AU2002309359B2 - Treatment of animal hair fibers with modified proteases - Google Patents
Treatment of animal hair fibers with modified proteases Download PDFInfo
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- AU2002309359B2 AU2002309359B2 AU2002309359A AU2002309359A AU2002309359B2 AU 2002309359 B2 AU2002309359 B2 AU 2002309359B2 AU 2002309359 A AU2002309359 A AU 2002309359A AU 2002309359 A AU2002309359 A AU 2002309359A AU 2002309359 B2 AU2002309359 B2 AU 2002309359B2
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- protease
- treatment
- wool
- proteases
- fiber
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- 108091005804 Peptidases Proteins 0.000 title claims abstract description 44
- 239000004365 Protease Substances 0.000 title claims abstract description 40
- 239000000835 fiber Substances 0.000 title claims abstract description 39
- 102000035195 Peptidases Human genes 0.000 title claims abstract description 21
- 241001465754 Metazoa Species 0.000 title claims abstract description 19
- 238000011282 treatment Methods 0.000 title claims description 40
- 210000004209 hair Anatomy 0.000 title claims description 14
- 238000000034 method Methods 0.000 claims abstract description 53
- 210000002268 wool Anatomy 0.000 claims abstract description 26
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 23
- 238000009792 diffusion process Methods 0.000 claims abstract description 6
- 239000000126 substance Substances 0.000 claims abstract description 4
- 235000002198 Annona diversifolia Nutrition 0.000 claims abstract description 3
- 241000282836 Camelus dromedarius Species 0.000 claims abstract description 3
- 241000283707 Capra Species 0.000 claims abstract description 3
- 241000282842 Lama glama Species 0.000 claims abstract description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 claims abstract description 3
- 241001494479 Pecora Species 0.000 claims abstract description 3
- 210000000085 cashmere Anatomy 0.000 claims abstract description 3
- 210000000050 mohair Anatomy 0.000 claims abstract description 3
- 239000000243 solution Substances 0.000 claims description 18
- 229920000642 polymer Polymers 0.000 claims description 13
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 9
- 108060008539 Transglutaminase Proteins 0.000 claims description 5
- 239000007864 aqueous solution Substances 0.000 claims description 5
- 102000003601 transglutaminase Human genes 0.000 claims description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 5
- 108010022999 Serine Proteases Proteins 0.000 claims description 4
- 102000012479 Serine Proteases Human genes 0.000 claims description 4
- 239000004372 Polyvinyl alcohol Substances 0.000 claims description 3
- 108090000787 Subtilisin Proteins 0.000 claims description 3
- 238000010006 anti-felting Methods 0.000 claims description 3
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 229920002451 polyvinyl alcohol Polymers 0.000 claims description 3
- 241000187747 Streptomyces Species 0.000 claims description 2
- 230000001580 bacterial effect Effects 0.000 claims description 2
- 238000007385 chemical modification Methods 0.000 claims description 2
- 239000000463 material Substances 0.000 abstract description 3
- 239000004744 fabric Substances 0.000 description 11
- 235000004879 dioscorea Nutrition 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 239000008351 acetate buffer Substances 0.000 description 5
- 230000015556 catabolic process Effects 0.000 description 5
- 238000006731 degradation reaction Methods 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 238000009950 felting Methods 0.000 description 5
- 230000002797 proteolythic effect Effects 0.000 description 5
- 230000002255 enzymatic effect Effects 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 3
- 238000009832 plasma treatment Methods 0.000 description 3
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 description 2
- 229910021538 borax Inorganic materials 0.000 description 2
- 229910052801 chlorine Inorganic materials 0.000 description 2
- 239000000460 chlorine Substances 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 239000004328 sodium tetraborate Substances 0.000 description 2
- 235000010339 sodium tetraborate Nutrition 0.000 description 2
- 239000004753 textile Substances 0.000 description 2
- 238000010792 warming Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 239000000080 wetting agent Substances 0.000 description 2
- 108091005658 Basic proteases Proteins 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000011256 aggressive treatment Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000004043 dyeing Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000002657 fibrous material Substances 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000002952 polymeric resin Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229920003002 synthetic resin Polymers 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- 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
-
- 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
- D06M13/00—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment
- D06M13/10—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment with compounds containing oxygen
- D06M13/12—Aldehydes; Ketones
- D06M13/123—Polyaldehydes; Polyketones
-
- 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
- D06M2101/00—Chemical constitution of the fibres, threads, yarns, fabrics or fibrous goods made from such materials, to be treated
- D06M2101/02—Natural fibres, other than mineral fibres
- D06M2101/10—Animal fibres
-
- 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
- D06M2101/00—Chemical constitution of the fibres, threads, yarns, fabrics or fibrous goods made from such materials, to be treated
- D06M2101/02—Natural fibres, other than mineral fibres
- D06M2101/10—Animal fibres
- D06M2101/12—Keratin fibres or silk
-
- 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
- D06M2200/00—Functionality of the treatment composition and/or properties imparted to the textile material
- D06M2200/45—Shrinking resistance, anti-felting properties
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Engineering & Computer Science (AREA)
- Textile Engineering (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
- Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)
- Cosmetics (AREA)
Abstract
A method of treating fibers of animal origin (wool from sheep, cashmere, rabbit, mohair, llama, goat, camel, among others), characterised in that it consists of bringing the fiber into contact with a solution of modified proteases, bonded or not to other substances, in order to increase its molecular weight and reduce its diffusion inside the fiber. It is intended that the cuticle of the fiber be the only accessible part to the protease attack, thus allowing an increase in the resistance to shrinkage and anti-felt finishing, in comparison with untreated material.
Description
WO 03/097927 PCT/PT02/00008 -1-
DESCRIPTION
"TREATMENT OF ANIMAL HAIR FIBERS WITH MODIFIED PROTEASES" Field of the invention The cuticle layer of animal hair fibers presents a scaly structure when observed by microscopy. The felting or shrinkage of these fabrics is due to the overlapping of these scales that surround the cortex (inner part of the fiber), in wet processes with high mechanical agitation. The removal of the cuticle layer makes it possible to eliminate the tendency of the protein fibers of animal origin to shrink. One possibility of anti-felt treatment would be the application of proteolytic treatments for the removal of the cuticle layer. This kind of treatment has been extensively studied since the beginning of the 2 0 th century, but without great achievements.
The reasons for this are primarily due to the following factors: Hair fibers of animal origin have a very variable composition, which depends on origin, race, climate and animal feeding. This diversity of animal fibers induces various susceptibilities to proteolytic treatments.
More aggressive treatments to induce a uniform anti-felting behaviour in all the fibers consequently cause unacceptable loss of strength.
Recent studies indicate that the lack of reproducibility of the proteolytic treatments and the degradations caused by such treatments are due to the diffusion of the enzymes inside the animal fibers.
WO 03/097927 PCT/PT02/00008 -2- Background to the invention The most commonly used method to confer dimensional stability on articles made from animal hair fibers is the INS/CSIRO Chlorine/Hercosett, which comprises a strong acid chlorine treatment, followed by the application of a polymer resin. This process results in an increased degree of shrinking resistance, but has a number of drawbacks: poor feel, limited durability, difficulties in dyeing and, more importantly today, it generates environmentally damaging waste.
Several authors have suggested methods to reduce the shrinkage of animal fibers, such as wool for instance, which do not result in the release of substances that are harmful to the environment. Among such processes, there are the enzymatic ones, as well as benign chemical processes such as lowtemperature plasma treatments. Plasma treatment is a dry process, which involves treating wool fiber material with electric gas discharges (so-called plasma). At present, there are serious obstacles, such as costs, compatibility and capacity, to large-scale commercialisation of a plasma treatment process.
Several enzymatic methods have been used in the treatment of wool. The patent JP-A 51099196 describes a process to treat wool fabrics with alkaline proteases. The patent JP-A 3213574 describes a method for the treatment of wool with transglutaminase or a solution having this enzyme. The patent US 6051033 describes a method of wool or wool fiber treatment with a proteolytic enzyme and tranglutaminase. WO 98/27264 describes a method to reduce the shrinking of wool that consists of bringing the fiber samples into contact with a solution ofperoxidase or oxidase under adequate conditions for the enzymatic reaction with wool. The patent US 6099588 relates a method to improve shrink resistance that may result in improvements in feel, appearance -0 3- 00 3 0 O and felting, among others, by the application of proteolytic enzymes in an aqueous solution, after treatment with an alkaline solution containing alcohol.
The patent US 5.529.928 refers to a process for obtaining wool with anti-felt finishing, a soft feel and with shrink resistance using an initial chemical oxidation t followed by a treatment with protease and warming. The patent EP 134267 uses a similar process, treating the fiber with proteolytic enzymes in the presence of salt, after the initial oxidative treatment. The patent EP 3.58386 describes a method of wool treatment that consists of a proteolytic treatment and one of, or both, an oxidative treatment (such as NaOCI) and treatment with polymer.
The necessity of establishing environmentally friendly (Ecofriendly) methods with better performances than the industrial processes currently used, creates a need for new processes that give a good shrink resistance, softness, appearance and anti-pilling behaviour. Therefore, a new methodology of enzymatic treatment of animal hair fibers is presented here.
Summary of the invention This invention relates to a new enzymatic process of animal hair fiber treatment, in which the proteases are chemically modified in order to increase their molecular weight and therefore reduce their diffusion inside the fiber. The cuticle will be the only accessible part to the proteolytic attack, which allows for the improvement of one or more wool properties, including their felting and shrinking, without damaging the fiber's interior.
00 O The present invention provides the following items to (14):
O
z (1)A method of treating fibers of animal original which comprises bringing the fiber into contact with a solution of protease that is modified to 0 increase its molecular weight in order to reduce C( its diffusion inside the fiber, being intended that Sthe cuticle of the fiber be the only accessible M, 10 part to protease attack, thus allowing an increase Sin the resistance to shrinkage and anti-felt C1 finishing, in comparison with untreated material.
(2)An anti-felting method of treating animal hair fibres characterized by the contact of the animal hair fibre with a solution of protease that is chemically modified by glutaraldehyde and/or yaminopropyltriethoxysilane to increase its molecular weight in order to reduce its diffusion inside the fibre.
(3)The method of claim 1 or 2 wherein the protease is modified by glutaraldehyde.
The method according to item or wherein the fibres are wool fibres from sheep, cashmere, rabbit, mohair, llama, goat, camel.
(5)The method according to item or comprising treatment of the fibers simultaneously with a protease and transglutaminase or a protease and glutaraldehyde.
(6)The method according to item or wherein the protease is of bacterial origin.
The method according to item or wherein the protease is a serine protease.
(8)The method according to items wherein the serine protease is a Subtilisin Carslberg.
(9)The method according to item or wherein N:\Sydney\Cases\Patent\55000-55999\P55025.AU\S iP55025 Specification 2008-8-12.doc 6/11/08 00 O the amount of protease used per Kg of wool, fiber or hair is in the range of 1 to 1000g.
O (10) The method according to item wherein the transglutaminase is derived from 5 Streptoverticillium sp.
(11) The method according to item or wherein h a treatment bath with recoverable and reusable Sprotease solution is used, thus reducing the costs of the treatment and the production of effluents, i 10 with concomitant savings in water consumption.
S(12) The method according to item or wherein CI the proteases are linked to soluble polymers.
(13) The method according to item or wherein soluble polymers in aqueous solutions are used as supports in the chemical modification of proteases.
(14) The method according to item wherein soluble polymers in aqueous solutions such as polyvinyl alcohol or polymers with hydroxyl groups.
The methodologies used to increase the molecular weight of the enzymes are based on the utilisation of a soluble polymer with hydroxyl groups activated with Xaminopropyltrietoxysilane and/or glutaraldehyde. The N kSydneyCases\Paten\55000-55999\P55025 Specfication 2008-8-12doc 6/1108 WO 03/097927 PCT/PT02/00008 -4glutaraldehyde may subsequently bind to another polymer chain, forming a polymeric net, or to an available protein NH 2 group.
Detailed Description and Examples The method consists of the treatment of the proteic material with a solution of modified proteolytic enzymes. Commercially available proteases from Sigma (Subtilisin kind) were used.
Immobilisation was performed on a soluble polymer, polyvinyl alcohol (Sigma), of average molecular weight 70000-100000, using glutaraldehyde (Aldrich), y-aminopropyltrietoxysilane and/or borax (Sigma) and polyethylenglycol (Sigma) of 10000 of average molecular weight.
The polymer at 6% solution in distilled water was dissolved with warming and stirring, activated, and was then added to a 2% (v/v) glutaraldehyde solution. This solution was kept under stirring at room temperature, for 2 hours. After this time, the solution was dialysed in 0.1 M pH acetate buffer for 24 hours and then in 0.05 M pH 3.95 acetate buffer for hours.
The enzymatic preparation in the desired concentration was added to the resulting solution, together with PEG and borax (0.05 pIg/mL) in 0.1 M pH 5.0 acetate buffer, and kept under stirring for 8 hours at room temperature. This solution was kept at 4°C until use. The immobilisation procedure did not cause any significant loss in activity.
WO 03/097927 PCT/PT02/00008 Example 1: Treatment of pure wool fabric with proteases: Samples of pure merino wool fabric (like animal hair fiber) of about 12 cmx 12 cm (of about 3 grams each) were placed in a recipient containing a solution of proteases being chemically modified or not, in a relation of 1/20 The treatment was performed at 37C, for periods of time ranging from 4 to 48 hours. The samples were removed from the solution, washed and air-dried. They were then subjected to tests to evaluate possible damage caused during the treatment.
To evaluate the quality of the fabric and the degree of damage caused in the wool treatment process, a qualitative test based on Garner (Garner Textile Laboratory Manual, vol. 5 Fibres, 3 rd Edition, 1967) was used. It was verified that the modified proteases did not induce fiber degradation when compared with free proteases. The control treatment itself (010 mM pH acetate buffer) presents a level of degradation higher than that presented by the fibers treated with modified enzymes.
The tendency of the fabrics to shrink was verified by washing the fabrics (11 x 6 cm) three times in distilled water containing 50 PL of a wetting agent for 60 minutes, at 50°C and 20 rpm, and the shrinkage was measured by the variation of the specimen dimensions. It was verified that only the enzymatically treated fabrics did not induce a significant shrinkage.
A panel of 5 experts evaluated the feel and appearance of the wool fabric and verifyied an increase in the properties of the protease treated fabrics compared to the control fabric.
WO 03/097927 PCT/PT02/00008 -6- Example 2: Treatment of pure wool yarns with proteases: Similar studies were conducted in yams of merino wool using the following parameters: samples of pure wool yam were placed in a recipient containing a solution of proteases being chemically modified or not, in a ratio of 1/20 The treatment was conducted at 37°C, for periods of time ranging from 4 to 48 hours. The samples were removed from the solution, washed and air-dried. They were then subjected to tests to evaluate possible damage caused during treatment.
To evaluate the yam quality and the degree of damage caused in the treatment process of this fiber, a qualitative test based on Garner (Garner W., Textile Laboratory Manual, vol. 5 Fibres, 3 r d Edition, 1967) was used. It was verified that the modified protease treatment does not induce degradation when compared with free protease treatment. The control treatment (10 mM pH acetate buffer) presented a level of degradation higher than that presented by the fibers treated with the modified enzymes. Tensile strength tests were performed on wool yams, and it was verified that only the yarns treated with free proteases induced a significant loss of strength.
The tendency to shrink was verified by washing the wool yams three times in distilled water having 50 4xL of a wetting agent for 60 minutes, at and 20 rpm, and shrinkage was quantified by the visual verification of yarn felting. It was verified that only the enzymatically treated yams did not induce felting.
A panel of 5 experts evaluated the appearance of the yarns and verified a better appearance of the yarns treated with proteases, compared to the control yarns.
In the claims which follow and in the preceding description of the invention, except where the context requires otherwise due to express language or necessary implication, the word "comprise" or variations such as "comprises" or "comprising" is used in an inclusive sense, i.e. to specify the presence of the stated features but not to preclude the presence or addition of further features in various embodiments of the invention.
It is to be understood that a reference herein to a prior art document does not constitute an admission that the document forms part of the common general knowledge in the art in Australia or any other country.
N:kSydney\CaseskPatent\55000-55999kP55O25 AU\Specis\P55O25AU Specification 2008-8-12.doc 6/11/08
Claims (12)
- 2. An anti-felting method of treating animal hair fibres characterized by the contact of the animal hair fibre with a solution of protease that is chemically modified by glutaraldehyde and/or y-aminopropyltriethoxysilane to increase its molecular weight in order to reduce its diffusion inside the fibre.
- 3. The method of claim 1 or 2, wherein the protease is modified by glutaraldehyde.
- 4. The method according to claim 1 or 2, wherein the fibres are wool fibres from sheep, cashmere, rabbit, mohair, llama, goat, camel.
- 5. The method according to claim 1 or 2, comprising treatment of the fibers simultaneously with a protease and transglutaminase or a protease and glutaraldehyde.
- 6. The method according to claim 1 or 2, wherein the protease is of bacterial origin.
- 7. The method according to claim 1 or 2, wherein the protease is a serine protease.
- 8. The method according to claim 7, wherein the serine protease that is a Subtilisin Carslberg.
- 9. The method according to claim 1 or 2, wherein the amount of protease used per Kg of wool, fiber or hair is in the range of 1 to 1000g. N:SydneyXCasesIPatent'.550O-55999IP55025.AU SpeciskP55025 AU Spefication 2008-8-12.doc 7/11108 00 O 10. The method according to claim 5, wherein the transglutaminase is derived from O Streptoverticillium sp.
- 11. The method according to claim 1 or 2, wherein a treatment bath with recoverable and reusable protease solution is used, thus reducing the h costs of the treatment and the production of C effluents, with concomitant savings in water consumption. M 10 12. The method according to claim 1 or 2, wherein Sthe proteases are linked to soluble polymers. CI 13. The method according to claim 1 or 2, wherein soluble polymers in aqueous solutions are used as supports in the chemical modification of proteases.
- 14. The method according to claim 13, wherein the soluble polymers in aqueous solutions are polyvinyl alcohol or polymers with hydroxyl groups.
- 15. The method according to claim 1, wherein the modified protease is bonded to other substances.
- 16. The method according to claim 1 or 2, substantially as hereinbefore described with reference to any one of the Examples. N:\Sydney\Cases\Patent55000-55999\P55025.AU\Specis\P55025AU Specification 2008-8-12.doc 6/11/08
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PCT/PT2002/000008 WO2003097927A1 (en) | 2002-05-21 | 2002-05-21 | Treatment of animal hair fibers with modified proteases |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2002309359A1 AU2002309359A1 (en) | 2003-12-02 |
| AU2002309359B2 true AU2002309359B2 (en) | 2009-01-08 |
Family
ID=29546559
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2002309359A Ceased AU2002309359B2 (en) | 2002-05-21 | 2002-05-21 | Treatment of animal hair fibers with modified proteases |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US20060121595A1 (en) |
| EP (1) | EP1507919B1 (en) |
| AT (1) | ATE390506T1 (en) |
| AU (1) | AU2002309359B2 (en) |
| DE (1) | DE60225850T2 (en) |
| WO (1) | WO2003097927A1 (en) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI119700B (en) * | 2002-12-16 | 2009-02-13 | Suedwolle Gmbh & Co Kg | Industrial biotechnology finishing process of wool and wool textile manufactured by this process |
| PT104124B (en) * | 2008-07-04 | 2011-10-14 | Univ Do Minho | GENETICALLY MODIFIED PROTEOLYTIC ENZYME FOR THE TREATMENT OF ANIMAL FIBERS IN ORDER TO INCREASE THE RESISTANCE OF THE SAME TO THE ENCOLHIMENTO, RESPECTIVE PROCESS OF OBTAINATION AND APPLICATION |
| CN102243169B (en) * | 2011-04-25 | 2012-11-14 | 上海嘉麟杰纺织品股份有限公司 | A method for detecting the degree of wool damage |
| CN102978956A (en) * | 2012-10-31 | 2013-03-20 | 江南大学 | Wool fabric complex phosphoesterasum padding-room temperature rolling yarding anti-felting tidying craft |
| CN103046385B (en) * | 2012-12-24 | 2014-08-27 | 江阴兴吴呢绒科技有限公司 | Manufacturing technique for machine washable slubbing pure wool fabric |
| US9222216B2 (en) | 2014-04-09 | 2015-12-29 | University Of Calcutta | Methods for enzymatic treatment of wool |
| CN108149417B (en) * | 2018-02-23 | 2020-06-09 | 上海嘉芮实业有限公司 | Fulling method of wool knitted garment, manufacturing process of wool strong fulling knitted fabric comprising fulling method and product of wool strong fulling knitted fabric |
| CN109972390B (en) * | 2019-03-15 | 2020-02-07 | 江南大学 | Method for performing anti-felting finishing on wool fabric by using protease K |
| CN115748038A (en) * | 2022-11-24 | 2023-03-07 | 桐乡市华家那羊绒服饰有限公司 | Production process of graphene cashmere roving yarn |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH06341067A (en) * | 1993-04-12 | 1994-12-13 | Osaka Prefecture | Processing agent for fiber structure and processing process |
| WO1999060200A1 (en) * | 1998-05-20 | 1999-11-25 | Novo Nordisk Biochem North America, Inc. | A method for enzymatic treatment of wool |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH564031A5 (en) * | 1968-03-29 | 1975-07-15 | Anvar | |
| EP0799344A1 (en) * | 1994-12-21 | 1997-10-08 | Novo Nordisk A/S | A method for enzymatic treatment of wool |
| US6051033A (en) * | 1998-05-20 | 2000-04-18 | Novo Nordisk Brochem North America Inc. | Method for enzymatic treatment of wool |
| US6099588A (en) * | 1999-02-23 | 2000-08-08 | Novo Nordisk Biochem North America, Inc. | Method for treatment of wool |
-
2002
- 2002-05-21 AU AU2002309359A patent/AU2002309359B2/en not_active Ceased
- 2002-05-21 WO PCT/PT2002/000008 patent/WO2003097927A1/en not_active Ceased
- 2002-05-21 DE DE60225850T patent/DE60225850T2/en not_active Expired - Fee Related
- 2002-05-21 US US10/515,139 patent/US20060121595A1/en not_active Abandoned
- 2002-05-21 EP EP02736309A patent/EP1507919B1/en not_active Expired - Lifetime
- 2002-05-21 AT AT02736309T patent/ATE390506T1/en not_active IP Right Cessation
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH06341067A (en) * | 1993-04-12 | 1994-12-13 | Osaka Prefecture | Processing agent for fiber structure and processing process |
| WO1999060200A1 (en) * | 1998-05-20 | 1999-11-25 | Novo Nordisk Biochem North America, Inc. | A method for enzymatic treatment of wool |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1507919B1 (en) | 2008-03-26 |
| AU2002309359A1 (en) | 2003-12-02 |
| DE60225850D1 (en) | 2008-05-08 |
| US20060121595A1 (en) | 2006-06-08 |
| WO2003097927A1 (en) | 2003-11-27 |
| ATE390506T1 (en) | 2008-04-15 |
| DE60225850T2 (en) | 2009-02-05 |
| EP1507919A1 (en) | 2005-02-23 |
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