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WO2009066785A1 - Fibre traitée et son procédé de fabrication - Google Patents

Fibre traitée et son procédé de fabrication Download PDF

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Publication number
WO2009066785A1
WO2009066785A1 PCT/JP2008/071282 JP2008071282W WO2009066785A1 WO 2009066785 A1 WO2009066785 A1 WO 2009066785A1 JP 2008071282 W JP2008071282 W JP 2008071282W WO 2009066785 A1 WO2009066785 A1 WO 2009066785A1
Authority
WO
WIPO (PCT)
Prior art keywords
treatment
fabric
fiber
protein
wheat protein
Prior art date
Application number
PCT/JP2008/071282
Other languages
English (en)
Japanese (ja)
Inventor
Mitsuo Ueda
Keiichi Yokoyama
Noriki Nio
Original Assignee
Ajinomoto Co., Inc.
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Ajinomoto Co., Inc. filed Critical Ajinomoto Co., Inc.
Priority to JP2009542615A priority Critical patent/JPWO2009066785A1/ja
Priority to EP08851101A priority patent/EP2213785A4/fr
Priority to CN200880116811A priority patent/CN101868575A/zh
Publication of WO2009066785A1 publication Critical patent/WO2009066785A1/fr
Priority to US12/766,005 priority patent/US20100203314A1/en

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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
    • D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
    • D06M15/01—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with natural macromolecular compounds or derivatives thereof
    • D06M15/15—Proteins or derivatives thereof
    • 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
    • Y10T—TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
    • Y10T428/00—Stock material or miscellaneous articles
    • Y10T428/249921—Web or sheet containing structurally defined element or component
    • 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
    • Y10T—TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
    • Y10T428/00—Stock material or miscellaneous articles
    • Y10T428/29—Coated or structually defined flake, particle, cell, strand, strand portion, rod, filament, macroscopic fiber or mass thereof
    • Y10T428/2913—Rod, strand, filament or fiber
    • Y10T428/2933—Coated or with bond, impregnation or core

Definitions

  • the present invention relates to a processed fiber using transdal protein, protein and peptide, and a method for producing the same.
  • the textile substrate for clothing was the last polyester that appeared in the 1950s, and no remarkable new fiber substrate has been developed since then. 1 9 ⁇ From the 0's onward, if there are insufficient properties of the fiber substrate itself, so-called fiber processing, such as spinning, is added, or a function is added later by chemical processing. ing. Improvements such as improving the wrinkle resistance of cotton, preventing shrinkage of wool, and chemically improving the shininess and sliminess of the surface of nylon and polyester are popular.
  • Transdalinase is one of the attractive enzymes that can satisfy the above-mentioned requirements. It binds dartamine and lysine residues in proteins, or incorporates primary amines into glutamine residues. It is an enzyme that catalyzes its action and is likely to be used in processing that acts on a polyamide-based fiber substrate and actively imparts new functions. In fact, in the field of textiles, several new processing methods have already been proposed that use transdermal taminase, mainly wool fibers.
  • transglutaminase catalyzes the reaction of binding glutamine and lysine, it is expected to act on fiber substrates with glutamine and lysine residues, or similar residues.
  • treatment with transglutaminase with wool as a target has been found to have effects such as cross-linking of glutamine and lysine residues in the wool substrate by enzyme-catalyzed reactions, increasing the strength of the wool.
  • the above-mentioned action is a new function-imparting process that cannot be expected with the use of cellulose hydrolase and protein hydrolase, which have been studied for practical use so far. It can be done.
  • the processing as described above requires that the fiber substrate has both glutamine and lysine residues at the same time, and the applicable fiber substrate is limited to some natural fibers such as wool.
  • Polyamide fibers other than wool such as silk and naiguchi, do not have sufficient amounts of dartamine and lysine residues or similar residues that transdaltaminase acts on. Even if it is done, a crosslinking reaction cannot be expected. In order to expect a binding or cross-linking reaction to such a substrate using transdal eveningase, it is necessary to add a third component having many reactive residues that are insufficient. For example, taking a silk fiber substrate as an example, silk contains very little lysine and dartamine residues. Therefore, even if it is treated as it is with transdal evening minase, the possibility of mutual reaction is low.
  • the present invention has been made in view of such a current situation, and eliminates the disadvantages of the background technology, and provides a fiber having excellent strength and water absorption and washing durability with a simple and low cost.
  • the object is to provide a method of manufacturing.
  • the present inventors have found a method of using a wheat protein partial hydrolyzate and arrived at the present invention. That is, the present invention is as follows.
  • a method for producing a processed fiber product characterized in that after the wheat protein partial hydrolyzate is adhered to the fiber surface, koji langle gluteinase is allowed to act.
  • the wheat protein partial hydrolyzate means a product obtained by partially hydrolyzing wheat dartene protein with an enzyme, acid, alkali, etc., and is not hydrolyzed wheat protein, Protein hydrolysates that have undergone excessive hydrolysis to amino acids are not included.
  • Commercially available enzyme-partially hydrolyzed wheat gluten protein for example, DMV WG E80G PU
  • DMV WG E80G PU can be used as it is, or it can be prepared by degrading wheat gluten with an appropriate proteolytic enzyme.
  • acid partially hydrolyzed wheat barley dulten protein and al force partially hydrolyzed wheat gluten protein can also be used.
  • the average molecular weight of the wheat protein partial hydrolyzate is preferably 7 0 0 to 50 0, 0 0 0 Da, more preferably 3, 0 0 0 to 4 0, OOOD a A range of about 5, 0 0 0 to 3 0, 0 0 0 Da is particularly preferable.
  • the method for attaching the wheat protein partial hydrolyzate to the fiber surface is not particularly limited.
  • the fiber is immersed in a solution obtained by dissolving or dispersing the wheat protein partial hydrolyzate in a solvent such as water, or
  • a wheat protein partial hydrolyzate may be present in either the single fiber filaments of the yarn bundles forming the fibers or in the gaps and surfaces of the staples. It only has to be fixed or coated on a bundle of single fiber filaments or staples.
  • the concentration of the physical solution is preferably 1 to 30 g ZL, and more preferably 3 to 10 g ZL in terms of cost and workability.
  • the amount of the wheat protein partial hydrolyzate adhered to the fiber surface is preferably 0.1 to 3 g per 1 g of fiber, and more preferably 0.3 to 1 g in terms of cost and workability.
  • Transdalinase used in the present invention (hereinafter sometimes referred to as TG) is an acyltransferase belonging to EC 2.3.2.13, and is used in proteins and peptides. It is an enzyme that has the activity of catalyzing the acyl transfer reaction using a residue as a donor and a lysine residue as an acceptor.
  • sources such as mammals, fish, and microorganisms.
  • the enzyme used in the present invention may be any enzyme having this activity, and any origin may be used. It may also be a recombinant enzyme. Examples thereof include those derived from microorganisms such as actinomycetes (see Japanese Patent No.
  • Microbial-derived transdalase minase commercially available from Ajinomoto Co., Inc. under the trade name “Activa” TG is an example of a transglutaminase used in the present invention.
  • Transdaltaminase is allowed to act by immersing the fiber in a solution containing wheat protein partial hydrolyzate and TG, or by immersing the fiber in a wheat protein partial hydrolyzate solution and then TG solution.
  • An example of this is the method of immersing in From the viewpoint of the enzymatic reactivity and stability of TG, ⁇ ⁇ ⁇ is preferably from 4 to 12, and more preferably from 5 to 8, in the solution containing TG of the wheat protein partial hydrolyzate and TG.
  • the reaction time of the enzyme is not particularly limited as long as the enzyme can act on the substrate substance. It may be very short or may be allowed to act for a long time. Minutes to 24 hours are preferred.
  • the reaction temperature may be any temperature as long as the enzyme maintains its activity, but it is preferable to operate at a temperature of 0 to 80 as a realistic temperature.
  • the optimal addition amount of TG is a solution containing a partial hydrolyzate of wheat protein and TG, or the TG concentration in the TG solution is 10 to 300 UZL, preferably 100 to 300 UZL, more preferably 100-300 UZL, is appropriate, but can be appropriately adjusted depending on the type of fiber, TG reaction time, TG reaction temperature, and the like. Even if it exceeds 3 0 0 0 UZL, there is an effect, but it is not worth the cost.
  • the amount of TG added is preferably 1 to 300 U for 1 g of fiber, and preferably 1 to 300 U for 1 g of wheat protein partial hydrolyzate. It can be adjusted as appropriate.
  • benzyloxycarbonyl-L-Dal Yuminuriguri The reaction was carried out using syn and hydroxylamine as substrates, and the resulting hydroxamic acid was formed into an iron complex in the presence of trichloroacetic acid, and then the absorbance at 525 nm was measured, and the amount of hydroxamic acid was determined by a calibration curve. Calculate the activity.
  • the amount of enzyme that produces 1 mol of hydroxamic acid per minute at 37, pH 6.0 was defined as 1 U.
  • the processed fiber according to the present invention refers to natural fibers such as wool, silk, and cotton, synthetic fibers such as nylon, polyester, and acrylic, and those made by blending, blending, and blending of these.
  • Protein fibers such as wool and silk, and polyamide fibers such as naydon have a transglutaminase reaction, and their terminal amino groups are also involved in cross-linking. improves.
  • Example 1 The following examples further illustrate the present invention. The present invention is not limited in any way by these examples. Example 1
  • Glutamine peptide A Wheat dartene protein partial hydrolyzate, DM V WG E 80 G P U (average molecular weight 9, 65 50 D)
  • Dartamine peptide B Wheat dartene protein partial hydrolyzate B: D MV WGE 80 GPA (average molecular weight 6 60 0 D)
  • Gelatin A Kishida Chemical's cow-derived Al-powered gelatin
  • Enzyme activity 100 g unit / g silk fabric UIS L 0803 silk 2-1 attached white fabric, double flat) Exhaust treatment was performed for 1 hour each at 40 in 100 ml of an aqueous solution containing the same amount (lg) of lumine peptide (A and B) and gelatin A, respectively. Then, after drying the silk fabric after the glutamine peptide and gelatin exhaustion treatment, in 100 ml Tris-HCl buffer (pH 7) containing 10 mg of transglutaminase (100 U / L), 40 t: 1 hour Enzyme treatment was performed and dried (as a control, TG treatment was also performed on silk fabric that was not subjected to protein exhaustion treatment).
  • the tear strength of the silk fabric after the treatment was measured by the pendulum method in accordance with JIS L 1096, and the tear strength (unit: 2 uton N) in the direction of cutting the warp was measured. Further, in order to examine how much the strength of the silk fabric by the above treatment is affected by repeated washing with water, the silk fabric after the above treatment was stirred for 10 minutes with a stirrer at 40 liters of distilled water at 40 liters. The washing process was repeated 3 times. Then, after the fabric was dried, the tear strength was measured by the same method as described above.
  • Glutamine peptide C Wheat dartene protein partial hydrolyzate, SWP 5 00 0 (molecular weight estimated from S D S—P AGE 5, 0 0 0 to 3 0, 0 0 0 D)
  • Daltamin peptide D Wheat dartene protein partial degradation product, self-made (average molecular weight 3, 0 0 0 D)
  • Glutamine Peptide E Wheat Dalten Protein Partial Degradation Product, Katayama Chemical Research Institute Dalpearl 30 (acid, alkaline hydrolysis, molecular weight 40, 0 0 0 to 50, 0 0 0 D)
  • wheat dartene was partially hydrolyzed with a protease (Bacillus amiguchi liquifaciens MRP protein) to a mean molecular weight of 300 D. After the completion of the reaction, insoluble materials were removed, and powder was prepared by drying with spray dry.
  • protease Bacillus amiguchi liquifaciens MRP protein
  • Table 3 shows the results. With regard to protein concentration, a remarkable effect was obtained at 1 gZL or higher, and the tear strength increased significantly as the concentration increased. With regard to the transdermal concentration, a significant increase in tear strength was confirmed at all concentrations tested. Table 3 Effect of protein concentration and transdal concentration on silk fiber strength
  • Polyester fabric JIS L 0803 'white fabric with polyester
  • glutamine peptide A or gelatin A in 100 ml of an aqueous solution containing the same amount (lg) of each as the weight of the fabric at 40 ° C for 1 hour each. Exhaust treatment was performed. Then, after drying the polyester fabric after the glutamine peptide A and gelatin A exhaustion treatment, in 100 ml of Tris-HCl buffer (pH 7) containing 10 mg of transdaltaminase (10 0 UZL), 40, 1 hour, TG treatment was performed and dried (as a control, polyester fabric that had not been subjected to protein exhaustion treatment was also subjected to enzyme treatment).
  • the tear strength of the polyester fabric after the treatment was measured by the pendulum method according to HS L 1096, and the tear strength (unit: Newton N) in the direction of cutting the warp was measured. Further, in order to evaluate the change in surface hydrophilicity of the fabric after the treatment, a water absorption test based on the HS L 1907 dropping method was conducted. In this dripping method, the water drop infiltration area (unit: cm2) after 1 minute of water dripping was measured. Further, In order to investigate how much the surface hydrophilicity of the polyester fabric by the above treatment is affected by repeated washing, the fabric after the above treatment is subjected to the JISL 0844 A-2 method (40 t: 5 g / detergent).
  • a repeated washing test was conducted according to the conditions of stirring (42 rpm, 30 minutes). Repeated washing was performed with the detergent added for the first time and without detergent for the second time. Then, after the washed fabric was dried, the surface hydrophilicity was measured by the same method as described above.
  • the tear resistance of the polyester fabric exhausted with dartamine peptide A was improved.
  • the polyester fabric exhausted with glutamine peptide A and gelatin A has a significantly improved surface hydrophilicity, but only the glutamine peptide retains the surface hydrophilicity after the washing test. . It was confirmed that surface hydrophilicity was improved even after washing by attaching glutamine peptide A to the polyester surface and allowing TG to act.
  • the only drawback of polyester is that it does not absorb water (sweat), and in order to compensate for this drawback, it is often blended with cotton. It was suggested that the disadvantages of polyester could be improved.
  • Nylon fabric (white cloth attached to JIS L 0803 nylon) Each lg was collected and exhausted for 1 hour each at 40 in 100 ml of an aqueous solution containing the same amount (lg) of glutamine peptide A or gelatin A as the weight of the fabric. Went. Then, after drying the nylon fabric after the glutamine peptide A and gelatin A exhaustion treatment, 100 ml of salmon squirrel containing 10 mg of transdaltaminase. In hydrochloric acid buffer (PH7) (100 UZL), 40 hours, 1 hour TG treatment was performed and dried (as a control, enzyme treatment was also applied to a knitted fabric not subjected to protein exhaustion treatment).
  • PH7 hydrochloric acid buffer
  • the tear strength of the nylon fabric after the treatment was measured by the pendulum method according to nSL 1096, and the tear strength (unit: Newton N) in the direction of cutting the warp was measured. Further, in order to evaluate the change in surface hydrophilicity of the fabric after the treatment, a water absorption test based on the HS L 1907 dropping method was conducted. In this dripping method, the water drop infiltration area (unit: cm2) 1 minute after water dripping was measured. Furthermore, in order to investigate how much the surface hydrophilicity of the nylon fabric treated by the above treatment is affected by repeated washing, the treated fabric was subjected to the JIS L 0844 A-2 method (40, detergent 5 g / A repeated washing test was conducted according to the conditions of stirring (42 rpm, 30 minutes). Repeated washing is performed with detergent added at the first time. The second time was performed without detergent. Then, after the washed fabric was dried, the surface hydrophilicity was measured by the same method as described above.
  • the nylon fabric that was exhausted with glutamine peptide A and gelatin A had improved tear strength.
  • the polyester fabric that was exhausted with glutamine peptide A and gelatin A showed the ability to improve surface hydrophilicity.
  • Glutamine peptide A showed a water droplet permeation area four times or more.
  • only glutamine peptide retained surface hydrophilicity after the washing test. It was confirmed that surface hydrophilicity is improved even after washing by attaching glutamine peptide A to the nylon surface and allowing TG to act on it.
  • Polyester fabric JISL 0803 polyester-attached white fabric 1. Collect 25 g of each, and for 1 hour each at 40 in 200 ml of an aqueous solution containing glutamine peptide A in the same amount (1.25 g) as the weight of the fabric. Exhaust treatment was performed. And after drying the peptide fabric after peptide exhaustion treatment, TG treatment in 200ml Tris-HCl buffer solution (pH7) containing 200mg of NAZE (1000U / L) at 40 for 1 hour, dried (as a control, protein exhaustion treatment, enzyme treatment Those that had not been subjected to protein exhaustion treatment were also carried out).
  • the fabric after the above treatment was subjected to repeated washing tests according to the conditions of JISL 0844 A-2 method (40, detergent 5 g / l, stirring 42 rpm, 30 minutes). Laundry was performed under the condition that detergent was added, followed by washing under the condition without detergent and letting it air dry once. Water absorption tests based on the JIS L 1907 dropping method were performed before washing, after washing once, after washing 5 times, and after washing 10 times. In this dropping method, the water permeation area (unit: cm2) after 1 minute of water dropping was measured.
  • Table 6 shows the results. Daltamin peptide A alone and not treated with transglutaminase had no effect after 5 launderings. In contrast, treatment with dartamine peptide A and transdalinase maintained the effect after 10 washes. Table 6 Effect of washing frequency on water drop surface area of TG treated polyester
  • Polyester fabric UIS L 0803 Polyester-attached white fabric 1.25 g is collected and glutamine peptide A is equal to the weight of the fabric (1.25 g), or 10 in 40 ml of an aqueous solution containing 1 (0.125 g) of 10 minutes. Each was exhausted for 1 hour. And the polyester fabric after peptide exhaustion treatment is dried Then, TG treatment was performed for 1 hour in 40 ml (10000 UZL, 1000 U / L, respectively) in 200 ml of Tris-HCl buffer (PH7) containing 2000 rag or 200 mg of transglutaminase, Dried (as a control, a protein exhaustion treatment was performed without enzyme treatment).
  • PH7 Tris-HCl buffer
  • the fabric after the above treatment was subjected to repeated washing tests according to the conditions of the L 0844 A-2 method (40, detergent 5 g / stirring 42 rpm, 30 minutes). Laundry was performed under the condition that detergent was added, followed by washing under the condition without detergent and letting it air dry once. Water absorption tests based on the JIS L 1907 dropping method were performed before washing, after washing once, after washing 5 times, and after washing 10 times. In this dropping method, the water permeation area (unit: cm2) after 1 minute of water dropping was measured.
  • Table 7 shows the results. When the enzyme concentration was increased 10 times, the peptide concentration was reduced to 1/10, and in both cases, the effect was retained until after 10 washes.
  • Polyester fabric J IS L 0803 white fabric with polyester
  • 40t 1 hour, glutamine peptide exhaustion treatment and transglutaminase treatment were performed simultaneously.
  • the fabric after the above treatment was subjected to repeated washing tests according to the conditions of JISL 0844 A-2 method (40 ° C., detergent 5 g / stirring 42 rpm, 30 minutes). Laundry was performed under the condition that detergent was added, followed by washing under the condition without detergent and letting it air dry once. Water absorption tests based on the JIS L 1907 dropping method were performed before washing, after washing once, after washing 5 times, and after washing 10 times. In this dropping method, the water permeation area (unit: cm2) was measured 1 minute after dropping. Table 8 shows the results. Even when the exhaustion treatment of dartamine peptide A and the transdalinase treatment were performed at the same time, the effect was retained even after 10 washes. Table 8
  • a fiber processed product having improved strength and excellent water absorption can be obtained simply and at low cost, and is extremely useful in the textile industry.

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  • 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)
  • Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

L'invention porte sur une fibre traitée présentant une résistance, une capacité d'absorption d'eau et une durabilité au lavage excellentes, que l'on peut fabriquer en liant un produit partiellement hydrolysé d'une protéine de blé à une fibre puis en laissant une transglutaminase agir sur la fibre.
PCT/JP2008/071282 2007-11-19 2008-11-18 Fibre traitée et son procédé de fabrication WO2009066785A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
JP2009542615A JPWO2009066785A1 (ja) 2007-11-19 2008-11-18 繊維加工物及びその製造法
EP08851101A EP2213785A4 (fr) 2007-11-19 2008-11-18 Fibre traitée et son procédé de fabrication
CN200880116811A CN101868575A (zh) 2007-11-19 2008-11-18 纤维加工物及其制造方法
US12/766,005 US20100203314A1 (en) 2007-11-19 2010-04-23 Processed fiber product, and method for production thereof

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP2007-299808 2007-11-19
JP2007299808 2007-11-19

Related Child Applications (1)

Application Number Title Priority Date Filing Date
US12/766,005 Continuation US20100203314A1 (en) 2007-11-19 2010-04-23 Processed fiber product, and method for production thereof

Publications (1)

Publication Number Publication Date
WO2009066785A1 true WO2009066785A1 (fr) 2009-05-28

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PCT/JP2008/071282 WO2009066785A1 (fr) 2007-11-19 2008-11-18 Fibre traitée et son procédé de fabrication

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US (1) US20100203314A1 (fr)
EP (1) EP2213785A4 (fr)
JP (1) JPWO2009066785A1 (fr)
KR (1) KR20100085083A (fr)
CN (1) CN101868575A (fr)
WO (1) WO2009066785A1 (fr)

Cited By (1)

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Publication number Priority date Publication date Assignee Title
WO2022149306A1 (fr) 2021-01-07 2022-07-14 ミテジマ化学株式会社 Procédé de modification des poils d'animaux

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Publication number Priority date Publication date Assignee Title
JPWO2012067201A1 (ja) * 2010-11-19 2014-05-19 大塚製薬株式会社 プロテオグリカン結合繊維製品及びその製造方法
CN103526577B (zh) * 2013-10-09 2015-07-15 南通大学 醋酸纤维的红色系保健功能染色方法

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WO2002081694A1 (fr) 2001-03-30 2002-10-17 Ajinomoto Co.,Inc. Procede de secretion et de production de proteine
WO2004078973A1 (fr) 2003-03-07 2004-09-16 Ajinomoto Co. Inc. Procede de production de transglutaminase microbienne
JP3873408B2 (ja) 1997-11-07 2007-01-24 味の素株式会社 バチルス属細菌由来のトランスグルタミナーゼの製造法
WO2008099898A1 (fr) 2007-02-15 2008-08-21 Ajinomoto Co., Inc. Transglutaminase ayant une liaison disulfure introduite dans celle-ci

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JPH0310589B2 (fr) 1984-09-25 1991-02-14 Akihiko Kato
JP2572716B2 (ja) 1987-03-04 1997-01-16 味の素株式会社 新規なトランスグルタミナーゼ
US5736356A (en) 1994-01-28 1998-04-07 Ajinomoto Co., Inc. Transglutaminase originating from Crassostrea gigas
WO1996006931A1 (fr) 1994-08-26 1996-03-07 Novo Nordisk A/S Transglutaminases microbiennes, leur production et leur utilisation
JPH093772A (ja) 1995-06-15 1997-01-07 Toray Ind Inc 繊維構造物およびその製造方法
JPH093773A (ja) 1995-06-16 1997-01-07 Toray Ind Inc 繊維構造物およびその製造方法
JPH1053964A (ja) * 1996-08-07 1998-02-24 Toray Ind Inc 繊維構造物およびその製造方法
JPH1175876A (ja) 1997-07-04 1999-03-23 Ajinomoto Co Inc 新規な微生物トランスグルタミナーゼの製造法
JP3873408B2 (ja) 1997-11-07 2007-01-24 味の素株式会社 バチルス属細菌由来のトランスグルタミナーゼの製造法
WO2001023591A1 (fr) 1999-09-30 2001-04-05 Ajinomoto Co., Inc. Procédé de production de transglutaminase
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EP2213785A1 (fr) 2010-08-04
CN101868575A (zh) 2010-10-20
JPWO2009066785A1 (ja) 2011-04-07
KR20100085083A (ko) 2010-07-28
US20100203314A1 (en) 2010-08-12

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