WO1993022428A1 - Methods for treating cotton-containing fabrics with cbh i enriched cellulase - Google Patents
Methods for treating cotton-containing fabrics with cbh i enriched cellulase Download PDFInfo
- Publication number
- WO1993022428A1 WO1993022428A1 PCT/US1993/004149 US9304149W WO9322428A1 WO 1993022428 A1 WO1993022428 A1 WO 1993022428A1 US 9304149 W US9304149 W US 9304149W WO 9322428 A1 WO9322428 A1 WO 9322428A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- cellulase
- components
- cbh
- type
- cotton
- Prior art date
Links
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- 239000002574 poison Substances 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 229920002239 polyacrylonitrile Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920000139 polyethylene terephthalate Polymers 0.000 description 1
- 239000005020 polyethylene terephthalate Substances 0.000 description 1
- ODGAOXROABLFNM-UHFFFAOYSA-N polynoxylin Chemical compound O=C.NC(N)=O ODGAOXROABLFNM-UHFFFAOYSA-N 0.000 description 1
- 229920006306 polyurethane fiber Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229940068984 polyvinyl alcohol Drugs 0.000 description 1
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 1
- 229920000915 polyvinyl chloride Polymers 0.000 description 1
- 239000004800 polyvinyl chloride Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000007639 printing Methods 0.000 description 1
- 239000002964 rayon Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000004627 regenerated cellulose Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000012260 resinous material Substances 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000009991 scouring Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000011083 sodium citrates Nutrition 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000005737 synergistic response Effects 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 229920002994 synthetic fiber Polymers 0.000 description 1
- 239000012209 synthetic fiber Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
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- 239000001993 wax Substances 0.000 description 1
- 230000003313 weakening effect Effects 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- RZLVQBNCHSJZPX-UHFFFAOYSA-L zinc sulfate heptahydrate Chemical compound O.O.O.O.O.O.O.[Zn+2].[O-]S([O-])(=O)=O RZLVQBNCHSJZPX-UHFFFAOYSA-L 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/02—After-treatment
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01091—Cellulose 1,4-beta-cellobiosidase (3.2.1.91)
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
-
- C11D2111/12—
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/911—Microorganisms using fungi
- Y10S435/945—Trichoderma
Definitions
- the present invention is directed to improved methods for treating cotton-containing fabrics with cellulase as well as to the fabrics produced from these methods.
- the improved methods of the present invention are directed to contacting cotton-containing fabrics with an aqueous solution containing a fungal cellulase composition which comprises a combination of exo-cellobiohydrolase I type components and endoglucanase components wherein the exo- cellobioh ⁇ drolase I type components are enriched relative to the endoglucanase type components.
- the resulting fabric possesses the expected enhancements in, for example, feel, appearance, and/or softening, etc., as compared to the fabric prior to treatment and the fabric also possesses reduced strength loss as compared to the fabric treated with a complete cellulase composition.
- cotton-containing fabrics can be treated with cellulase in order to impart desirable properties to the fabric.
- cellulase has been used to improve the feel and/or appearance of cotton- containing fabrics, to remove surface fibers from cotton-containing knits, for imparting a stone washed appearance to cotton-containing denims and the like.
- a common problem associated with the treatment of such cotton-containing fabrics with a cellulase solution is that the treated fabrics exhibit significant strength loss as compared to the untreated fabric. Strength loss arises because the cellulase hydrolyzes cellulose ( ⁇ -1 ,4-glucan linkages) which, in turn, can result in a breakdown of a portion of the cotton polymer. As more and more cotton polymers are disrupted (broken down), the tensile strength of the fabric is reduced.
- fungal sources of cellulase are known to secrete very large quantities of cellulase and further because fermentation procedures for such fungal sources as well as isolation and purification procedures for isolating the cellulase are well known in the art, it would be particularly advantageous to use such fungal cellulases in the methods for improving feel and/or appearance.
- the present invention is directed to the discovery that heretofore known methods for treating cotton-containing fabrics with fungal cellulases can be improved by employing a fungal cellulase composition enriched in CBH I type cellulase components relative to EG components.
- a cellulase composition which contains a weight ratio of CBH i type components to EG type components of greater than about 10:1 is capable of imparting enhancements to the treated fabric with regard to feel, appearance and softness, color enhancement, and/or a stone washed appearance as compared to fabric before treatment with such a cellulase composition.
- the cellulase composition employed to treat cotton-containing fabrics is tailored so as to contain sufficiently high concentrations of CBH I type components so as to be strength loss resistant.
- the present invention is directed to an improved method for the treatment of cotton-containing fabrics with a fungal cellulase composition
- said improvement comprises employing a fungal cellulase composition which comprises CBH I type cellulase components and EG type cellulase components wherein the protein weight ratio of CBH I type components to EG type components is greater than about 10:1.
- the cellulase composition employed herein comprises CBH I type components and one or more EG type components wherein said cellulase composition has a protein weight ratio of CBH I type components to all EG type components of greater than 20:1.
- the present invention is directed to an improved method for the treatment of cotton-containing fabrics with an aqueous fungal cellulase solution wherein said method is conducted with agitation of the cellulase solution, under conditions so as to produce a cascading effect of the cellulase solution over the fabric wherein said improvement comprises employing a fungal cellulase composition which comprises CBH I type components and one or more EG type components wherein said cellulase composition has a protein weight ratio of all CBH I type components to all EG type components of greater than 10:1.
- the fungal cellulase composition employed herein comprises CBH I type components and one or more EG type components wherein said cellulase composition has a protein weight ratio of CBH I type components to all EG type components of greater than 20:1.
- Cotton-containing fabrics treated by the methods of this invention have the expected enhancement(s) as compared to the fabric prior to treatment while exhibiting reduced strength loss as compared to the fabric treated with a complete cellulase composition.
- the reduced strength loss evidences that the methods of this invention are strength loss resistant.
- the present invention is directed to a cotton-containing fabric treated in the methods of this invention as defined above.
- FIG. 1 is an outline of the construction of p ⁇ CBH!pvr4.
- FIG. 2 is an outline of the construction of p ⁇ EGIpyrG-3.
- FIG. 3 illustrates deletion of the e ⁇ ll gene by integration of the Hindi!! fragment from p ⁇ EGIpyrG-3 at the e ⁇ ll locus on one of the T. reesei chromosomes.
- FIG. 4 is an outline of the construction of pA ⁇ EGII-1.
- the methods of this invention are improvements in prior art methods for treating cotton-containing fabrics with cellulase.
- the improvement comprises using a specific cellulase composition which imparts the desired enhancement(s) to the fabric while minimizing strength loss in the fabric.
- cotton-containing fabric refers to sewn or unsewn fabrics made of pure cotton or cotton blends including cotton woven fabrics, cotton knits, cotton denims, cotton yarns and the like.
- the amount of cotton in the fabric should be at least about 40 percent by weight cotton; preferably, more than about 60 percent by weight cotton; and most preferably, more than about 75 percent by weight cotton.
- the companion material employed in the fabric can include one or more non cotton fibers including synthetic fibers such as polyamide fibers (for example, nylon 6 and nylon 66), acrylic fibers (for example, polyacrylonitrile fibers), and polyester fibers (for example, polyethylene terephthalate), poly vinyl alcohol fibers (for example, Vinylon), poly vinyl chloride fibers, pol ⁇ vinylidene chloride fibers, polyurethane fibers, poly urea fibers and aramid fibers. It is contemplated that regenerated cellulose, such as rayon, could be used as a substitute for cotton in the methods of this invention.
- synthetic fibers such as polyamide fibers (for example, nylon 6 and nylon 66), acrylic fibers (for example, polyacrylonitrile fibers), and polyester fibers (for example, polyethylene terephthalate), poly vinyl alcohol fibers (for example, Vinylon), poly vinyl chloride fibers, pol ⁇ vinylidene chloride fibers, polyurethane fibers, poly urea fibers and aramid
- finishing means the application of a sufficient amount of finish to a cotton-containing fabric so as to substantially prevent cellulolytic activity of the cellulase on the fabric.
- Finishes are generally applied at or near the end of the manufacturing process of the fabric for the purpose of enhancing the properties of the fabric, for example, softness, drapability, etc., which additionally protects the fabric from reaction with cellulases.
- Finishes useful for finishing a cotton-containing fabric are well known in the art and include resinous materials, such as melamine, glyoxal, or ureaformaldehyde, as well as waxes, silicons, fiuorochemicais and quaternaries. When so finished, the cotton-containing fabric is substantially less reactive to cellulase.
- cellulase or “cellulase composition” refers to the enzyme composition derived from fungal sources or microorganisms genetically modified so as to incorporate and express all or part of the cellulase genes obtained from a fungal source (sometimes referred to a ("fungal cellulase composition").
- Cellulases act on cellulose and its derivatives to hydrolyze cellulose and give primary products, glucose and ceilobiose.
- Fungal cellulases are distinguished from cellulases produced from non-fungal sources including microorganisms such as actinomycetes, gliding bacteria (myxobacteria) and true bacteria. Fungi capable of producing cellulases useful in preparing cellulase compositions described herein are disclosed in British Patent No. 2 094 826A, the disclosure of which is incorporated herein by reference.
- cellulases generally have their optimum activity in the acidic or neutral pH range although some fungal cellulases are known to possess significant activity under neutral and slightly alkaline conditions, i.e., for example, cellulase derived from Humicola insole ⁇ s is known to have activity in neutral to slightly alkaline conditions.
- Cellulases are known to be comprised of several enzyme classifications having different substrate specificity, enzymatic action patterns, and the like. Additionally, enzyme components within each classification can exhibit different molecular weights, different degrees of glycosylation, different isoelectric points, different substrate specificity etc. For example, cellulases can contain cellulase classifications which include endoglucanases (EGs), exo- cellobioh ⁇ droiases (CBHs), /S-glucosidases (BGs), etc.
- EGs endoglucanases
- CBHs exo- cellobioh ⁇ droiases
- BGs /S-glucosidases
- a cellulase composition produced by a naturally occurring fungal source and which comprises one or more CBH and EG components wherein each of these components is found at the ratio produced by the fungal source is sometimes referred to herein as a "complete cellulase system" or a “complete cellulase composition” to distinguish it from the classifications and components of cellulase isolated therefrom, from incomplete cellulase compositions produced by bacteria and some fungi, or from a cellulase composition obtained from a microorganism genetically modified so as to overproduce, underproduce, or not produce one or more of the CBH and/or EG components of cellulase.
- 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 p_ ⁇ r se in the art.
- Endoglucanase (“EG) type components refer to all of those cellulase components or combination of components which exhibit textile activity properties similar to the endoglucanase components of
- Trichoderma reesei the endoglucanase components of Trichoderma reesei (specifically, EG I, EG II, EG 111, and the like either alone or in combination) impart improved feel, improved appearance, softening, color enhancement, and/or a stone washed appearance to cotton-containing fabrics (as compared to the fabric prior to treatment) when these components are incorporated into a textile treatment medium and the fabric is treated with this medium.
- endoglucanase type components are those fungal cellulase components which impart improved feel, improved appearance, softening, color enhancement, and/or a stone washed appearance to cotton-containing fabrics (as compared to the fabric before treatment) when these components are incorporated into a medium used to treat the fabrics and which impart reduced strength loss to cotton-containing fabrics as compared to the strength loss arising from treatment with a complete cellulase system derived from Trichoderma reesei.
- Such endoglucanase type components may not include components traditionally classified as endoglucanases using traditional biochemical activity tests.
- traditional activity tests are based on the ability of the component (a) to hydrolyze soluble cellulose derivatives such as carboxy methyicellulose (CMC), thereby reducing the viscosity of CMC containing solutions, (b) to readily hydrolyze hyd rated forms of cellulose such as phosphoric acid swollen cellulose (e.g., Walseth cellulose) and hydrolyze less readily the more highly crystalline forms of cellulose (e.g., Avicel, Solkafloc, etc.).
- CMC carboxy methyicellulose
- endoglucanase type components as those components of fungal cellulase which possess similar textile activity properties as possessed by the endoglucanase components of Trichoderma reesei.
- Cellulases can contain more than one EG type component.
- the different components generally have different isoelectric points, different molecular weights, different degrees of glycosylation, different substrate specificity, different enzymatic action patterns, etc.
- the different isoelectric points of the components allow for their separation via ion exchange chromatography and the like.
- the isolation of components from different fungal sources is known in the art. See, for example, Jrin et at., International Application WO 89/09259, Wood et al., Biochemistry and Genetics of Cellulose Degradation, pp. 31 to 52 (1988); Wood et al., Carbohydrate Research, Vol. 190, pp. 279 to 297 (1989); Hydrin, Methods in Enzymology, Vol. 160, pp. 234 to 242 (1988); and the like. The entire disclosure of each of these references is incorporated herein by reference.
- combinations of EG type components may give a synergistic response in improving softening, color retention/restoration and feel as compared to a singly EG type component.
- a single EG type component may be more stable or have a broader spectrum of activity over a range of pHs.
- the EG type components employed in this invention can be either a single EG type component or a combination of two or more EG type components.
- the EG type component may be derived from the same or different fungal sources. It is contemplated that EG type components can also be derived from bacterially derived cellulases.
- CBH type Exo-cellobiohydrolase type
- CBH type components refer to those fungal cellulase components which exhibit textile activity properties similar to CBH I and/or CBH II cellulase components of
- Trichoderma reesei when used in the absence of EG type cellulase components (as defined above), the CBH I and CBH II components of Trichoderma reesei alone do not impart any significant enhancements in feel, appearance, color enhancement and/or stone washed appearance to the so treated cotton-containing fabrics.
- concentration of EG type components approaches that of whole cellulase which has a ratio of about 2.5:1 enhanced strength loss occurs to the cotton-containing fabrics, as compared to cellulase compositions containing a ratio of CBH I type to EG type components of greater than 5:1.
- CBH I type components and CBH II type components refer to those fungal cellulase components which exhibit textile activity properties similar to CBH I and CBH II components of Trichoderma reesei. respectively.
- this includes the property of enhancing strength loss of cotton-containing fabrics when used in a ratio with EG type components of between 5:1 to 1 :5.
- the CBH l type components of Trichoderma reesei can impart an incremental cleaning benefit. Additionally, it is contemplated that the
- CBH II type cellulase components refer to those components which exhibit exocellobiohydrolase activity similar to that of CBH II derived from J ⁇ reesei. Accordingly, the cellulase composition employed in the compositions of the present invention can contain CBH II type cellulase components in addition to CBH I type cellulase components and EG components. When so employed, the amount of CBH II type cellulase components is generally from about 0.001 to about 30 weight percent relative to the CBH I type cellulase component in the compositions. However, in the preferred embodiment, the cellulase composition contains no CBH II type cellulase components.
- CBH II when employed at the same concentrations as CBH I, will not demonstrate the same cleaning benefits when combined with EG components that CBH I type cellulase components do. It is contemplated that CBH II may provide softening when combined with EG components.
- Trichoderma reesei Trichoderma reesei.
- such components (a) are competitively inhibited by cellobiose (K- approximately 1 mM); (b) are unable to hydrolyze to any significant degree substituted celluloses, such as carbox ⁇ methylcellulose, etc.; and (c) hydrolyze phosphoric acid swollen cellulose and to a lesser degree highly crystalline cellulose.
- cellobiose K- approximately 1 mM
- CBH components fungal cellulase components which are characterized as CBH components by such activity tests, will impart improved feel, appearance, softening, color enhancement, and/or a stone washed appearance to cotton-containing fabrics with minimal strength loss when used alone in the cellulase composition.
- exo-cellobiohydroiases as EG type components because these components possess similar functional properties in textile uses as possessed by the endoglucanase components of Trichoderma reesei.
- Fungal cellulase compositions enriched in CBH type components can be obtained by purification techniques.
- the complete cellulase system can be purified into substantially pure components by recognized separation techniques well published in the literature, including ion exchange chromatography at a suitable pH, affinity chromatography, size exclusion and the like.
- ion exchange chromatography usually anion exchange chromatography
- the requisite amount of the desired components could be recombined.
- Mixtures of cellulase components having the requisite ratio of CBH I type components to EG type cellulase components can 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 coordinated regulated by the microorganism.
- recombinant techniques as set forth in the Examples can alter the relative ratio of CBH I type components to EG type components so as to produce a mixture of cellulase components having a relatively high ratio of CBH I type components to EG type components.
- a preferred method for the preparation of cellulase compositions enriched in CBH type components is by genetically modifying a microorganism so as to be incapable of producing one or more EG type components and/or overproducing CBH I type components preferably without producing any heterologous protein.
- a requisite amount of the cellulase produced by such modified microorganism could be combined with the cellulase produced by the natural microorganism (i.e., containing EG type components) so as to provide for a cellulase composition containing CBH I type components and one or more EG type components wherein said cellulase composition has a protein weight ratio of CBH I type components to all EG type components of greater than 10:1.
- the deletion of the genes responsible for producing EG I type, EG Ii and/or EG III type cellulase components would have the effect of enriching the amount of CBH I components present in the cellulase composition.
- a requisite amount of one or more EG type components purified by conventional procedures can be added to a cellulase composition produced from a microorganism genetically engineered so as to be incapable of producing EG type components so as to achieve a specified ratio of CBH I type components to EG type components, i.e., a cellulase composition free of all EG type components so as to be enriched in CBH I type components can be formulated to contain 1 weight percent of an EG type component merely by adding this amount of a purified EG type component to the cellulase composition.
- ⁇ -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 cellooligosaccharides (“cellobiose”) and give glucose as the sole product.
- BG components do not adsorb onto or react with cellulose polymers. Furthermore, such BG components are competitively inhibited by glucose (K, approximately 1 mM). While in a strict sense,
- 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, moderate or 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 aryi-glucosidases. It should be noted that not all aryl giucosidases are
- BG components in that some do not hydrolyze cellobiose.
- the presence or absence of BG components in the cellulase composition can be used to regulate the activity of any CBH components in the composition. Specifically, because cellobiose is produced during cellulose degradation by CBH components, and because high concentrations of cellobiose are known to inhibit CBH activity, and further because such cellobiose is hydrolyzed to glucose by BG components, the absence of BG components in the cellulase composition will "turn-off" CBH activity when the concentration of cellobiose reaches inhibitory levels.
- one or more additives can be added to the cellulase composition to effectively "turn-off", directly or indirectly, some or all of the CBH I type activity as well as other CBH activity.
- a cellulase composition containing added amounts of BG components may increase overall hydrolysis of cellulase if the level of cellobiose generated by the CBH components becomes restrictive of such overall hydrolysis in the absence of added BG components.
- Fungal cellulases 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. Either a single BG component or a combination of BG components can be employed.
- the BG component When employed in textile treatment solutions, the BG component is generally added in an amount sufficient to prevent inhibition by cellobiose of any CBH and EG components, and particularly CBH I type cellulase components, by cellobiose.
- the amount of BG component added depends upon the amount of cellobiose produced in the textile composition which can be readily determined by the skilled artisan.
- the weight percent of BG component relative to any CBH type components present in the cellulase composition is preferably from about 0.2 to about 10 weight percent and more preferably, from about 0.5 to about 5 weight percent.
- Preferred cellulases for use in preparing the cellulase compositions used in this invention are those obtained from
- Trichoderma reesei Trichoderma konin ⁇ ii. Penicillium sp.. Humicola insolens. and the like.
- Certain cellulases are commercially available, i.e., CELLUCAST (available from Novo Industry, Copenhagen, Denmark), RAPIDASE (available from Gist Brocades, N.V., Delft, Holland), CYTOLASE 123 (available from Genencor International, South
- buffer refers to art recognized acid/base reagents which stabilize the cellulase solution against undesired pH shifts during the cellulase treatment of the cotton-containing fabric.
- cellulase activity is pH dependent. That is to say that a specific cellulase composition will exhibit cellulolytic activity within a defined pH range with optimal cellulolytic activity generally being found within a small portion of this defined range.
- the specific pH range for cellulolytic activity will vary with each cellulase composition. As noted above, while many cellulases will exhibit cellulolytic activity within an acidic to neutral pH profile, there are some cellulase compositions which exhibit DCiuioiytic activity in an alkaline pH profile.
- the pH of the initial cellulase solution could be outside the range required for cellulase activity. It is further possible for the pH to change during treatment of the cotton-containing fabric, for example, by the generation of a reaction product which alters the pH of the solution. In either event, the pH of an unbuffered cellulase solution could be outside the range required for cellulolytic activity. When this occurs, undesired reduction or cessation of cellulolytic activity in the cellulase solution occurs. For example, if a cellulase having an acidic activity profile is employed in a neutral unbuffered aqueous solution, then the pH of the solution may result in lower cellulolytic activity. On the other hand, the use of a cellulase having a neutral or alkaline pH profile in a neutral unbuffered aqueous solution should initially provide significant cellulolytic activity.
- the pH of the cellulase solution should be maintained within the range required for cellulolytic activity.
- One means of accomplishing this is by simply monitoring the pH of the system and adjusting the pH as required by the addition of either an acid or a base.
- the pH of the system is preferably maintained within the desired pH range by the use of a buffer in the cellulase solution.
- a sufficient amount of buffer is employed so as to maintain the pH of the solution within the range wherein the employed cellulase exhibits activity.
- the specific buffer employed is selected in relationship to the specific cellulase composition employed.
- the buffer(s) selected for use with the cellulase composition employed can be readily determined by the skilled artisan taking into account the pH range and optimum for the cellulase composition employed as well as the pH of the cellulase solution.
- the buffer employed is one which is compatible with the cellulase composition and which will maintain the pH of the cellulase solution within the pH range required for optimal activity.
- Suitable buffers include sodium citrate, ammonium acetate, sodium acetate, disodium phosphate, and any other art recognized buffers.
- Degradation resistant refers to the diminished capacity of a cellulase composition of this invention to degrade cotton fabric. In general, degradation of cotton fabric by a cellulase composition is measured by the degree of thinning, weakening and/or tearing produced in the cotton fabric.
- Degradation is measured by testing the tensile strength of each garment/swatch.
- the tensile strength of cotton-containing fabrics can be measured in a warp and fill direction which are at right angles to each other. Accordingly, the term "warp tensile strength” as used herein refers to the tensile strength of the cotton-containing fabric as measured along the length of the cotton-containing fabric whereas the term “fill tensile strength” refers to the tensile strength of the cotton- containing fabric as measured across the width of the cotton-containing fabric.
- the tensile strength of the resulting cotton-containing fabric treated with a cellulase solution is compared to its tensile strength prior to treatment with the cellulase solution so as to determine the strength reducing effect of the treatment. If the tensile strength is reduced too much, the resulting cotton-containing fabric will easily tear and/or form holes. Accordingly, it is desirable to maintain a tensile strength (both warp and fill) after treatment which is at least about 50% of the tensile strength before treatment.
- the tensile strength of cotton-containing fabrics is readily conducted following ASTM D1682 test methodology. Equipment suitable for testing the tensile strength of such fabrics include a Scott tester or an Instron tester, both of which are commercially available. In testing the tensile strength of cotton-containing fabrics which have been treated with cellulase solutions, care should be taken to prevent fabric shrinkage after treatment and before testing. Such shrinkage would result in erroneous tensile strength data.
- the CBH II component when employed at the same concentrations as CBH I, may provide softening.
- the CBH II component is substituted for the CBH I component, when softening is desired.
- the ratio of CBH I and CBH II components to EG components is preferably 10:1 and more preferably 20:1.
- the present invention is directed to the discovery that beneficial properties heretofore imparted to cotton-containing fabrics by whole cellulase or by cellulase containing substantial amounts of EG type components can also be imparted to cotton-containing fabrics by cellulase compositions containing some EG components albeit at a ratio of CBH I type components to EG type components of greater than 10:1 to 400:1 and preferably from greater than 10:1 to about 100:1. At higher ratios of CBH I type components to EG type components the beneficial effects of these cellulase compositions become more evident with repeated treatments. In addition, to imparting the desired beneficial properties, the cellulase compositions described herein achieve such beneficial properties with reduced strength loss.
- Enhancements to the cotton-containing fabric are achieved by those methods heretofore used.
- cotton-containing fabrics having improved feel can be achieved as per Japanese Patent Application Nos. 58-36217 and 58-54032, as well as Ohishi et al., "Reformation of Cotton Fabric by Cellulase” and JTN December 1988 journal article "What's New - Weight Loss Treatment to Soften the
- methods for improving both the feel and appearance of cotton-containing fabrics include contacting the fabric with an aqueous solution containing cellulase under conditions so that the solution is agitated and so that a cascading effect of the cellulase solution over the cotton-containing fabric is achieved.
- Such methods result in improved feel and appearance of the so treated cotton-containing fabric and are described in U.S. Serial No. 07/598,506, filed October 16, 1990 and which is incorporated herein by reference in its entirety.
- the treatment of the cotton-containing fabric with cellulase is conducted prior to finishing the cotton- containing fabric.
- the present invention is an improvement over prior art methods for treating cotton-containing fabrics insofar as the present invention employs a specific cellulase composition which minimizes strength loss in the treated fabric.
- the cellulase composition employed herein is a fungal cellulase composition which comprises a CBH I type components and EG type components wherein the cellulase composition has a weight ratio of CBH I type components to all EG type components of greater than 10:1.
- the use of the cellulase compositions described herein also result in fabric/color enhancement of stressed cotton- containing fabrics.
- the fabric can become stressed and when so stressed, it will contain broken and disordered fibers. Such fibers detrimentally impart a worn and dull appearance to the fabric.
- the so stressed fabric is subject to fabric/color enhancement. This is believed to arise by removal of some of the broken and disordered fibers which has the effect of restoring the appearance of the fabric prior to becoming stressed.
- these cellulase compositions may cause less redeposition of dye.
- the cellulase compositions described above are employed in an aqueous solution which contains cellulase and other optional ingredients including, for example, a buffer, a surfactant, a scouring agent, and the like.
- concentration of the cellulase composition employed in this solution is generally a concentration sufficient for its intended purpose. That is to say that an amount of the cellulase composition is employed to provide the desired enhancement(s) to the cotton-containing fabric.
- the amount of the cellulase composition employed is also dependent on the equipment employed, the process parameters employed (the temperature of the cellulase solution, the exposure time to the cellulase solution, and the like), the cellulase activity (e.g., a cellulase solution will require a lower concentration of a more active cellulase composition as compared to a less active cellulase composition), and the like.
- concentration of the cellulase composition can be readily determined by the skilled artisan based on the above factors as well as the desired effect.
- the concentration of the cellulase composition in the cellulase solution employed herein is from about 0.01 gram/liter of cellulase solution to about 50.0 grams/liter of cellulase solution; and more preferably, from about 0.05 grams/liter of cellulase solution to about 10.0 gram/liter of cellulase solution.
- the cellulase concentration recited above refers to the weight of total protein).
- the concentration of buffer in the aqueous cellulase solution is that which is sufficient to maintain the pH of the solution within the range wherein the employed cellulase exhibits activity which, in turn, depends on the nature of the cellulase employed.
- concentration of buffer employed will depend on several factors which the skilled artisan can readily take into account.
- the buffer as well as the buffer concentration are selected so as to maintain the pH of the cellulase solution within the pH range required for optimal cellulase activity. In general, buffer concentration in the cellulase solution is about 0.005 N and greater.
- the concentration of the buffer in the cellulase solution is from about 0.01 to about 0.5 N, and more preferably, from about 0.05 to about 0.15 N. It is possible that increased buffer concentrations in the cellulase solution may enhance the rate of tensile strength loss of the treated fabric.
- the cellulase solution can optionally contain a small amount of a surfactant in order to improve wettability.
- the amount of surfactant used is generally less than about
- Suitable surfactants include any surfactant compatible with the cellulase and the fabric including, for example, anionic, non-ionic and ampholytic surfactants.
- Suitable anionic surfactants for use herein 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 poiyoxyalkylene ethers, as well as higher fatty acid alkanoiamides or alkylene oxide adduct thereof, fatty acid glycerine monoesters, and the like.
- the liquor ratios i.e., the ratio of weight of cellulase solution to the weight of fabric, employed herein is generally an amount sufficient to achieve the desired enhancement in the cotton-containing fabric and is dependent upon the process used and the enhancement to be achieved.
- the liquor ratios are generally from about 0.1 :1 and greater, and more preferably greater than about 1 : 1 and even more preferably greater than about 10:1.
- Use of liquor ratios of greater than about 50:1 are usually not preferred from an economic viewpoint.
- Reaction temperatures for cellulase treatment are governed by two competing factors. Firstly, higher temperatures generally correspond to enhanced reaction kinetics, i.e., faster reactions, which permit reduced reaction times as compared to reaction times required at lower temperatures.
- reaction temperatures are generally at least about 30°C and greater.
- cellulase is a protein which loses activity beyond a given reaction temperature which temperature is dependent on the nature of the cellulase used. Thus, if the reaction temperature is permitted to go too high, then the cellulolytic activity is lost as a result of the denaturing of the cellulase.
- the maximum reaction temperatures employed herein are generally about 65 °C.
- reaction temperatures are generally from about 30 °C to about 65 °C; preferably, from about 35 °C to about 60°C; and more preferably, from about 35°C to about 50°C.
- Reaction times are generally from about 0.1 hours to about 24 hours and, preferably, from about 0.25 hours to about 5 hours.
- the cotton-containing fabrics treated in the methods described above using such cellulase compositions possess reduced strength loss as compared to the same cotton-containing fabric treated in the same manner with a complete cellulase composition.
- a concentrate can be prepared for use in the methods described herein.
- Such concentrates would contain concentrated amounts of the cellulase composition described above, buffer and surfactant, preferably in an aqueous solution.
- the concentrate can readily be diluted with water so as to quickly and accurately prepare cellulase solutions having the requisite concentration of these additives.
- such concentrates will comprise from about 0.1 to about 50 weight percent of a cellulase composition described above (protein); from about 10 to about 50 weight percent buffer; from about 10 to about 50 weight percent surfactant; and from about 0 to 80 weight percent water.
- aqueous concentrates When aqueous concentrates are formulated, these concentrates can be diluted by factors of from about 2 to about 200 so as to arrive at the requisite concentration of the components in the cellulase solution. As is readily apparent, such concentrates will permit facile formulation of the cellulase solutions as well as permit feasible transportation of the concentration to the location where it will be used.
- the cellulase composition as described above can be added to the concentrate either in a liquid diluent, in granules, in emulsions, in gels, in pastes, and the like. Such forms are well known to the skilled artisan.
- the cellulase composition is generally a granule, a powder, an agglomerate and the like.
- the granules are preferably formulated so as to contain a cellulase protecting agent. See, for instance, U.S. Serial No. 07/642,669, filed January 17, 1991 as Attorney Docket No. 010055-073 and entitled "GRANULES CONTAINING BOTH AN
- the granules can be formulated so as to contain materials to reduce the rate of dissolution of the granules into the wash medium. Such materials and granules are disclosed in U.S. Serial No. 07/642,596, filed on January 17, 1991 , as Attorney Docket No. GCS171-US1 and entitled “GRANULAR COMPOSITIONS", which application is incorporated herein by reference in its entirety.
- cellulase compositions described herein can additionally be used in a pre-wash and as a pre-soak either as a liquid or a spray. It is still further contemplated that the cellulase compositions described herein can also be used in home use as a stand alone composition suitable for enhancing color and appearance of fabrics. See, for example, U.S. Patent No. 4,738,682, which is incorporated herein by reference in its entirety.
- CYTOLASE 123 cellulase a commercially available cellulase system (from Genencor international, Inc., South San Francisco,
- the fractionation was done using columns containing the following resins: Sephadex G-25 gel filtration resin from Sigma Chemical Company (St. Louis, Missouri), QA Trisacryl M anion exchange resin and SP Trisacryl M cation exchange resin from IBF
- 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. konin ⁇ ii. Penicillium sp. and the like.
- the purpose of this example is to determine the softness effect of the cellulase composition in the absence of a surfactant.
- the washing machine (Unimac 50 lb. capacity, rotary drum) is filled with 9.5 gallons of cold water.
- the buffer 42 grams of citric aci anhydrous and 101 grams of sodium phosphate dibasic) are added to the washing machine.
- the temperature of the wash liquor is adjusted to 40°C and the test cellulase composition added. If required, the pH is adjusted to pH 5.0 by adding citric acid or sodium phosphate.
- Three 100% cotton terry towels, 25" x 46" are washed for 45 minutes at 37 rpm at 60-80°C and then extracted for 2 minutes at a maximum rpm o 460.
- the towels are rinsed in 24 gallons of water at 34°C for 5 minutes.
- the towels are again extracted for 2 minutes at a maximum rpm of 460.
- the towels are dried in a conventional drier for 50 minute on the high temperature setting of approximately 60-80°C.
- the towels are then labeled (to prevent panelists from ascertaining how the fabric had been treated) and tested for softness by a group of panelists by whole fabric feel and by mechanized test methods.
- the panelists evaluate the fabrics by a preference for "softer” and “rougher” fabric.
- the first set of fabrics analyzed is treated with an EG I and EG II deleted cellulase composition prepared from Trichoderma reesei genetically modified in a manner similar to that described below, so as to be incapable of expressing EG I and EG II.
- EG I and EG II comprises up to about 23 percent of the cellulase composition
- deletion of this component results in enriched levels of all of the CBH components.
- CBH I to EG ratio is about 12:1.
- the second set of fabrics analyzed are tested with a control solution which does not contain a cellulase composition.
- the EG l/ll deleted cellulase composition comprises a cellulase composition containing CBH I and EG components wherein the weight ratio of CBH I to EG components is at least 10:1.
- a cellulase composition comprising CBH I and EG components where the protein weight ratio of CBH I components to EG components is at least
- the pyr4 gene encodes orotidine-5'-monophosphate decarboxylase, an enzyme required for the biosynthesis of uridine.
- the toxic inhibitor 5-fluoroorotic acid (FOA) is incorporated into uridine by wild-type cells and, thus, poisons the cells.
- FOA 5-fluoroorotic acid
- cells defective in the oyr4 gene are resistant to this inhibitor but require uridine for growth. It is, therefore, possible to select for pyr4 derivative strains using FOA.
- spores of T. reesei strain RL-P37 (Sheir-Neiss, G. and Montenecourt, B.S., Appl. Microbial. Biotechnol., 20, p.
- a cbhl gene encoding the CBH I protein was cloned from the genomic DNA of T. reesei strain RL-P37 by hybridization with an oligonucleotide probe designed on the basis of the published sequence for this gene using known probe synthesis methods (Shoemaker et al.,
- the cbhl gene resides on a 6.5 kb Pstl fragment and was inserted into Pstl cut pUC4K (purchased from Pharmacia Inc., Piscataway, New Jersey) replacing the Kan r gene of this vector using techniques known in the art, which techniques are set forth in Maniati et al. (1989) and incorporated herein by reference.
- the resulting plasmid, pUC4K::cbh1 was then cut with Hindlll and the larger fragment of about 6 kb was isolated and relegated to give pUC4K::cbh1 ⁇ H/H (see FIG. 1 ). This procedure removes the entire cbhl coding sequence and approximately 1.2 kb upstream and 1.5 kb downstream of flanking sequences. Approximately, 1 kb of flanking
- the T. reesei pyr4 gene was cloned as a 6.5 kb Hindlll fragmen of genomic DNA in pUC18 to form pTpyr2 (Smith et al., 1991 ) following the methods of Maniatis et al., supra.
- the plasmid pUC4K::cbhl ⁇ H/H was cut with Hindlll and the ends were dephosphorylated with calf intestinal alkaline phosphatase. This end dephosphorylated DNA was iigated with the 6.5 kb Hindlll fragment containing the T. reesei pyr4 gene to give p ⁇ CBHloyr4.
- FIG. 1 illustrates the construction of this plasmid.
- Mycelium was obtained by inoculating 100 ml of YEG (0.5% yeast extract, 2% glucose) in a 500 ml flask with about 5 x 10 7 T. reesei GC69 spores (the oyr4 ' derivative strain). The flask was then incubated at 37°C with shaking for about 16 hours. The mycelium was harvested by centrifugation at 2,750 x g.
- the harvested mycelium was further washed in a 1.2 M sorbitol solution and resuspended in 40 ml of a solution containing 5 mg/ml Novozym R 234 solution (which is the trade name for a multicomponent enzyme system containing 1 ,3- alpha-glucanase, 1 ,3-beta-glucanase, laminarinase, xylanase, chitinase and protease from Novo Biolabs, Danbury, Connecticut); 5 mg/ml
- Example 5 200 ⁇ of the protoplast suspension prepared in Example 5 was added to 20 ⁇ of EcoRI digested P ⁇ CBHIPV ⁇ 4 (prepared in Example 4) in TE buffer (10 mM Tris, pH 7.4; 1 mM EDTA) and 50 ⁇ l of a polyethylene glycol (PEG) solution containing 25% PEG 4000, 0.6 M
- the T. reesei eol1 gene which encodes EG I has been cloned as a 4.2 kb Hindlll fragment of genomic DNA from strain RL-P37 by hybridization with oligonucieotides synthesized according to the published sequence (Pentilla et al., 1986, Gene, 45: 253-263; van Arsdell et al. f 1987, Bio/Technology, 5_: 60-64).
- This DNA fragment was inserted at the Hindlll site of pUCIOO.
- An internal 1 kb EcoRV fragment which extended from a position close to the middle of the EG I coding sequence to a position beyond the 3' end of the coding sequence was removed by enzyme digestion and was replaced by iigation with a 2.2 kb BamHl - Hindlll fragment containing the cloned A.
- ni ⁇ er PV ⁇ G gene Wang et al., 1988, Nucl. Acids Res., 16, p. 2339) to give p ⁇ EGIpyrG-3 (FIG. 2). Transformation of a oyr4 deficient strain of T.
- the eol3 gene encoding EG II (also referred to in the literature as EG III), was cloned from T. reesei strain RL-P37 as a 4 kb Pstl genomic DNA fragment by hybridization with oligonucleotides synthesized according to the published sequence (Saloheimo et al., 1988, Gene,
- This DNA fragment was inserted into the Pstl site of pUC18.
- This plasmid, pEGIl was subsequently digested with EcoRV to remove the entire EG Ii coding region on an approximately 2 kb segment extending from a position approximately 180 bp 5' of the EGII coding region to a position a few hundred base pairs beyond the end of the coding region.
- This segment was replaced with an Ssol fragment of Asper ⁇ illus nidulans genomic DNA containing the amdS gene (Corric et al., 1987, Gene, 53:63-71 ) to create plasmid PA ⁇ EG1I-1 (See FIG. 4).
- Wild-type strains of T. reesei are u ⁇ abie to grow on acetamide as a sole nitrogen source. Transformation with the amdS gene confers this ability and this is the basis for the selection system for transformants containing this gene.
- Protoplasts of strain ⁇ EGI-3 were transformed, by the methods described in Examples 5 and 6, with pA ⁇ EGII-1 which had been digested with Hindlll and EcoRI and transformants able to grow on acetamide were selected. Subsequently, DNA was extracted from stable transformants, digested with Pstl. subjected to agarose gel electrophoresis and blotted onto a membrane filter. The filter was hybridized with radiolabelled pA ⁇ EGII-1. Homologous integration of the Hindlll-EcoRI fragment from pA ⁇ EGII-1 , which contained e ⁇ !3 flanking regions and amdS. at the genomic eo!3 locus in a transformant lead to the 4 kb genomic Pstl fragment containing the e ⁇ !3 gene being replaced by smaller Pstl fragments including two which would be approximately
- strain ⁇ EG-1 This strain has deletions in both the EGI and EGII encoding genes and consequently is unable to produce either of these proteins.
Abstract
Description
Claims
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
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EP93910999A EP0640127A1 (en) | 1992-05-01 | 1993-05-03 | Methods for treating cotton-containing fabrics with cbh i enriched cellulase |
JP5519577A JPH07506404A (en) | 1992-05-01 | 1993-05-03 | Method of treating cotton-containing fabric with cellulase rich in CBH I |
AU42298/93A AU678356B2 (en) | 1992-05-01 | 1993-05-03 | Methods for treating cotton-containing fabrics with CBH I enriched cellulase |
FI945122A FI945122A (en) | 1992-05-01 | 1994-10-31 | Method of treating cotton fabrics with CBH I enriched cellulase |
Applications Claiming Priority (2)
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US87895092A | 1992-05-01 | 1992-05-01 | |
US07/878,950 | 1992-05-01 |
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WO1993022428A1 true WO1993022428A1 (en) | 1993-11-11 |
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PCT/US1993/004149 WO1993022428A1 (en) | 1992-05-01 | 1993-05-03 | Methods for treating cotton-containing fabrics with cbh i enriched cellulase |
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US (1) | US5668009A (en) |
EP (1) | EP0640127A1 (en) |
JP (1) | JPH07506404A (en) |
AU (1) | AU678356B2 (en) |
CA (1) | CA2134446A1 (en) |
FI (1) | FI945122A (en) |
WO (1) | WO1993022428A1 (en) |
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WO1996034945A1 (en) * | 1995-05-05 | 1996-11-07 | Röhm Enzyme Finland OY | Cellulase composition for treatment of cellulose-containing textile materials |
US5858767A (en) * | 1996-11-25 | 1999-01-12 | Rohm Enzyme Finland Oy | Cellulase composition for biofinishing cellulose-containing textile materials |
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US5874293A (en) * | 1996-11-25 | 1999-02-23 | Rohm Enzyme Finland Oy | Cellulase composition for treating cellulose-containing textile material |
US6184019B1 (en) | 1995-10-17 | 2001-02-06 | Röhm Enzyme Finland OY | Cellulases, the genes encoding them and uses thereof |
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-
1993
- 1993-05-03 CA CA002134446A patent/CA2134446A1/en not_active Abandoned
- 1993-05-03 EP EP93910999A patent/EP0640127A1/en not_active Ceased
- 1993-05-03 WO PCT/US1993/004149 patent/WO1993022428A1/en not_active Application Discontinuation
- 1993-05-03 JP JP5519577A patent/JPH07506404A/en active Pending
- 1993-05-03 AU AU42298/93A patent/AU678356B2/en not_active Ceased
-
1994
- 1994-10-31 FI FI945122A patent/FI945122A/en not_active Application Discontinuation
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1995
- 1995-03-09 US US08/401,126 patent/US5668009A/en not_active Expired - Lifetime
Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
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WO1991005841A1 (en) * | 1989-10-19 | 1991-05-02 | Genencor International, Inc. | Degradation resistant detergent compositions |
WO1992006183A1 (en) * | 1990-10-05 | 1992-04-16 | Genencor International, Inc. | Methods for treating cotton-containing fabrics with cellulase |
Non-Patent Citations (1)
Title |
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THE BIOCHEMICAL JOURNAL vol. 260, 1989, pages 37 - 43 THOMAS M. WOOD ET AL 'The mechanism of fungal cellulase action' * |
Cited By (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1995019989A1 (en) * | 1994-01-19 | 1995-07-27 | Pfizer Inc. | PORE FORMING PEPTIDES FROM $i(GEOLYCOSA RIOGRANDE) |
WO1996034945A1 (en) * | 1995-05-05 | 1996-11-07 | Röhm Enzyme Finland OY | Cellulase composition for treatment of cellulose-containing textile materials |
US6184019B1 (en) | 1995-10-17 | 2001-02-06 | Röhm Enzyme Finland OY | Cellulases, the genes encoding them and uses thereof |
US6723549B2 (en) | 1995-10-17 | 2004-04-20 | Ab Enzymes Oy | Cellulases, the genes encoding them and uses thereof |
US7273748B2 (en) | 1995-10-17 | 2007-09-25 | Ab Enzymes Oy | Cellulases, the genes encoding them and uses thereof |
US7323326B2 (en) | 1995-10-17 | 2008-01-29 | Ab Enzymes Oy | Cellulases, the genes encoding them and uses thereof |
US5858767A (en) * | 1996-11-25 | 1999-01-12 | Rohm Enzyme Finland Oy | Cellulase composition for biofinishing cellulose-containing textile materials |
US5874293A (en) * | 1996-11-25 | 1999-02-23 | Rohm Enzyme Finland Oy | Cellulase composition for treating cellulose-containing textile material |
US5866407A (en) * | 1997-03-18 | 1999-02-02 | Iogen Corporation | Method and enzyme mixture for improved depilling of cotton goods |
Also Published As
Publication number | Publication date |
---|---|
EP0640127A1 (en) | 1995-03-01 |
JPH07506404A (en) | 1995-07-13 |
AU4229893A (en) | 1993-11-29 |
CA2134446A1 (en) | 1993-11-11 |
FI945122A0 (en) | 1994-10-31 |
US5668009A (en) | 1997-09-16 |
AU678356B2 (en) | 1997-05-29 |
FI945122A (en) | 1994-10-31 |
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