WO2021105330A1 - Compositions and polymers useful for such compositions - Google Patents

Abstract

The present invention is directed towards compositions comprising (A) at least one polymer comprising (a) a core that bears one to 3 moieties of the general formula (I) wherein Z are different or the same and selected from C2-C12-alkylene and C3-C12-cycloalkylene wherein C2-C12-alkylene and C3-C12-cycloalkylene may be non-substituted or substituted with one or more O-C1-C4-alkyl groups and wherein C3-C12-cycloalkylene may be non-substituted or bear one to three methyl groups. X1 is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, preferred are methyl and more preferred is hydrogen, and n is in the range of from 1 to 4, (b) polyalkylene oxide chains.

Description

Compositions and polymers useful for such compositions

The present invention is directed towards compositions comprising (A) at least one polymer comprising

(a) a core that bears one to 3 moieties of the general formula (I)

wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-Ci-C₄-alkyl groups and wherein C3-Ci2-cycloalkylene may bear one to three methyl groups,

X¹ is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, preferred are methyl and more preferred is hydrogen, n is in the range of from 1 to 4,

(b) polyalkylene oxide chains.

Furthermore, the present invention is directed to polymers useful for such compositions, and to a process for making such polymers.

Laundry detergents have to fulfil several requirements. They need to remove all sorts of soiling from laundry, for example all sorts of pigments, clay, fatty soil, and dyestuffs including dyestuff from food and drinks such as red wine, tea, coffee, and fruit including berry juices. Laundry de tergents also need to exhibit a certain storage stability. Especially laundry detergents that are liquid or that contain hygroscopic ingredients often lack a good storage stability, e.g. enzymes tend to be deactivated.

Fatty soilings are still a challenge in laundering. Although numerous suggestions for removal have been made - polymers, enzymes, surfactants - solutions that work well are still of interest. It has been suggested to use a lipase to support fat removal but many builders - especially in liquid laundry detergents - do not work well with lipase. It was therefore an objective to provide a detergent composition that fulfils the requirements discussed above. It was further an objective to provide ingredients that fulfil the above require ments, and it was an objective to provide a process to make such ingredients and detergent compositions.

Accordingly, the compositions defined at the outset have been found, hereinafter also referred to as inventive compositions or compositions according to the present invention.

Inventive compositions comprise (A) least one polymer comprising

(a) a core that bears one to 3 moieties of the general formula (I)

wherein Z are different or the same and selected from

C₂-Ci2-alkylene, for example -CH2CH2-, -(CH₂)3-, -(CH₂)4-, -(CH₂)5-, -(CH₂)6-, -(CH₂)8-, -(CH₂)IO-, -(CH₂)i2-, wherein C2-Ci2-alkylene may be straight-chain or branched, non-substituted or substi tuted with one or more 0-Ci-C₄-alkyl groups and

C3-Ci2-cycloalkylene, wherein C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-Ci-C₄-alkyl groups, and where C3-Ci2-cycloalkylene may bear one to three me thyl groups, preferably C₅-Cio-cycloalkylene such as 1 ,3-cyclopentylene, 1 ,2-cyclopentylidene, 1 ,2-cyclohexylene, 1 ,3-cyclohexylene, 1 ,4-cyclohexylene, 1 -methyl-2, 4-cyclohexylene, 1 - methyl-2, 6-cyclohexylene, 1 ,3-cycloheptylene, 1 ,4-cylooctylene, 1 ,5-cyclooctylene, wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-Ci-C₄-alkyl groups and wherein C3-Ci2-cycloalkylene may be non-substituted or bear one to three methyl groups,

X¹ is selected from hydrogen and methyl and ethyl and combinations of at least two of the fore going, preferred are methyl and more preferred is hydrogen, preferred is hydrogen, n is in the range of from 1 to 4, preferably 1 to 3 and more preferably 1 to 2,

The free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or -CH₂-CH(X¹)-0-CHX¹-CH₂-N-Z-N units, or hydrogen atoms. In embodiments with molecular weights M_w of 10,000 g/mol or more, the free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or -CH₂-CH(X¹)-0-CHX¹-CH₂-N-Z-N units.

In one embodiment of the present invention, all Z in polymer (A) are selected from cyclo hexylene and cyclopentylene, each non-substituted or substituted with one to two methyl or methoxy groups.

Preferably, Z are isomers to each other and/or differ in the variable n. Even more preferably, Z are isomers.

A preferred example of Z is a combination - thus a mixture of isomers - according to the formu lae

Asterisks^* refer to sites in Z that are connected to N atoms.

In one embodiment of the present invention, polymer (A) has an average molecular weight M_w in the range of from 1 ,000 to 80,000 g/mol, preferably 5,000 to 50,000 g/mol. The average mo lecular weight may be determined, e.g., by gel permeation chromatography (GPC) in tetrahydro- furan (THF) as mobile phase, with linear polymethyl methacrylate (“PMMA”) as standard.

In one embodiment of the present invention, polymer (A) has a molecular weight distribution M_w/M_n in the range of from 1 .1 to 2.5. In one embodiment of the present invention, polymer (A) has a Hazen colour number in the range of from 20 to 500, determined in a 10 % weight aqueous solution.

In one embodiment of the present invention, polymer (A) has an OH value, measured according to DIN 53240 (2013), in the range of from 20 to 650, preferably 30 to 100 mg KOH/g polymer (A).

In one embodiment of the present invention, polymer (A) has a total amine value in the range of from 10 to 650, preferably 10 to 510 and more preferably 10 to 80 mg KOH/g polymer (A), de termined according to ASTM D2074-07.

Polymer (A) furthermore bears

(b) polyalkylene oxide chains. Said polyalkylene oxide chains may be derived from C2-C4- alkylene oxide. Examples of C2-C4-alkylene oxides are ethylene oxide („EO“), propylene ox ide (“PO”), butylene oxide (“BuO”), and combinations of at least two of the foregoing, for example ethylene oxide and propylene oxide or ethylene oxide and butylene oxide. Pre ferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.

In one embodiment of the present invention, inventive compositions comprise at least one en zyme. Enzymes are identified by polypeptide sequences (also called amino acid sequences herein). The polypeptide sequence specifies the three-dimensional structure including the “ac tive site” of an enzyme which in turn determines the catalytic activity of the same. Polypeptide sequences may be identified by a SEQ ID NO. According to the World Intellectual Property Of fice (WIPO) Standard ST.25 (1998) the amino acids herein are represented using three-letter code with the first letter as a capital or the corresponding one letter.

Any enzyme according to the invention relates to parent enzymes and/or variant enzymes, both having enzymatic activity. Enzymes having enzymatic activity are enzymatically active or exert enzymatic conversion, meaning that enzymes act on substrates and convert these into prod ucts. The term “enzyme” herein excludes inactive variants of an enzyme.

A “parent” sequence (of a parent protein or enzyme, also called “parent enzyme”) is the starting sequence for introduction of changes (e.g. by introducing one or more amino acid substitutions, insertions, deletions, or a combination thereof) to the sequence, resulting in “variants” of the parent sequences. The term parent enzyme (or parent sequence) includes wild-type enzymes (sequences) and synthetically generated sequences (enzymes) which are used as starting se quences for introduction of (further) changes. The term “enzyme variant” or “sequence variant” or “variant enzyme” refers to an enzyme that differs from its parent enzyme in its amino acid sequence to a certain extent. If not indicated otherwise, variant enzyme “having enzymatic activity” means that this variant enzyme has the same type of enzymatic activity as the respective parent enzyme.

In describing the variants of the present invention, the nomenclature described as follows is used:

Amino acid substitutions are described by providing the original amino acid of the parent en zyme followed by the number of the position within the amino acid sequence, followed by the substituted amino acid. Amino acid deletions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by^*. Amino acid insertions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, an insertion at position 180 of lysine next to glycine is designated as “Gly180Glyl_ys” or “G180GK”. In cases where a substitution and an insertion occur at the same position, this may be indicated as S99SD+S99A or in short S99AD. In cases where an amino acid residue identical to the existing amino acid residue is inserted, degeneracy in the nomenclature arises. If for example a glycine is inserted after the glycine in the above example this would be indicated by G180GG. Where different al terations can be introduced at a position, the different alterations are separated by a comma, e.g. “Arg170Tyr, Glu” represents a substitution of arginine at position 170 with tyrosine or glu tamic acid. Alternatively different alterations or optional substitutions may be indicated in brack ets e.g. Arg170[Tyr, Gly] or Arg170{Tyr, Gly}; or in short R170 [Y,G] or R170 {Y, G}; or in long R170Y, R170G.

Enzyme variants may be defined by their sequence identity when compared to a parent en zyme. Sequence identity usually is provided as “% sequence identity” or “% identity”. For calcu lation of sequence identities, in a first step a sequence alignment has to be produced. According to this invention, a pairwise global alignment has to be produced, meaning that two sequences have to be aligned over their complete length, which is usually produced by using a mathemati cal approach, called alignment algorithm. According to the invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. (1979) 48, p. 443-453). Prefer ably, the program “NEEDLE” (The European Molecular Biology Open Software Suite (EM BOSS)) is used for the purposes of the current invention, with using the programs default pa rameter (gap open=10.0, gap extend=0.5 and matrix=EBLOSUM62). According to this invention, the following calculation of %-identity applies: %-identity = (identical residues / length of the alignment region which is showing the respective sequence of this in vention over its complete length)^*100.

According to this invention, enzyme variants may be described as an amino acid sequence which is at least n% identical to the amino acid sequence of the respective parent enzyme with “n” being an integer between 10 and 100. In one embodiment, variant enzymes are 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 when compared to the full-length amino acid sequence of the parent en zyme, wherein the enzyme variant has enzymatic activity.

“Enzymatic activity” means the catalytic effect exerted by an enzyme, which usually is ex pressed as units per milligram of enzyme (specific activity) which relates to molecules of sub strate transformed per minute per molecule of enzyme (molecular activity). Variant enzymes may have enzymatic activity according to the present invention when said enzyme variants ex hibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the enzymatic activity of the respective parent enzyme.

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

In one embodiment of the present invention, inventive compositions comprise (B) at least one lipase, hereinafter also referred to as lipase (B).

“Lipases”, “lipolytic enzyme”, “lipid esterase”, all refer to enzymes of EC class 3.1.1 (“carboxylic ester hydrolase”). Such a lipase (B) may have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1 .3), cutinase activity (EC 3.1.1 .74; enzymes having cutinase activity may be called cutinase herein), sterol esterase activity (EC 3.1 .1.13) and/or wax-ester hydrolase activity (EC 3.1.1 .50). Lipases (B) include those of bacterial or fungal origin.

Commercially available lipase (B) include but are not limited to those sold under the trade names Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A/S), Preferenz™ L (DuPont), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM). In one aspect of the present invention, lipase (B) is selected from the following: lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (7. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. insolens as described in WO 96/13580; lipases derived from Rhizomucor miehei as described in WO 92/05249; lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. from P. alcali- genes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381 ,

WO 96/00292), P. cepacia (EP 331376), P. stutzeri ( GB 1372034), P. fluorescens, Pseudomo nas sp. strain SD705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), Pseudomonas mendocina (WO 95/14783), P. glumae (WO 95/35381 , WO 96/00292); lipase from Streptomyces griseus (WO 2011/150157) and S. pristinaespiralis (WO 2012/137147), GDSL-type Streptomyces lipases (WO 2010/065455); lipase from Thermobifida fusca as dis closed in WO 2011/084412; lipase from Geobacillus stearothermophilus as disclosed in WO 2011/084417; Bacillus lipases, e.g. as disclosed in WO 00/60063, lipases from B. subtilis as disclosed in Dartois et al. (1992), Biochemica et Biophysica Acta, 1131 , 253-360 or WO 2011/084599, B. stearothermophilus (JP S64-074992) or B. pumilus (WO 91/16422); lipase from Candida antarctica as disclosed in WO 94/01541. Suitable lipases (B) include also those which are variants of the above described lipases which have lipolytic activity. Such suitable lipase variants are e.g. those which are developed by methods as 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 e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.

Suitable lipases (B) include also those that are variants of the above described lipases which have lipolytic activity. Suitable lipase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment lipase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least

80%, at least 85%, at least 90%, at least 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 the parent enzyme as disclosed above.

Lipases (B) have “lipolytic activity”. The methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71). E.g. the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl pal- mitate (pNP-Palmitate, C:16) and releases pNP which is yellow and can be detected at 405 nm. In one embodiment, lipase (B) is selected from fungal triacylglycerol lipase (EC class 3.1.1 .3). Fungal triacylglycerol lipase may be selected from lipases of Thermomyces lanuginosa. In one embodiment, at least one Thermomyces lanuginosa lipase is selected from triacylglycerol lipase according to amino acids 1-269 of SEQ ID NO: 2 of US5869438 and variants thereof having lipolytic activity.

Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity which 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 poly peptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.

Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing conservative mutations only, which do not pertain the functional domain of amino acids 1- 269 of SEQ ID NO: 2 of US 5,869,438. Lipase variants of this embodiment having lipolytic ac tivity may 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.

Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing at least the following amino acid substitutions when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: T231 R and N233R. Said lipase variants may further comprise one or more of the following amino acid exchanges when compared to amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438: Q4V, V60S, A150G, L227G, P256K.

Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing at least the amino acid substitutions T231 R, N233R, Q4V, V60S, A150G, L227G, P256K within the polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438and are at least 95%, at least 96%, or at least 97% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438.

Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity compris ing the amino acid substitutions T231 R and N233R within amino acids 1-269 of SEQ ID NO: 2 of US5869438 and are at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438. Thermomyces lanuginosa lipase may be a variant of amino acids 1 -269 of SEQ ID NO: 2 of US5869438 having lipolytic activity, wherein the variant of amino acids 1-269 of SEQ ID NO: 2 of US 5,869,438is characterized in containing the amino acid substitutions T231 R and N233R. Said lipase may be called Lipex herein.

In one embodiment of the present invention, a combination of at least two of the foregoing li pases (B) may be used.

In one embodiment of the present invention, lipases (B) are included in inventive composition in such an amount that a finished inventive composition has a lipolytic enzyme activity in the range of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition. A Lipase Unit (LU) is that amount of lipase which produces 1 pmol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30° C.; pH=9.0; substrate is an emulsion of 3.3 wt. % of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca²⁺ and 20 mmol/l NaCI in 5 mmol/l Tris-buffer.

In one embodiment of the present invention, inventive compositions comprise (D) at least one protease (D), hereinafter also referred to as protease (D).

In one embodiment, at least one protease (D) is selected from the group of serine endopepti- dases (EC 3.4.21), most preferably selected from the group of subtilisin type proteases (EC 3.4.21.62). Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction. A serine protease in the context of the present invention may be selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1 ), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71 ), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21 .79), kallikrein (e.g., EC 3.4.21 .34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21 .5), and subtilisin. Subtilisin is also known as subtilopeptidase, e.g., EC 3.4.21.62, the latter hereinafter also being referred to as “subtilisin”. The subtilisin related class of serine proteases shares a common amino acid se quence defining a catalytic triad which distinguishes them from the chymotrypsin related class of serine proteases. Subtilisins and chymotrypsin related serine proteases both have a catalytic triad comprising aspartate, histidine and serine.

Proteases are active proteins exerting “protease activity” or “proteolytic activity”. Proteolytic ac tivity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a de fined course of time. The methods for analyzing proteolytic activity are well-known in the literature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381-395). Proteolytic activity may be determined by using Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate. pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in release of yellow color of free pNA which can be quantified by measuring OD405.

Proteolytic activity may be provided in units per gram enzyme. For example, 1 U protease may correspond to the amount of protease which sets free 1 pmol folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37°C (casein as substrate).

Proteases of the subtilisin type (EC 3.4.21.62) may be bacterial proteases originating from a microorganism selected from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fuso- bacterium, Helicobacter, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

In one aspect of the invention, at least one protease (D) is selected from Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagu- lans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacil lus subtilis, or Bacillus thuringiensis protease.

In one embodiment of the present invention, at least one protease (D) is selected from the fol lowing: subtilisin from Bacillus amyloliquefaciens BRN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, p. 811 -819 and JA Wells et al. (1983) in Nucleic Acids Research, Vol ume 11 , p. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Acids Res, Vol 13, p. 8913-8926); subtilisin PB92 (original sequence of the alkaline prote ase PB92 is described in EP 283075 A2); subtilisin 147 and/or 309 (Esperase®, Savinase®, respectively) as disclosed in WO 89/06279; subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95/23221 ; subtilisin from Bacillus alcalophilus (DSM 11233) disclosed in DE 10064983; subtilisin from Bacillus gibsonii (DSM 14391) as disclosed in WO 2003/054184; sub tilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017; subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974; subtilisin from Bacillus gibsonii (DSM 14393) dis- closed in WO 2003/054184; subtilisin having SEQ ID NO: 4 as described in WO 2005/063974; subtilisin having SEQ ID NO: 4 as described in WO 2005/103244; subtilisin having SEQ ID NO: 7 as described in WO 2005/103244; and subtilisin having SEQ ID NO: 2 as described in appli cation DE 102005028295.4.

Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221 , WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2011/036264, and WO 2011/072099. Suitable exam ples comprise especially variants of subtilisin protease derived from SEQ ID NO:22 as de scribed in EP 1921147 (which is the sequence of mature alkaline protease from Bacillus !entus DSM 5483) with amino acid substitutions in 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 the BPN' numbering), which have proteolytic activity. In one embodiment, such a protease is not mutated at positions Asp32, His64 and Ser221 (according to BPN’ numbering).

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 which is at least 80% identical thereto and has proteo lytic activity. In one embodiment, said protease is characterized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity. In one embodiment, said protease comprises one or more further substitutions: (a) threonine at posi tion 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) combina tions of two or more amino acids according to (a) to (h).

At least one protease (D) may 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 combina tions according to (i) together with the amino acid 101 E, 101 D, 101 N, 101Q, 101 A, 101G, or 101 S (according to BPN’ numbering). In one embodiment, said protease is characterized by comprising the mutation (according to BPN’ numbering) R101 E, or S3T + V4I + V205I, or R101 E and S3T, V4I, and V205I, or S3T + V4I + V199M + V205I + L217D, and having proteo- lytic activity. A protease having a sequence according to SEQ ID NO: 22 as described in EP 1921147 with 101 E may be called Lavergy herein.

In one embodiment, protease according to SEQ ID NO:22 as described in EP 1921147 is char acterized by comprising the mutation (according to BPN’ numbering) S3T + V4I + S9R + A15T + V68A + D99S + R101S + A103S + 1104V + N218D, and having proteolytic activity.

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

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

In the context of the present invention, lipase (B) and/or protease (D) is deemed called stable when its enzymatic activity “available in application” equals at least 60% when compared to the initial enzymatic activity before storage. An enzyme may be called stable within this invention if its enzymatic activity available in 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 91%, at least 92%, at least 93%, at least

94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% when compared to the initial enzymatic activity before storage.

Subtracting a% from 100% gives the “loss of enzymatic activity during storage” when compared to the initial enzymatic activity before storage. In one embodiment, an enzyme is stable accord ing to the invention when essentially no loss of enzymatic activity occurs during storage, i.e. loss in enzymatic activity equals 0% when compared to the initial enzymatic activity before stor age. Essentially no loss of enzymatic activity within this invention may mean that the loss of enzymatic activity is less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 9%, less than 8%, less than 7%, less than 6%, less than 5%.

In one embodiment of the present invention, inventive compositions comprise

(C) at least one anionic surfactant, hereinafter also being referred to as anionic surfactant (C).

Examples of anionic surfactants (C) are alkali metal and ammonium salts of Cs-Cis-alkyl sulfates, of Cs-Cis-fatty alcohol polyether sulfates, of sulfuric acid half-esters of ethoxylated C₄- Ci2-alkylphenols (ethoxylation: 1 to 50 mol of ethylene oxide/mol), C12-C18 sulfo fatty acid alkyl esters, for example of C12-C18 sulfo fatty acid methyl esters, furthermore of Ci2-Ci8-alkylsulfonic acids and of Cio-Cis-alkylarylsulfonic acids. Preference is given to the alkali metal salts of the aforementioned compounds, particularly preferably the sodium salts.

Further examples of anionic surfactants (C) are soaps, for example the sodium or potassium salts of stearic acid, oleic acid, palmitic acid, ether carboxylates, and alkylether phosphates.

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

R¹-0(CH₂CH₂0)_X-S0₃M (II) wherein

R¹ n-Cio-Cis-alkyl, especially with an even number of carbon atoms, for example n-decyl, n- dodecyl, n-tetradecyl, n-hexadecyl, or n-octadecyl, preferably Cio-Ci4-alkyl, and even more preferably n-Ci2-alkyl, x being a number in the range of from 1 to 5, preferably 2 to 4 and even more preferably 3.

M being selected from alkali metals, preferably potassium and even more preferably sodium.

In anionic surfactant (C), x may be an average number and therefore n is not necessarily a whole number, while in individual molecules according to formula (I), x denotes a whole num ber.

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

Inventive compositions may comprise ingredients other than the aforementioned. Examples are non-ionic surfactants, fragrances, dyestuffs, biocides, preservatives, enzymes, hydrotropes, builders, viscosity modifiers, polymers, buffers, defoamers, and anti-corrosion additives.

Preferred inventive compositions may contain one or more non-ionic surfactants.

Preferred non-ionic surfactants are alkoxylated alcohols, di- and multiblock copolymers of eth ylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or pro pylene oxide, alkyl polyglycosides (APG), hydroxyalkyl mixed ethers and amine oxides. Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds of the general formula (III a)

in which the variables are defined as follows:

R² is identical or different and selected from hydrogen and linear Ci-Cio-alkyl, preferably in each case identical and ethyl and particularly preferably hydrogen or methyl,

R³ is selected from C₃-C22-alkyl, branched or linear, for example n-C₃Hi , n-CioH_2i, n-Ci2H₂5, n-Ci₄H₂₉, n-Ci₆H₃₃ or n-CisH₃₇,

R⁴ is selected from Ci-Cio-alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1 ,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl or isodecyl,

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

In one embodiment, compounds of the general formula (II) may be block copolymers or random copolymers, preference being given to block copolymers.

Other preferred examples of alkoxylated alcohols are, for example, compounds of the general formula (III b)

in which the variables are defined as follows:

R² is identical or different and selected from hydrogen and linear CrCo-alkyl, preferably iden tical in each case and ethyl and particularly preferably hydrogen or methyl,

R⁵ is selected from C6-C2o-alkyl, branched or linear, in particular n-CsHi , n-CioH_2i, n-Ci2H₂5, n-Ci3H₂ , n-Ci5H3i , n-Ci4H₂9, n-Ci6H33, n-CisH37, a is a number in the range from zero to 10, preferably from 1 to 6, b is a number in the range from 1 to 80, preferably from 4 to 20, d is a number in the range from zero to 50, preferably 4 to 25.

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

Compounds of the general formula (III) may be block copolymers or random copolymers, pref erence being given to block copolymers.

Further suitable nonionic surfactants are selected from di- and multiblock copolymers, com posed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, espe cially linear C4-Ci6-alkyl polyglucosides and branched Cs-Ci4-alkyl polyglycosides such as com pounds of general average formula (IV) are likewise suitable.

wherein:

R⁶ is Ci-C4-alkyl, in particular ethyl, n-propyl or isopropyl, R⁷ is -(CH₂)₂-R⁶, G¹ is selected from monosaccharides with 4 to 6 carbon atoms, especially from glucose and xylose, y in the range of from 1.1 to 4, y being an average number,

Further examples of non-ionic surfactants are compounds of general formula (V) and (VI)

AO is selected from ethylene oxide, propylene oxide and butylene oxide,

EO is ethylene oxide, CH₂CH₂-0,

R⁸ selected from Cs-Cis-alkyl, branched or linear, and R⁵ is defined as above.

A³0 is selected from propylene oxide and butylene oxide, w is a number in the range of from 15 to 70, preferably 30 to 50, w1 and w3 are numbers in the range of from 1 to 5, and w2 is a number in the range of from 13 to 35.

An overview of suitable further nonionic surfactants can be found in EP-A 0 851 023 and in DE- A 198 19 187.

Mixtures of two or more different nonionic surfactants selected from the foregoing may also be present.

Other surfactants that may be present are selected from amphoteric (zwitterionic) surfactants and anionic surfactants and mixtures thereof. Examples of amphoteric surfactants are those that bear a positive and a negative charge in the same molecule under use conditions. Preferred examples of amphoteric surfactants are so- called betaine-surfactants. Many examples of betaine-surfactants bear one quaternized nitrogen atom and one carboxylic acid group per molecule. A particularly preferred example of amphoter ic surfactants is cocamidopropyl betaine (lauramidopropyl betaine).

Examples of amine oxide surfactants are compounds of the general formula (VII)

R⁹R^{1 0}R^{1 1}N O (VII) wherein R⁹, R¹⁰, and R^{1 1} are selected independently from each other from aliphatic, cycloali phatic or C2-C4-alkylene Cio-C2o-alkylamido moieties. Preferably, R⁹ is selected from C8-C20- alkyl or C2-C4-alkylene Cio-C2o-alkylamido and R¹⁰ and R^{1 1} are both methyl.

A particularly preferred example is lauryl dimethyl aminoxide, sometimes also called lauramine oxide. A further particularly preferred example is cocamidylpropyl dimethylaminoxide, some times also called cocamidopropylamine oxide.

In one embodiment of the present invention, inventive compositions may contain 0.1 to 60 % by weight of at least one surfactant, selected from non-ionic surfactants, amphoteric surfactants and amine oxide surfactants.

In a preferred embodiment, inventive solid detergent compositions for cleaners and especially those for automatic dishwashing do not contain any anionic surfactant.

Inventive compositions may contain at least one bleaching agent, also referred to as bleach. Bleaching agents may be selected from chlorine bleach and peroxide bleach, and peroxide bleach may be selected from inorganic peroxide bleach and organic peroxide bleach. Preferred are inorganic peroxide bleaches, selected from alkali metal percarbonate, alkali metal perborate and alkali metal persulfate.

Examples of organic peroxide bleaches are organic percarboxylic acids, especially organic per- carboxylic acids.

In inventive compositions, alkali metal percarbonates, especially sodium percarbonates, 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, for example combinations of sodium carbonate and sodium sulfate.

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

Inventive compositions may comprise, for example, in the range from 3 to 10% by weight of chlorine-containing bleach.

Inventive compositions may comprise one or more bleach catalysts. Bleach catalysts can be selected from bleach-boosting transition metal salts or transition metal complexes such as, for example, 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 and also cobalt-, iron-, copper- and rutheni um-amine complexes can also be used as bleach catalysts.

Inventive compositions may comprise one or more bleach activators, for example N- methylmorpholinium-acetonitrile salts (“MMA salts”), trimethylammonium acetonitrile salts, N- acylimides such as, for example, N-nonanoylsuccinimide, 1 ,5-diacetyl-2,2-dioxohexahydro- 1 ,3,5-triazine (“DADHT”) or nitrile quats (trimethylammonium acetonitrile salts).

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

Examples of fragrances are benzyl salicylate, 2-(4-tert.-butylphenyl) 2-methylpropional, com mercially available as Lilial®, and hexyl cinnamaldehyde.

Examples of dyestuffs 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.

Inventive compositions may contain one or more preservatives or biocides. Biocides and pre servatives prevent alterations of inventive liquid detergent compositions due to attacks from microorganisms. Examples of biocides and preservatives are BTA (1 ,2,3-benzotriazole), ben- zalkonium chlorides, 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, iodopropynyl butyl- carbamate (“IPBC”), dichlorodimethylhydantoine (“DCDMH”), bromochlorodimethylhydantoine (“BCDMH”), and dibromodimethylhydantoine (“DBDMH”).

Examples of viscosity modifiers are agar-agar, carragene, tragacanth, gum arabic, alginates, pectins, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, cross- linked poly(meth)acrlyates, for example polyacrlyic acid cross-linked with bis-(meth)acrylamide, furthermore silicic acid, clay such as - but not limited to - montmorrilionite, zeolite, dextrin, and casein.

Hydrotropes in the context with the present invention are compounds that facilitate the dissolu tion of compounds that exhibit limited solubility in water. Examples of hydrotropes are organic solvents such as ethanol, isopropanol, ethylene glycol, 1 ,2-propylene glycol, and further organic solvents that are water-miscible under normal conditions without limitation. Further examples of suitable hydrotropes are the sodium salts of toluene sulfonic acid, of xylene sulfonic acid, and of cumene sulfonic acid.

Examples of polymers other than polymer (A) are especially polyacrylic acid and its respective alkali metal salts, especially its sodium salt. A suitable polymer is in particular polyacrylic acid, preferably with an average molecular weight M_w in the range from 2,000 to 40,000 g/mol. pref erably 2,000 to 10,000 g/mol, in particular 3,000 to 8,000 g/mol, each partially or fully neutral ized with alkali, especially with sodium. Suitable as well are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid and/or fumaric acid. Polyacrylic acid and its respective alkali metal salts may serve as soil anti-redeposition agents.

Further examples of polymers are polyvinylpyrrolidones (PVP). Polyvinylpyrrolidones may serve as dye transfer inhibitors.

Further examples of polymers are polyethylene terephthalates, polyoxyethylene terephthalates, and polyethylene terephthalates that are end-capped with one or two hydrophilic groups per molecule, hydrophilic groups being selected from CH₂CH₂CH2-S03Na, CH₂CH(CH₂-SC>3Na)₂, and CH₂CH(CH₂S0₂Na)CH₂-S0₃Na.

Examples of buffers are monoethanolamine and N,N,N-triethanolamine.

Examples of defoamers are silicones. Inventive compositions are not only good in cleaning soiled laundry with respect to organic fatty soil such as oil. Inventive liquid detergent compositions are very useful for removing non- bleachable stains such as, but not limited to stains from red wine, tea, coffee, vegetables, and various fruit juices like berry juices from laundry. They still do not leave residues on the clothes.

In order to be suitable as liquid laundry compositions, inventive compositions may be in bulk form or as unit doses, for example in the form of sachets or pouches. Suitable materials for pouches are water-soluble polymers such as polyvinyl alcohol.

In a preferred embodiment of the present invention, inventive compositions are liquid or gel- type.

In one embodiment of the present invention, inventive compositions are liquid or gel-type and have a pH value in the range of from 7 to 9, preferably 7.5 to 8.5.

In one embodiment of the present invention, inventive compositions are liquid or gel-type and have a total solids content in the range of from 8 to 80%, preferably 10 to 50%, determined by drying under vacuum at 80°C.

Another aspect of the present invention is related to polymers (A), hereinafter also referred to as inventive polymers (A) or simply as polymers (A). Inventive polymers (A) comprise

(a) a core that bears one to 3 moieties of the general formula (I)

wherein Z are different or the same and selected from

C2-Ci2-alkylene, for example -CH2CH2-, -(CH₂)3-, -(CH₂)4-, -(CH₂)5-, -(CH₂)6-, -(CH₂)8-, -(CH₂)IO-, wherein C2-Ci2-alkylene may be straight-chain or branched, non-substituted or substituted with one or more 0-Ci-C₄-alkyl groups and C3-Ci2-cycloalkylene, wherein C3-Ci2-cycloalkylene may be non-substituted or substitut ed with one or more 0-Ci-C₄-alkyl groups, and where C3-Ci2-cycloalkylene may bear one to three methyl groups, preferably C₅-Cio-cycloalkylene such as 1 ,3-cyclopentylene, 1 ,2-cyclopentylidene, 1 ,2-cyclohexylene, 1 ,3-cyclohexylene, 1 ,4-cyclohexylene, 1- methyl-2, 4-cyclohexylene, 1 -methyl-2, 6-cyclohexylene, 1 ,3-cycloheptylene, 1 ,4- cylooctylene, 1 ,5-cyclooctylene, wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non-substituted or substituted with one or more 0-Ci-C₄-alkyl groups and wherein C3-Ci2-cycloalkylene may be non- substituted or bear one to three methyl groups,

X¹ is selected from hydrogen and methyl, preferred is hydrogen, n is in the range of from 1 to 4, preferably 1 to 3 and more preferably 1 to 2,

(b) polyalkylene oxide chains.

The free valences on the nitrogen atoms in formula (I) bear polyalkylene chains (b) or -CH₂-CH(X¹)-0-CHX¹-CH₂-N-Z-N units, or hydrogen atoms.

Preferably, Z are isomers to each other and/or differ in the variable n. Even more preferably, Z are isomers.

A preferred example of Z is a combination - thus a mixture of isomers - according to the formu lae

Asterisks^* refer to sites in Z that are connected to N atoms. In one embodiment of the present invention, polymer (A) has an average molecular weight M_w in the range of from 1 ,000 to 80,000 g/mol, preferably 5,000 to 50,000 g/mol. The average mo lecular weight may be determined, e.g., by gel permeation chromatography in tetrahydrofuran (THF) as mobile phase, with linear polymethyl methacrylate (“PMMA”) as standard.

In one embodiment of the present invention, inventive polymer (A) has a molecular weight dis tribution M_w/M_n in the range of from 1 .1 to 2.5.

In one embodiment of the present invention, inventive polymer (A) has a Hazen colour number in the range of from 20 to 500, determined in a 10 % weight aqueous solution.

In one embodiment of the present invention, inventive polymer (A) has an OH value, measured according to DIN 53240 (2013), in the range of from 20 to 650, preferably 30 to 100 mg KOH/g polymer (A).

In one embodiment of the present invention, inventive polymer (A) has a total amine value in the range of from 10 to 650, preferably 10 to 510 and more preferably 10 to 80 mg KOH/g polymer (A), determined according to ASTM D2074-07.

Inventive polymers (A) are excellently suited as or for the manufacture of inventive composi tions.

In one aspect, the invention is directed to a method of improving the cleaning performance of a liquid detergent composition, by adding a polymer (A) according to the invention to a detergent composition preferably comprising at least one lipase and/or at least one protease.

The term "improved cleaning performance" herein may indicate that the polymer (A) provides better, i.e. improved, properties in stain removal under relevant cleaning conditions, when com pared to the cleaning performance of a detergent composition lacking polymer (A). In one em bodiment, “improved cleaning performance” means that the cleaning performance of a deter gent comprising polymer (A) and at least one enzyme, preferably at least one lipase (B) and/or at least one protease (D), is improved when compared to the cleaning performance of a deter gent comprising polymer (A) and no enzyme. In one embodiment, “improved cleaning perfor mance” means that the cleaning performance of a detergent comprising polymer (A) and an enzyme, preferably lipase (B) and/or protease (D), is improved when compared to the cleaning performance of a detergent comprising at least one enzyme, preferably at least one lipase (B) and/or at least one protease (D) and no polymer (A). The term "relevant cleaning conditions" herein refers to the conditions, particularly cleaning temperature, time, cleaning mechanics, suds concentration, type of detergent and water hard ness, actually used in laundry machines, automatic dish washers or in manual cleaning pro cesses.

A further aspect of the present invention relates to a process for making inventive polymers (A), hereinafter also referred to as inventive process. The inventive process comprises steps (a), (b) and (y):

(a) reacting a diamine according to general formula H2-N-Z-NH2 with alkylene oxide in a mo lar ratio alkylene oxide : diamine of from 4:1 to 1 :1 , preferably 2.5:1 to 1 :0.7 with alkylene oxide being selected from ethylene oxide and propylene oxide, thereby forming an inter mediate,

(b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate,

(y) reacting the polycondensate from step (b) with at least one C2-C4-alkylene oxide in one or more steps.

Steps (a), (b) and (y) are described in more detail below.

In step (a), a diamine according to general formula H2-N-Z-NH2 is reacted with an alkylene ox ide. The variable Z has been defined above. For the purpose of the present invention, mixtures of isomeric diamines are considered “a diamine”. For example, diamino-methylcyclohexane is usually generated as a mixture of various isomers

Alkylene oxides reacted in step (a) are selected from ethylene oxide („EO“), propylene oxide (“PO”), and mixtures of the foregoing. Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide. In step (a), the molar ratio alkylene oxide : diamine is in the range of from 4:1 to 1 :1 , preferably 2.5:1 to 1 :0.7.

Step (a) may be performed with or without a solvent. In embodiments wherein diamine accord ing to general formula H₂-N-Z-NH₂ is liquid at reaction temperature it is preferred to use said diamine in bulk. In embodiments wherein diamine according to general formula H₂-N-Z-NH₂ is solid at reaction temperature it is preferred to use a solvent. Suitable solvents are aprotic sol vents, for example hydrocarbons such as toluene and ethers, e.g. di-n-butyl ether.

In one embodiment of the present invention, step (a) may include dilution of diamine according to general formula H₂-N-Z-NH₂ with water before alkoxylation, for example in a ratio diamine : water of 100 : 1 to 1 :1 , especially from 20 : 1 to 5 :1 by weight.

Preferably, step (a) is carried out in the absence of a catalyst.

In one embodiment of the present invention, step (a) is performed at a reaction temperature from 90 to 150°C, preferably from 100 to 135°C.

In one embodiment of the present invention, step (a) may be carried out at a pressure of up to 15 bar, preferably up to 10 bar, for example 1 to 8 bar. Preferred vessels for carrying out step (a) are autoclaves and tubular reactors.

In one embodiment of the present invention, step (a) has a duration in the range of from 30 minutes to 10 hours, preferably 1 hour to 7 hours. Step (a) may be carried out under an inert gas atmosphere, for example nitrogen or a noble gas. In another embodiment, step (a) is carried out under an atmosphere of alkylene oxide. Inert gas atmosphere is preferred. From step (a), an intermediate is formed. It is possible to work up the intermediate, for example by removal of unreacted alkylene oxide and of water, if present, or to use the intermediate from step (a) without further work-up. Said removal of unreacted al kylene oxide and of water, if present, may be performed by evaporation at a pressure in the range of from 500 mbar to 0 mbar, preferred: 100 mbar to 20 mbar and at a temperature in the range of from 20 to 120 °C, preferred are 60 to 100 °C. The intermediate from step (a) is usually a mixture of compounds, a main component being H-AO-NH-Z-NH-AO-H, with AO being CH2CH2-O or CH₂CH(CH₃)-0, and the degree of alkoxylation is usually an average number.

In step (b), the intermediate from step (a) is subjected to polycondensation under catalysis of at least one acidic catalyst.

Suitable acidic catalysts for step (b) are selected from organic sulfonic acids such as para- toluene sulfonic acid, sulfuric acid and phosphorus-bearing acids, preferred are H3PO3, H3PO4, and hypophosphorous acid (H3PO2), even more preferred are H3PO4 and H3PO2. Lewis acids such as, but not limited to AICI3, FeC , diethyl tin dilaurate, and Ti(0-ferf.butyl)4 may serve as catalyst as well.

The acidic catalyst can be applied in bulk or as aqueous solution.

In one embodiment of the present invention, the catalyst is added generally in an amount of 0.001 to 10 mole-%, preferably of 0.005 to 7, more preferably 0.01 to 5 mol-%, based on the amount of intermediate from step (a).

Step (b) may be carried out by using a solvent. Examples of solvents that can be used to per form the inventive process are aromatic and/or (cyclo)aliphatic hydrocarbons and their mixtures, and halogenated hydrocarbons. Preference is given monoalkylated or polyalkylated benzenes and naphthalenes and mixtures thereof.

Preferred aromatic hydrocarbon mixtures are those predominantly comprising aromatic C to C_M hydrocarbons and possibly encompassing a boiling range from 110 to 300 °C, particular preference being given to toluene, 0-, m- or p-xylene, trimethylbenzene isomers, tetra- methylbenzene isomers, ethylbenzene, cumene, tetrahydronaphthalene, and mixtures compris ing them. Examples thereof are the Solvesso® grades from ExxonMobil Chemical, especially Solvesso® 100 (CAS No. 64742-95-6, predominantly Cg and Cio aromatics, boiling range about 154 to 178 °C), 150 (boiling range about 182 - 207°C), and 200 (CAS No. 64742-94-5), and also the Shellsol® grades from Shell. Hydrocarbon mixtures comprising paraffins, cycloparaf fins, and aromatics are also available commercially under the names Kristalloel (e.g., Kristalloel 30, boiling range about 158 to 198°C or Kristalloel 60: CAS No. 64742-82-1), white spirit (like wise, for example, CAS No. 64742-82-1 ) or solvent naphtha (light: boiling range about 155 to 180 °C, heavy: boiling range about 225 to 300 °C).

Halogenated hydrocarbons are, for example, chlorobenzene and dichlorobenzene or its isomer mixtures. Examples of esters are n-butyl acetate, ethyl acetate, 1 -methoxyprop-2-yl acetate, and 2-methoxyethyl acetate. Examples of ethers are THF, dioxane, and the dimethyl, diethyl or di-n-butyl ethers of ethylene glycol.

Examples of (cyclo)aliphatic hydrocarbons are decalin, alkylated decalin, and isomer mixtures of linear or branched alkanes and/or cycloalkanes.

Preferred solvents are those that form low-boiling azeotropic mixtures with water and thus facili tate removal of water.

Preference is given, though, to not using a solvent for carrying out step (b).

In a preferred embodiment, step (b) is carried out in a way that the temperature during polycon densation does not exceed 240 °C. For example, the polycondensation is carried out at temper atures in the range of from 100 to 230 °C, preferably 150 to 210 °C. Even more preferably, the temperature during polycondensation does not exceed 210 °C.

In one embodiment of the present invention, step (b) is carried out in a way that the duration of the polycondensation is one to 25 hours, preferably 1 to 15 hours, more preferably 2 to 10 hours.

In one embodiment of the present invention, step (b) can be carried out at a pressure in the range of from 0.5 bar to 20 bar, while normal pressure being preferred. In a preferred embodi ment, the inventive process is being performed at normal pressure. In an alternative embodi ment, step (b) is carried out in vacuo or at a pressure in the range of from 1 mbar to 0.5 bar. Step (b) is preferably followed by removal or blow-off of residual monomers, for example, by distilling them off at normal pressure or at reduced pressure, e. g., in the range of from 0.1 to 0.75 bar. In one embodiment of step (b), water or other volatile products released during the polyconden sation can be removed from the reaction mixture in order to accelerate the reaction, such re moval being accomplished by distillation, for example, and optionally under reduced pressure. The removal of water or of other low molecular mass reaction by-products can also be assisted by passing through the reaction mixture a stream of gas which is substantially inert under the reaction conditions (stripping), such as nitrogen, for example, or a noble gas such as helium, neon or argon, for example.

In one embodiment of the present invention, 0.4 to 1.0 and preferably 0.4 to 0.7 mol H2O moles of water per mole of intermediate from step (a) are removed in step (b).

By performing step (b), a polycondensate is obtained. Said polycondensate is usually a mixture of compounds, e.g., with a different value of the variable n, or with branching or cross-linking.

For example, in embodiments wherein H2N-Z-NH2 is selected from 2,4-diamino- methylcyclohexane and alkylene oxide is ethylene oxide and 0.5 mole of water are removed from the intermediate, a mixture containing the below compounds is made.

An - optional - step of work-up may include the deactivation of catalyst used in step (b).

In step (y), polycondensate from step (b) is reacted with at least one C₂-C₄-alkylene oxide. Ex amples of C₂-C₄-alkylene oxides are ethylene oxide („EO“), propylene oxide (“PO”), butylene oxide (“BuO”), and mixtures of at least two of the foregoing. Preferred are propylene oxide and ethylene oxide, more preferred is ethylene oxide.

Step (y) is preferably carried out in the presence of a catalyst, for example a base or a double metal cyanide. In one embodiment of the present invention, step (g) is carried out in the presence of a base. Suitable bases such as potassium hydroxide, sodium hydroxide, sodium or potassium alkoxides such as potassium methylate (KOCH₃), potassium tert-butoxide, sodium ethoxide and sodium methylate (NaOCH₃), preferably from potassium hydroxide and sodium hydroxide. Further ex amples of catalysts are alkali metal hydrides and alkaline earth metal hydrides such as sodium hydride and calcium hydride, and alkali metal carbonates such as sodium carbonate and potas sium carbonate. Preference is given to the alkali metal hydroxides, preference being given to potassium hydroxide and sodium hydroxide, and to alkali metal alkoxides, particular preference being given to potassium t-butoxide in t-butanol, sodium n-hexanolate in n-hexanol, and to so dium methanolate in n-nonanol. Typical use amounts for the base are from 0.05 to 10% by weight, in particular from 0.5 to 2% by weight, based on the total amount of polycondensate from step (b) and C2-C4-alkylene oxide.

In one embodiment of the present invention, step (g) is carried out in the presence of a double metal cyanide. Double-metal cyanides, hereinafter also referred to as double metal cyanide compounds or DMC compounds, usually comprise at least two different metals, at least one of them being selected from transition metals and the other one being selected from transition metals and alkali earth metals, and furthermore cyanide counterions. Particularly suitable cata lysts for the alkoxylation are double-metal cyanide compounds which contain zinc, cobalt or iron or two thereof. Berlin blue, for example, is particularly suitable.

Preference is given to using crystalline DMC compounds. In a preferred embodiment, a crystal line DMC compound of the Zn-Co type which comprises zinc acetate as further metal salt com ponent is used as catalyst. Such compounds crystallize in monoclinic structure and have a platelet-like habit.

In one embodiment of the present invention, the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from hexacyano cobaltates.

In one embodiment of the present invention, the inventive synthesis is carried out in the pres ence of at least one double-metal cyanide selected from compounds according to general for mula (VIII)

M¹_ri[M²(CN)_r2(A)_r3]_r4-r⁶ M¹_r7X²_mi r⁸(H₂0) r⁵L- kP (VIII), wherein M¹ is at least one metal ion chosen from the group consisting of Zn²⁺, Fe²⁺, Fe³⁺, Co³⁺, Ni²⁺,

Mn²⁺, Co²⁺, Sn²⁺, Pb²⁺, Mo⁴⁺, Mo⁶⁺, Al³⁺, V⁴⁺, V⁵⁺, Sr²⁺, W⁴⁺, W⁶⁺, Cr²⁺, Cr³⁺, Cd²⁺, Hg²⁺, Pd²⁺, Pt²⁺, V²⁺, Mg²⁺, Ca²⁺, Ba²⁺, Cu²⁺, La³⁺, Ce³⁺, Ce⁴⁺, Eu³⁺, Ti³⁺, Ti⁴⁺, Ag⁺, Rh²⁺, Rh³⁺, Ru²⁺, Ru³⁺,

M² is at least one metal ion chosen from the group consisting of Fe²⁺, Fe³⁺, Co²⁺, Co³⁺, Mn²⁺,

Mn³⁺, V⁴⁺, V⁵⁺, Cr²⁺, Cr³⁺, Rh³⁺, Ru²⁺, lr³⁺, and in a way that M¹ and M² are not identical,

A and X², independently of one another, are anions selected from the group consisting of halide, hydroxide, sulfate, carbonate, cyanide, thiocyanate, isocyanate, cyanate, carboxylate, oxalate, nitrate, nitrosyl, hydrogensulfate, phosphate, dihydrogenphosphate, hydrogenphosphate or hy- drogencarbonate,

L is a ligand chosen from the group consisting of alcohols, aldehydes, ketones, ethers, polyeth ers, esters, polyesters, polycarbonate, ureas, amides, primary, secondary and tertiary amines, ligands with pyridine nitrogen, nitriles, sulfides, phosphides, phosphites, phosphanes, phospho- nates and phosphates, k is greater than or equal to zero, and up to 6. The variable k can be a whole number or a frac tion.

P is an organic additive, selected for example from polyethers, polyesters, polycarbonates, poly- alkylene glycol sorbitan esters, polyalkylene glycol glycidyl ethers, polyacrylamides, poly(acrylamide-co-acrylic acid), polyacrylic acids, poly(acrylamide-co-maleic acid), polyacrylo nitriles, polyalkyl acrylates, polyalkyl methacrylates, polyvinyl methyl ethers, polyvinyl ethyl ethers, polyvinyl acetates, polyvinyl alcohol, poly-N-vinylpyrrolidone, poly(N-vinylpyrrolidone-co- acrylic acid), polyvinyl methyl ketone, poly(4-vinylphenol), poly(acrylic acid-co-styrene), oxazo- line polymer, maleic acid and maleic anhydride copolymers, hydroxyethylcellulose, polyace tates, ionic surface-active and interface-active compounds, bile acid or salts thereof, esters or amides, carboxylic esters of polyhydric alcohols and glycosides. r1 , r2, r3, r4, r⁷ and ml are chosen such that the electroneutrality of the compound (I) is en sured, where each f and r³ may be 0, r⁵ is the number of ligand molecules, for example a fraction or an integer greater than zero, or zero, r6 and r6, independently of one another, are fractions or integers greater than zero, or zero.

In one embodiment, the upper limits of r⁵, r⁶, and r⁸ are each 6.

Double-metal cyanide compounds can be used as powder, paste or suspension or be moulded to give a moulding, be introduced into mouldings, foams or the like or be applied to mouldings, foams or the like.

Preferably, the DMC catalyst used for step (y), based on polycondensate obtained in step (b), is from 5 to 2000 ppm (i.e. mg of catalyst per kg of product), preferably less than 1000 ppm, in particular less than 500 ppm, particularly preferably less than 100 ppm, for example less than 50 ppm or 35 ppm, particularly preferably less than 25 ppm; ppm referring to mass-ppm (parts per million) of polycondensate obtained in step (b).

Step (y) may be carried out in bulk, embodiment (i), or in an organic solvent, embodiment (ii). In embodiment (i), water can be removed from the polycondensate obtained in step (b). Such wa ter removal can be done by heating to a temperature in the range of from 80 to 150°C under a reduced pressure in the range of from 0.01 to 0.5 bar and distilling off the water.

In one embodiment of the present invention, step (y) is carried out at a reaction temperature in the range of from 70 to 200°C and preferably from 100 to 180°C.

In one embodiment of the present invention, step (y) is carried out once per synthesis of in ventive polymer (A). In an alternative embodiment, step (y) is carried out several time, for ex ample up to four times per synthesis of an inventive polymer (A), for example with the same or preferably with different C2-C4-alkylene oxides. It is, for example, possible to subject a polycon densate obtained in step (b) to a first alkoxylation (y1) with ethylene oxide and to subject the product from step (y1) to a second alkoxylation (y2), for example with propylene oxide.

In one embodiment of the present invention, step (y) is carried out at a pressure of up to 10 bar and in particular up to 8 bar, for example 1 to 8 bar.

In one embodiment of the present invention, the reaction time of step (y) is generally in the range of from 0.5 to 12 hours. Examples of suitable organic solvents for embodiment (ii) of step (g) are nonpolar and polar aprotic organic solvents. Examples of particularly suitable nonpolar aprotic solvents include ali phatic and aromatic hydrocarbons such as hexane, cyclohexane, toluene and xylene. Examples of particularly suitable polar aprotic solvents are ethers, in particular cyclic ethers such as tetra- hydrofuran and 1 ,4-dioxane, furthermore N,N-dialkylamides such as dimethylformamide and dimethylacetamide, and N-alkyllactams such as N-methylpyrrolidone. It is as well possible to use mixtures of at least two of the above organic solvents. Preferred organic solvents are xy lene and toluene.

In embodiment (ii), the solution obtained in the first step, before or after addition of catalyst and solvent, is dewatered before being subjected to alkylene oxide, said water removal advanta geously being done by removing the water at a temperature in the range of from 120 to 180°C, preferably supported by a stream of nitrogen. The subsequent reaction with the alkylene oxide may be effected as in embodiment (i). In embodiment (i), alkoxylated polyalkylenimines accord ing to the invention is obtained directly in bulk and may be dissolved in water, if desired. In em bodiment (ii), for work-up organic solvent is typically replaced by water. Alkoxylated polyalkylen imines (B) according to the invention may alternatively be isolated in bulk.

An - optional - step of work-up may include the deactivation of catalyst used in step (g), in the case of basic catalysts by neutralization.

The inventive process does not require bleaching steps or reductive removal of impurities.

The present invention is further illustrated by working examples.

General remarks: percentages refer to % by weight unless expressly stated otherwise. GPC was carried out with THF as mobile phase, with linear PMMA as internal standard Hydroxyl values (OH values) were determined according to 53240 (2013).

Amine values were determined according to ASTM D2074-07.

The Hazen colour number was determined according to DIN ISO 6271 , ASTM D 1209, with spectrophotometric detection. (2° norm observer, normal light, layer thickness 11 mm, against distilled water). I. Synthesis of inventive polymers

1.1 Synthesis of inventive polymer (A.1)

Step (a.1)

A 2-L steel autoclave was charged with 256 g methylcyclohexyldiamine (MCDA) as 4:1 mixture of 2,4-diamines and 2,6-diamines:

and 43 g water and then heated to 100 °C. Then, 30 g of ethylene oxide were dosed into the autoclave. The start of an exothermic reaction was observed. Subsequently, 146 g of ethylene oxide were dosed into the autoclave within 4 hours. The system was kept at 100 °C for further 6 hours. After hat, the mixture is removed from the autoclave and residual EO and water were stripped under reduced pressure (20 mbar) at 80 °C for two hours. 430 g of intermediate were obtained as a yellow viscous liquid.

Analytics:

OH value: 939 mg KOH/g

Amine value: total amines: 469 mg KOH/g, primary amines: 61 mg KOH /g, secondary amines: 259 mg KOH/g, tertiary amines: 149 mg KOH/g

Step (b.1): polycondensation:

A 500 ml. four-neck flask equipped with stirrer, distillation bridge, N₂ inlet, and internal ther mometer was charged with 315 g of the intermediate from step (a.1) and 1.6 g of a 50% aque ous solution of hypophosphorous acid. The resulting reaction mixture was heated to 200 °C and then stirred at 200 °C under nitrogen for 2 hours while the distillate was collected. Then the temperature was reduced to 80 °C and the resulting polycondensate was collected as a viscous liquid. OH value: 609 mg KOH/g

GPC: M_n: 960 g/mol, M_w: 2160 (g/mol)

Step (g1.1): ethoxylation

A 2-liter steel autoclave was charged with 92 g of polycondensate from step (b.1) and 3.9 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under re duced pressure. Then the residue was heated to 120 °C and 30 g of ethylene oxide were added within 10 minutes. After start of the exothermic reaction, 851 g of ethylene oxide were added within 12 hours. The resultant reaction mixture was maintained at 120 °C for 6 hours and then cooled to 80 °C. The autoclave was vented and discharged. Residual EO was stripped from the residue under reduced pressure at 80 °C. An amount of 987 g of inventive polymer (A.1) was obtained.

Analytics:

OH value: 76 mg KOH/g Amine value: 44 mg KOH/g

1.2 Synthesis of inventive polymer (A.2)

Step (g2.2): propoxylation

A 2-liter steel autoclave was charged with 292 g of inventive polymer (A.1) and 2.3 g of aqueous KOH (48%) and heated to 100 °C. Then, the water was removed at 100 °C under reduced pres sure. Then the residue was heated to 130 °C and 50 g of propylene oxide were added within 10 minutes. After start of the exothermic reaction, 229 g of propylene oxide were added within 6 hours. The resultant reaction mixture was maintained at 130 °C for 6 hours and then cooled to 100 °C. The autoclave was vented and discharged. Residual PO was stripped under reduced pressure at 80 °C. An amount of 575 g of inventive polymer (A.2) as a brown solid material were obtained.

Analytics:

OH value: 47 mg KOH/g Amine value: 24 mg KOH/g II. Washing performance

All tests were carried out with inventive polymer (A.2).

Lipase (B.1): Lipex® 100 L, a lipase commercially available from Novozymes Quantities of the respective enzyme are tel quel.

The primary wash performance of the inventive polymer (A.2) was tested in the washing ma chine preparing wash solutions using water of 14°dH hardness (2.5 mmol/L; Ca:Mg:HC034:1 :8) containing 3.0-4.0 g/L of the liquid test detergent L.1 , see composition in Table 1 , and 0.7-1.0% of inventive polymer (A.2) and/or in combination with 0.1% by weight (B.1) and 0.5% by weight (C.1).

Table 1 . L.1 Ingredients of base mixture for a liquid detergent formulation

For the performance test in the washing machine (Miele SOFTTRONIC W 1935 WTL, 30°C, short program, 1200 rpm, 3.5 kg ballast load), four multi-stain monitors (MS1 , MS2) were washed together with two SBL-2004 sheets (wfk Testgewebe GmbFI, DE; corresponding to 32 grams of ballast soil) as additional soil ballast. The multi-stain monitors MS1 and MS2 (Table 2) contain respectively 8 and 4, standardized soiled fabrics, of respectively 5.0 x 5.0 cm and 4.5x4.5 cm size, all of them stitched on two sides to a polyester carrier. Table 2. Multi-stain monitors for the washing machine tests MS1 :

CFT C-S-10: butterfat with colorant on cotton CFT C-S-62: lard, colored on cotton CFT C-S-78: soybean oil with pigment on cotton EMPA 112: cocoa on cotton EMPA 141/1 : lipstick on cotton

EMPA 125: soiling on cotton fabric, sensitive to surfactants as well as to lipases wfk20D: pigment and sebum-type fat on polyester/cotton mixed fabric CFT C-S-70: chocolate/mousse cream on cotton

MS2:

CFT C-S-10: butterfat with colorant on cotton CFT C-S-62: lard, colored on cotton CFT C-S-61 : beef fat, colored on cotton

CFT PC-S-04: Saturated with colored olive oil on Polyester/Cotton (65/35)

The total level of cleaning was evaluated using color measurements. Reflectance values of the stains on the monitors were measured using a sphere reflectance spectrometer (SF 500 type from Datacolor, USA, wavelength range 360-700 nm, optical geometry d/8°) with a UV cutoff filter at 460 nm. In this case, with the aid of the CIE-Lab color space classification, the bright ness L^*, the value a^* on the red - green color axis and the b^* value on the yellow - blue color axis, were measured before and after washing and averaged for the respective stains of the monitor. The change of the color value (Delta E, DE) value, defined and calculated automatical-

ly by the evaluation color tools on the following formula is a measure of the achieved cleaning effect. All experiments were repeated three times to fur nish an average number.

Higher Delta E values show better cleaning. For each stain, a difference of 1 unit can be detect ed visually by a skilled person. A non-expert can visually detect 2 units easily. The DE values of the formulations for the 8 and 4 stains of correspondingly MS1 and MS2 and for selected single stains are shown in Table 3. In the tests, an additional cleaning performance benefit can be seen with the inventive polymer, also in combination with lipase (B.1).

Table 3. Results of washing machine test fabric monitors

In an additional experiment. The respective formulations were stored for 28 days at each 30 and 37°C, then, the washing experiments were repeated. No significant deterioration of the activities of the respective enzymes was observed. Lipase activity was determined by employing para-nitrophenol-valerate (2.4 mM pNP-C5 in 100 mM Tris pH 8.0, 0.01% Triton X100) as a substrate. The absorption at 405 nm was measured at 20°C every 30 seconds over 5 minutes. The slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase. Protease activity was determined by employing Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc- AAPF-pNA, short AAPF) as substrate. pNA is cleaved from the substrate molecule by proteolyt ic cleavage, resulting in release of yellow color of free pNA which was determined by measuring OD405. Measurements were performed at 20°C.

Claims

Patent claims

1. Composition comprising

(A) at least one polymer comprising

(a) a core that bears one to 3 moieties of the general formula (I)

wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non- substituted or substituted with one or more 0-Ci-C₄-alkyl groups and wherein C3- Ci2-cycloalkylene may bear one to three methyl groups,

X¹ is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4,

(b) polyalkylene oxide chains.

2. Composition according to claim 1 wherein all Z are selected from cyclohexylene and cy- clopentylene, each non-substituted or substituted with one to 2 methyl or methoxy groups.

3. Composition according to claim 1 or 2 wherein said composition additionally comprises (B) at least one lipase.

4. Composition according to claim 3 wherein said composition comprises a lipase (B) that is selected from selected from triacylglycerol lipases (EC 3.1.1.3).

5. Composition according to any of the preceding claims wherein said composition compris es

(C) at least one anionic surfactant.

6. Composition according to any of the preceding claims wherein such composition is gel- type or liquid at ambient temperature.

7. Composition according to any of the preceding claims wherein said polymer (A) has an average molecular weight M_w in the range of from 1 ,000 to 80,000 g/mol.

8. Composition according to any of the preceding claims wherein Z is selected from combi nations of

9. Use of a composition according to any of the preceding claims for laundry care.

10. Polymer comprising

(a) a core that bears one to 3 moieties of the general formula (I)

wherein Z are different or the same and selected from C2-Ci2-alkylene and C3-C12- cycloalkylene wherein C2-Ci2-alkylene and C3-Ci2-cycloalkylene may be non- substituted or substituted with one or more OCi-C4-alkyl groups and wherein C3-C12- cycloalkylene may be non-substituted or bear one to three methyl groups,

X¹ is selected from hydrogen and methyl and ethyl and combinations of at least two of the foregoing, n is in the range of from 1 to 4,

(b) polyalkylene oxide chains.

11 . Polymer according to claim 10 having an average molecular weight M_w in the range of from 1 ,000 to 80,000 g/mol.

12. Polymer according to claim 10 or 11 wherein all Z are selected from cyclohexylene and cyclopentylene, each non-substituted or substituted with one to 2 methyl or methoxy groups.

13. Polymer according to any of claims 10 to 12 wherein Z is selected from combinations of

14. Process for making polymers according to any of claims 10 to 13 comprising the steps of (a) reacting a diamine according to general formula H₂-N-Z-NH₂ with alkylene oxide in a molar ratio alkylene oxide : diamine of from 4:1 to 1 :1 with alkylene oxide being se lected from ethylene oxide and propylene oxide, thereby forming an intermediate,

(b) subjecting the intermediate from step (a) to polycondensation under catalysis of at least one acidic catalyst, thereby obtaining a polycondensate,

(y) reacting the polycondensate from step (b) with at least one C₂-C4-alkylene oxide in one or more steps.

15. Method of improving the cleaning performance of a liquid detergent composition, by add ing a polymer (A) according to claims 10 to 13 to a detergent composition preferably com prising at least one lipase (B) and/or at least one protease (D).