Patent Application
20240400945
The present invention is directed towards a composition comprising
Furthermore, the present invention is directed to polymers (A) useful for such compositions, and to a process for making such polymers (A).
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 detergents 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.
In addition, greying of laundry is still a significant problem. The greying is assigned to redeposition of soil during washing. In order to reduce redeposition of soil, specific native or modified polysaccharides such as polysaccharides treated with gaseous or liquid SO2 have been developed. Numerous ingredients have been suggested with various structures, see, e.g., WO 2015/091160, EP 3 266 858 A1 and EP 3 226 858 A1, but still leave room for improvement, and the anti-greying performance of such compounds is still not sufficient. Therefore, there is a continuous need for improved anti-greying agents which can be used in a laundry process. In particular, it is desirable to provide an anti-greying agent which reduces greying of a washed fabric.
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 requirements, 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 contain at least on polymer (A) that comprises several building blocks:
Said building blocks will be described in more detail below.
Backbone (a) bears one forty β-aminoalcohol groups or β-amino-(alkylenoxide) groups.
The term β-aminoalcohol groups refers to —N—CH(Ra)—CH2—O-groups with Ra being selected from methyl and especially hydrogen. Specific examples are N—CH2CH2OH-groups, N—(CH2CH2O)2H-groups, N—CH2CH(CH3)OH-groups and N—(CH2CH(CH3)O)2H-groups, and combinations of at least two of the aforementioned. In polymer (A) and after esterification, the hydrogen on the OH group is replaced by a carboxyl group.
The term β-amino-(alkylenoxide) groups refers to —N(AO)x-groups and to —N[(AO)x]2-groups, with AO being a variable selected from ethylene oxide (EO) and propylene oxide (PO) and combinations, and x being in the range of from 2 to 10. In embodiments wherein AO refers to combinations of EO and PO, they are usually arranged block-wise rather than statistically. Preferably, at least half of all AO is EO. More preferably, all AO are EO.
In one embodiment of the present invention, backbone (a) is selected from alkoxylated triethanolamine, alkoxylated N,N′-bis-(3-aminopropyl)-ethylenediamine, alkoxylated polyethylenimine, alkoxylated N,N-bis(2-aminoethyl)-1,2-ethanediamine 1,1-bis(2-hydroxyethyl)-ethanolamine and alkoxylated compounds of methyldiaminocyclohexane (“MCDA”), see below formulae.
MCDA is usually present as mixture of isomers, methyl-2,4-diaminocyclohexane and methyl-2,6-diaminocyclohexane in a ratio of about 4:1.
In alkoxylated triethanolamine, alkoxylated N,N′-bis-(3-aminopropyl)-ethylenediamine, alkoxylated polyethylenimine, alkoxylated N,N-bis(2-aminoethyl)-1,2-ethanediamine 1,1-bis(2-hydroxyethyl)-ethanolamine and alkoxylated compounds of methyldiaminocyclohexane (“MCDA”), alkoxylation may, for example, be selected from propoxylation, butoxylation and ethoxylation, preference being given to ethoxylation and combinations of ethoxylation and propoxylation, even more preferred is ethoxylation, thus, without either of propoxylation and butoxylation. In embodiments wherein combinations of ethoxylation and propoxylations are provided, the ethylene oxide units and propylene oxide units are arranged blockwise rather than randomly.
The term “polyethylenimine” in the context of the present invention does not only refer to polyethylenimine homopolymers but also to polyalkylenimines containing NH—CH2—CH2—NH structural elements together with other alkylene diamine structural elements, for example NH—CH2—CH2—CH2—NH structural elements, NH—CH2—CH(CH3)—NH structural elements, NH—(CH2)4—NH structural elements, NH—(CH2)6—NH structural elements or (NH—(CH2)8—NH structural elements but the NH—CH2—CH2—NH structural elements being in the majority with respect to the molar share. Preferred polyethylenimines contain NH—CH2—CH2—NH structural elements being in the majority with respect to the molar share, for example amounting to 60 mol-% or more, more preferably amounting to at least 70 mol-%, referring to all alkylenimine structural elements. In a special embodiment, the term polyethylenimine refers to those polyalkylenimines that bear only one or zero alkylenimine structural element per molecule that is different from NH—CH2—CH2—NH.
In one embodiment of the present invention, the average molecular weight Mw of polyethylenimines before alkoxylation is in the range of from 500 to 100,000 g/mol, preferably up to 50,000 g/mol and more preferably from 800 up to 25,000 g/mol. The average molecular weight Mw of polyethylenimines may be determined by gel permeation chromatography (GPC), with 1.5% by weight aqueous formic acid as eluent and cross-linked poly-hydroxyethyl methacrylate as stationary phase.
In one embodiment of the present invention, polyalkylenimines before alkoxylation display a polydispersity Q=Mw/Mn of at least 3.5, preferably in the range of from 3.5 to 10, more preferably in the range of from 4 to 9 and even more preferably from 4.0 to 5.5. In other embodiments of the present invention, polyalkylenimines display a polydispersity Q=Mw/Mn of 3.4 at most, for examples in the range of from 1.1 to 3.0, more preferably in the range of from 1.3 to 2.5 and even more preferably from 1.5 to 2.0.
Polyethylenimines before alkoxylation may have a linear or branched structure. Branches may be alkylenamino groups such as, but not limited to —CH2—CH2—NH2 groups or (CH2)3—NH2-groups. Longer branches may be, for examples, —(CH2)3—N(CH2CH2CH2NH2)2 or —(CH2)2—N(CH2CH2NH2)2 groups. Highly branched polyethylenimines are, e.g., polyethylenimine dendrimers or related molecules with a degree of branching in the range from 0.25 to 0.95, preferably in the range from 0.30 to 0.80 and particularly preferably at least 0.5. The degree of branching can be determined for example by 13C-NMR or 15N-NMR spectroscopy, preferably in D2O, and is defined as follows:
with D (dendritic) corresponding to the fraction of tertiary amino groups, L (linear) corresponding to the fraction of secondary amino groups and T (terminal) corresponding to the fraction of primary amino groups.
Within the context of the present invention, branched polyethylenimines are polyethylenimines with DB in the range from 0.25 to 0.95, particularly preferably in the range from 0.30 to 0.90% and very particularly preferably at least 0.5. Such branched polyethylenimines may be made by polymerization of aziridine.
In the context of the present invention, CH3-groups are not being considered as branches.
Preferred polyethylenimines are those that exhibit little or no branching, thus predominantly linear or linear polyethylenimine backbones. In another embodiment, preferred polyethylenimines are branched polyethylenimines.
If as block (a) a backbone based on a di-ethoxylated MCDA is provided, usually a mixture of compounds is provided:
and the respective isomers based on the 2,6-diamine.
Polymer (A) may contain one or more backbones (a) that have different or preferably the same structure and that may be connected to each other through a block (b) or (c).
In one embodiment of the present invention, polymer (A) has 1 to 15 backbones (a) per molecule, preferably 3 to 7.
In polymer (A), some of the hydroxyl groups of β-aminoalcohol groups or β-amino-(alkylenoxide) groups are esterified with a mono- or diacid of a polyalkylene oxide of which at least 50 mol-% of the alkylene oxide groups are ethylene oxide groups, block (b).
In block (b), the alkylene oxide groups that are not ethylene oxide are preferably selected from propylene oxide, especially 1,2-propylene oxide (“PO”), and butylene oxide, especially 1,2-butylene oxide (“BuO”). Preferred alkylene oxide other than ethylene oxide is PO.
Preferred mono- and diacids of polyalkylene oxide and preferred monomethyl ethers of a monoacid of a polyalkylene oxide are compounds according to general formula (II)
X1—(AO′)y—CH2—COOH (II)
wherein
In a preferred embodiment of the present invention, diacids according to formula (II) contain the respective monoacid as an impurity, for example up to 15 mol-%, preferably 1 to 12 mol-%.
In a preferred embodiment of the present invention, mono-acids according to formula (II) contain both the respective diacid and the non-oxidized diol as impurities, for example up to 50 mol-% in total.
In polymer (A), some of the hydroxyl groups of the β-aminoalcohol groups or β-amino-(alkylenoxide) groups of backbone (a) may be esterified with (c) aliphatic C4-C10-di- or tricarboxylic acid.
Examples of suitable aliphatic C4-C10-dicarboxylic acids are succinic acid, glutaric acid, adipic acid, suberic acid, pimelic acid, azelaic acid and sebacic acid. Aliphatic C4-C10-dicarboxylic acids may bear functional groups other than carboxyl groups, for example alcohol groups. Examples of suitable aliphatic C4-C10-dicarboxylic acids that bear functional groups other than carboxyl groups are tartaric acid, malic acid
Of the aliphatic C4-C10-tricarboxylic acids, C6-C8-tricarboxylic acids are preferred. Examples of suitable aliphatic C4-C10-tricarboyxclic acids are propane-1,2,3-tricarboxylic acid. Aliphatic C4-C10-tricarboxylic acids may bear functional groups other than carboxyl groups, for example alcohol groups. Examples of suitable aliphatic C4-C10-tricarboxylic acids that bear functional groups other than carboxyl groups are citric acid and isocitric acid and oxalosuccinic acid. Citric acid is particularly preferred as C6-C8-tricarboxylic acid.
In one embodiment of the present invention, some of the hydroxyl groups are esterified with only one aliphatic C4-C10-dicarboxylic acid. In other embodiments, some of the hydroxyl groups are esterified with a mixture of aliphatic C4-C10-dicarboxylic acid and aliphatic C4-C10-tricarboxylic acid, for example with a combination of adipic acid and citric acid or a combination of sebacic acid and citric acid or with a combination of adipic acid with sebacic acid and citric acid.
In a preferred embodiment, at least one block (c) per molecule of polymer (A) is esterified with of the hydroxyl groups of the β-aminoalcohol groups or β-amino-(alkylenoxide) groups of two different backbones (a), for example one to five blocks (c).
In one embodiment of the present invention, the molar ratio of block (b) to block (c) is in the range of from 1:25 to 5:1, for example from 1:10 to 1:5.
In one embodiment of the present invention, all carboxylic groups of block(s) (c) are esterified. It is preferred, though, that some carboxylate groups remain as free acids.
In one embodiment of the present invention, polymer (A) has a molecular weight distribution Mw/Mn in the range of from 1.1 to 6.0.
In one embodiment of the present invention, polymer (A) has an average molecular weight Mw in the range of from 2,500 to 100,000 g/mol, preferably 3,400 to 25,000 g/mol. The average molecular weight may be determined, e.g., by gel permeation chromatography (GPC) in 0.1 M aqueous NaCl solution containing 0.1% by weight trifluoric acid as mobile phase, or in hexafluoroisoropanol (“HFIP”), each time preferably with TSKgel as stationary phase.
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 10 to 2000, preferably 25 to 700 mg KOH/g polymer (A).
Inventive compositions may comprise impurities that stem from the synthesis of polymer (A), for example unreacted mono- or diacid of polyalkylene oxide of which at least 50 mol-% of the alkylene oxide groups are ethylene oxide groups, and polyesters based on monoacid of polyalkylene oxide of which at least 50 mol-% of the alkylene oxide groups are ethylene oxide groups.
In one embodiment of the present invention, inventive compositions comprise at least one enzyme. Enzymes are identified by polypeptide sequences (also called amino acid sequences herein). The polypeptide sequence specifies the three-dimensional structure including the “active 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 Office (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 products. 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 sequences 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 enzyme 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 “Gly180GlyLys” 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 alterations 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 glutamic acid. Alternatively, different alterations or optional substitutions may be indicated in brackets, 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 enzyme. Sequence identity usually is provided as “% sequence identity” or “% identity”. For calculation 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 mathematical 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). Preferably, 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 parameter (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 invention 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 enzyme, wherein the enzyme variant has enzymatic activity.
“Enzymatic activity” means the catalytic effect exerted by an enzyme, which usually is expressed as units per milligram of enzyme (specific activity) which relates to molecules of substrate transformed per minute per molecule of enzyme (molecular activity). Variant enzymes may have enzymatic activity according to the present invention when said enzyme variants exhibit 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
“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 (T. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. insolens as described in WO 96/13580; lipases 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. alcaligenes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381, WO 96/00292), P. cepacia (EP 331376), P. stutzeri (GB 1372034), P. fluorescens, Pseudomonas 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 disclosed 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 palmitate (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 U.S. Pat. No. 5,869,438 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 polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising conservative mutations only, which do not pertain the functional domain of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438. Lipase variants of this embodiment having lipolytic activity 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 U.S. Pat. No. 5,869,438.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising at least the following amino acid substitutions when compared to amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438: T231R 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 U.S. Pat. No. 5,869,438: Q4V, V60S, A150G, L227G, P256K.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising at least the amino acid substitutions T231R, N233R, Q4V, V60S, A150G, L227G, P256K within the polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438 and are at least 95%, at least 96%, or at least 97% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438.
Thermomyces lanuginosa lipase may be selected from variants having lipolytic activity comprising the amino acid substitutions T231R and N233R within amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438 and are at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438.
Thermomyces lanuginosa lipase may be a variant of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438 having lipolytic activity, wherein the variant of amino acids 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438is characterized in containing the amino acid substitutions T231R 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 lipases (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 μmol 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 NaCl in 5 mmol/l Tris-buffer.
In one embodiment of the present invention, inventive compositions comprise
In one embodiment, at least one protease (D) is selected from the group of serine endopeptidases (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 sequence 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 activity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a defined 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 μmol 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, Fusobacterium, Helicobacter, Ilyobacter, 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 coagulans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus thuringiensis protease.
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. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 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 protease 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; subtilisin 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) disclosed 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 application 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 examples comprise especially variants of subtilisin protease derived from SEQ ID NO:22 as described in EP 1921147 (which is the sequence of mature alkaline protease from Bacillus lentus 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 proteolytic activity. In one embodiment, said protease is characterized by having amino acid glutamic acid, or aspartic acid, or asparagine, or glutamine, or alanine, or glycine, or serine at position 101 (according to BPN′ numbering) and has proteolytic activity. In one embodiment, said protease comprises one or more further 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 (205), (h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or 217G), (i) combinations 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 combinations according to (i) together with the amino acid 101E, 101D, 101N, 101Q, 101A, 101G, or 101S (according to BPN′ numbering). In one embodiment, said protease is characterized by comprising the mutation (according to BPN' numbering) R101E, or S3T+V4I+V205I, or R101E and S3T, V4I, and V205I, or S3T+V4I+V199M+V205I+L217D, and having proteolytic activity. A protease having a sequence according to SEQ ID NO: 22 as described in EP 1921147 with 101E may be called Lavergy herein.
In one embodiment, protease according to SEQ ID NO:22 as described in EP 1921147 is characterized by comprising the mutation (according to BPN′ numbering) S3T+V4I+S9R+A15T+V68A+D99S+R101S+A103S+I104V+N218D, and by having proteolytic activity.
Inventive compositions 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 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 according 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 storage. 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
Examples of anionic surfactants (C) are alkali metal and ammonium salts of C8-C18-alkyl sulfates, of C8-C18-fatty alcohol polyether sulfates, of sulfuric acid half-esters of ethoxylated C4-C12-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 C12-C18-alkylsulfonic acids and of C10-C18-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 (III)
R1—O(CH2CH2O)x1—SO3M (III)
wherein
In anionic surfactant (C), x1 may be an average number and therefore n is not necessarily a whole number, while in individual molecules according to formula (III a), x denotes a whole number.
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 ethylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or propylene 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:
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.
Other preferred examples of alkoxylated alcohols are, for example, compounds of the general formula (III b)
in which the variables are defined as follows:
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 a) and (III b) may be block copolymers or random copolymers, preference being given to block copolymers.
Further suitable nonionic surfactants are selected from di- and multiblock copolymers, composed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, especially linear C4-C16-alkyl polyglucosides and branched C8-C14-alkyl polyglycosides such as compounds of general average formula (IV) are likewise suitable.
wherein:
Further examples of non-ionic surfactants are compounds of general formula (V) and (VI)
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 amphoteric surfactants is cocamidopropyl betaine (lauramidopropyl betaine).
Examples of amine oxide surfactants are compounds of the general formula (VII)
wherein R9, R10, and R11 are selected independently from each other from aliphatic, cycloaliphatic or C2-C4-alkylene C10-C20-alkylamido moieties. Preferably, R9 is selected from C8-C20-alkyl or C2-C4-alkylene C10-C20-alkylamido and R10 and R11 are both methyl.
A particularly preferred example is lauryl dimethyl aminoxide, sometimes also called lauramine oxide. A further particularly preferred example is cocamidylpropyl dimethylaminoxide, sometimes 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 percarboxylic 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 ruthenium-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, commercially 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 preservatives prevent alterations of inventive liquid detergent compositions due to attacks from microorganisms. Examples of biocides and preservatives are BTA (1,2,3-benzotriazole), benzalkonium 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 particularly of interest are the following antimicrobial agents and/or preservatives:
The invention thus further pertains to a method of preserving an inventive composition against microbial contamination or growth, which method comprises addition of 2-phenoxyethanol.
The invention thus further pertains to a method of providing an antimicrobial effect on textiles after treatment with an inventive composition containing 4,4′-dichloro 2-hydroxydiphenyl ether (DCPP).
Examples of viscosity modifiers are agar-agar, carragene, tragacanth, gum arabic, alginates, pectins, hydroxyethyl cellulose, hydroxypropyl cellulose, starch, gelatin, locust bean gum, crosslinked poly(meth)acrylates, for example polyacrylic 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 dissolution 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 Mw in the range from 2,000 to 40,000 g/mol. preferably 2,000 to 10,000 g/mol, in particular 3,000 to 8,000 g/mol, each partially or fully neutralized 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—SO3Na, CH2CH(CH2—SO3Na)2, and CH2CH(CH2SO2Na)CH2—SO3Na.
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.
A further aspect of the present invention is therefore the use of inventive compositions for laundry care. Laundry care in this context includes laundry cleaning.
In another aspect, inventive compositions are useful for hard surface cleaning. A further aspect of the present invention is therefore the use of inventive compositions for hard surface cleaning.
In the context of the present invention, the term “composition for hard surface cleaning” includes cleaners for home care and for industrial or institutional applications. The term “composition for hard surface cleaning” includes compositions for dishwashing, especially hand dishwash and automatic dishwashing and ware-washing, and compositions for hard surface cleaning such as, but not limited to compositions for bathroom cleaning, kitchen cleaning, floor cleaning, descaling of pipes, window cleaning, car cleaning including truck cleaning, furthermore, open plant cleaning, cleaning-in-place, metal cleaning, disinfectant cleaning, farm cleaning, high pressure cleaning, but not laundry detergent compositions. A special embodiment of compositions for hard surface cleaning are automatic dishwashing compositions.
In the context of the present invention, the terms “compositions for hard surface cleaning” and “compositions for hard surface cleaners” are used interchangeably.
In the context of the present invention and unless expressly stated otherwise, percentages in the context of ingredients of laundry detergent compositions are percentages by weight and refer to the total solids content of the respective laundry detergent composition. In the context of the present invention and unless expressly stated otherwise, percentages in the context of ingredients of detergent composition for hard surface cleaners are percentages by weight and refer to the total solids content of the detergent composition for hard surface cleaning.
Inventive compositions when used for automatic dishwashing preferably contain
Examples of sequestrants (E) are alkali metal salts of MGDA (methyl glycine diacetic acid), GLDA (glutamic acid diacetic acid), IDS (iminodisuccinate), EDTA, and polymers with complexing groups like, for example, polyethylenimine in which 20 to 90 mole-% of the N-atoms bear at least one CH2COO− group, and their respective alkali metal salts, especially their sodium salts, for example MGDA-Na3, GLDA-Na4, or IDS-Na4.
Preferred sequestrants are those according to general formula (IX a)
[CH3—CH(COO)—N(CH2—COO)2]M3-x2Hx2 (IX a)
wherein M is selected from ammonium and alkali metal cations, same or different, for example cations of sodium, potassium, and combinations of at least two of the foregoing. Ammonium may be substituted with alkyl but non-substituted ammonium NH4+ is preferred. Preferred examples of alkali metal cations are sodium and potassium and combinations of sodium and potassium, and even more preferred in compound according to general formula (II a) all M are the same and they are all Na;
[OOC—CH2CH2—CH(COO)—N(CH2—COO)2]M4-x3Hx3 (IX b)
wherein M is as defined above, and x3 in formula (IX b) is in the range of from zero to 2.0, preferably to 1.0,
[OOC—CH2—CH(COO)]—N—CH(COO)—CH2—COO]M4-x4Hx4 (IX c)
wherein M is as defined above, and x4 in formula (IX c) is in the range of from zero to 2.0, preferably to 1.0.
In one embodiment of the present invention, said inventive composition contains a combination of at least two of the foregoing, for example a combination of chelating agent according to general formula (IX a) and a chelating agent according to general formula (IX b).
Chelating agents according to the general formulae (IX a) and (IX b) are preferred. Even more preferred are chelating agents according to the general formula (IX a).
In one embodiment of the present invention, compound according to general formula (IX a) is selected from ammonium or alkali metal salt of racemic MGDA and from ammonium and alkali metal salts of mixtures of L- and D-enantiomers according to formula (IX a), said mixture containing predominantly the respective L-isomer with an enantiomeric excess (ee) in the range of from 5 to 99%, preferably 5 to 95%, more preferably from 10 to 75% and even more preferably from 10 to 66%.
In one embodiment of the present invention, 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 the racemic mixture or preferably predominantly the respective L-isomer, for example with an enantiomeric excess (ee) in the range of from 5 to 99%, preferably 15 to 95%.
The enantiomeric excess of compound according to general formula (IX a) may be determined by measuring the polarization (polarimetry) or preferably by chromatography, for example by HPLC with a chiral column, for example with one or more cyclodextrins as immobilized phase or with a ligand exchange (Pirkle-brush) concept chiral stationary phase. Preferred is determination of the ee by HPLC with an immobilized optically active amine such as D-penicillamine in the presence of copper (+II) salt. The enantiomeric excess of compound according to general formula (IX b) salts may be determined by measuring the polarization (polarimetry).
Due to the environmental concerns raised in the context with the use of phosphates, it is preferred that advantageous compositions are free from phosphate. “Free from phosphate” should be understood in the context of the present invention as meaning that the content of phosphate and polyphosphate is in sum in the range of from detection level to 1% by weight, preferably from 10 ppm to 0.2% by weight, determined by gravimetry.
In one embodiment of the present invention, inventive compositions contain in the range of from 0.5 to 50% by weight of sequestrant (E), preferably 1 to 35% by weight, referring to the total solids content.
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 at ambient temperature. In another preferred embodiment of the present invention, inventive compositions are solid at ambient temperature, for example powders or tabs.
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 embodiments where inventive compositions are solid, their pH value may be in the range of from 7.5 to 11, determined after dissolving 1 g/100 ml in distilled water and at ambient temperature. In embodiments where inventive compositions are used for hard surfaces like tiles, for example bathroom tiles, their pH value may even be acidic, for example from 3 to 6.
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) have been described above.
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 polymers (A) provide better, i.e. improved, properties in stain removal under relevant cleaning conditions, when compared to the cleaning performance of a detergent composition lacking polymer (A). In one embodiment, “improved cleaning performance” means that the cleaning performance of a detergent comprising polymer (A) and at least one enzyme, preferably at least one hydrolase (B), especially at least one lipase (B) and/or at least one protease (D), is improved when compared to the cleaning performance of a detergent comprising polymer (A) and no enzyme. In one embodiment, “improved cleaning performance” means that the cleaning performance of a detergent comprising polymer (A) and an enzyme, preferably hydrolase (B), more 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 hydrolase (B), preferably 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 hardness, actually used in laundry machines, automatic dish washers or in manual cleaning processes.
Inventive polymers (A) are excellently suited as or for the manufacture of inventive compositions. Inventive polymers (A) show biodegradability.
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 (α), (β), and, optionally, step (γ):
Steps (α), (β) and the optional step (γ) are described in more detail below. Steps (β) and (γ) may be performed simultaneously or subsequently in any order, preferred is subsequently in the order of performing step (γ)—if present-before step (β).
In step (α), a backbone molecule is provided that corresponds to backbone (a). Such backbone molecule is partially or fully alkoxylated with one to 10 C2-C4-alkoxy groups per NH unit, preferably fully alkoxylated with one to 10 C2-C4-alkoxy groups per NH unit of underlying amines such as polyethylenimine, N,N-bis(2-aminoethyl)-1,2-ethanediamine 1,1-bis(2-hydroxyethyl)-ethanolamine and MCDA.
In one embodiment of the present invention, such partial or full alkoxylation is performed with ethylene oxide or with combinations of ethylene oxide and propylene oxide or butylene oxide wherein in such combinations at least 50 mol-% ethylene oxide.
In step (β), backbone (a) or an ester resulting from step (γ), see below, is reacted with a mono- or diacid or preferably with a mixture of mono- and diacid of polyalkylene oxide of which at least 50 mole-% of the alkylene oxide units are ethylene oxide, or or with the monomethyl ether of a monoacid of a polyalkylene oxide of which at least 50 mol-% of the alkylene oxide groups are ethylene oxide groups. Preferred are those according to formula (II), vide supra.
Mono- and diacids of polyalkylene oxide of which at least 50 mole-% of the alkylene oxide units are ethylene oxide may be made by oxidation of one or both hydroxyl groups of the respective polyalkylene glycols with Pt on charcoal as catalyst.
The respective monomethyl ethers may be synthesized by oxidation of the respective monomethyl-capped polyalkylene glycol, for example with Pt on charcoal as catalyst.
In one embodiment of the present invention, step (β) is performed in the presence of a catalyst.
Step (B) may be carried out at temperatures in the range of from 20 to 180° C. In embodiments wherein ester(s), in particular C1-C2-alkyl esters are used, such as adipic acid diethyl ester, diethyl succinate, adipic acid dimethyl ester, dimethyl succinate, sebacic acid dimethyl ester, sebacic acid diethyl ester, diethyl, triethyl citrate or the like, temperatures in the range of from 25 to 150° C. are preferred. In embodiments wherein anhydride(s) are applied, for example succinic anhydride, 25 to 150° C. are preferred. In embodiments wherein the respective free acid(s) are used, temperatures in the range of from 100 to 180° C. are preferred. Especially in embodiments wherein temperatures of 100° C. or more are applied it is preferred to ramp up the temperature.
Step (β) may be performed at any pressure, for example from 10 mbar to 10 bar. Preferred are ambient pressure and pressures below, for example 10 to 500 mbar.
In the course of step (β), water is formed. It is preferred to remove such water, for example by distilling them off. Suitable tools are Dean-Stark apparatuses, distillation bridges, water eliminators, and other apparatuses that may serve for removal of water by distillation.
Step (β) may be performed in the absence or presence of a solvent. Suitable solvents are aromatic solvents like toluene, aliphatic hydrocarbons or cycloaliphatic solvents, for example decane, cyclohexane, n-heptane and the like. It is preferred, though, to perform step (β) in the absence of a solvent, especially when the reaction mixture is liquid at the reaction temperature.
Examples of suitable catalysts are especially acidic catalysts, for example inorganic acids and organic acids.
Acidic inorganic catalysts for the purposes of the present invention include for example sulfuric acid, phosphoric acid, phosphonic acid, hypophosphorous acid H3PO2, aluminum sulfate hydrate, alum, acidic silica gel (pH value 5 to 6) and acidic alumina. Suitable are as well, for example, aluminum compounds of the general formula Al(ORb)3 and titanates of the general formula Ti(ORb)4 as acidic inorganic catalysts, the residues Rb each being identical or different and being chosen independently of one another from
Preferably the residues R5 in Al(OR5)3 and Ti(OR5)4 are each identical and chosen from isopropyl or 2-ethylhexyl.
Preferred acidic organometallic catalysts are chosen for example from dialkyltin oxides (Rb)2SnO with Rb being as defined above. One particularly preferred representative of acidic organometallic catalysts is di-n-butyltin oxide, available commercially in the form of oxo-tin.
Preferred acidic organic catalysts are acidic organic compounds containing, for example, phosphate groups, sulfonic acid groups, sulfate groups or phosphonic acid groups. Particular preference is given to sulfonic acids such as para-toluenesulfonic acid, or methanesulfonic acid for example. Acidic ion exchangers can also be used as acidic organic catalysts, examples being polystyrene resins which contain sulfonic acid groups and have been crosslinked with about 2 mol % of divinylbenzene. Particularly preferred is methanesulfonic acid.
Combinations of two or more of the aforementioned catalysts can also be used. Another possibility is to use those organic or organometallic or else inorganic catalysts which are in the form of discrete molecules, in an immobilized form.
If the use of acidic inorganic, organometallic or organic catalysts is desired, the amount of catalyst used in accordance with the invention is from 0.01 to 10% by weight, preferably from 0.1 to 2% by weight, more preferably 0.2 to 1% by weight, each based on the total amount of the reactants.
In another embodiment of the present invention, step (β) is performed without a catalyst.
In one embodiment of the present invention, step (β) has a duration in the range of from 30 minutes up to 15 hours.
The optional step (γ) includes reacting said backbone (a) with at least one dicarboxylic or tricarboxylic acid, or, in each case, with their respective anhydrides or C1-C4-alkylesters.
In the course of step (γ), water or an alcohol is formed, for example methanol or ethanol. It is preferred to remove such byproducts, for example by distilling them off. Suitable tools are Dean-Stark apparatuses, distillation bridges, water eliminators, and other apparatuses that may serve for removal of water or alcohols by distillation.
With respect to temperature, pressure, set-up, catalyst and duration, the esterification in step (γ) may be performed under the same conditions as the esterification in step (β), mutatis mutandis.
In one embodiment of the present invention, the reaction in step (β) and—if applicable—step (γ) leads to a complete conversion of all carboxylic acid or ester or anhydride groups of the respective dicarboxylic or tricarboxlic acid or with a mixture of the foregoing, or, in each case, with their respective anhydrides or C1-C4-alkylesters. It is observed, though, that in many embodiments the conversion of ester or carboxylic acid groups or anhydride groups is incomplete, which results in the ester still bearing carboxylic acid groups or C1-C4-alkylester groups. The completeness of the reaction may be assessed by determining the acid number, for example according to EN ISO 660:2009).
The inventive process is preferably carried out in a way that the molar ratio of carboxyl groups to hydroxyl groups is in the range of from 0.9:1 to 1.1:1, preferably 0.95:1 to 1.05:1, more preferably 0.98:1.00 to 1.02:1.00, thereby obtaining an ester. In this context, an anhydride group counts as two carboxyl groups.
In one embodiment of the present invention, further groups of, e.g., citric acid or its C1-C4-esters may react, for example the hydroxyl group. However, since the hydroxyl group of citric acid is not very reactive, it preferred that it is not reacted.
The ester resulting from step (γ) may be isolated and purified, for example by removal of solvent, if applicable, or by neutralization of acid. Especially in embodiments of step (γ) in which neither a catalyst nor a solvent was used it is preferred to transfer the resultant ester to step (β) without further purification steps. In addition, a catalyst of step (γ) may also used for step (β).
In embodiments where in step (α), a backbone molecule is provided of which not all amino groups are alkoxylated, in step (β) or (γ) some amide formation is observed as a side reaction.
In embodiments where steps (β) and (γ) are performed simultaneously, both acidic compounds are added to backbone molecule (a) and reacted under conditions as outlined above.
By performing step (β) and, if applicable, step (γ), an inventive polymer (A) is obtained.
The resultant polymer (A) may be used with and without purification and work-up operations. As work-up operations, a deactivation of the catalyst may be performed, if applicable, for example by neutralization. Other work-up operations are bleaching, for example with peroxide such as H2O2. However, it is preferred to not perform bleaching steps.
By-products such as unreacted starting materials or polycondensates of mono-acid of poly-alkylene glycols usually do not have an impact on the performance of inventive polymers (A).
By the inventive process, inventive polymers (A) are obtained.
The present invention is further illustrated by working examples.
Reactions were carried out under nitrogen atmosphere unless expressly noted otherwise.
Percentages refer to % by weight unless expressly stated otherwise.
GPC was carried out with THE as mobile phase, with linear PMMA as internal standard and hexafluoroisopropanol (“HFIP”) as solvent
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).
rpm: revolutions per minute
Synthesis data and analytical data of exemplified inventive polymers (A) are summarized in Table 3. Some exemplified syntheses are disclosed below.
A 3.5-liter steel autoclave was charged with 896 g methylcyclohexyldiamine (MCDA, 7 mol) as 4:1 mixture of 2,4-diamines and 2,6-diamines, and 450 g water and then heated to 100° C. Then, 250 g of ethylene oxide were dosed into the autoclave within 10 minutes. The start of an exothermic reaction was observed. Subsequently, 982 g of ethylene oxide (“EO”) were dosed into the autoclave within 6 hours, total amount of EO: 28 mol. 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. 2.35 kg of backbone molecule (a.4) were obtained as a yellow viscous liquid.
A 3.5-liter steel autoclave was charged with 1.28 kg methylcyclohexyldiamine (MCDA, 10 mol) as 4:1 mixture of 2,4-diamines and 2,6-diamines, and 340 g water and then heated to 100° C. Then, 240 g of propylene oxide were dosed into the autoclave within 10 minutes. The start of an exothermic reaction was observed. Subsequently, 880 g of PO were dosed into the autoclave within 6 hours, total amount of PO: 16 mol. The reaction mixture was kept at 100° C. for further 6 hours. After that, the mixture was removed from the autoclave and residual PO and water were stripped under reduced pressure (20 mbar) at 80° C. for two hours. 2.56 kg of backbone molecule (a.5) were obtained as a yellow viscous liquid.
The protocol of step (α.4) was followed but with addition of 475 g instead of 1.051 kg of PO. An amount of 1.95 kg of backbone (a.6) were obtained as a yellow viscous liquid.
A 250-ml flask equipped with stirrer, Dean-Stark apparatus, nitrogen inlet and inside thermometer was charged with 136 g of backbone (a.6) (0.63 mol), citric acid (8.1 g, 4.22 mmol), sebacic acid (91 g, 0.45 mol). Methanesulfonic acid was added in accordance with Table 3. The reaction mixture was then heated to 160° C. (inside temperature). Water distilled off. Stirring at 160° C. was continued under nitrogen for 4.8 hours. Then, 58 g (b.1) was added and heating and water removal were continued for 1.5 hours. The resultant polymer (A.6.1) was collected as a solid material (276 g).
GPC in HFIP: Mn 4800 g/mol, Mw 21,500 g/mol
Acid number: 165 mg KOH/g
A 250-ml flask equipped with stirrer, Dean-Stark apparatus, nitrogen inlet and inside thermometer was charged with 150 g of backbone molecule (a.6) (0.69 mol) and succinic acid (64.9 g, 0.55 mol). Methanesulfonic acid was added in accordance with Table 3. The reaction mixture was then heated to 160° C. (inside temperature). Water was distilled off. Stirring at 160° C. was continued under nitrogen for 4.8 hours. Then, 63.2 g (b.8) was added and heating and water removal were continued for 1.5 hours. The resultant polymer (A.6.8) was collected as a solid material (358 g).
GPC in HFIP: Mn 3116 g/mol, Mw 17,600 g/mol
Acid number: 116 mg KOH/g
GPC in HFIP: Mn 788 g/mol, Mw 33,000 g/mol
Acid number: 165 mg KOH/g
A 250 ml flask with temperature control, nitrogen inlet, Dean-Stark apparatus, and overhead stirrer was charged with 95.8 g backbone (a.17). Then 227 g (b.8) were added and the resultant mixture was heated to 140° under nitrogen atmosphere and stirred for 8 hours while water was distilled off. Subsequently, the resultant polymer (A. 17.8) was cooled to ambient temperature and obtained as a brownish material, 314 g.
II. Washing performance (
II.1 Laundry cleaning
The primary wash performance of inventive polymers was tested in the washing machine preparing wash solutions using water of 14° dH hardness (2.5 mmol/L; Ca: Mg: HCO3 4:1:8) containing 3.0 g/L of the liquid test detergent L. 1, see composition in Table 4.1 or 4.2, and 2.0% of an inventive polymer (A) according to Table 3.
Anti greying tests were also executed in a launderometer with 1I beakers (LP2 type from SDL Atlas, Inc.). One wash cycle (60 min.) was run at 25° C. containing the wash-solution (0.25 L) together with multi-stain monitors (MSM1 and MSM2, one each) and a cotton ballast fabric of 2.5 g (fabric to liquor ratio of 1:10). After the 1 cycle, the multi stain monitors were rinsed in water, followed by drying at ambient room temperature overnight. The multi-stain monitors MSM1 and MSM2 (Table 5) contain respectively 8 and 4 standardized soiled fabrics, of respectively 5.0×5.0 cm and 4.5×4.5 cm size and stitched on two sides to a polyester carrier.
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 brightness 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, ΔE) value, defined and calculated automatically by the evaluation color tools on the following formula,
is a measure of the achieved cleaning effect. All experiments were repeated three times to provide a representative average number.
Higher Delta E values show better cleaning. For each stain, a difference of 1 unit can be detected visually by a skilled person. A non-expert can visually detect 2 units easily. The ΔE values of the formulations for the 4, 8 and 11 stains of correspondingly MSM1 and MSM2 and for some selected single stains are shown in Tables 6.1 and 6.2.
General: the tests were carried out in accordance with the OECD Guidelines. According to the OECD guidelines a test is valid if:
Biodegradation in sewage was tested in triplicate using the OECD 301F manometric respirometry method. OECD 301F is an aerobic test that measures biodegradation of a sewage sample by measuring the consumption of oxygen. To a measured volume of sewage, 100 mg/L test substance, which is the nominal sole source of carbon, was added along with the inoculum (aerated sludge taken from the municipal sewage treatment plant, Mannheim, Germany). This sludge was stirred in a closed flask at a constant temperature (25° C.) for 28 days. The consumption of oxygen is determined by measuring the change in pressure in the closed flask using an Oxi TopC. Carbon dioxide evolved was absorbed in a solution of sodium hydroxide. Nitrification inhibitors were added to the flask to prevent consumption of oxygen due to nitrification. The amount of oxygen taken up by the microbial population during biodegradation of the test substance (corrected for uptake by a blank inoculum run in parallel) is expressed as a percentage of ThOD (theoretical oxygen demand, which is measured by the elemental analysis of the compound). A positive control glucose/glutamic acid is run along with the test samples for each cabinet as reference.
Calculations: Theoretical oxygen demand: Amount of O2 required to oxidize a compound to its final oxidation products. This amount is calculated using the elemental analysis data. % Biodegradation
The results of biodegradability tests are summarized in Table 7.
| Number | Date | Country | Kind |
|---|---|---|---|
| 21202497.0 | Oct 2021 | EP | regional |
| Filing Document | Filing Date | Country | Kind |
|---|---|---|---|
| PCT/EP22/77699 | 10/5/2022 | WO |
