EP1867708B1 - Waschmittelzusammensetzungen - Google Patents

Waschmittelzusammensetzungen Download PDF

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Publication number
EP1867708B1
EP1867708B1 EP06124858.9A EP06124858A EP1867708B1 EP 1867708 B1 EP1867708 B1 EP 1867708B1 EP 06124858 A EP06124858 A EP 06124858A EP 1867708 B1 EP1867708 B1 EP 1867708B1
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EP
European Patent Office
Prior art keywords
ksm
enzyme
ferm
composition according
sodium
Prior art date
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Revoked
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EP06124858.9A
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English (en)
French (fr)
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EP1867708A1 (de
Inventor
Neil Joseph Procter & Gamble Lant
Johan P&G Eurocor NV Smets
Charles David Procter & Gamble Bragg
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Procter and Gamble Co
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Procter and Gamble Co
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First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=38667162&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP1867708(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Priority claimed from EP06115574A external-priority patent/EP1882731A1/de
Priority claimed from EP06116782A external-priority patent/EP1867707B1/de
Priority claimed from EP06116780A external-priority patent/EP1876226B1/de
Priority claimed from EP06116784.7A external-priority patent/EP1876227B2/de
Priority to PL06124858T priority Critical patent/PL1867708T3/pl
Priority to EP06124858.9A priority patent/EP1867708B1/de
Application filed by Procter and Gamble Co filed Critical Procter and Gamble Co
Priority to CA2652774A priority patent/CA2652774A1/en
Priority to BRPI0713668-4A priority patent/BRPI0713668A2/pt
Priority to JP2009514977A priority patent/JP2009539399A/ja
Priority to PCT/IB2007/052308 priority patent/WO2007144855A1/en
Priority to ARP070102655A priority patent/AR061495A1/es
Priority to US11/818,652 priority patent/US20090291875A1/en
Priority to MX2008016229A priority patent/MX295029B/es
Publication of EP1867708A1 publication Critical patent/EP1867708A1/de
Publication of EP1867708B1 publication Critical patent/EP1867708B1/de
Application granted granted Critical
Revoked legal-status Critical Current
Anticipated expiration legal-status Critical

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase

Definitions

  • This invention relates to cleaning compositions comprising cellulose derivatives.
  • the invention also relates to detergent compositions comprising cellulose enzyme, such as bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4).
  • cellulose enzyme such as bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4).
  • the invention also relates to processes for making and using such products.
  • Cellulase enzymes have been used in detergent compositions for many years now for their known benefits of depilling, softness and colour care.
  • the use of most of cellulases has been limited because of the negative impact that cellulase may have on the tensile strength of the fabrics' fibers by hydrolysing crystalline cellulose.
  • cellulases with a high specificity towards amorphous cellulose have been developed to exploit the cleaning potential of cellulases while avoiding the negative tensile strength loss.
  • alkaline endo-glucanases have been developed to suit better the use in alkaline detergent conditions.
  • Novozymes in WO02/099091 discloses a novel enzyme exhibiting endo-beta-glucanase activity (EC 3.2.1.4) endogenous to the strain Bacillus sp. , DSM 12648; for use in detergent and textile applications.
  • Novozymes further describes in WO04/053039 detergent compositions comprising an anti-redeposition endo-glucanase and its combination with certain cellulases having increased stability towards anionic surfactant and/or further specific enzymes.
  • Kao's EP 265 832 describes novel alkaline cellulase K, CMCase I and CMCase II obtained by isolation from a culture product of Bacillus sp KSM-635.
  • Kao further describes in EP 1 350 843 , alkaline cellulase which acts favourably in an alkaline environment and can be mass produced readily because of having high secretion capacity or having enhanced specific activity.
  • Anionically modified cellulose derivatives such as carboxymethyl cellulose (CMC) are established anti-redeposition polymers in detergent compositions.
  • CMC carboxymethyl cellulose
  • the combination of celluloses with CMC has been disclosed, for example in GB-A-2095275 .
  • the present inventors have found that the combination of a specific alkaline bacterial cellulose and specific modified celluloses leads to a significant improvement in cotton stain repellency. Whilst not wishing to be bound by theory, it is believed that over multiple wash cycles, the modified cellulose derivatives deposit on cotton items and are acted upon by the bacterial alkaline cellulose so as to seal pores in the fibres of the laundered fabric surface. This results in a fabric surface which is less likely to form strong associations with particulate soils. There is therefore an improvement in the appearance of the laundered fabric and improved cleaning.
  • the present invention relates to a composition
  • a composition comprising a modified cellulose derivative having a molecular weight from 20 000 to 500 000 kDaltons and a cellulase enzyme, characterised in that the cellulase enzyme is a bacterial alkaline enzyme exhibiting endo-beta 1,4-glucanase activity (E.C.3.2.1.4) and the weight ratio of the modified cellulose component to the active cellulose enzyme protein is from 20:1 to 10000:1.
  • the compositions of the invention do not contain 0.7 to 0.9 wt % sodium nonanoyloxybenzene sulphonate.
  • the compositions of the invention do not contain 10 wt % sodium perborate monohydrate.
  • compositions of the invention typically do contain less than 8 % by weight and/or greater than 8.5 % by weight sodium sulphate (anhydrous), more specifically do not contain 8.0 to 8.3 wt% sodium sulphate.
  • the present invention also includes a composition comprising a modified cellulose derivative or mixtures thereof and a cellulase enzyme characterised in that the weight ratio of the modified cellulose derivative to the active cellulase enzyme protein is from 1:1 to 10000:1 and wherein the composition does not contain 0.7 to 0.9 % by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate, and does not contain 10 % by weight based on the total composition, of sodium perborate monohydrate, the enzyme producing reducing ends levels of greater than 5mM in the Enzyme Test defined below.
  • the inventors have found that the effectiveness of the endo-beta-(1,4)-glucanase / modified cellulose derivative combination is driven by short oligosaccharide products formed on hydrolysis of the polymer.
  • the present inventors have found that the most effective combinations involve the use of modified cellulose derivative as described herein and an endo-beta-(1,4)-glucanase which provides effective hydrolysis of CMC polymer down to small oligosaccharides as measured using reducing ends analysis as follows, adapted from J. Karlsson et al., Biopolymers, 2002, v63, pp. 32-40
  • CMC 250kDa weight average molecular mass, DS 0.7, supplied by Aldrich, Stenheim, Germany
  • 10g/L in 50mM sodium acetate pH 5.0 was hydrolysed with an excess of enzyme, 2betaM, for a prolonged hydrolysis time, 72hours.
  • the hydrolysates were then cooled to +4°C before carrying out reducing ends analysis using the dinitrosalicyclic acid reagent, according to the protocol described in M. Bailey et al, Enzyme Microb. Technol.,1981, v3, pp 153-157 , with glucose being used for the standard curve.
  • the endo-beta-(1,4)-glucanase enzymes required for the present invention produce reducing ends levels of greater than 5mM in this test, which correlates to ⁇ 10% reducing ends.
  • Preferred enzymes produce reducing end levels of greater than 10%, preferably greater than 12% or even greater than 15%, using the Enzyme Test.
  • cleaning composition includes, unless otherwise indicated, granular or powder-form all-purpose or “heavy-duty” washing agents, especially laundry detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy-duty liquid types; liquid fine-fabric detergents; as well as cleaning auxiliaries such as bleach additives and "stain-stick” or pre-treat types.
  • modified cellulose derivative comprises polymers comprising a cellulose backbone wherein the cellulose is substituted with at least one substituent or modifying group. A monomer of cellulose is shown below. R1, R2 and R3 show the positions in the cellulose monomer available for substitution. In the natural cellulose polymer, these groups comprise a hydrogen atom.
  • the modified cellulose derivative required according to the present invention comprise a substituent at one or more of these positions in the polymer.
  • the modifying groups will be non-ionic or anionic groups, producing nonionically or anionically modified cellulose, respectively.
  • the modified cellulose derivative may be provided by other beta-1,4-linked polysaccharides such as xyloglucan (e.g. derived from Tamarind seed gum), glucomannan (e.g. Konjac glucomannan), galactomannan (e.g. derived from guar gum or locust bean gum), side-chain branched galactomannan (e.g. Xanthan gum), chitosan or a chitosan salt.
  • xyloglucan e.g. derived from Tamarind seed gum
  • glucomannan e.g. Konjac glucomannan
  • galactomannan e.g. derived from guar gum or locust bean gum
  • an alpha-1,4-linked polysaccharide may also be present.
  • the natural polysaccharides, whether beta-1,4 or alpha-1,4, can be modified with amines (primary, secondary, tertiary), amides, esters, ethers, urethanes, alcohols, carboxylic acids, tosylates, sulfonates, sulfates, nitrates, phosphates and mixtures thereof.
  • suitable derivatives are given in WO 06/117071 (Unilever ), such as carboxymethyl Locust Bean gum and Locust Bean gum ethyl sulfonate.
  • Preferred are anionically modified cellulose derivatives such as carboxymethyl cellulose.
  • compositions of the present invention typically may contain from 0.00002% to 0.15%, from 0.00005% to 0.12%, or even from 0.0002% to 0.02% or even 0.005% to 0.025% by weight of pure enzyme, of one or more endoglucanase(s).
  • the balance of any aspects of the aforementioned cleaning compositions is made up of cellulose derivative and one or more adjunct materials.
  • the endoglucanase to be incorporated into the detergent composition of the present invention is one or more bacterial alkaline enzyme(s) exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4).
  • alkaline endoglucanase shall mean an endoglucanase having an optimum pH above 7 and retaining greater than 70% of its optimal activity at pH10.
  • the endoglucanase is a bacterial polypeptide endogenous to a member of the genus Bacillus.
  • the alkaline enzyme exhibiting endo-beta-1,4-glucanase activity is a polypeptide containing (i) at least one family 17 carbohydrate binding module (Family 17 CBM) and/or (ii) at least one family 28 carbohydrate binding module (Family 28 CBM).
  • Family 17 CBM Family 17 carbohydrate binding module
  • Family 28 CBM Family 28 carbohydrate binding module
  • said enzyme comprises a polypeptide (or variant thereof) endogenous to one of the following Bacillus species: Bacillus sp .
  • Bacillus sp As described in: AA349 (DSM 12648) WO 2002/099091A (Novozymes) p2, line 25 WO 2004/053039A (Novozymes) p3, line19 KSM S237 EP 1350843A (Kao) p3, line 18 1139 EP 1350843A (Kao) p3, line 22 KSM 64 EP 1350843A (Kao) p3, line 24 KSM N131 EP 1350843A (Kao) p3, line 25 KSM 635, FERM BP 1485 EP 265 832A (Kao) p7, line 45 KSM 534, FERM BP 1508 EP 0271044 A (Kao) p9, line 21 KSM 539, FERM BP 1509 EP 0271044 A (Kao)
  • Suitable endoglucanases for the compositions of the present invention are: 1) An enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), which has a sequence of at least 90%, preferably 94%, more preferably 97% and even more preferably 99%, 100% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:1 (Corresponding to SEQ ID NO:2 in WO02/099091 ); or a fragment thereof that has endo-beta-1,4-glucanase activity, when identity is determined by GAP provided in the GCG program using a GAP creation penalty of 3.0 and GAP extension penalty of 0.1.
  • alkaline cellulase variants are obtained by substituting the amino acid residue of a cellulase having an amino acid sequence exhibiting at least 90%, preferably 95%, more preferably 98% and even 100% identity with the amino acid sequence represented by SEQ. ID NO:2 (Corresponding to SEQ.
  • alkaline cellulase having an amino acid sequence exhibiting at least 90% homology with the amino acid sequence represented by SEQ. ID NO:2 include alkaline cellulases having an amino acid sequence exhibiting preferably at least 95% homology, more preferably at least 98% homology, with the amino acid sequence represented by SEQ. ID NO:2.
  • alkaline cellulase derived from Bacillus sp. strain 1139 (Eg1-1139) Fukumori, et al., J. Gen.
  • Microbiol., 132, 2329-2335 (91.4% homology), alkaline cellulases derived from Bacillus sp. strain KSM-64 (Eg1-64) ( Sumitomo, et al., Biosci. Biotechnol. Biochem., 56, 872-877, 1992 ) (homology: 91.9%), and cellulase derived from Bacillus sp. strain KSM-N131 (Eg1-N131b) (Japanese Patent Application No. 2000-47237 ) (homology: 95.0%).
  • the amino acid is preferably substituted by: glutamine, alanine, proline or methionine, especially glutamine is preferred at position (a), asparagine or arginine, especially asparagine is preferred at position (b), proline is preferred at position (c), histidine is preferred at position (d), alanine, threonine or tyrosine, especially alanine is preferred at position (e), histidine, methionine, valine, threonine or alanine, especially histidine is preferred at position (f), isoleucine, leucine, serine or valine, especially isoleucine is preferred at position (g), alanine, phenylalanine, valine, serine, aspartic acid, glutamic acid, leucine, isoleucine, tyrosine, threonine, methionine or glycine, especially alanine, phenylalanine or serine is preferred at position (h), isole
  • amino acid residue at a position corresponding thereto can be identified by comparing amino acid sequences by using known algorithm, for example, that of Lipman-Pearson's method, and giving a maximum similarity score to the multiple regions of similarity in the amino acid sequence of each alkaline cellulase.
  • the position of the homologous amino acid residue in the sequence of each cellulase can be determined, irrespective of insertion or depletion existing in the amino acid sequence, by aligning the amino acid sequence of the cellulase in such manner (Fig. 1 of EP 1 350 843 ). It is presumed that the homologous position exists at the three-dimensionally same position and it brings about similar effects with regard to a specific function of the target cellulase.
  • alkaline cellulase having an amino acid sequence exhibiting at least 90% homology with SEQ. ID NO:2, specific examples of the positions corresponding to (a) position 10, (b), position 16, (c) position 22, (d) position 33, (e) position 39, (f) position 76, (g) position 109, (h) position 242, (i) position 263, (j) position 308, (k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position 564 and (p) position 608 of the alkaline cellulase (Eg1-237) represented by SEQ.
  • Egl-237 Egl-1139 Egl-64 Egl-N131b (a) 10Leu 10Leu 10Leu 10Leu (b) 16Ile 16Ile 16Ile nothing corresponding thereto (c) 22Ser 22Ser 22Ser None corresponding thereto (d) 33Asn 33Asn 33Asn 19Asn (e) 39Phe 39Phe 39Phe 25Phe (f) 76Ile 76Ile 76Ile 62Ile (g) 109Met 109Met 109Met 95Met (h) 242Gln 242Gln 242Gln 228Gln (i) 263Phe 263Phe 263Phe 249Phe 0) 308Thr 308Thr 308Thr 294Thr (k) 462Asn 461Asn 461Asn 448Asn (l) 466Lys 465Lys 465Lys 452
  • the modified cellulose derivative required in the present invention comprises a polymer comprising a cellulose backbone.
  • the cellulose may be anionically or nonionically modified, preferably anionically modified.
  • a monomer of cellulose is shown below.
  • R1, R2 and R3 show the positions in the cellulose monomer available for substitution.
  • these groups comprise a hydrogen atom.
  • the modified cellulose derivative useful herein comprises substituents at one or more of these positions.
  • anionic substitution one or more of these positions in the polymer are substituted with an anionic group for example, one of the following anionic groups, in its acid or salt form, preferably sodium (given here) or potassium salt form.
  • the anionically modified cellulose derivative may also comprise non-ionic substituent groups in which one or more of positions R1, R2 and R3 may be substituted with nonionic groups, for example,
  • Non-limiting examples of suitable modified cellulose derivatives are the sodium or potassium salts of carboxymethyl cellulose, carboxyethyl cellulose, sulfoethyl cellulose, sulfopropyl cellulose, cellulose sulfate, phosphorylated cellulose, carboxymethyl hydroxyethyl cellulose, carboxymethyl hydroxypropyl cellulose, sulfoethyl hydroxyethyl cellulose, sulfoethyl hydroxypropyl cellulose, carboxymethyl methyl hydroxyethyl cellulose, carboxymethyl methyl cellulose, sulfoethyl methyl hydroxyethyl cellulose, sulfoethyl methyl cellulose, carboxymethyl ethyl hydroxyethyl cellulose, carboxymethyl ethyl cellulose, sulfoethyl ethyl hydroxyethyl cellulose, sulfoethyl ethyl cellulose,
  • the modified cellulose derivative may be provided by a nonionically modified cellulose derivative instead of or in addition to the anionically modified cellulose polymer.
  • nonionically modified cellulose polymers include methyl cellulose, ethyl cellulose, propyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, methyl hydroxyethyl cellulose, ethyl hydroxyethyl cellulose, dodecyl hydroxyethyl cellulose, ethyl hydroxypropyl cellulose, cellulose acetate, methyl hydroxypropyl cellulose, methyl ethyl hydroxyethyl cellulose, butyl glycidyl ether-hydroxyethyl cellulose, and lauryl glycidyl ether-hydroxyethyl cellulose
  • modified cellulose derivatives have a weight average molecular mass of at least 20 000 or at least 50 000 or even at least 100 000 or even at least 150 000 kDaltons.
  • the weight average molecular mass of the modified cellulose derivative will generally be no greater than 500 000, or no greater than 300 000 or no greater than 250 000kDa.
  • Preferred degrees of substitution (DS) are from 0.3, or 0.4, or 0.45 up to for example 0.7 or even 0.8 or even 0.9.
  • modified methyl celluloses such as CMC, with such molecular weights and/or degrees of substitution and/or levels as described herein.
  • the level of modified cellulose derivative in the detergent compositions of the invention is typically from at least 0.005 or 0.01 wt% or 0.02 or at least 0.05 wt% or even at least 0.1 wt% based on the total weight of detergent composition. Typically, the levels will be no greater than 5% by weight or even no greater than 2% by weight or even no greater than 1.5% by weight of the detergent composition. In a particularly preferred embodiment of the invention the weight ratio of modified cellulose derivative to active cellulase enzyme protein is from 1:1 to 10000:1, preferably 20:1 to 1000:1, most preferably 30:1 to 800:1.
  • Cellulose derivatives such as methyl celluloses have been incorporated into detergent compositions for many years. They deposit onto cotton fabric surfaces to form a negatively charged soil-repellant layer, which repels soils reducing deposition onto a fabric surface.
  • the present inventors have found that cellulose derivatives having a much lower molecular weight than is traditionally used can provide further surprising benefits as they act as anti-redeposition aids by suspending soils in the wash liquor.
  • These cellulose derivatives may be formed in situ by reaction of specific cellulose agent pre-cursors.
  • the modified cellulose derivative may be added as a dry particulate component comprising for example greater than 50 % or even greater than 60 % or 70 % or 80% by weight, up to 100 % by weight modified cellulose derivative.
  • the modified cellulose derivative may be incorporated into the detergent compositions of the invention as part of a processed particle formed by a conventional detergent particle-making process, such as spray-drying, agglomeration or extrusion.
  • the amount of modified cellulose derivative in such particle will be at least 0.1 % or 0.5 or 1 % by weight and is likely to be less than 70% and more likely, less than 60 % or 50 %, 40%, 30% or even less than 20 % or 10% by weight of the processed particle.
  • Introducing the modified cellulose derivative as part of a processed detergent particle may be particularly preferred especially for detergent compositions containing low levels of phosphate and/or zeolite builders; for example less than 15% by weight of the total detergent composition or even less than 14% or 12 % or 10 % or 8 % down to 0 % by weight phosphate and/or zeolite builders. This may be preferred as it may promote uniform distribution of the cellulose throughtout the wash liquor on addition of the detergent composition to water, by helping solubility of the cellulose derivative.
  • the processed detergent particle may comprise any other conventional detergent ingredients or components thereof such as any of the adjunct materials described below or, for example as described in JP 2002 265999 (Kao ) or in any of the processes described below under the sub-heading "Processes of Making Compositions".
  • such particles may comprise at least 1, or at least 5 or 10 % by weight up to 15 or 20 or 30 % by weight polymeric polycarboxylate polymer such as acrylic acid and/or maleic acid-based homo- or co- polymers (e.g. Sokalan polymers from BASF), based on the weight of the processed particle.
  • the processed particles may comprise anionic, non-ionic, cationic, zwitterionic and/or amphoteric surfactants or mixtures thereof. Amounts may be form 1 to 70 % by weight, or 2 to 60% or from5 to 850 % by weight based on the total weight of the processed particle.
  • processed particles may comprise non-ionic surfactant optionally in combination with anionic and/or cationic surfactants. Suitable surfactants are described in the "Surfactants" section of the description.
  • suitable non-ionic surfactants include alkyl alkoxylated surfactant, e.g ethoxylated surfactants having a degree of alkoxylation from 3 to 20 or even higher such as 20 to 50.
  • Processed particles may comprise sodium silicate (especially 1 to 2 ratio) in amounts from 1 to 30 % by weight or 2 to 25 % by weight or from 5 to 20 % by weight.
  • Preferred compositions according to the invention comprise polymeric polycarboxylate polymers and in such an amount that the weight ratio of polymeric polycarboxylate to modified cellulose derivative is at least 2:1, more preferably at least 2.5:1 and most preferably at least 3:1 or even 4:1 or 5:1. Such ratios may also be preferred in the processed particles discussed above, where polymeric polycarboxylate is present.
  • the bulk density of the composition of the invention and/or more specifically the modified cellulose derivative-containing particles is typically at least 450 g/l or at least 550g/l or 650g/l or at least 700g/l, up to 1500g/l.
  • Bulk density is measured by means of a simple funnel and cup device consisting of a conical funnel mounted rigidly on a base and provided with a flap valve at its lower extremity to allow the contents of the funnel to be emptied into an axially aligned cylindrical cup disposed below the funnel.
  • the funnel is 130 mm high and has internal diameters of 130 mm and 40 mm at its respective upper and lower extremities. It is mounted so that the lower extremity is 140 mm above the upper surface of the base.
  • the cup has an overall height of 90 mm, an internal height of 87 mm and an internal diameter of 84 mm. Its nominal volume is 500 ml.
  • the funnel is filled with powder by hand pouring, the flap valve is opened and powder is allowed to overfill the cup.
  • the filled cup is removed from the frame and excess powder is removed from the cup by passing a straight edged implement eg. a knife, across its upper edge.
  • the filled cup is then weighed and the value obtained for the weight of powder doubled to provide a bulk density of g/litre. Replicate measurements are made and an average of three results provides the bulk density.
  • a detergent composition comprising oligosaccharides having a weight average molecular mass of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of an enzyme as defined above with an anionically modified cellulose having an average molecular weight from 30 000 to 500 000 kDa.
  • an aqueous wash liquor comprising a detergent composition wherein the oligosaccharide is comprised in amounts from 0.5ppm to 1000 ppm, or from 0.8 to 1500 ppm or from 1.0 to 1000ppm.
  • oligosaccharide having a weight average molecular mass of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of an enzyme as described above, with an anionically or nonionically, preferably anionically modified cellulose derivative having a weight average molecular mass from 30 000 to 500 000 kDa, for preparation of a detergent composition, for soil suspension.
  • a detergent composition comprising an enzyme as described above and at least 2 wt%, or even at least 5 wt%, 10 wt%, 15, 20 wt% or higher for example up to 50 wt% or 40 wt% or 30 wt% or 25 wt% , of a phosphate builder salt, at least 25, or 30 or 40 or 45 or 50 or even 55 wt% up to 100 wt% or 90 wt% or 80 wt% of said phosphate builder comprising pyrophosphate builder.
  • This pyrophosphate builder may be formed in situ by spray drying a composition comprising sodium or other salt of tri polyphosphate or acid form in a spray drying process in which the temperature and/or air flow and/or other chemical constituents in the spray drying slurry are controlled to provide the desired reaction of the tripolyphosphate to pyrophosphate salt.
  • the process may be operated for example as described in WO03/091378 or US4310431 .
  • adjuncts illustrated hereinafter are suitable for use in the instant compositions and may be desirably incorporated in certain embodiments of the invention, for example to assist or enhance cleaning performance, for treatment of the substrate to be cleaned, or to modify the aesthetics of the cleaning composition as is the case with perfumes, colorants, dyes or the like.
  • the precise nature of these additional components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the cleaning operation for which it is to be used.
  • Suitable adjunct materials include, but are not limited to, surfactants, builders, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents and/or pigments.
  • suitable examples of such other adjuncts and levels of use are found in U.S. Patent Nos. 5,576,282 , 6,306,812 B1 and 6,326,348 B1 that are incorporated by reference. When one or more adjuncts are present, such one or more adjuncts may be present as detailed below:
  • the peracid and/or bleach activator is generally present in the composition in an amount of from about 0.1 to ab out 60 wt%, from about 0.5 to about 40 wt% or even from about 0.6 to about 10 wt% based on the composition.
  • One or more hydrophobic peracids or precursors thereof may be used in combination with one or more hydrophilic peracid or precursor thereof.
  • the amounts of hydrogen peroxide source and peracid or bleach activator may be selected such that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1:1 to 35:1, or even 2:1 to 10:1.
  • the cleaning compositions according to the present invention may comprise a surfactant or surfactant system wherein the surfactant can be selected from nonionic surfactants, anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants, semi-polar nonionic surfactants and mixtures thereof.
  • surfactant is typically present at a level of from about 0.1% to about 60%, from about 1% to about 50% or even from about 5% to about 40% by weight of the subject composition.
  • the cleaning compositions of the present invention may comprise one or more detergent builders or builder systems.
  • the subject composition will typically comprise at least about 1%, from about 5% to about 60% or even from about 10% to about 40% builder by weight of the subject composition.
  • Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicate builders and polycarboxylate compounds, ether hydroxypolycarboxylates, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof.
  • the cleaning compositions herein may contain a chelating agent.
  • Suitable chelating agents include copper, iron and/or manganese chelating agents and mixtures thereof.
  • the subject composition may comprise from about 0.005% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the subject composition.
  • the cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents.
  • Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
  • the dye transfer inhibiting agents may be present at levels from about 0.0001% to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.
  • Fluorescent whitening agent - The cleaning compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent.
  • Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulphonic acid derivative type of fluorescent whitening agents include the sodium salts of:
  • fluorescent whitening agents of the structure: wherein R1 and R2, together with the nitrogen atom linking them, form an unsubstituted or C1-C4 alkyl-substituted morpholino, piperidine or pyrrolidine ring, preferably a morpholino ring (commercially available as Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India)
  • fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins.
  • Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt %.
  • Fabric hueing agents- dyes or pigments which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions thus altering the tint of said fabric through absorption of visible light.
  • Fluorescent whitening agents emit at least some visible light.
  • fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum.
  • Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments.
  • Suitable dyes include small molecule dyes and polymeric dyes.
  • Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.I.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in WO2005/03274 , WO2005/03275 , WO2005/03276 and co-pending European application no o6116780.5 filed 7 July 2006 .
  • C.I. Colour Index
  • compositions of the present invention can also contain dispersants.
  • Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
  • the cleaning compositions can comprise one or more other enzymes which provide cleaning performance and/or fabric care benefits.
  • suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, other cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, ß-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and amylases, or mixtures thereof.
  • compositions of the present invention will further comprise a lipase, for further improved cleaning and whitening performance.
  • a typical combination is an enzyme cocktail that may comprise, for example, a protease and lipase in conjunction with amylase.
  • the aforementioned additional enzymes may be present at levels from about 0.00001% to about 2%, from about 0.0001% to about 1% or even from about 0.001% to about 0.5% enzyme protein by weight of the composition.
  • Enzyme Stabilizers - Enzymes for use in detergents can be stabilized by various techniques.
  • the enzymes employed herein can be stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions that provide such ions to the enzymes.
  • a reversible protease inhibitor such as a boron compound, can be added to further improve stability.
  • Catalytic Metal Complexes - Applicants' cleaning compositions may include catalytic metal complexes.
  • One type of metal-containing bleach catalyst is a catalyst system comprising a transition metal cation of defined bleach catalytic activity, such as copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations, an auxiliary metal cation having little or no bleach catalytic activity, such as zinc or aluminum cations, and a sequestrate having defined stability constants for the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra(methylenephosphonic acid) and water-soluble salts thereof.
  • Such catalysts are disclosed in U.S. 4,430,243 .
  • compositions herein can be catalyzed by means of a manganese compound.
  • a manganese compound Such compounds and levels of use are well known in the art and include, for example, the manganese-based catalysts disclosed in U.S. 5,576,282 .
  • Cobalt bleach catalysts useful herein are known, and are described, for example, in U.S. 5,597,936 ; U.S. 5,595,967 . Such cobalt catalysts are readily prepared by known procedures, such as taught for example in U.S. 5,597,936 , and U.S. 5,595,967 .
  • compositions herein may also suitably include a transition metal complex of ligands such as bispidones ( WO 05/042532 A1 ) and/or macropolycyclic rigid ligands - abbreviated as "MRLs".
  • ligands such as bispidones ( WO 05/042532 A1 ) and/or macropolycyclic rigid ligands - abbreviated as "MRLs”.
  • MRLs macropolycyclic rigid ligands - abbreviated as "MRLs”.
  • the compositions and processes herein can be adjusted to provide on the order of at least one part per hundred million of the active MRL species in the aqueous washing medium, and will typically provide from about 0.005 ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or even from about 0.1 ppm to about 5 ppm, of the MRL in the wash liquor.
  • Suitable transition-metals in the instant transition-metal bleach catalyst include, for example, manganese, iron and chromium.
  • Suitable MRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.
  • Suitable transition metal MRLs are readily prepared by known procedures, such as taught for example in WO 00/32601 , and U.S. 6,225,464 .
  • Solvents - Suitable solvents include water and other solvents such as lipophilic fluids.
  • suitable lipophilic fluids include siloxanes, other silicones, hydrocarbons, glycol ethers, glycerine derivatives such as glycerine ethers, perfluorinated amines, perfluorinated and hydrofluoroether solvents, low-volatility nonfluorinated organic solvents, diol solvents, other environmentally-friendly solvents and mixtures thereof.
  • Softening system the compositions of the invention may comprise a softening agent such as clay and optionally also with flocculants and enzymes; optionally for softening through the wash.
  • a softening agent such as clay and optionally also with flocculants and enzymes; optionally for softening through the wash.
  • compositions of the present invention can be formulated into any suitable form and prepared by any process chosen by the formulator, non-limiting examples of which are described in Applicants' examples and in U.S. 4,990,280 ; U.S. 20030087791A1 ; U.S. 20030087790A1 ; U.S. 20050003983A1 ; U.S. 20040048764A1 ; U.S. 4,762,636 ; U.S. 6,291,412 ; U.S. 20050227891A1 ; EP 1070115A2 ; U.S. 5,879,584 ; U.S. 5,691,297 ; U.S. 5,574,005 ; U.S. 5,569,645 ; U.S. 5,565,422 ; U.S. 5,516,448 ; U.S. 5,489,392 ; U.S. 5,486,303 all of which are incorporated herein by reference.
  • the present invention includes a method for laundering a fabric.
  • the method comprises the steps of contacting a fabric to be laundered with a said cleaning laundry solution comprising at least one embodiment of Applicants' cleaning composition, cleaning additive or mixture thereof.
  • the fabric may comprise most any fabric capable of being laundered in normal consumer use conditions.
  • the solution preferably has a pH of from about 8 to about 10.5.
  • the compositions may be employed at concentrations of from about 500 ppm to about 15,000 ppm in solution.
  • the water temperatures typically range from about 5 °C to about 90 °C.
  • the water to fabric ratio is typically from about 1:1 to about 30:1.
  • Granular laundry detergent compositions designed for handwashing or top-loading washing machines. 1 (wt %) 2 (wt %) 3 (wt %) 4 (wt %) 5 (wt %) 6 (wt %) Linear alkylbenzenesulfonate 20 22 20 10 20 20 C 12-14 Dimethylhydroxyethyl ammonium chloride 0.7 0.2 1 0 0.0 0 AE3S 0.9 1 0.9 3.2 0.5 0.9 AE7 0.0 0.0 0.0 0.0 0.0 3 Sodium tripolyphosphate 5 25 4 3 2 0.0 Zeolite A 0.0 1 0.0 1 4 1 1.6R Silicate (SiO 2 :Na 2 O at ratio 1.6:1) 4 5 2 3 3 5 Sodium Carbonate 9 20 10 17 5 23 Polyacrylate MW 4500 1 0.6 1 1 1.5 1 Carboxymethyl Cellulose 1 0.3 0.3 0.1 1.1 0.9 Celluclean® (15.6mg/g) 0.1 0.2 0.1 0.2 0.3 0.1 Savinase®
  • Granular laundry detergent compositions designed for front-loading automatic washing machines. 7 (wt%) 8 (wt%) 9 (wt%) 10 (wt%) 11 (wt%) 12 (wt%) Linear alkylbenzenesulfonate 8 7.1 7 6.5 7.5 7.5 AE3S 0 4.8 0 5.2 4 4 AE7 2.2 0 3.2 0 0 0 C 10-12 Dimethyl hydroxyethylammonium chloride 0.75 0.94 0.98 0.98 0 0 0 Crystalline layered silicate ( ⁇ -Na 2 Si 2 O 5 ) 2.0 0 2.0 0 0 0 0 Zeolite A 7 0 7 0 2 2 Citric Acid 3 5 3 4 2.5 3 Sodium Carbonate 15 20 14 20 23 23 Silicate 2R (SiO 2 :Na 2 O at ratio 2:1) 0.08 0 0.11 0 0 0 Soil release agent 0.75 0.72 0.71 0.72 0 0 Acrylic Acid/Maleic Acid Copolymer 1.1 3.7 1.0
  • compositions is used to launder fabrics at a concentration of 7000 to 10000 ppm in water, 20-90 °C, and a 5:1 water:cloth ratio.
  • the typical pH is about 10.

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Claims (16)

  1. Zusammensetzung, umfassend ein modifiziertes Cellulose-Derivat mit einem Molekulargewicht von 20000 bis 500000 kDaltons, oder Mischungen davon, und ein Cellulaseenzym, dadurch gekennzeichnet, dass das Gewichtsverhältnis des modifizierten Cellulose-Derivats zu dem aktiven Cellulaseenzymprotein von 20:1 bis 10000:1 beträgt und, wobei die Zusammensetzung nicht 0,7 bis 0,9 Gew.-% der Gesamtzusammensetzung an Natriumnonanoyloxybenzolsulfonat enthält, und nicht 10 Gew.-%, bezogen auf die Gesamtzusammensetzung, an Natriumperboratmonohydrat enthält, in der das Enzym ein bakterielles alkalisches Enzym ist, das endo-beta-1,4-Glucanaseaktivität aufweist (E.C. 3.2.1.4).
  2. Zusammensetzung nach Anspruch 1, wobei das Enzym ein auf ein Mitglied der Gattung Bacillus endogenes bakterielles Polypeptid ist.
  3. Zusammensetzung nach einem der Ansprüche 1 oder 2, wobei das Enzym ein Polypeptid ist, enthaltend (i) mindestens ein Familie-17-Kohlenhydrat-Bindungsmodul und/oder (ii) mindestens ein Familie-28-Kohlenhydrat-Bindungsmodul.
  4. Zusammensetzung nach einem der Ansprüche 1 bis 3, wobei das Enzym ein Polypeptid umfasst, das auf eine der folgenden Bacillus-Species endogen ist, die ausgewählt sind aus der Gruppe bestehend aus: AA349 (DSM 12648), KSM S237, 1139, KSM 64, KSM N131, KSM 635 (FERM BP 1485), KSM 534 (FERM BP 1508), KSM 53 (FERM BP 1509), KSM 577 (FERM BP 1510), KSM 521 (FERM BP 1507), KSM 580 (FERM BP 1511), KSM 588 (FERM BP 1513), KSM 597 (FERM BP 1514), KSM 522 (FERM BP 1512), KSM 3445 (FERM BP 1506), KSM 425 (FERM BP 1505), und Mischungen davon.
  5. Zusammensetzung nach einem der Ansprüche 1 bis 4, wobei das Enzym ausgewählt ist aus der Gruppe bestehend aus:
    (i) der Endoglucanase mit der Aminosäuresequenz von Positionen 1 bis Position 773 von SEQ-ID Nr. 1;
    (ii) einer Endoglucanase mit einer Sequenz von mindestens 90 %, vorzugsweise 94 %, mehr bevorzugt 97 % und noch mehr bevorzugt 99 %, 100 % Identität mit der Aminosäure-Sequenz von Position 1 bis Position 773 von SEQ-ID Nr. 1; oder ein Fragment davon hat Endo-beta-1,4-Glucanase-Aktivität, wenn die Identität mittels dem im GCG-Programm bereitgestellten GAP mit einer GAP Creation Penalty von 3,0 und einer GAP Extension Penalty von 0,1 bestimmt wird; (iii) Mischungen davon.
  6. Zusammensetzung nach einem der Ansprüche 1 bis 5, wobei das Enzym eine alkalische Endoglucanase-Variante ist, die durch Ersetzen des Aminosäurerests einer Cellulase mit einer Aminosäuresequenz erhalten wird, die mindestens 90 %, vorzugsweise 95 %, mehr bevorzugt 98 %, 100 % Identität mit der Aminosäuresequenz aufweist, die durch SEQ-ID Nr. 2 dargestellt ist, in (a) Position 10, (b) Position 16, (c) Position 22, (d) Position 33, (e) Position 39, (f) Position 76, (g) Position 109, (h) Position 242, (i) Position 263, (j) Position 308, (k) Position 462, (I) Position 466, (m) Position 468, (n) Position 552, (o) Position 564, und/oder (p) Position 608 in SEQ-ID Nr. 2 und/oder in einer damit entsprechenden Position mit einem anderen Aminosäurerest aufweist.
  7. Zusammensetzung nach Anspruch 5, wobei das Enzym gekennzeichnet ist durch mindestens eine der folgenden Substitutionen:
    (a) an Position 10: Glutamin, Alanin, Prolin oder Methionin, vorzugsweise Glutamin;
    (b) an Position 16: Asparagin oder Arginin, vorzugsweise Asparagin;
    (c) an Position 22: Prolin;
    (d) an Position 33: Histidin;
    (e) an Position 39: Alanin, Threonin oder Tyrosin, vorzugsweise Alanin;
    (f) an Position 76: Histidin, Methionin, Valin, Threonin oder Alanin, vorzugsweise Histidin;
    (g) an Position 109: Isoleucin, Leucin, Serin oder Valin, vorzugsweise Isoleucin;
    (h) an Position 242: Alanin, Phenylalanin, Valin, Serin, Asparaginsäure, Glutaminsäure, Leucin, Isoleucin, Tyrosin, Threonin, Methionin oder Glycin, vorzugsweise Alanin, Phenylalanin oder Serin;
    (i) an Position 263: Isoleucin, Leucin, Prolin oder Valin, vorzugsweise Isoleucin;
    (j) an Position 308: Alanin, Serin, Glycin oder Valin, vorzugsweise Alanin;
    (k) an Position 462: Threonin, Leucin, Phenylalanin oder Arginin, vorzugsweise Threonin;
    (l) an Position 466: Leucin, Alanin oder Serin, vorzugsweise Leucin;
    (m) an Position 468: Alanin, Asparaginsäure, Glycin oder Lysin, vorzugsweise Alanin;
    (n) an Position 552: Methionin;
    (o) an Position 564: Valin, Threonin oder Leucin, vorzugsweise Valin; und/oder
    (p) an Position 608: Isoleucin oder Arginin, vorzugsweise Isoleucin.
  8. Zusammensetzung nach Anspruch 6 oder Anspruch 7, wobei das Enzym ausgewählt ist aus der Gruppe bestehend aus den folgenden Endoglucanase-Varianten: Egl-237, Egl-1139, Egl-64, Egl-N131b und Mischungen davon.
  9. Zusammensetzung nach einem der Ansprüche 1 bis 3, wobei das Enzym eine alkalische Cellulase K mit den folgenden physikalischen und chemischen Eigenschaften ist:
    (1) Aktivität: Mit einer Cx-Enzymaktivität der Wirkung auf Carboxymethylcellulose zusammen mit einer schwachen C1-Enzymaktivität und einer schwachen beta-Glucoxidase-Aktivität;
    (2) Spezifität auf Substraten: Wirkung auf Carboxymethylcellulose (CMC), kristalline Cellulose, Avicell, Cellobiose, und p-Nitrophenylcellobiosid (PNPC);
    (3) Mit einem Arbeits-pH-Wert im Bereich von 4 bis 12 und einem pH-Wert-Optimum im Bereich von 9 bis 10;
    (4) Mit stabilen pH-Werten von 4,5 bis 10,5 und 6,8 bis 10, beim Stehenlassen bei 40 °C 10 Minuten bzw. 30 Minuten;
    (5) Wirkt in einem breiten Temperaturbereich von 10 bis 65 °C mit einer optimalen Temperatur bei etwa 40 °C;
    (6) Einflüsse von Chelatbildnern: Die Aktivität wird nicht beeinträchtigt durch Ethylendiamintetraessigsäure (EDTA), Ethylenglycol-bis-(β-aminoethylether)N,N,N',N"-tetraessigsäure (EGTA), N,N-bis(carboxymethyl)glycin (Nitriltriessigsäure) (NTA), Natriumtripolyphosphat (STPP) und Zeolit;
    (7) Einflüsse von oberflächenaktiven Mitteln: Unterliegt wenig Hemmung der Aktivität mittels oberflächenaktiven Mitteln, wie linearen Natriumalkylbenzolsulfonaten (LAS), Natriumalkylsulfaten (AS), Natriumpolyoxyethylenalkylsulfaten (ES), Natrium-alpha-olefinsulfonaten (AOS), Natrium-alpha-sulfonierten aliphatischen Säureestern (alpha-SFE), Natriumalkylsulfonaten (SAS), sekundären Polyoxyethylenalkylethern, Fettsäuresalzen (Natriumsalzen), und Dimethyldialkylammoniumchlorid;
    (8) Weist eine starke Beständigkeit gegenüber Proteinasen auf; und
    (9) Molekulargewicht (bestimmt durch Gelchromatographie): Mit einen Maximumpeak bei 180.000 ± 10.000,
  10. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das bakterielle alkalische Enzym, das endo-beta-1,4-Glucanaseaktivität aufweist, aus reinem Enzym in einer Konzentration von 0,00005 % bis 0,15 %, vorzugsweise von 0,0002 % bis 0,02 %, oder mehr bevorzugt von 0,0005 % bis 0,01 Gew.-% besteht.
  11. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das Gewichtsverhältnis von modifiziertem Cellulose-Derivat zu aktivem Cellulaseenzymprotein bis zu 1000:1, vorzugsweise von 30:1 bis 800:1, beträgt.
  12. Zusammensetzung nach einem der vorstehenden Ansprüche, in der das modifizierte Cellulose-Derivat ein Molekulargewicht von von 100 000 bis 300 000 kDaltons aufweist.
  13. Zusammensetzung nach einem der vorstehenden Ansprüche, in der das modifizierte Cellulose-Derivat in der Zusammensetzung aus einer Konzentration von 0,02 bis 5 %, vorzugsweise von 0,05 bis 2 Gew.-% oder mehr bevorzugt von 0,1 bis 1,5 Gew.-% besteht.
  14. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das modifizierte Cellulose-Derivat ausgewählt ist aus der Gruppe bestehend aus anionisch und nichtionisch modifizierten Cellulosen, die vorzugsweise anionisch modifiziert sind.
  15. Zusammensetzung nach einem der vorstehenden Ansprüche, wobei das modifizierte Cellulose-Derivat einen durchschnittlichen Substitutionsgrad von 0,3 bis 0,9, vorzugsweise 0,4 bis 0,8 aufweist.
  16. Verfahren zum Reinigen und/oder Behandeln einer Oberfläche oder eines Stoffes, umfassend die Schritte des wahlweisen Waschens und/oder Spülens der Oberfläche oder des Stoffes, Kontaktierens der Oberfläche oder des Stoffes mit der Zusammensetzung nach einem der vorstehenden Ansprüche, dann wahlweise Waschen und/oder Spülen der Oberfläche oder des Stoffes.
EP06124858.9A 2006-06-16 2006-11-27 Waschmittelzusammensetzungen Revoked EP1867708B1 (de)

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PL06124858T PL1867708T3 (pl) 2006-06-16 2006-11-27 Kompozycje detergentu
EP06124858.9A EP1867708B1 (de) 2006-06-16 2006-11-27 Waschmittelzusammensetzungen
MX2008016229A MX295029B (es) 2006-06-16 2007-06-15 Composiciones detergentes.
CA2652774A CA2652774A1 (en) 2006-06-16 2007-06-15 Detergent compositions
US11/818,652 US20090291875A1 (en) 2006-06-16 2007-06-15 Detergent compositions
ARP070102655A AR061495A1 (es) 2006-06-16 2007-06-15 Composiciones detergentes
PCT/IB2007/052308 WO2007144855A1 (en) 2006-06-16 2007-06-15 Detergent compositions
BRPI0713668-4A BRPI0713668A2 (pt) 2006-06-16 2007-06-15 composições detergentes
JP2009514977A JP2009539399A (ja) 2006-06-16 2007-06-15 洗剤組成物

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EP06115574A EP1882731A1 (de) 2006-06-16 2006-06-16 Waschmittelzusammensetzungen
US81915506P 2006-07-07 2006-07-07
EP06116784.7A EP1876227B2 (de) 2006-07-07 2006-07-07 Waschmittelzusammensetzungen
EP06116780A EP1876226B1 (de) 2006-07-07 2006-07-07 Waschmittelzusammensetzungen
EP06116782A EP1867707B1 (de) 2006-06-16 2006-07-07 Waschmittelzusammensetzungen
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