stearic acid, oleic acid, palmitic acid, ether carboxylic acid esters and alkyl ether phosphates.

[0090] In a preferred embodiment of the present invention, the anionic surfactant (C) is selected from compounds according to the general formula (I)

[0091] R 1 -O(CH 2 CH 2 O) x1 -SO 3 M (I)

[0092] wherein

[0093] R 1 n-C 10 -C 18 -alkyl, especially 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, and even more preferably n-C 12 -alkyl,

[0094] x1 is a number in the range of 1 to 5, preferably 2 to 4 and even more preferably 3.

[0095] M is selected from alkali metals, preferably potassium and even more preferably sodium.

[0096] In the anionic surfactant (C), x1 can be an average value and thus x1 is not necessarily an integer, while in a single molecule according to formula (I), x1 represents an integer.

[0097] In one embodiment of the present invention, the composition of the present invention may contain 0.1% to 60% by weight, preferably 5% to 50% by weight of the anionic surfactant (C).

[0098] The composition of the present invention may contain components other than the aforementioned components. Examples are nonionic surfactants, fragrances, dyes, biocides, preservatives, enzymes, hydrotropes, builders, viscosity regulators, polymers, buffers, defoamers and anti-corrosion additives.

[0099] The preferred compositions of the present invention may contain one or more nonionic surfactants.

[0100] Preferred nonionic surfactants are alkoxylated alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide, reaction products of sorbitan with ethylene oxide or propylene oxide, alkyl polyglycosides (APG), hydroxyalkyl mixed ethers, and amine oxides.

[0101] Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds having the general formula (II)

[0102]

[0103] where the variables are defined as follows:

[0104] R 2 is the same or different and is selected from hydrogen and straight-chain C 1 -C 10 -alkyl, preferably the same in each case and being ethyl and particularly preferably hydrogen or methyl,

[0105] R 3 is selected from branched or straight-chain C 8 -C 22 -alkyl, such as n-C 8 H 17 、n-C 10 H 21 、n-C 12 H 25 、n-C 14 H 29 、n-C 16 H 33 or n-C 18 H 37 ,

[0106] R 4 is selected from C 1 -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,

[0107] The variables e and f are in the range from 0 to 300, where the sum of e and f is at least 1, preferably in the range from 3 to 50. Preferably, e is in the range from 1 to 100 and f is in the range from 0 to 30.

[0108] In one embodiment, the compound having the general formula (II) can be a block copolymer or a random copolymer, preferably a block copolymer.

[0109] Other preferred examples of alkoxylated alcohols are, for example, compounds having the general formula (III)

[0110]

[0111] wherein the variables are defined as follows:

[0112] R 2 are the same or different and are selected from hydrogen and straight-chain C 1 -C 0 -alkyl, preferably the same in each case and being ethyl and particularly preferably hydrogen or methyl,

[0113] R 5 is selected from branched or straight-chain C 6 -C 20 -alkyl, especially n-C 8 H 17 、n-C 10 H 21 、n-C 12 H 25 、n-C 13 H 27 、n-C 15 H 31 、n-C 14 H 29 、n-C 16 H 33 、n-C 18 H 37 ,

[0114] a is a number in the range from 0 to 10, preferably from 1 to 6,

[0115] b is a number in the range from 1 to 80, preferably from 4 to 20,

[0116] d is a number in the range from 0 to 50, preferably from 4 to 25.

[0117] The sum of a + b + d is preferably in the range from 5 to 100, even more preferably in the range from 9 to 50.

[0118] The compounds having the general formulas (III a) and (III b) can be block copolymers or random copolymers, preferably block copolymers.

[0119] Other suitable nonionic surfactants are selected from diblock and multiblock copolymers composed of ethylene oxide and propylene oxide. Other suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, especially linear C 4 -C 16 -alkyl polyglucosides and branched C 8 -C 14 -alkyl polyglycosides, such as compounds having the average general formula (IV) are also suitable.

[0120]

[0121] Wherein:

[0122] R 6 is C 1 -C 4 -alkyl, especially ethyl, n-propyl or isopropyl,

[0123] R 7 is -(CH 2 ) 2 -R 6 ,

[0124] G 1 is selected from monosaccharides having 4 to 6 carbon atoms, especially selected from glucose and xylose,

[0125] y1 is in the range of 1.1 to 4, and y1 is an average number.

[0126] Further examples of nonionic surfactants are compounds having the general formulas (V) and (VI)

[0127]

[0128] AO is selected from ethylene oxide, propylene oxide and butylene oxide,

[0129] EO is ethylene oxide, CH 2 CH 2 -O,

[0130] R 8 is selected from branched or linear C 8 -C 18 -alkyl, and R 5 is as defined above.

[0131] A 3 O is selected from propylene oxide and butylene oxide,

[0132] w is a number in the range of 15 to 70, preferably 30 to 50,

[0133] w1 and w3 are numbers in the range of 1 to 5, and

[0134] w2 is a number in the range of 13 to 35.

[0135] An overview of suitable additional nonionic surfactants can be found in EP-A 0 851 023 and DE-A 198 19187.

[0136] Mixtures of two or more different nonionic surfactants selected from these may also be present.

[0137] Other surfactants that may be present are selected from zwitterionic (amphoteric) surfactants and anionic surfactants and mixtures thereof.

[0138] Examples of amphoteric surfactants are those that carry a positive and a negative charge in the same molecule under the use conditions. Preferred examples of amphoteric surfactants are the so-called betaine-surfactants. Many examples of betaine-surfactants carry one quaternized nitrogen atom and one carboxylic acid group per molecule. Particularly preferred examples of amphoteric surfactants are cocoamidopropyl betaine (lauramidopropyl betaine).

[0139] Examples of amine oxide surfactants are compounds having the general formula (VII)

[0140] R 9 R 10 R 11 N→O (VII)

[0141] wherein R 9 、R 10 and R 11 are each independently selected from aliphatic, cycloaliphatic or C 2 -C 4 -alkylene C 10 -C 20 -alkylamido moieties. Preferably, R 9 is selected from C 8 -C 20 -alkyl or C 2 -C 4 -alkylene C 10 -C 20 -alkylamido and R 10 and R 11 are both methyl.

[0142] Particularly preferred examples are lauryldimethylamine oxide, sometimes also called lauramine oxide. Another particularly preferred example is cocoamidopropyl dimethylamine oxide, sometimes also called cocoamidopropylamine oxide.

[0143] 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.

[0144] In a preferred embodiment, the solid detergent compositions for cleaning agents according to the present invention and especially those for automatic dishwashing do not contain any anionic surfactants.

[0145] The composition of the present invention may contain at least one bleaching agent, also known as bleach. The bleaching agent may be selected from chlorine bleaching agents and peroxide bleaching agents, and the peroxide bleaching agents may be selected from inorganic peroxide bleaching agents and organic peroxide bleaching agents. Preferred are inorganic peroxide bleaching agents selected from alkali metal percarbonates, alkali metal perborates, and alkali metal persulfates.

[0146] Examples of organic peroxide bleaching agents are organic percarboxylic acids, especially organic percarboxylic acids.

[0147] In the composition of the present invention, alkali metal percarbonates, especially sodium percarbonate, are preferably used in coated form. Such coatings may be of organic or inorganic nature. Examples are glycerol, sodium sulfate, silicate, sodium carbonate, and combinations of at least two of the foregoing, such as a combination of sodium carbonate and sodium sulfate.

[0148] Suitable chlorine bleaching agents are, for example, 1,3-dichloro-5,5-dimethylhydantoin, N-chlorosulfonamide, chloramine T, chloramine B, sodium hypochlorite, calcium hypochlorite, magnesium hypochlorite, potassium hypochlorite, potassium dichloroisocyanurate, and sodium dichloroisocyanurate.

[0149] The composition of the present invention may contain, for example, a chlorine bleaching agent in the range of 3% to 10% by weight.

[0150] The composition of the present invention may contain one or more bleaching catalysts. The bleaching catalysts may be selected from transition metal salts or transition metal complexes that promote bleaching, such as manganese-, iron-, cobalt-, ruthenium-, or molybdenum-salen complexes or carbonyl complexes. Manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium, and copper complexes with nitrogen-containing tripod ligands, as well as cobalt-, iron-, copper-, and ruthenium-amine complexes, can also be used as bleaching catalysts.

[0151] The composition of the present invention may contain one or more bleach activators, such as N-methylmorpholinium-acetonitrile salt (“MMA salt”), trimethylammonium acetonitrile salt, N-acylimides such as N-nonanoyl succinimide, 1,5-diacetyl-2,2-dioxohexahydro-1,3,5-triazine (“DADHT”), or nitrile quaternary ammonium salts (trimethylammonium acetonitrile salt).

[0152] Further examples of suitable bleach activators are tetraacetylethylenediamine (TAED) and tetraacetylhexanediamine.

[0153] Examples of perfumes are benzyl salicylate, commercially available 2-(4-tert-butylphenyl)-2-methylpropanal, and hexyl cinnamal. as

[0154] 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.

[0155] The compositions of the present invention may contain one or more preservatives or biocides. Biocides and preservatives prevent the liquid detergent compositions of the present invention from being altered due to attack by microorganisms. Examples of biocides and preservatives are BTA (1,2,3-benzotriazole), benzalkonium chloride, 1,2-benzisothiazolin-3-one ("BIT"), 2-methyl-2H-isothiazol-3-one ("MIT"), and 5-chloro-2-methyl-2H-isothiazol-3-one ("CIT"), benzoic acid, sorbic acid, butyl iodopropargylcarbamate ("IPBC"), dichlorodimethylhydantoin ("DCDMH"), bromochlorodimethylhydantoin ("BCDMH"), and dibromodimethylhydantoin ("DBDMH").

[0156] Particularly interesting examples are the following antimicrobial agents and / or preservatives:

[0157] 4,4'-dichloro-2-hydroxy diphenyl ether (CAS No. 3380-30-1), other names: 5-chloro-2-(4-chlorophenoxy)phenol, triclosan, DCPP, which is commercially available as a 30 wt% solution of 4,4'-dichloro-2-hydroxy diphenyl ether in 1,2-propanediol under the trade name HP 100;

[0158] and

[0159] 2-phenoxyethanol (CAS No. 122-99-6, other names: phenoxyethanol, methylphenyl glycol, phenoxetol, ethylene glycol phenyl ether, ethylene glycol monophenyl ether, PE);

[0160] 2-bromo-2-nitropropane-1,3-diol (CAS No. 52-51-7, other names: 2-bromo-2-nitro-1,3-propanediol, BN, Myacide AS); glutaraldehyde (CAS No. 111-30-8, other names: 1,5-pentanedial, pentane-1,5-dial, glutaral, glutardialdehyde, GA, GA 50, GA); glyoxal (CAS No. 107-22-2; other names: ethanedial, oxylaldehyde, 1,2-ethanedial, GL); 2-butyl-benz[d]isothiazol-3-one (BBIT, CAS No. 4299-07-4); 2-methyl-2H-isothiazol-3-one (MIT, CAS No. 2682-20-4); 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); mixture of 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) (CMIT / MIT mixture, CAS No. 55965-84-9); 1,2-benzisothiazol-3(2H)-one (BIT, CAS No. 2634-33-5);

[0161] Hexa-2,4-dienoic acid (sorbic acid, CAS No. 110-44-1) and its salts, such as calcium sorbate, sodium sorbate, (E,E)-hexa-2,4-dienoic acid potassium salt (potassium sorbate, CAS No. 24634-61-5); lactic acid and its salts; especially sodium lactate, L-(+)-lactic acid (CAS No. 79-33-4);

[0162] Benzoic acid (CAS No. 65-85-0, CAS No. 532-32-1) and benzoates, 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 No. 8001-54-5, 63449-41-2, 91080-29-4, 68989-01-5, 68424-85-1, 68391-01-5, 61789-y71-7, 85409-22-9);

[0163] 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).

[0164] The biocide or preservative can be added to the composition in a concentration of 0.001% to 10% relative to the total weight of the composition of the present invention. Preferably, the composition of the present invention contains 2-phenoxyethanol in a concentration of 0.1% to 2% or 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP) in a concentration of 0.005% to 0.6%.

[0165] Accordingly, the present invention further relates to a method of preserving the composition of the present invention against microbial contamination or growth, the method comprising adding 2-phenoxyethanol.

[0166] Accordingly, the present invention further relates to a method of providing an antimicrobial effect on textiles treated with the composition of the present invention containing 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP).

[0167] Examples of viscosity regulators are agar, carrageenan, tragacanth, gum arabic, alginates, pectin, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, crosslinked poly(meth)acrylates, such as polyacrylic acid crosslinked with bis-(meth)acrylamide, and in addition silicic acid, clays such as but not limited to montmorillonite, zeolites, dextrin and casein.

[0168] Hydrotropes in the context of the present invention are compounds that promote the dissolution of compounds that exhibit limited solubility in water. Examples of hydrotropes are organic solvents such as ethanol, isopropanol, ethylene glycol, 1,2-propanediol, and further organic solvents miscible with water under normal conditions, but not limited thereto. Further examples of suitable hydrotropes are the sodium salts of toluenesulfonic acid, xylenesulfonic acid and cumenesulfonic acid.

[0169] Examples of polymers other than polymer (A) are in particular polyacrylic acid and its corresponding alkali metal salts, in particular its sodium salts. Suitable polymers are in particular polyacrylic acid, preferably having an average molecular weight M wIn the range of 2,000 to 40,000 g / mol, preferably 2,000 to 10,000 g / mol, especially 3,000 to 8,000 g / mol, each is partially or completely neutralized with an alkali metal, especially sodium. Also suitable are copolymerized polycarboxylates, especially those of acrylic acid and methacrylic acid, and those of acrylic acid or methacrylic acid with maleic acid and / or fumaric acid. Polyacrylic acid and its corresponding alkali metal salts can be used as anti-fouling redeposition agents.

[0170] Another example of a polymer is polyvinylpyrrolidone (PVP). Polyvinylpyrrolidone can be used as a dye transfer inhibitor.

[0171] Another example of a polymer is polyethylene terephthalate, polyethylene terephthalate oxide, and polyethylene terephthalate capped at each molecule with one or two hydrophilic groups selected from CH 2 CH 2 CH 2 -SO 3 Na, CH 2 CH(CH 2 -SO 3 Na) 2 and CH 2 CH(CH 2 SO 2 Na)CH 2 -SO 3 Na.

[0172] Examples of buffering agents are monoethanolamine and N,N,N-triethanolamine.

[0173] Examples of defoaming agents are silicones.

[0174] The compositions of the present invention are not only good at cleaning organic fatty dirt on dirty clothes, such as oil. The liquid detergent compositions of the present invention are very useful for removing non-bleachable stains from clothes, such as but not limited to stains from red wine, tea, coffee, vegetables, and various fruit juices like berry juice. They also do not leave residues on clothes.

[0175] Therefore, another aspect of the present invention is the use of the compositions of the present invention for clothing care. In this context, clothing care includes clothing cleaning.

[0176] In another aspect, the compositions of the present invention can be used for hard surface cleaning. Therefore, another aspect of the present invention is the use of the compositions of the present invention for hard surface cleaning.

[0177] In the context of the present invention, the term "composition for hard surface cleaning" includes cleaning agents for household care and industrial or institutional applications. The term "composition for hard surface cleaning" includes compositions for dishwashing, especially manual and automatic dishwashing and warewashing, and compositions for hard surface cleaning, such as but not limited to compositions for bathroom cleaning, kitchen cleaning, floor cleaning, pipe descaling, window cleaning, automotive cleaning (including truck cleaning), and in addition open plant cleaning, in-situ cleaning, metal cleaning, disinfectant cleaning, farm cleaning, high-pressure cleaning, but not laundry detergent compositions. A particular embodiment of the composition for hard surface cleaning is an automatic dishwashing composition.

[0178] In the context of the present invention, the terms "composition for hard surface cleaning" and "composition for hard surface cleaner" are used interchangeably.

[0179] In the context of the present invention and unless otherwise expressly stated, in the case of the ingredients of a laundry detergent composition, the percentages are by weight and refer to the total solids content of the corresponding laundry detergent composition. In the context of the present invention and unless otherwise expressly stated, in the case of the ingredients of a detergent composition for hard surface cleaning, the percentages are by weight and refer to the total solids content of the detergent composition for hard surface cleaning.

[0180] When used for automatic dishwashing, the composition of the present invention preferably contains

[0181] (E) at least one builder component selected from aminopolycarboxylic acids and preferably their alkali metal salts, also referred to in the context of the present invention as complexing agent (E) or polyvalent chelating agent (E). In the context of the present invention, the terms polyvalent chelating agent and chelating agent are used interchangeably.

[0182] Examples of polyvalent chelating agent (E) are MGDA (methylglycine diacetic acid), GLDA (glutamic acid diacetic acid), IDS (iminodisuccinate), EDTA and polymers having complexing groups, such as the alkali metal salts of polyethyleneimine (where 20 to 90 mol-% of the N atoms carry at least one CH 2 COO - group), and their corresponding alkali metal salts, especially their sodium salts, such as MGDA-Na 3 、GLDA-Na 4 or IDS-Na 4 .

[0183] Preferred polyvalent chelating agents are those according to general formula (IX a)

[0184] [CH 3 -CH(COO)-N(CH2 -COO) 2 M 3-x2 H x2 (IX a)

[0185] wherein M is selected from ammonium and alkali metal cations, which may be the same or different, such as cations of sodium, potassium and combinations of at least two of the foregoing. Ammonium may be alkyl-substituted, but unsubstituted ammonium NH 4 + is preferred. Preferred examples of alkali metal cations are sodium and potassium and combinations of sodium and potassium, and even more preferably all M in the compound according to general formula (II a) are the same and they are all Na;

[0186] and x2 in formula (II a) ranges from 0 to 1.0,

[0187] or (IX b)

[0188] [OOC-CH 2 CH 2 -CH(COO)-N(CH 2 -COO) 2 M 4-x3 H x3 (IX b)

[0189] wherein M is as defined above, and x3 in formula (IX b) ranges from 0 to 2.0, preferably up to 1.0,

[0190] or (IX c)

[0191] [OOC-CH 2 -CH(COO)]-N-CH(COO)-CH 2 -COO]M 4-x4 H x4 (IX c)

[0192] wherein M is as defined above, and x4 in formula (IX c) ranges from 0 to 2.0, preferably up to 1.0.

[0193] In one embodiment of the present invention, the composition of the present invention contains a combination of at least two of the foregoing, such as a combination of a chelating agent according to general formula (IX a) and a chelating agent according to general formula (IX b).

[0194] Chelating agents according to general formulas (IX a) and (IX b) are preferred. Even more preferred is the chelating agent according to general formula (IX a).

[0195] In one embodiment of the present invention, the compound according to general formula (IX a) is selected from the ammonium salts or alkali metal salts of racemic MGDA and the ammonium salts and alkali metal salts of a mixture of L- and D-enantiomers according to formula (IX a), said mixture mainly containing the corresponding L-isomer and having an enantiomeric excess (ee) in the range of 5% to 99%, preferably 5% to 95%, more preferably 10% to 75% and even more preferably 10% to 66%.

[0196] In one embodiment of the present invention, the compound according to general formula (IX b) is selected from at least one alkali metal salt of a mixture of L- and D-enantiomers according to formula (IX b), said mixture containing a racemic mixture or preferably mainly containing the corresponding L-isomer, for example having an enantiomeric excess (ee) in the range of 5% to 99%, preferably 15% to 95%.

[0197] The enantiomeric excess of the compound according to general formula (IX a) can be determined by measuring the polarization (polarimetry) or preferably by chromatography, for example by HPLC with a chiral column, for example using one or more cyclodextrins as the stationary phase or using the ligand exchange (Pirkle-brush) concept chiral stationary phase. Preferably, the ee is determined by HPLC using an immobilized optically active amine, such as D-penicillamine, in the presence of a copper (+II) salt. The enantiomeric excess of the compound according to the salt of general formula (IX b) can be determined by measuring the polarization (polarimetry).

[0198] Due to the environmental problems caused by the use of phosphates, the preferred advantageous compositions are phosphate-free. "Phosphate-free" should be understood in the context of the present invention to mean that the total content of phosphates and polyphosphates is in the range from the detection level determined by gravimetry to 1% by weight, preferably from 10 ppm to 0.2% by weight.

[0199] In one embodiment of the present invention, the composition of the present invention contains a polyvalent chelating agent (E) in the range of 0.5% to 50% by weight, preferably 1% to 35% by weight, based on the total solids content.

[0200] To be suitable as a laundry detergent composition, the composition of the present invention can be in bulk form or in unit dosage form, for example in the form of sachets or pouches. The materials suitable for pouches are water-soluble polymers such as polyvinyl alcohol.

[0201] In a preferred embodiment of the present invention, the composition of the present invention is liquid or gel-type at ambient temperature. In another preferred embodiment of the present invention, the composition of the present invention is solid at ambient temperature, such as powder or tablets.

[0202] In one embodiment of the present invention, the composition of the present invention is in liquid or gel form and has a pH value in the range of 7 to 9, preferably 7.5 to 8.5. In embodiments where the composition of the present invention is solid, their pH value determined after dissolving at 1 g / 100 ml in distilled water and at ambient temperature can be in the range of 7.5 to 11. In embodiments where the composition of the present invention is used for hard surfaces such as tiles, for example bathroom tiles, their pH value can even be acidic, for example 3 to 6.

[0203] In one embodiment of the present invention, the composition of the present invention is in liquid or gel form and has a total solids content in the range of 8% to 80%, preferably 10% to 50%, determined by drying at 80 °C under vacuum.

[0204] Another aspect of the present invention relates to polymer (A), also hereinafter referred to as the present invention polymer (A) or simply polymer (A). The present invention polymer (A) is the same as polymer (A), and they have been described above.

[0205] In one embodiment of the present invention, the present invention polymer (A) has an average molecular weight M in the range of 750 to 350,000 g / mol, preferably 3,000 to 50,000 g / mol. w . The molecular weight can be determined by GPC using water as the eluent.

[0206] In one embodiment of the present invention, the present invention polymer (A) has a Hazen color number in the range of 20 to 500 determined in a 10% by weight aqueous solution.

[0207] The present invention polymer (A) may contain impurities resulting from the synthesis of polymer (A), such as unreacted sugars (b) based on monosaccharides, disaccharides or polysaccharides respectively, or unreacted main chain (a) (especially in embodiments where the main chain (a) bears less than 5 primary amino groups per molecule), or reducing polyols based on monosaccharides, disaccharides or polysaccharides. The amount of impurities can be in the range of 0.5% to 10% by weight, more preferably in the range of 2% to 5% by weight.

[0208] In one aspect, the present invention relates to a method for improving the cleaning performance of a liquid detergent composition, which method comprises adding the present invention polymer (A) according to the present invention to a detergent composition preferably containing at least one lipase and / or at least one protease.

[0209] In the present text, the term "improved cleaning performance" may mean that the polymer (A) provides better, i.e., improved, stain removal characteristics under relevant cleaning conditions when compared to the cleaning performance of a detergent composition lacking the polymer (A). In one embodiment, "improved cleaning performance" means that the cleaning performance of a detergent containing the 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), is improved when compared to the cleaning performance of a detergent containing the polymer (A) but no enzyme. In one embodiment, "improved cleaning performance" means that the cleaning performance of a detergent containing the polymer (A) and an enzyme, preferably a hydrolase (B), more preferably a lipase (B) and / or a protease (D), is improved when compared to the cleaning performance of a detergent containing at least one enzyme, preferably at least one hydrolase (B), preferably a lipase (B) and / or at least one protease (D) and lacking the polymer (A).

[0210] In the present text, the term "relevant cleaning conditions" refers to the conditions actually used in a washing machine, a dishwashing machine or during a manual cleaning process, in particular the cleaning temperature, time, cleaning mechanism, foam concentration, type of detergent and water hardness.

[0211] The polymer (A) of the present invention is very suitable for use in the composition of the present invention or for the manufacture of the composition of the present invention. The polymer (A) of the present invention exhibits biodegradability.

[0212] A further aspect of the present invention relates to a method for preparing the polymer (A) of the present invention, also referred to hereinafter as the method of the present invention. The method of the present invention comprises steps (α) and (β):

[0213] (α) providing a backbone molecule (a) which is an aliphatic compound having at least 4 amino groups per molecule, at least one of these amino groups being a - (CH 2 ) a -NH 2 group, where the variable a is selected from 2 to 4,

[0214] (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 an aminoborane.

[0215] Steps (α) and (β) are described in more detail below.

[0216] The backbone molecule (a) has been described in more detail above.

[0217] The ratio of the main-chain molecule (a) and the sugar molecule based on monosaccharide, disaccharide or polysaccharide is preferably selected in such a way that the molar amount of the "aldehyde" group corresponds to at least 40 mol-%, preferably 40 to 100 mol-%, more preferably 45 to 90 mol-% of the primary amino groups of the main chain (a).

[0218] In one embodiment of the present invention, the main-chain molecule (a) is provided in bulk. However, the reaction is preferably carried out in solution, and it is advantageous to provide the main-chain molecule (a) in solution. Suitable solvents are water and mixtures of water and alcohols such as methanol and ethanol, diols such as ethylene glycol, propylene glycol and diethylene glycol, and polyethylene glycols such as those having an average molecular weight M up to 500 g / mol n of polyethylene glycol, wherein the water content is preferably at least 70% by weight. The solubility of many sugars in organic solvents is limited, and thus water and combinations of water with methanol or ethanol are preferred.

[0219] Step (β) includes the reduction of the sugar molecule and the coupling with the main-chain molecule (a).

[0220] Step (β) can be carried out at a temperature in the range from ambient temperature to 120 °C. Preferably it is 25 °C to 70 °C. In the case of solvents such as methanol and ethanol, the boiling temperature is the upper limit. Even more preferably it is 40 °C to 65 °C.

[0221] In one embodiment of the present invention, especially when using hydrogen in the presence of a catalyst, step (β) is carried out at a pressure in the range from 1 to 200 bar (absolute). In another embodiment of the present invention, especially when using aminoborane as a reducing agent, step (β) is carried out at a pressure in the range from 1 to 5 bar (absolute), especially at ambient pressure.

[0222] In one embodiment of the present invention, especially when using hydrogen in the presence of a catalyst, step (β) is carried out at a temperature in the range from 25 °C to 125 °C. In another embodiment of the present invention, especially when using aminoborane as a reducing agent, step (β) is carried out at a temperature in the range from 20 °C to 100 °C.

[0223] Examples of suitable catalysts are hydrogenation catalysts such as, but not limited to, Raney metals (such as Raney nickel) and supported metal catalysts (such as Ru, Rh or Pd on carbon, silica or ZrO 2 2).

[0224] Examples of suitable aminoboranes are especially aromatic aminoboranes, such as aniline-BH 3, Methylpyridine boranes such as α-methylpyridine borane, pyridine borane, pyridine tetrahydroborato zinc, and other boron-based reducing agents such as sodium cyanoborohydride, sodium triacetoxyborohydride, sodium borohydride, and titanium isopropoxide / sodium borohydride.

[0225] Each of hydrogen and aminoborane is used in at least a stoichiometric amount, preferably in an amount in excess of the reducible "aldehyde" group of the sugar molecule.

[0226] Step (β) is preferably carried out at a slightly acidic pH value, such as 3 to 6.5, preferably 3.5 to 5.5. The pH value can be adjusted by adding carboxylic acids (such as but not limited to formic acid or acetic acid).

[0227] Without being bound by any theory, we assume that in the first reaction, the amino group reacts with the "aldehyde" group under the conditions of ring opening and formation of hemiaminal, and then the hemiaminal is reduced to a secondary amino group.

[0228] In one embodiment of the present invention, the reaction time of step (β) is generally in the range of 1 to 36 hours.

[0229] When methanol is used as the solvent, the polymer (A) of the present invention precipitates.

[0230] After completing step (β), the polymer (A) of the present invention is usually obtained as a solution or a precipitate. Post-treatment steps can be carried out, such as but not limited to deactivation or precipitation of the catalyst. The unreacted borane and the borane reaction product can be removed together with the supernatant solvent or removed by filtration - the polymer (A) of the present invention preferably precipitates and the boron compound remains in the solution.

[0231] By carrying out the method of the present invention, the polymer of the present invention is obtained in good yield and sufficient purity.

[0232] The present invention is further illustrated by working examples.

[0233] General description:

[0234] The amount and type of amine substituted by residues (such as the main chain (a) and the polymer (A)) and optionally the presence of hydrogen can be determined by identifying primary, secondary, and tertiary amino groups in 13 13C-NMR, as described for polyethyleneimine in Lukovkin G.M. et al.: Europ. Polymer Journal 1973, 9, 559-565 and St. Pierre T. et al., Geckle M.: ACS Polym. Prep. 1981, 22, 128-129.

[0235] 13 The 13C-NMR spectra were recorded on a Bruker AV-401 instrument in CDCl 3 3 at ambient temperature. 1 The 1H-NMR spectra were recorded on a Bruker AV-401 instrument in CDCl 3 3 or CD 3 3OD at ambient temperature.

[0236] Percentages are % by weight, unless otherwise specified.

[0237] The degree of modification (DM) of the polymers of the invention can be determined by 1 1H-NMR spectroscopy and is defined as:

[0238] DM = (moles of reducing sugar reacted with amino groups) / (moles of primary amino groups available on the polyamine backbone) × 100%

[0239] The determination of dextrose equivalent ("DE") is described in "Analytical Methods of the Member Companies of the Corn Refiners Association, Inc. part Dextrose [Corn Refiners Association, Inc.'s member companies' analytical methods dextrose section]"; or in Official Journal of the European Community [European Community Official Journal] issue L239 / 44 of 22.9.79 (First Council Directive 79 / 796 / EEC of 26 July 1979).

[0240] The following starting materials were used:

[0241] (a.1): linear ε-polylysine, K-value 19.6, determined in a 1% aqueous solution by weight, commercially available from JNC Corp., Japan

[0242] (a.2): branched polylysine, K-value 12.5, synthesis see below

[0243] (a.3): N4-amine, commercially available from BASF SE

[0244] (a.4): branched polyethyleneimine, M w w = 800 g / mol (GPC, in water as eluent), commercially available from BASF SE

[0245] (b.1): D-maltose

[0246] (b.2): Maltodextrin, DE 17.8, purchased from Cpur series

[0247] (b.3): Maltodextrin, DE 28.0, purchased from Cpur series

[0248] (b.4): Maltodextrin, DE 37.7, purchased from Cpur series

[0249] (b.5): D-Glucose

[0250] (a.2) Manufacturing:

[0251] Step (α.2): Charge a 1000 ml four-necked flask equipped with a stirrer, internal thermometer, gas inlet tube, condenser with a vacuum connection, and Dean-Stark receiver with 500 g of an aqueous solution of L-lysine (50 wt%). Heat the solution with stirring to an internal temperature of 160 °C with continuous water removal. After a reaction time of 4.5 hours, distill off the water under reduced pressure (670 mbar). When 272 g of water distillate is collected, discharge the highly viscous polymer into a silicone container as quickly as possible while it is still hot and flowable. The k-value of the resulting backbone molecule (a.2) is determined to be 12.5 in a 1% by weight aqueous solution.

[0252] Step (α.5): Charge a 1000 ml four-necked flask equipped with a stirrer, internal thermometer, gas inlet tube, condenser with a vacuum connection, and Dean-Stark receiver with 500 g of an aqueous solution of L-lysine (50 wt%). Heat the solution with stirring to an internal temperature of 160 °C with continuous water removal. After a reaction time of 3.5 hours, further distill off the water under reduced pressure (670 mbar). Finally, 255 g of water distillate is collected, and the highly viscous polymer is discharged into silicone. The resulting backbone molecule (a.5) is determined to be 9.8.

[0253] Steps (α.1), (α.3): The backbone molecules (a.1) and (a.3) are used in a commercially available form

[0254] Step (α.4): Before step (β), degas the backbone molecule (a.4) in a rotary evaporator

[0255] Step (β) with aminoborane: Step (β1). Step (β) with hydrogen / catalyst: Step (β2).

[0256] I. Synthesis of the polymer (A) of the present invention

[0257] I.1 Synthesis of the copolymer of the present invention using α - methylpyridine borane as a reducing agent

[0258] I.1.1 Step (β1.1) - Synthesis of the polymer (A.1) of the present invention

[0259] In a 250 ml round - bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 20.0 g of (a.1) was dissolved in 110 g of water: acetic acid 10:1 wt under stirring. Then, 24.6 g of (b.1) was added to the solution in powder form, and subsequently a solution of 7.30 g of α - methylpyridine borane in 50 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed anymore.

[0260] Work - up: The pH value was adjusted to 4 by adding aqueous HCl solution (1 M), and (A.1) was precipitated in excess methanol (1:10 wt.). The precipitate was collected by filtration and dried in a vacuum oven at 40 °C.

[0261] The polymer (A.1) of the present invention was obtained, DM: 47%. M n : 13,315 g / mol, M w : 13,952 g / mol.

[0262] I.1.2 Step (β1.2) - Synthesis of the polymer (A.2) of the present invention

[0263] In a 250 ml round - bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 20 g of (a.1) was dissolved in 110 g of water: acetic acid 10:1 wt under stirring. Then, 57.2 g of (b.1) was added to the solution in powder form, and subsequently a solution of 17.0 g of α - methylpyridine borane in 50 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed anymore. After work - up as carried out 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.

[0264] I.1.3 Step (β1.3) - Synthesis of the polymer (A.3) of the present invention

[0265] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 10.0 g of (a.2) was dissolved in 60 g of water:acetic acid 10:1 wt with stirring. Then, 28.6 g of (b.1) was added to the solution in powder form, followed by dropwise addition of a solution of 4.25 g of α-methylpyridine borane in 25 ml of methanol. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed any longer. After work-up as carried out 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.

[0266] I.1.4 Step (β1.4) - Synthesis of the polymer (A.4) of the present invention

[0267] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 4.0 g of (a.1) was dissolved in 70 g of water:acetic acid 10:1 wt. with stirring. Then, 31.6 g of (b.2) was added to the solution in powder form, followed by dropwise addition of a solution of 3.34 g of α-methylpyridine borane in 5 ml of methanol. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed any longer. After work-up as carried out 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.

[0268] I.1.5 Step (β1.5) - Synthesis of the polymer (A.5) of the present invention

[0269] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 4.0 g of (a.2) was dissolved in 70 g of water:acetic acid 10:1 wt. with stirring. Then, 31.6 g of (b.2) (DE = 17.8) was added to the solution in powder form, followed by dropwise addition of a solution of 3.34 g of α-methylpyridine borane in 5 ml of methanol. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed any longer. After work-up as carried out above, the polymer (a.5) of the present invention was obtained, DM: 58%, M n : 8,704 g / mol and M w : 18,551 g / mol.

[0270] I.1.6 Step (β1.6) - Synthesis of the Polymer (A.6) of the Invention

[0271] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser, and a gas bubbler, 60.0 g (b.1) was dissolved in 110 g of water: acetic acid 10:1 wt. with stirring. Then, 20.0 g (a.4) was added to the solution, and subsequently, a solution of 18.8 g of α-methylpyridine borane in 50 ml of methanol was added dropwise. The pH value 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 was transparent and no visible bubbles were formed anymore. After the post-treatment was carried out as above, the polymer (A.6) of the invention was obtained, DM: 48%, M n : 1,336 g / mol and M w : 1,781 g / mol.

[0272] I.1.7 Step (β1.7) - Synthesis of the Polymer (A.7) of the Invention

[0273] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser, and a gas bubbler, 25.3 g (b.1) was dissolved in 70 g of water: acetic acid 10:1 wt. with stirring. Then, 3.0 g (a.4) was added to the solution, and subsequently, a solution of 2.67 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value 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 was transparent and no visible bubbles were formed anymore. After the post-treatment was carried out as above, the polymer (A.7) of the invention was obtained, DM: 48%, M n : 3,060 g / mol, M w : 4,663 g / mol.

[0274] I.1.8 Step (β1.8) - Synthesis of the Polymer (A.8) of the Invention

[0275] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser, and a gas bubbler, 3.0 g (a.5) was dissolved in 70 g of water: acetic acid 10:1 wt. with stirring. Then, 20.8 g (b.2) was added to the solution, and subsequently, a solution of 2.20 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value 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 was transparent and no visible bubbles were formed anymore. After the post-treatment was carried out as above, the polymer (A.8) of the invention was obtained, DM: 97%, M n : 4,763 g / mol, M w: 6,789 g / mol.

[0276] I.2 Copolymerization of the Invention by Catalytic Hydrogenation

[0277] I.2.1 General Scheme

[0278] In a 300-mL autoclave (stainless steel V4A) with an inclined blade stirrer, electric heating, internal temperature cascade control; H metering via iterative differential pressure metering 2 and a magnetically coupled stirrer under pressure, 45 g of the corresponding sugar (b) was dissolved in water to obtain a 100-ml 50 wt.% solution. The resulting solution was mixed with the corresponding main chain (a) to obtain a 1:1 DE / amine molar ratio, see Table 2. A 2.25-g amount of the catalyst - Ru on carbon was added. The autoclave was purged with nitrogen and then with hydrogen. Then, it was cold-pressurized with 10 bar of hydrogen. The reactor was heated to 60 °C at a hydrogen pressure of 100 bar for 12 hours and stirred at 500 rpm. Then, the autoclave was cooled to ambient temperature, expanded, and degassed. The resulting reaction mixture was purified by a freeze-drying procedure. Freeze-drying conditions: Freeze-drying in a refrigerator at approximately 75 °C and in a condenser (in the room) at -70 °C. Freeze-dryer Sublimator EKS100. The sample was rapidly cooled to approximately -50 °C in the first chamber. The compressor then created a "vacuum" with a maximum pressure of 6.10 mbar in the second chamber. This strong negative pressure caused the moisture to enter the second chamber from the product chamber through the valve. Then, the resulting polymer was washed with 50 ml of methanol and then dried.

[0279] I.2.2 Specific Examples in Tabular Form

[0280] Table 2: Manufacture of the Polymers of the Invention

[0281] Polymer Main chain (a) Main chain [g] <![CDATA[Mol NH 2 Group]]> (b) Water [g] (A.10) (a.3) 10.75 1.14 (b.3) 55.75 (A.11) (a.4) 165 1.00 (b.4) 61.50 (A.12) (a.3) 10.21 1.14 (b.5) 66.75

[0282] II. Washing Tests

[0283] II.1 Tests with Polymers (A.1) to (A.8)

[0284] For the test procedure based on L.1, as a softener formulation, 10 g of dipalmitoylethylhydroxyethylmonium methosulfate and 0.3 g of CaCl 2 were mixed. Water was added to a total of 100 g. The pH value was 4.

[0285] Table 3: Composition of the Base Mixtures L.1 and L.2 for Liquid Detergent Formulations

[0286]

[0287]

[0288] EO: Ethylene Oxide

[0289] According to Table 5, a test soil mixture was prepared by mixing 75% deionized water, 20% yellow clay (Japanese Industrial Standard (JIS) soil), 3.75% peanut oil (Luhua oil, Shandong) and 1.25% mineral oil. Specifically, first the 20% clay dispersion was added to water and homogenized by stirring at 6,500 rpm for 10 min. Then, the mixture of the two oils was added slowly and the whole mixture was homogenized for another 10 min.

[0290] A stirring type detergency washing machine (Terg-o-meter) (RHLG-IV, from Shanghai Bank Equipment Co., Ltd, China.) using 12 cylinders with corresponding rotor blades as the washing unit was used to simulate the laundry process in the laboratory generally following GBT 13174-2008.

[0291] Before washing, all the fabrics used were pretreated with a softener. 7 g of the above softener formulation was diluted with 10 L of tap water (25 °C) and transferred to a Haier mini washing machine MW-PQ28SW. 300 g of the fabrics to be used were loaded into the washing machine and stirred for 3 min. Then the treated fabrics were transferred to another washing machine of the same model without rinsing, spin-dried for 1 min, and then dried at 40 °C for 1 h.

[0292] The washing unit was operated at a stirring speed of 120 revolutions per minute (rpm), each containing 1 L of hard water (100 ppm Ca:Mg = 3:2). Three pieces of each type of white test fabric (15 pieces in total) were washed together with 10 g of the clay and oil mixture in the same cylinder at 30 °C in a washing liquor containing 0.93 g of a detergent having the formulation shown in Table 3. After washing, the fabrics were taken out of the washing unit, drained and rinsed twice in 10 L of tap water for 30 s. The washing cycle was repeated twice with a new clay and oil mixture and a new washing liquor. After rinsing in the third washing cycle, the test fabrics were changed to air drying. The details of the washing cycle are summarized in Table 4.

[0293] The anti-greying performance is characterized by the difference in remission values measured at 457 nm with a spectrophotometer Elrepho 2000 from Datacolor before washing (but for case L.1, after softener treatment) and after washing. The smaller the remission difference (ΔR), the better the performance. The results are summarized in Table 6.

[0294] For test procedure L.2, a slightly modified method was followed using a yellow clay - oil mixture (WFK soil oil mixture).

[0295] A Tergotometer (RHLQ-IV from RIDCI) with a single cylinder including a corresponding rotor blade as the washing unit was used to simulate the laundry process in the laboratory generally following GBT 13174-2008. The washing unit was operated at the same agitation speed of 120 rpm, each filled with 1 L of water. The white test fabric was washed together with 10 g of the test soil mixture in the same cylinder at 30 °C in a washing liquor containing the detergent formulation as shown in Table 3. After washing, the fabric was removed from the washing unit, drained and rinsed twice in 10 L of tap water for 30 seconds. The washing cycle was repeated three times with fresh yellow clay and oil mixture and fresh washing liquor. After rinsing in the third washing cycle, the test fabric was dried. The details of the washing cycle are summarized in Table 4.

[0296] The anti-greying performance is characterized by the difference in remission values (ΔR) measured at 457 nm with a spectrophotometer Elrepho 2000 from Datacolor. The clean fabric before washing was compared with the washed fabric after washing. The smaller the remission difference (ΔR), the better the performance. The results are summarized in Table 7.

[0297] Table 4: Details of the washing experiment

[0298]

[0299]

[0300] Table 5: Composition of the test soil

[0301]

[0302] Table 6: Washing results with the inventive formulation based on L.1

[0303] Added polymer (A) ΔR, sum of all fabrics None 243.14 (A.1) 221.66 (A.2) 218.20 (A.3) 214.96 (A.6) 207.13

[0304] The lower the ΔR value, the lower the degree of greying.

[0305] Table 7: Washing results with the formulations of the invention based on L.2

[0306]

[0307]

[0308] II.2 Tests with the polymers (A.10) to (A.14) of the invention

[0309] The following protocol was used:

[0310]

[0311] Color measurements were used to evaluate the overall level of cleaning. Reflectance values of the stains on the monitor were measured using a spherical reflectance spectrometer with a UV cut-off filter at 460 nm (type SF 500 from Datacolor Inc., USA, wavelength range 360 - 700 nm, optical geometry d / 8°). In this case, with the aid of CIE-Lab color space classification, the luminance L*, the a* value on the red-green color axis, and the b* value on the yellow-blue color axis were measured before and after washing, and the corresponding stains on the monitor were averaged. The value of the color change (ΔE), automatically defined and calculated by the color evaluation tool based on the following formula, is a measure of the cleaning effect achieved:

[0312]

[0313] All experiments were repeated three times to provide representative averages. Higher ΔE values indicate better cleaning. For each stain, a difference of 1 unit can be detected visually by a skilled person. A non-expert can easily detect a difference of 2 units visually.

[0314] Table 8

[0315]

[0316]

[0317] III. Biodegradation test

[0318] Overview: The test was carried out according to OECD guidelines. According to the OECD guidelines, the test is valid if the following conditions are met:

[0319] 1. The reference substance reaches 60% within 14 days.

[0320] 2. By the end of the test, the difference between the extreme values of the test replicates is less than 20%.

[0321] 3. The oxygen uptake of the blank inoculum is 20 to 30 mg O 2 / l and must never be greater than 60 mg O2 / l.

[0322] 4. The pH value measured at the end of the test must be between 6 and 8.5.

[0323] Description of the test method used in the context of the present invention:

[0324] The biodegradation in sewage was tested three times using the OECD 301F respirometry method. OECD 301F is an aerobic test that measures the biodegradation of sewage samples by measuring oxygen consumption. 100 mg / L of the test substance (which is the nominal sole carbon source) and an inoculum (aerobic sludge taken from a municipal sewage treatment plant in Shanghai, China (polymers (A.1) to (A.8)) or Mannheim, Germany) were added to the measured volume of sewage. This sludge was stirred in a closed flask at a constant temperature (25 °C) for 28 days. The oxygen consumption was determined by measuring the pressure change in the closed flask using an Oxi Top C. The carbon dioxide evolved was absorbed in a sodium hydroxide solution. A nitrification inhibitor was added to the flask to prevent oxygen consumption due to nitrification. The amount of oxygen taken up by the microbial population during the biodegradation of the test substance (corrected by the uptake of a blank inoculum run in parallel) was expressed as a percentage of the ThOD (theoretical oxygen demand, which is measured by elemental analysis of the compound). For each compartment, a positive control glucose / glutamate was run as a reference together with the test samples.

[0325] Calculation: Theoretical oxygen demand: The amount of O 2 required to oxidize the compound to its final oxidation products. This amount was calculated using elemental analysis data.

[0326] % Biodegradation

[0327] Experimental O 2 Uptake × 100 and divided by the theoretical oxygen demand

[0328] The results of the biodegradability test are summarized in Table 9.

[0329] Table 9: Results of the biodegradation test

[0330] Polymer 28 days (%) 56 days (%) (A.1) 36 46 (A.4) 46 47 (A.5) 52 55 (A.7) 51 52 (A.8) 69 71 (A.11) 30 33 (A.12) 49 55

[0331] IV. Synthesis of the polymers (A.13) to (A.17) of the present invention

[0332] The following starting materials were used:

[0333] (a.1): Linear ε-polylysine, K-value 19.6, determined in a 1% aqueous solution by weight, commercially available from JNC Corporation, Japan

[0334] (a.2): Branched polylysine, K-value 12.5, synthesis see below

[0335] (a.3): N4-amine, commercially available from BASF SE

[0336] (a.4): Branched polyethyleneimine, Mw = 800 g / mol (GPC, in water as eluent), commercially available from BASF

[0337] (a.5): Branched polylysine, K-value 9.8, synthesis see below

[0338] (a.6): Branched polylysine, K-value 10.7, synthesis see below

[0339] (a.7): Branched polylysine, K-value 11.0, synthesis see below

[0340] (b.1): D-Maltose

[0341] (b.2): Maltodextrin, DE 17.8, purchased from Cpur series

[0342] (b.3): Maltodextrin, DE 28.0, purchased from Cpur series

[0343] (b.4): Maltodextrin, DE 37.7, purchased from Cpur series

[0344] (b.5): D-Glucose

[0345] (b.6): Maltodextrin, DE 9.0, purchased from Roquette Glucidex series

[0346] (b.7): Cellulose, DE16.7, purchased from Sigma-Aldrich

[0347] Manufacture of (a.2):

[0348] Step (α.6): Branched polylysine K-value 10.7

[0349] Charge a 1000 ml four-necked flask equipped with a stirrer, an internal thermometer, a gas inlet tube, a condenser with a vacuum connection, and a Dean-Stark receiver with 500 g of an aqueous solution of L-lysine (50 wt%). Heat the solution with stirring to an internal temperature of 160 °C with continuous water removal. After a reaction time of 4.0 hours, distill off the water under reduced pressure (670 mbar). When 260 g of water distillate is collected, discharge the highly viscous polymer into a silicone container as quickly as possible while it is still hot and flowable. The k-value of the resulting main-chain molecule (a.6) is determined to be 10.7 in a 1% aqueous solution by weight.

[0350] Step (α.7): Branched polylysine K-value 11.0

[0351] Charge a 1000 ml four-necked flask equipped with a stirrer, an internal thermometer, a gas inlet tube, a condenser with a vacuum connection, and a Dean-Stark receiver with 500 g of an aqueous solution of L-lysine (50 wt%). Heat the solution with stirring to an internal temperature of 160 °C with continuous water removal. After a reaction time of 4.0 hours, distill off the water under reduced pressure (670 mbar). When 262 g of water distillate is collected, discharge the highly viscous polymer into a silicone container as quickly as possible while it is still hot and flowable. The k-value of the resulting main-chain molecule (a.7) is determined to be 11.0 in a 1% aqueous solution by weight.

[0352] Synthesis of the polymer (A) of the present invention

[0353] Synthesize the copolymer of the present invention using α-methylpyridine borane as a reducing agent

[0354] Polymer (A.13) of the present invention

[0355] In a 250 ml round-bottomed flask equipped with a magnetic stirrer, a condenser, and a gas bubbler, dissolve 3.0 g (a.6) in 70 g of water:acetic acid 10:1 wt. with stirring. Then, add 20.8 g (b.2) to the solution, and subsequently add dropwise a solution of 2.20 g of α-methylpyridine borane in 5 ml of methanol. The pH value at the start of the reaction is between 3.5 and 4.5. Gas evolution is observed. Allow the reactants to react at 85 °C for 24 h. After post-treatment as described above, obtain the polymer (A.13) of the present invention, DM: 72%, Mn: 5,426 g / mol, Mw: 6,974 g / mol.

[0356] Polymer (A.14) of the present invention

[0357] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 3.0 g (a.6) was dissolved in 90 g of water: acetic acid 10:1 wt. under stirring. Then, 42.0 g (b.6) was added to the solution, and subsequently a solution of 2.25 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reaction was carried out at ambient temperature until the reaction mixture was transparent and no visible bubbles were formed any longer. After post-treatment as above, the polymer (A.14) of the present invention was obtained, DM: 48%, Mn: 6,913 g / mol, Mw: 17,322 g / mol.

[0358] Polymer (A.15) of the present invention

[0359] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 2.7 g (a.2) was dissolved in 90 g of water: acetic acid 10:1 wt. under stirring. Then, 42.0 g (b.6) was added to the solution, and subsequently a solution of 2.25 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reactants were reacted at 85 °C for 24 h. After post-treatment as above, the polymer (A.15) of the present invention was obtained, DM: 44%, Mn: 12,252 g / mol, Mw: 50,844 g / mol.

[0360] Polymer (A.16) of the present invention

[0361] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser and a gas bubbler, 4.0 g (a.1) was dissolved in 90 g of water: acetic acid 10:1 wt. under stirring. Then, 47.4 g (b.2) was added to the solution, and subsequently a solution of 3.34 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reactants were reacted at 60 °C for 24 h. After post-treatment as above, the polymer (A.16) of the present invention was obtained, DM: 86%, Mn: 50,570 g / mol, Mw: 61,292 g / mol.

[0362] Polymer (A.17) of the present invention

[0363] In a 250 ml round-bottom flask equipped with a magnetic stirrer, a condenser, and a gas bubbler, 3.0 g (a.7) was dissolved in 70 g of water: acetic acid 10:1 wt. with stirring. Then, 18.50 g (b.7) was added to the solution, and subsequently, a solution of 2.25 g of α-methylpyridine borane in 5 ml of methanol was added dropwise. The pH value at the start of the reaction was between 3.5 and 4.5. Gas evolution was observed. The reactants were allowed to react at 60 °C for 24 h. After post-treatment as described above, the polymer (A.17) of the present invention was obtained, with DM: 66%, Mn: 5,166 g / mol, and Mw: 8,594 g / mol.

[0364] V. Biodegradability of the polymers (A.13) to (A.17) of the present invention

[0365] Table 10: Results of biodegradation tests

[0366] Polymer 28 days (%) 56 days (%) (A.13) 68 68 (A.14) 72 79 (A.15) 69 72 (A.16) 69 69 (A.17) 63 68

[0367] VI. Detergency performance of the polymers (A.13) to (A.17) of the present invention

[0368] Anti-greying performance

[0369] Test 1 Yellow clay Asian conditions

[0370] Using a stir-type washing machine with detergency (RHLG-IV, from Shanghai Bank Equipment Co., Ltd., China) including 12 cylinders with corresponding rotor blades as the washing unit, generally following GBT 13174-2008, the laundry process was simulated in the laboratory. The washing units were operated at the same stirring speed of 120 revolutions per minute (rpm), and each was filled with 1 L of washing liquid. The white test fabric was washed in the same cylinder with 10 g of yellow clay and oil mixture at 30 °C in the washing liquid containing the detergent formulation as shown in Table xx. After washing, the fabric was taken out from the washing unit, drained, rinsed twice in 10 L of tap water for 30 seconds each time, and dried in air. The details of the washing cycle are summarized in Table xx.

[0371] The anti-greying performance was characterized by the remission R value of the dirty fabric after washing, and was determined by measuring the fabric with a spectrophotometer Elrepho 2000 from Delta Color Company at 457 nm. The higher the remission R value, the better the performance. The results are summarized in Table xx.

[0372] Table 11: Composition of the liquid detergent formulation.

[0373]

[0374]

[0375] Table 12: Details of the washing experiment

[0376]

[0377] Table 13: Washing results

[0378] Additive R, sum of all fabrics Blank 344.20 PA25 357.98 HP20 355.92 Maltodextrin-g-PAA graft Bio Bverde 790 354.69 (A.8) 350.20 (A.13) 352.51 (A.14) 354.33 (A.15) 354.32 (A.16) 361.42 (A.17) 350.40

[0379] Compatibility with liquid laundry detergent formulations

[0380] Table 14: Ingredients of the liquid detergent formulation

[0381]

[0382]

[0383] Table 15: Compatibility of additives in the liquid detergent formulation

[0384]

Claims

1. An aqueous detergent composition comprising (A) at least one polymer comprising (a) The main chain, which is derived from an aliphatic compound having at least 4 amino groups per molecule, and at least one of these amino groups is -(CH 2 ) a -NH 2 group, the variable a is selected from 2 to 4, and at least 40 mol-% of the said CH 2 -(CH 2 ) a -NH 2 groups are used (b) Sugars based on monosaccharides, disaccharides or polysaccharides are converted in the formation of a secondary amino group having the general formula -(CH 2 ) a -NH-CH 2 -.

2. The composition according to claim 1, wherein, the main chain (a) is selected from H 2 N-(CH 2 ) 3 -NH-CH 2 CH 2 -N(CH 2 ) 3 -NH 2 , polyethyleneimine, and a (poly)peptide having on average at least two lysine moieties as structural units.

3. The composition according to claim 1 or 2, wherein, The main chain (a) is selected from branched polyethyleneimines having an average molecular weight M w in the range of 500 to 20,000 g / mol.

4. The composition according to claim 1 or 2, wherein, The main chain (a) is selected from ε-polylysine having a molecular weight M w in the range of 1,000 to 8,000 g / mol.

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

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

7. The composition according to any one of the preceding claims, wherein, the composition additionally comprises (B) at least one hydrolase.

8. Use of the composition according to any one of the preceding claims for fabric care.

9. A polymer comprising (a) A main chain derived from an aliphatic compound having at least 4 amino groups per molecule, at least one of these amino groups being a -(CH 2 ) a -NH 2 group, the variable a being selected from 2 to 4, wherein at least 40 mol-% of said -(CH 2 ) a -NH 2 groups are used (b) Sugars based on monosaccharides, disaccharides or polysaccharides are transformed under the formation of secondary amino groups having the general formula -(CH 2 ) a -NH-CH 2 -.

10. The polymer according to claim 9, having an average molecular weight M in the range from 750 to 350,000 g / mol w .

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

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

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

14. A method for preparing the polymer according to any one of claims 9 to 12, the method comprising the steps of: (α) Provide a main-chain molecule (a), which is an aliphatic compound having at least 4 amino groups per molecule, and at least one of these amino groups is -(CH 2 ) a -NH 2 group, and the variable a is selected from 2 to 4. (β) reacting the main chain 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 an aminoborane.

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

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