EP0496783A1 - Abbaubeständige reinigungszusammensetzungen. - Google Patents

Abbaubeständige reinigungszusammensetzungen.

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Publication number
EP0496783A1
EP0496783A1 EP90915577A EP90915577A EP0496783A1 EP 0496783 A1 EP0496783 A1 EP 0496783A1 EP 90915577 A EP90915577 A EP 90915577A EP 90915577 A EP90915577 A EP 90915577A EP 0496783 A1 EP0496783 A1 EP 0496783A1
Authority
EP
European Patent Office
Prior art keywords
components
cellulase
cbh
detergent composition
type
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
EP90915577A
Other languages
English (en)
French (fr)
Other versions
EP0496783B1 (de
EP0496783A4 (en
Inventor
Nancy J Bjork
Kathleen A Clarkson
Pushkaraj T Lad
Geoffrey L Weiss
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Danisco US Inc
Original Assignee
Genencor International Inc
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Publication date
Application filed by Genencor International Inc filed Critical Genencor International Inc
Publication of EP0496783A1 publication Critical patent/EP0496783A1/de
Publication of EP0496783A4 publication Critical patent/EP0496783A4/en
Application granted granted Critical
Publication of EP0496783B1 publication Critical patent/EP0496783B1/de
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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
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase

Definitions

  • the present invention relates to detergent compositions which have improved degradation resistance to cotton fabrics. More particularly, the present invention relates to detergent compositions containing a combination of exo- cellobiohydrolase I type cellulase components and endoglucanase components wherein the exo-cellobiohydrolase I type cellulase components are enriched relative to the endoglucanse type cellulase.
  • Such detergent compositions provide excellent cleaning especially of cotton garments while also providing substantially reduced degradation of the cotton fabric in the garment.
  • Cellulases are known in the art as enzymes that hydrolyze cellulose ( ⁇ -l,4-glucan linkages) thereby resulting in the formation of glucose, cellobiose, celloogisaccharide, and the like. While cellulases are produced in fungi, bacteria and the like, those produced by fungi have been given the most attention because fungi typically produce a complete cellulase system capable of degrading crystalline forms of cellulose and such cellulases can be readily produced in large quantities via fermentation procedures. In fact, as noted in "Methods in Enzymology M , 160. 25, pages 234 et seg.
  • a cellulase system produced by a given microorganism is comprised of several different enzyme components including those identified as exo-cellobiohydrolases (EC 3.2.1.91) (“CBH”), endoglucanases (EC 3.2.1.4) (“EG”) , ⁇ -glucosidase (EC 3.2.1.21) ( M BG H ) .
  • CBH exo-cellobiohydrolase
  • EG endoglucanases
  • M BG H ⁇ -glucosidase
  • T_. reesei which contains 2 CBHs, i.e., CBH I and CBH II, and at least 2 EGs, i.e., EG I and EG II.
  • the ratio of CBH I components to EG components (including all of the EG components) in naturally occurring cellulases does not exceed about 5:1.
  • CBH I components genetic Control of Environmental Pollutants, Gilbert S. Omenn Editor, Chapter — “Microbial Enzymes and Ligno- Cellulase Utilization", Hollaender Publishing
  • CBH I and CBH II derived from either T.. reesei or P.. funiculosum synergistically interact in solubilizing cotton fibers.
  • Shoemaker et al. Bio/Technology, October 1983, discloses that CBH I (derived from X. reesei) , by itself, has the highest binding affinity but the lowest specific activity of all forms of cellulose.
  • the substrate specificity and mode of action of the different cellulase components varies from component to component which may account for the synergy of the combined components.
  • the current accepted mechanism of cellulase action is that endoglucanase components first break internal ⁇ -l,4-glucosidic bonds in regions of low crystallinity of the cellulose thereby creating chain ends which are recognized by CBH components.
  • the CBH components bind preferentially to the non-reducing end of the cellulose to release cellobiose as the primary product.
  • ⁇ -Glucosidase components act on cellooligosaccharides, e.g., cellobiose, to give glucose as the sole product.
  • Cellulases are also known in the art to be useful in detergent compositions either for the purpose of enhancing the cleaning ability of the composition or as a softening agent. When so used, the cellulase will degrade a portion of the cellulosic material, e.g., cotton fabric, in the wash which in one manner or another facilitates the cleaning and/or softening of the cotton fabric. While the exact cleaning mechanism of cotton fabrics by cellulase is not fully understood, the cleaning of cotton fabrics by cellulase has been attributed to its cellulolytic activity. Thus, for instance, U.S. Patent No.
  • the present invention is directed to the discovery that detergent compositions containing cellulase compositions having enriched CBH I type cellulase components relative to the EG components provide excellent cleaning of cotton garments while at the same time having a reduced capability to degrade cotton fabrics.
  • the present invention is directed to detergent compositions comprising at least one surface active agent and a cleaning effective amount of a cellulase composition wherein said cellulase composition contains a weight ratio of CBH I type cellulase components to EG components of greater than about 5:1.
  • Such compositions are particularly useful as laundry detergents.
  • the present invention is directed to a method for enhancing the degradation resistance to cotton fabric of a detergent composition containing cellulase which comprises employing a cellulase composition containing a weight ratio of CBH I type cellulase components to EG components of greater than about 5:1.
  • the present invention generally relates to detergent compositions containing enriched CBH I type cellulase components relative to the EG components.
  • Such compositions possess excellent cleaning abilities while exhibiting reduced degradation potential against cotton fabrics relative to cellulase not enriched in CBH I type cellulase components.
  • the reduced degradation potential against cotton fabrics possessed by the compositions of this invention is surprising in view of the fact that the compositions contain enriched amounts of CBH I type cellulase components.
  • the presence of CBH is the distinguishing feature of cellulases that are able to degrade crystalline cellulose which in turn has been implicated in the degradation of cotton fabric.
  • the excellent cleaning properties of the compositions of this invention are also surprising because CBH I (derived from _. reesei) has been shown to have the lowest specific activity of all cellulase components derived from T_. reesei on all forms of cellulose.
  • Cellulase refers to the multi-enzyme system which acts on crystalline forms of cellulose and its derivatives to hydrolyze cellulose and give primary products, glucose and cellobiose.
  • Such cellulases are synthesized by a large number of microorganisms including fungi, actinomycetes, gliding bacteria (myxobacteria) and true bacteria.
  • Some microorganisms capable of producing cellulases useful in detergent compositions are disclosed in British Patent No. 2 094 826A, the disclosure of which is incorporated herein by reference. Most cellulases generally have their optimum activity in the acidic or neutral pH range.
  • alkaline cellulases i.e., cellulases showing optimum activity in neutral or alkaline media
  • Microorganisms producing alkaline cellulases are disclosed in U.S. Patent No. 4,822,516, the disclosure of which is incorporated herein by reference.
  • Other references disclosing alkaline cellulases are EPA Publication No. 269,977 and EPA Publication No. 265,832, the disclosures of which are also incorporated herein by reference.
  • Cellulase produced by a microorganism is known to be comprised of several enzyme classes (components) having different substrate specificity, enzymatic action patterns, molecular weights and degree of glycosylation, isoelectric points, etc.
  • enzyme classes include EGs, CBHs, BGs, etc.
  • EGs EGs
  • CBHs CBHs
  • BGs BGs
  • EGs CBHs
  • BGs BGs
  • EGs a specific EG produced by one microorganism will be different in primary amino acid sequence compared to EGs produced by other microorganisms, they may be classified similarly in terms of families based on sophisticated sequence comparison such as hydrophobic cluster analysis, substrate specificity, specific activity, and/or isoelectric point.
  • all EGs have similar underlying degradation properties against cellulose derivatives. See Henrissat et al..
  • EGs are related by their degradation mechanisms on cellulose and in particular on soluble cellulose derivatives. By definition, all reduce the viscosity of soluble cellulose derivatives. Accordingly, the present invention does not require the use of a cellulase derived from a specific microorganism. Moreover, EGs and CBHs produced by one microorganism may or may not behave synergistically with EGs and CBHs produced by another microorganism. See Wood, supra. Accordingly, in a preferred embodiment, the EG components employed in combination with the CBH I type cellulase components in the compositions of this invention are derived from the same microorganism. However, as noted above, the specific microorganism from which these co ponents are obtained is not critical to this invention.
  • Cellulase produced by a microorganism is sometimes referred to herein as a "cellulase system" to distinguish it from the classes and components of cellulase isolated therefrom.
  • cellulase systems can be produced either by solid or submerged culture, including batch, fed-batch and continuous-flow processes.
  • the collection and purification of the cellulase systems from the fermentation broth can also be effected by procedures known per se in the art.
  • Endoglucanase (“EG”) components refer to all of those components of cellulase which exhibit endoglucanase type activity; that is to say that such components hydrolyze soluble cellulose derivatives such as carboxymethylcellulose (CMC) , thereby reducing the viscosity of such solutions.
  • CMC carboxymethylcellulose
  • EGs readily hydrolyze hydrated forms of cellulose such as phosphoric acid swollen cellulose or Walseth cellulose and hydrolyze less readily the more highly crystalline forms of cellulose.
  • Such enzyme components act on internal regions of the polymer in more or less random manner resulting in a rapid decrease in polymer chain length together with a slow increase in the number of reducing ends.
  • the rapid decrease in chain length of the cellulose polymer is evidenced by the decrease in viscosity of a cellulose solution acted upon by EG components.
  • the viscosity of the solution is related to the molecular weight of the cellulose polymers. Accordingly, when the polymer is broken into two components, the viscosity necessarily decreases because of the decrease in molecular weight of the cellulosic polymer chain.
  • EGs have been previously referred to as CM-cellulases or C ⁇ cellulases.
  • Cellulases produced by microorganisms generally contain more than one EG component with as many as six or more components possible. This multiplicity is likely, in part, to be the result of artifacts in the purification methods.
  • the different components generally have different isoelectric points which allow for their separation via ion exchange chromatography and the like. In general, combinations of EG components will give a synergistic response in activity on cellulose as compared to the single components. Accordingly, the EG components employed in this invention can be either a single EG component or a combination of two or more EG components.
  • Exo-cellobiohydrolase refers to those components which exhibit exo-cellobiohydrolase activity; that is to say that such components degrade cellulose by hydrolyzing cellobiose from the non-reducing end of the cellulose polymer chains. It should be noted that cellobiose is a strong competitive inhibitor for CBH (K f approximately lmM) . CBH is further characterized by an inability to hydrolyze to any significant degree substituted celluloses, such as carboxymethylcellulose, etc. CBH, similar to EG, hydrolyzes phosphoric acid swollen cellulose or Walseth cellulose and to a lesser degree highly crystalline cellulose. CBHs have been previously referred to as C 1 cellulases.
  • CBH exhibits multiplicity and there are two CBHs from T. reesei, CBH I and CBH II.
  • CBH I type cellulase components refer to those components which exhibit similar cleaning performance as that exhibited by CBH I derived from T_. reesei when combined with EG components.
  • CBH I type cellulase components exhibit both similar cleaning performance and similar exo-cellobiohydrolase activity to that of CBH I derived from T. reesei; that is to say that such components have a strong binding affinity for cellulose fibers with no apparent preference for the non-reducing end, that is CBH I type activity binds strongly to all accessible regions of the cellulose and concomitantly has low hydrolytic activity.
  • such components can give up to 10% glucose as a secondary product with cellobiose being the primary product.
  • CBH II type cellulase components refer to those components which exhibit exo- cellobiohydrolase activity similar to that of CBH II derived from T. reesei; that is to say that such components act as true exo-cellobiohydrolase in binding and hydrolyzing cellulose from the non-reducing end of the cellulose polymer to give cellobiose as the sole product. Such components bind less strongly to cellulose and apparently only to the non-reducing ends and have a much higher hydrolytic rate as compared to CBH I type cellulase components. The rate of hydrolysis is greatly enhanced with the addition of BG which relieves inhibitory effects of cellobiose.
  • the cellulase composition employed in the detergent compositions of the present invention can contain CBH II type cellulase components in addition to CBH I type cellulase components and EG components.
  • the amount of CBH II type cellulase components is generally from about 0.001 to about 10 weight percent relative to the CBH I type cellulase component in the detergent compositions.
  • the cellulase composition contains no CBH II type cellulase components.
  • ⁇ -Glucosidase (BG) components refer to those components of cellulase which exhibit BG activity; that is to say that such components will act from the non-reducing end of cellobiose and other soluble eellooligosaccharides and give glucose as the sole product.
  • BG components do not adsorb or react with cellulose polymers. Furthermore, such BG components are competitively inhibited by glucose (K, approximately lmM) .
  • BG components are not literally cellulases because they cannot degrade cellulose, such BG components are included within the definition of the cellulase system because these enzymes facilitate the overall degradation of cellulose by further degrading the inhibitory cellulose degradation products (particularly cellobiose) produced by the combined action of CBH components and EG components. Without the presence of BG components, little hydrolysis of crystalline cellulose will occur.
  • BG components are often characterized on aryl substrates such as p-nitrophenol B-D-glucoside (PNPG) and thus are often called aryl-glucosidases. It should be noted that not all aryl glucosidases are BG components, in that some do not hydrolyze the natural substrate cellobiose.
  • PNPG p-nitrophenol B-D-glucoside
  • BG components produced by microorganisms can contain more than one BG component.
  • the different components generally have different isoelectric points which allow for their separation via ion exchange chromatography and the like. Because BG components degrade cellobiose which is known to inhibit the action of exo-cellobiohydrolases, such BG components can be included in the compositions of the present invention. If included, either a single BG component or a combination of BG components can be employed. When included in the detergent composition, the BG component is generally added in an amount sufficient to prevent inhibition of the CBH and particularly, CBH I type cellulase components, by cellobiose.
  • the amount of BG component added depends upon the amount of cellobiose produced in the detergent wash which can be readily determined by the skilled artisan. However, when employed, the weight percent of BG component relative to CBH I type cellulase components in the detergent composition is generally from about 0.2 to about 5 weight percent.
  • Degradation Resistant refers to the diminished capacity of a detergent composition containing a cellulase composition of this invention to degrade cotton fabric.
  • degradation of cotton fabric by a cellulase containing detergent is measured by the degree of thinning, weakening and/or tearing produced in the cotton fabric over a repeated number of washings with the cellulase containing detergent followed after each washing with drying in a mechanical dryer.
  • a mechanical dryer after washing facilitates this analysis insofar as the movement of the dryer during its operation stretches and pulls the garment, which, if substantially degraded, can result in tearing of the fabric.
  • the degradation resistance of detergent compositions containing the cellulase components as per this invention can be readily determined by measuring the degradation of identical sets of cotton clothing or cotton swatches after a repeated number of washing/drying cycles under identical conditions; one set being washed with the detergent composition of this invention, and the other being washed with a detergent composition containing a cellulase system (preferably produced from the same organism) having a ratio of CBH I type cellulase components to EG components of about 2.5:1. At the completion of at least 20 washing/drying cycles, the sets of cotton clothing are evaluated for degradation.
  • Degradation is measured by testing the tensile strength of each garment/swatch for each set and a summation of all of the ratings for each set is then divided by the number of garments/swatches in the set so as to provide an average tensile strength.
  • the term "degradation resistant" means that the average tensile strength after at least 20 washing/drying cycle for the set of garments/swatches treated with the detergent composition of this invention is significantly higher than the average tensile strength of the set of garments/swatches treated with a detergent composition containing the cellulase system described above.
  • the detergent compositions of this invention will result in at least a ten percent (10%) increase, and more preferably a twenty percent (20%) increase, in the average tensile strength for the set of garments/swatches treated with a detergent composition of this invention as compared to the average tensile strength of the set of garments/swatches treated with a detergent composition containing the cellulase system described above.
  • detergent compositions which employ a cellulase will be rendered degradation resistant if the cellulase employed in the detergent contains a weight ratio of CBH I type cellulase components to EG components of greater than about 5:1. More preferably, the weight ratio of CBH I type cellulase components to EG components is about 10:1 or more; even more preferably about 20:1 or more and still more preferably about 40:1 or more.
  • detergent compositions of this invention will also result in reduced harshness i.e., softening, of the washed garments.
  • the amount of cellulase and the ratio of CBH I type cellulase components to EG components employed in detergent compositions is the amount of cellulase and the ratio of CBH I type cellulase components to EG components employed in detergent compositions and not the relative rate of hydrolysis of the individual enzymatic components in producing reducing sugars from cellulose which imparts the improved cleaning of cotton garments.
  • CBH II type cellulase components do not substitute for CBH I type cellulase components (at the levels tested) in providing cleaning benefits when combined with EG components in detergent compositions.
  • the amount of the cellulase composition generally employed in the detergent compositions of this invention is an amount sufficient to impart improved cleaning of cotton garments.
  • the cellulase compositions are employed from about 0.002 weight percent to about 10 weight percent relative to the total detergent composition. More preferably, the cellulase compositions are employed from about 0.01 weight percent to about 5 weight percent relative to the total detergent composition.
  • the cellulase composition can be added to such detergent compositions either in a liquid diluent, or as granules, or as an emulsion. Such forms are well known to the skilled artisan.
  • the EG components and/or CBH II type cellulase components are primarily responsible for degrading cotton fabric.
  • EG components are required to provide the synergistic mixture of enzymes which results in improved cleaning.
  • the present invention is directed to the discovery that the desired increase in cleaning can be achieved by using a detergent composition containing only small amounts of EG component(s) , i.e., less than that found in cellulases naturally produced by microorganisms.
  • a detergent composition containing only small amounts of EG component(s) , i.e., less than that found in cellulases naturally produced by microorganisms.
  • Cellulase compositions having the requisite ratio of CBH I type cellulase components to EG components can be prepared by purifying the cellulase system into its components and then recombining the requisite amount of the components to achieve the desired ratio of components. In this manner, it is also possible to create cellulase compositions having little or no amounts of certain components, i.e., one can prepare a cellulase composition to be free of CBH II type cellulase components, or free of all EG components except either EG-I type cellulase components (i.e., an EG component having endoglucanase properties similar to EG-I derived from T.
  • EG-I type cellulase components i.e., an EG component having endoglucanase properties similar to EG-I derived from T.
  • the cellulase compositions employed in the detergent compositions of this invention will be free of CBH II type cellulase components.
  • CBH II type cellulase components when employed at the same levels as CBH I, do not significantly enhance the cleaning properties of the detergent composition when enriched relative to the EG components.
  • cellulase system employed to isolate the respective components is not critical, although certain cellulase systems may be preferred over others, i.e., an alkaline cellulase may be preferred over an acidic cellulase for use in laundry detergent compositions wherein the detergent wash solution is generally alkaline.
  • an acid cellulase can be used in a pre-washing step in the appropriate solution or at an intermediate pH where sufficient activity to provide cleaning benefits still exists.
  • the cellulase could be employed as a pre-soak either as a liquid or a spray, for example, as a spot remover.
  • Preferred cellulases for use in this invention are those obtained from Trichoderma reesei. T_. konin ii. Pencilium sp. , and the like. Certain cellulases are commercially available, i.e., CELLUCAST (available from Novo Industry,
  • the cellulase system can be purified into separate components by art recognized separation techniques including ion exchange chromatography at a suitable pH, affinity chromatography, size exclusion and the like.
  • ion exchange chromatography it is possible to separate the cellulase components by eluting with a pH gradient, or a salt gradient, or both a pH and a salt gradient.
  • cellulase systems having the requisite ratio of CBH I type cellulase components to EG components could be prepared by means other than isolation and recombination of the components.
  • many attempts to modify the fermentation conditions for a natural microorganism in order to give relatively high ratios of CBH to EG components have failed likely because CBH and EG components are coordinately regulated by the microorganism.
  • recombinant techniques such as gene disruption can alter the relative ratio of CBH I type cellulase component to EG components so as to produce a cellulase system having a relatively high ratio of CBH I type cellulase component to EG components.
  • the detergent compositions of this invention employ a surface active agent, i.e., surfactant, including anionic, non-ionic and ampholytic surfactants well known for their use in detergent compositions.
  • a surface active agent i.e., surfactant, including anionic, non-ionic and ampholytic surfactants well known for their use in detergent compositions.
  • Suitable anionic surfactants for use in the detergent composition of this invention include linear or branched alkylbenzenesulfonates; alkyl or alkenyl ether sulfates having linear or branched alkyl groups or alkenyl groups; alkyl or alkenyl sulfates; olefinsulfonates; alkanesulfonates and the like.
  • Suitable counter ions for anionic surfactants include alkali metal ions such as sodium and potassium; alkaline earth metal ions such as calcium and magnesium; ammonium ion; and alkanolamines having 1 to 3 alkanol groups of carbon number 2 or 3.
  • Ampholytic surfactants include quaternary ammonium salt sulfonates, betaine-type ampholytic surfactants, and the like. Such ampholytic surfactants have both the positive and negative charged groups in the same molecule.
  • Nonionic surfactants generally comprise polyoxyalkylene ethers, as well as higher fatty acid alkanolamides or alkylene oxide adduct thereof, fatty acid glycerine monoesters, and the like.
  • Suitable surfactants for use in this invention are disclosed in British Patent Application No. 2 094 826 A, the disclosure of which is incorporated herein by reference.
  • the surfactant is generally employed in the detergent compositions of this invention in an amount from about 1 weight percent to about 95 weight percent of the total detergent composition and preferably from about 5 weight percent to about 45 weight percent of the total detergent composition.
  • the detergent compositions of this invention can additionally contain the following components: Hydrolase except cellulase
  • Such hydrolases include carboxylate ester hydrolase, thioester hydrolase, phosphate monoester hydrolase, and phosphate diester hydrolase which act on the ester bond; glycoside hydrolase which acts on glycosyl compounds; an enzyme that hydrolyzes N-glycosyl compounds; thioether hydrolase which acts on the ether bond; and ⁇ -amino-acyl-peptide hydrolase, peptidyl- amino acid hydrolase, acyl-amino acid hydrolase, dipeptide hydrolase, and peptidyl-peptide hydrolase which act on the peptide bond.
  • carboxylate ester hydrolase, glycoside hydrolase, and peptidyl- peptide hydrolase Preferable among them are carboxylate ester hydrolase, glycoside hydrolase, and peptidyl- peptide hydrolase.
  • Suitable hydrolases include (1) proteases belonging to petidyl-peptide hydrolase such as pepsin, pepsin B, rennin, trypsin, chymotrypsin A, chymotrypsin B, elastase, enterokinase, cathepsin C, papain, chymopapain, ficin, thrombin, fibrinolysin, renin, subtilisin, aspergillopeptidase A, collagenase, clostridiopeptidase B, kallikrein, gastrisin, cathepsin D.
  • proteases belonging to petidyl-peptide hydrolase such as pepsin, pepsin B, rennin, trypsin, chymotrypsin A, chymotrypsin B, elastase, enterokinase, cathepsin C, papain, chymopapain
  • glycoside hydrolases (cellulase which is an essential ingredient is excluded from this group) ⁇ -amylase, ⁇ -amylase, gluco amylase, invertase, lysozyme, pectinase, chitinase, and dextranase.
  • glycoside hydrolases are o-amylase and ⁇ -amylase.
  • carboxylate ester hydrolase including carboxyl esterase, lipase, pectin esterase, and chlorophyllase. Especially effective among them is lipase.
  • Protease 200 "Enzyme L-W” (obtained from fungi, not from bacteria) (Miles Chemical Company, Elkhart, Ind.); “Rhozyme P-ll Cone”, “Pectinol”, “Lipase B”, “Rhozyme PF”, “Rhozyme J-25” (Rohm & Haas, Genencor, South San Francisco, CA) ; “Ambrozyme 200” (Jack Wolf & Co., Ltd., Subsidiary of Nopco Chemical Company, Newark,
  • the hydrolase other than cellulase is incorporated into the detergent composition as much as required according to the purpose. It should preferably be incorporated in an amount of 0.001 to 5 weight percent, and more preferably 0.02 to 3 weight percent, in terms of purified one.
  • This enzyme should be used in the form of granules made of crude enzyme alone or in combination with other components in the detergent composition. Granules of crude enzyme are used in such an amount that the purified enzyme is 0.001 to 50 weight percent in the granules. The granules are used in an amount of 0.002 to 20 and preferably 0.1 to 10 weight percent.
  • Such cationic surfactants and long-chain fatty acid salts include saturated or unsaturated fatty acid salts, alkyl or alkenyl ether carboxylic acid salts, ⁇ -sulfofatty acid salts or esters, amino acid-type surfactants, phosphate ester surfactants, quaternary ammonium salts including those having 3 to 4 alkyl substituents and up to 1 phenyl substituted alkyl substituents.
  • Suitable cationic surfactants and long-chain fatty acid salts are disclosed in British Patent Application No. 2 094 826 A, the disclosure of which is incorporated herein by reference.
  • the composition may contain from about 1 to about 20 weight percent of such cationic surfactants and long-chain fatty acid salts.
  • the composition may contain from about 0 to about 50 weight percent of one or more builder components selected from the group consisting of alkali metal salts and alkanolamine salts of the following compounds: phosphates, phosphonates, phosphonocarboxylates, salts of amino acids, aminopolyacetates high molecular electrolytes, non-dissociating polymers, salts of dicarboxylic acids, and aluminosilicate salts.
  • Suitable divalent sequestering gents are disclosed in British Patent Application No. 2 094 826 A, the disclosure of which is incorporated herein by reference.
  • the composition may contain from about 1 to about 50 weight percent, preferably from about 5 to about 30 weight percent, based on the composition of one or more alkali metal salts of the following compounds as the alkalis or inorganic electrolytes: silicates, carbonates and sulfates as well as organic alkalis such as triethanolamine, diethanolamine, monoethanolamine and trilsopropanolamine.
  • composition may contain from about 0.1 to about 5 weight percent of one or more of the following compounds as antiredeposition agents: polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone and carboxymethylcellulose.
  • a combination of carboxymethylcellulose or/and polyethylene glycol with the cellulase composition of the present invention provides for an especially useful dirt removing composition.
  • carboxymethylcellulose For removing the decomposition of carboxymethylcellulose by the cellulase in the detergent, it is desirable that carboxymethylcellulose is granulated or coated before the incorporation in the composition.
  • cellulase of the present invention in combination with a bleaching agent such as sodium percarbonate, sodium perborate, sodium sulfate/hydrogen peroxide adduct and sodium chloride/hydrogen peroxide adduct or/and a photo-sensitive bleaching dye such as zinc or aluminum salt of sulfonated phthalocyanine further improves the deterging effects.
  • a bleaching agent such as sodium percarbonate, sodium perborate, sodium sulfate/hydrogen peroxide adduct and sodium chloride/hydrogen peroxide adduct or/and a photo-sensitive bleaching dye such as zinc or aluminum salt of sulfonated phthalocyanine
  • bluing agents and fluorescent dyes may be incorporated in the composition, if necessary.
  • Suitable bluing agents and fluorescent dyes are disclosed in British Patent Application No. 2 094 826 A, the disclosure of which is incorporated herein by reference.
  • caking inhibitors may be incorporated in the powdery detergent:p- toluenesulfonic acid salts, xylenesulfonic acid salts, acetic acid salts, sulfosuccinic acid salts, talc, finely pulverized silica, clay, calcium silicate (such as Micro-Cell of Johns Manville Co.), calcium carbonate and magnesium oxide.
  • the cellulase composition of this invention are deactivated in some cases in the presence of copper, zinc, chromium, mercury, lead, manganese or silver ions or their compounds.
  • Various metal chelating agents and metal-precipitating agents are effective against these inhibitors. They include, for example, divalent metal ion sequestering agents as listed in the above item with reference to optional additives as well as magnesium silicate and magnesium sulfate.
  • Cellobiose, glucose and gluconolactone act sometimes as the inhibitors. It is preferred to avoid the co-presence of these saccharides with the cellulase as far as possible. In case the co-presence in unavoidable, it is necessary to avoid the direct contact of the saccharides with the cellulase by, for example, coating them.
  • Long-chain-fatty acid salts and cationic surfactants act as the inhibitors in some cases. However, the co-presence of these substances with the cellulase is allowable if the direct contact of them is prevented by some means such as tableting or coating.
  • the above-mentioned masking agents and methods may be employed, if necessary, in the present invention.
  • Cellulase-activators vary depending on variety of the cellulases. In the presence of proteins, cobalt and its salts, magnesium and its salts, and calcium and its salts, potassium and its salts, sodium and its salts or monosaccharides such as mannose and xylose, the cellulases are activated and their deterging powers are improved remarkably.
  • the antioxidants include, for example, tert- butyl-hydroxytoluene, 4,4'-butylidenebis(6-tert- butyl-3-methylphenol) , 2,2'-butylidenebis(6-tert- butyl-4-methylphenol) , monostyrenated cresol, distyrenated cresol, monostyrenated phenol, distyrenated phenol and l,l-bis(4- hydroxyphenyl)cyclohexane.
  • the solubilizers include, for example, lower alcohols such as ethanol, benzenesulfonate salts, lower alkylbenzenesulfonate salts such as p- toluenesulfonate salts, glycols such as propylene glycol, acetylbenzenesulfonate salts, acetamides, pyridinedicarboxylic acid amides, benzoate salts and urea.
  • lower alcohols such as ethanol
  • benzenesulfonate salts lower alkylbenzenesulfonate salts such as p- toluenesulfonate salts
  • glycols such as propylene glycol
  • acetylbenzenesulfonate salts acetamides
  • pyridinedicarboxylic acid amides pyridinedicarboxylic acid amides
  • the detergent composition of the present invention can be used in a broad pH range of from acidic to alkaline pH.
  • perfumes, preservatives, dyes and the like can be used, if desired, with the detergent compositions of this invention.
  • a detergent base used in the present invention is in the form of a powder, it may be one which is prepared by any known preparation methods including a spray-drying method and a granulation method.
  • the detergent base obtained particularly by the spray-drying method and/or spray-drying granulation method are preferred.
  • the detergent base obtained by the spray-drying method is not restricted with respect to preparation conditions.
  • the detergent base obtained by the spray-drying method is hollow granules which are obtained by spraying an aqueous slurry of heat-resistant ingredients, such as surface active agents and builders, into a hot space.
  • the granules have a size of from 50 to 2000 micrometers.
  • perfumes, enzymes, bleaching agents, inorganic alkaline builders may be added.
  • various ingredients may also be added after the preparation of the base.
  • the detergent base When the detergent base is a liquid, it may be either a homogeneous solution or an inhomogeneous dispersion.
  • CYTOLASE 123 cellulase a commercially available cellulase system (from Genencor, Inc., South San Francisco, CA) derived from Trichodermia reesei. was fractionated.
  • the normal distribution of cellulase components in this cellulase system is as follows:
  • the fractionation was done using columns containing the following resins: Sephadex G-25 gel filtration resin from Sigma Chemical Company (St. Louis, Mo) , QA Trisacryl M anion exchange resin and SP Trisacryl M cation exchange resin from IBF Biotechnics (Savage, Md) .
  • CYTOLASE 123 cellulase, 0.5g was desalted using a column of 3 liters of Sephadex G-25 gel filtration resin with 10 M sodium phosphate buffer at pH 6.8. The desalted solution, was then loaded onto a column of 20 ml of QA Trisacryl M anion exchange resin. The fraction bound on this column contained CBH I and EG I.
  • cellulase systems which can be separated into their components include CELLUCAST (available from Novo Industry, Copenhagen, Denmark) , RAPIDASE (available from Gist Brocades, N.V. , Delft, Holland) , and cellulase systems derived from T_. koningii, Penicillum sp. and the like.
  • Gloves are worn when handling swatches in order to avoid introducing any foreign components onto the swatches.
  • Label swatches include duplicates and controls Measure reflectance of each swatch
  • ratios of CBH I component to EG II component greater than 5:1 provide excellent cleaning of the cotton swatches at a level almost as good as ratios of CBH I component to EG II component of 5:1 or less.
  • a 50:1 ratio of CBH I component to EG II component provides about 91 percent of the cleaning ability of a 5:1 ratio of these two cellulase components.
  • the degradation potential of the detergent composition containing this cellulase composition is reduced relative to
  • detergent compositions containing cellulase compositions having greater amounts of EG components are provided.
  • Table II sets forth the increase in reflectance resulting from the use of a cellulase system derived from Trichodermia reesei in the procedure set forth above. As noted in Example 1 above, such cellulase has an approximate ratio of 2.5:1 of CBH I component to EG components (i.e., EG I plus EG II).
  • the detergent compositions of this invention provide excellent cleaning of cotton swatches at a level almost on par with detergent compositions containing a cellulase system.
  • the reflectance resulting from using 500 ppm CBH I component and 10 ppm EG II component in the above procedure was 56.85 (Table I) or about 86 percent of the reflectance resulting from using 500 ppm of the cellulase system.
  • This data further shows that excellent cleaning can be obtained in spite of the fact that a sizeable portion of the EG components have been removed from the composition.
  • Table III The results of this procedure are set forth in Table III below. This table indicates the increase in reflectance for cellulase compositions used in this procedure and which have the amounts of EG I and EG II components (comprised of equal amounts of EG I and EG II components) indicated by the x-axis and the amounts of CBH I component indicated by the y- axis.
  • a 10:1 ratio of CBH I component to EG components i.e., 100 ppm CBH I to 10 ppm EG I plus EG II
  • a 25:1 ratio of CBH I component to EG component i.e., 500 ppm CBH I to 20 ppm EG I plus EG II
  • the degradation potential of the detergent composition containing this cellulase composition is reduced relative to detergent compositions containing cellulase compositions having greater amounts of EG components.
  • Table III above, Table IV below sets forth the increase in reflectance resulting from the use of a cellulase system derived from Trichodermia reesei in the procedure set forth above. As noted in Example 1 above, such cellulase has an approximate ratio of 2.5:1 of CBH I component to EG components, i.e., EG I plus EG II.
  • the detergent compositions of this invention e.g., containing an enriched fraction of CBH I type cellulase component relative to the EG components
  • the detergent compositions of this invention are capable of providing a level of cleaning on par with a cellulase system in spite of the fact that a sizeable portion of the EG components have been removed from the composition.
  • CBH I type cellulase component and EG components could be substituted in place of CBH I component and EG I and II components employed in Examples II and III to provide a degradation resistant detergent composition having excellent cleaning.
  • Such CBH I type cellulase components can be obtained from T. koningii. Pencilium sp. and the like.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Professional, Industrial, Or Sporting Protective Garments (AREA)
  • Portable Nailing Machines And Staplers (AREA)
  • Nozzles For Electric Vacuum Cleaners (AREA)
EP90915577A 1989-10-19 1990-10-03 Abbaubeständige reinigungszusammensetzungen Expired - Lifetime EP0496783B1 (de)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US422814 1982-09-24
US42281489A 1989-10-19 1989-10-19
PCT/US1990/005618 WO1991005841A1 (en) 1989-10-19 1990-10-03 Degradation resistant detergent compositions

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EP0496783A1 true EP0496783A1 (de) 1992-08-05
EP0496783A4 EP0496783A4 (en) 1993-02-24
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US5320960A (en) * 1992-04-03 1994-06-14 Genencor International, Inc. Method of preparing solution enriched in xylanase using low molecular weight alcohol, organic salt and inorganic salt
US5688290A (en) * 1989-10-19 1997-11-18 Genencor International, Inc. Degradation resistant detergent compositions based on cellulase enzymes
CA2093422C (en) * 1990-10-05 2001-04-03 DETERGENT COMPOSITIONS CONTAINING LOW CBH I CONTENT CELLULASE COMPOSITIONS
US5290474A (en) * 1990-10-05 1994-03-01 Genencor International, Inc. Detergent composition for treating cotton-containing fabrics containing a surfactant and a cellulase composition containing endolucanase III from trichoderma ssp
US5328841A (en) * 1990-10-05 1994-07-12 Genencor International, Inc. Methods for isolating EG III cellulase component and EG III cellulase in polyethylene glycol using inorganic salt and polyethylene glycol
DK0551386T3 (da) * 1990-10-05 2004-05-10 Genencor Int Fremgangsmåde til behandling af bomuldsholdige stoffer med cellulase
US5650322A (en) * 1990-10-05 1997-07-22 Genencor International, Inc. Methods for stonewashing fabrics using endoglucanases
DE69133035T2 (de) * 1991-01-16 2003-02-13 The Procter & Gamble Company, Cincinnati Kompakte Waschmittelzusammensetzungen mit hochaktiven Cellulasen
US5520838A (en) * 1991-01-16 1996-05-28 The Procter & Gamble Company Compact detergent compositions with high activity cellulase
CA2107206A1 (en) * 1991-03-29 1992-09-30 Kathleen A. Clarkson Methods for treating cotton-containing fabrics with cellulase
EP0551408B2 (de) * 1991-06-11 2012-08-15 Genencor International, Inc. Cellulasezusammensetzungen mit einem defizit an komponenten des typs-cbh i enthaltende reinigungsmittelzusammensetzungen
US5352243A (en) * 1992-02-28 1994-10-04 Genencor International, Inc. Methods of enhancing printing quality of pigment compositions onto cotton fabrics
WO1993022414A1 (en) * 1992-05-01 1993-11-11 Genencor International, Inc. Degradation resistant detergent compositions based on cellulase enzymes
CA2134446A1 (en) * 1992-05-01 1993-11-11 Kathleen A. Clarkson Methods for treating cotton-containing fabrics with cbh i enriched cellulase
US6251144B1 (en) 1992-06-12 2001-06-26 Genencor International, Inc. Enzymatic compositions and methods for producing stonewashed look on indigo-dyed denim fabric and garments
WO1993025655A1 (en) * 1992-06-12 1993-12-23 Genencor International, Inc. Enzymatic compositions and methods for producing stonewashed look on indigo-dyed denim fabric
EP0702713B1 (de) * 1993-06-11 2002-01-30 Genencor International, Inc. Enzymatische verfahren und verwendung von enzymen zur herstellung von stone wash aussehen auf indigo gefärbtem gewebe
WO1998004663A1 (en) * 1996-07-30 1998-02-05 The Procter & Gamble Company Detergent composition comprising two cellulase components, with and without a cellulose-binding domain
MX2007008050A (es) * 2005-01-06 2007-08-21 Novozymes Inc Polipeptidos que tienen actividad de celobiohidrolasa y polinucleotidos que codifican para los mismos.

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JPH04507114A (ja) 1992-12-10
MX172884B (es) 1994-01-18
ATE132181T1 (de) 1996-01-15
WO1991005841A1 (en) 1991-05-02
CA2067162C (en) 2004-12-14
JPH0639597B2 (ja) 1994-05-25
CA2067162A1 (en) 1991-04-20
DE69024499D1 (de) 1996-02-08
FI921662A (fi) 1992-04-14
AU642437B2 (en) 1993-10-21
DE69024499T2 (de) 1996-07-11
DK0496783T3 (da) 1996-03-04
FI921662A0 (fi) 1992-04-14
EP0496783A4 (en) 1993-02-24
ES2084039T3 (es) 1996-05-01
AU6540990A (en) 1991-05-16

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