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WO2009066785A1 - Processed fiber product, and method for production thereof - Google Patents

Processed fiber product, and method for production thereof 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
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WO
WIPO (PCT)
Prior art keywords
treatment
fabric
fiber
protein
wheat protein
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/JP2008/071282
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French (fr)
Japanese (ja)
Inventor
Mitsuo Ueda
Keiichi Yokoyama
Noriki Nio
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Ajinomoto Co Inc
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Ajinomoto Co Inc
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Filing date
Publication date
Application filed by Ajinomoto Co Inc filed Critical Ajinomoto Co Inc
Priority to EP08851101A priority Critical patent/EP2213785A4/en
Priority to CN200880116811A priority patent/CN101868575A/en
Priority to JP2009542615A priority patent/JPWO2009066785A1/en
Publication of WO2009066785A1 publication Critical patent/WO2009066785A1/en
Priority to US12/766,005 priority patent/US20100203314A1/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • DTEXTILES; PAPER
    • D06TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06MTREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M16/00Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
    • D06M16/003Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
    • DTEXTILES; PAPER
    • D06TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06MTREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M15/00Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
    • D06M15/01Treating 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
    • D06M15/15Proteins or derivatives thereof
    • YGENERAL 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
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10TTECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
    • Y10T428/00Stock material or miscellaneous articles
    • Y10T428/249921Web or sheet containing structurally defined element or component
    • YGENERAL 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
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10TTECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
    • Y10T428/00Stock material or miscellaneous articles
    • Y10T428/29Coated or structually defined flake, particle, cell, strand, strand portion, rod, filament, macroscopic fiber or mass thereof
    • Y10T428/2913Rod, strand, filament or fiber
    • Y10T428/2933Coated 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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  • Engineering & Computer Science (AREA)
  • Textile Engineering (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Biochemistry (AREA)
  • Microbiology (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

A processed fiber product having excellent strength, water-absorbability and washing durability can be produced by attaching a partially hydrolyzed product of a wheat protein to a fiber and then allowing a transglutaminase to act on the fiber.

Description

繊維加工物及びその製造法 技術分野  Processed fiber and its manufacturing method

本発明はトランスダル夕ミナ一ゼとタンパク質、 ペプチドを用いる繊維 加工物及びその製造法に関するものである。 背景技術  The present invention relates to a processed fiber using transdal protein, protein and peptide, and a method for producing the same. Background art

衣料用、の繊維基質は 1 9 5 0年代に出現したポリエステルを最後とし て、 それ以来顕著な新規繊維基質が開発されていない。 1 9 δ 0年代以降 は、 繊維基質そのものの性質に不十分なところがあれば、 紡糸などの繊維 化の際に工夫を凝らすか、 化学加工で後から機能を付加するいわゆる繊維 加工などが行われている。 綿の防しわ性の改善や、 羊毛の収縮防止、 ナイ ロンやポリエステルの表面の照り感ゃぬめり感を化学的に改善する加工 などが普及している。  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 δ 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.

1 9 9 0年代に至り、 天然繊維を夕一ゲッ トとして、 天然繊維の衣料材 料としての欠点を、 酵素を利用して補おうとするいわゆる酵素加工が発展 してきた。 綿を代表とするセルロース繊維を対象としてセルロース加水分 解酵素によってセルロース表面を一部加水分解し、 より柔らかく風合いの よい繊維を得る加工や、 羊毛を対象として、 羊毛のクチクル表面をタンパ ク加水分解酵素によって一部加工し、 羊毛の洗濯収縮を改善する加工など が検討されてきて、一部実用化に至っている。また、同様の加工において、 合成繊維も対象になりつつある。 本来基質とはなりえないと思われてきた 合成高分子であっても、 酵素が一部作用することが見いだされてきて、 ナ イロンゃアクリル、 ポリエステルなどを対象として、 酵素で表面を加工す る試みが始まっている。  Since the 1990s, so-called enzyme processing has been developed that uses natural fibers as an evening target and uses enzymes to compensate for the shortcomings of natural fibers as clothing materials. Cellulose hydrolyzing enzyme, which is representative of cotton, is partially hydrolyzed by cellulose hydrolyzing enzyme to obtain a softer and more textured fiber, and wool is targeted at the surface of wool cuticles. Processing that has been partially processed with enzymes to improve washing shrinkage of wool has been studied, and some have been put to practical use. In the same process, synthetic fibers are also being targeted. Synthetic polymers that were originally thought to be non-substrates have been found to have some effects on enzymes, and the surface of enzymes such as nylon and acrylic and polyester is processed with enzymes. Attempts have started.

しかしながら、 酵素の繊維加工への応用は非常に活発になってきている 一方で、 上記の加工に利用される酵素のほとんどが加水分解酵素で、 繊維 基質の表面を適度に削り取るという加工以外の作用は期待できず、 用途や 機能に大きな制限がある。 繊維基質に元来持っていない機能を持たせよう と期待するには、 加水分解酵素ではなく、 化学結合反応を触媒する酵素の 活用が望まれている。 However, the application of enzymes to fiber processing has become very active. On the other hand, most of the enzymes used in the above processing are hydrolytic enzymes, and the effects other than processing are that the surface of the fiber substrate is scraped off appropriately. Cannot be expected, There is a big limitation on the function. In order to expect the fiber substrate to have a function that it does not originally have, it is desired to use an enzyme that catalyzes a chemical bonding reaction, not a hydrolase.

トランスダル夕ミナーゼは上記のような要望を満たし得る魅力的な酵 素の一つであり、 タンパク質中のダルタミン残基とリジン残基を結合させ る、 あるいは、 グルタミン残基に一級アミンを取り込ませる作用を触媒す るもので、 ポリアミ ド系の繊維基質に働きかけ、 能動的に新しい機能を付 与する加工に利用できる可能性の高い酵素である。 実際に、 繊維の分野に おいても、 すでに羊毛繊維を主体として、 トランスダルタミナ一ゼを利用 した新しい加工法が数件提案されている。  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.

トランスグル夕ミナーゼはグルタミンとリジンを結合させる反応を触 媒するので、 グルタミンとリジン残基、 あるいはその類似残基を持つ繊維 基質に作用することが期待でぎる。 実際に、 羊毛をターゲッ トとして、 ト ランスグルタミナーゼで処理すると、 羊毛基質内のグルタミン残基とリシ ン残基が酵素触媒反応によって架橋され、 羊毛の強度が増加することなど の効果が見いだされている (Enzyme and M i c rob i a l Techno l ogy 34 (2004) p64-72) o  Since 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. In fact, 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. (Enzyme and M ic rob ial Techno l ogy 34 (2004) p64-72) o

上記のような作用は、 これまで実用化に向けて検討されてきたセルロー ス加水分解酵素や、 夕ンパク質加水分解酵素の利用では到底期待できない 新しい機能付与加工であって、 今後の発展が期待できるものである。 しか しながら、 上記のような加工は繊維基質にグルタミンおよびリジンの両方 の残基を同時に併せ持つていることが必要で、 適用できる繊維基質が羊毛 など、 一部の天然繊維に限定されてしまう。  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. However, 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.

絹やナイ口ンなどの羊毛以外のポリアミ ド繊維ではトランスダルタミ ナ一ゼが作用するダルタミンおよびリジン残基、 あるいは類似する残基が 十分な量存在せず、 たとえそのまま トランスダル夕ミナーゼで処理をして も架橋反応が期待できない。 このような基質に対してトランスダル夕ミナ ーゼを使って結合あるいは架橋反応を期待するためには、 不足する反応性 残基を多く持った第 3成分を付加する必要がある。 たとえば絹繊維基質を 例にとると、 絹にはリジン残基もダルタミン残基も含有量が非常に少ない ので、 そのままではトランスダル夕ミナーゼで処理しても、 相互の反応の 可能性が低いが、 グルタミンゃリジンを多く含んだぺプチドをあらかじめ 絹に処理しておき、 それらをトランスダル夕ミナーゼで一括して処理する と、 反応に関与できる残基の密度が増加し、 繊維基質と第 3成分とがー緒 に結合され、 結果として効果的な架橋反応が起こることが期待できる。 ま た、 導入する第 3成分に、 種々の機能性の材料をあらかじめ付加しておけ ば、 繊維基質に酵素触媒反応を利用して効果的に機能性物質を導入できる 可能性も出てくる。 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. When processed in this way, the density of residues that can participate in the reaction increases, and the fiber substrate and the third component are bound together, resulting in an effective crosslinking reaction. In addition, if various functional materials are added in advance to the third component to be introduced, there is a possibility that a functional substance can be effectively introduced into the fiber substrate using an enzyme-catalyzed reaction.

また、 ナイロンなどの合成繊維基質であっても、 トランスダル夕ミナ一 ゼの基質となりうる反応性残基があれば、 第 3成分の添加で合成繊維基質 の残基と第 3成分とが反応する可能性が期待でき、 絹の場合と同様に、 第 3成分を介した架橋反応や、 効率的な機能性物質の導入も可能となりうる。 このような観点から、 ゼラチン^ポリエステル表面にコーティングする 方法 (特開平 9一 3 7 7 2号公報) が提案され、 ゼラチンをコーティング することで透湿度、 吸湿度の高い繊維が得られることが開示されている。 この方法では、 製膜性の観点から トランスダル夕ミナーゼを含む高濃度 ( 30w t % ) のゼラチン水溶液をポリエステル表面にコーティングしてい るが、 塗布中にコーティ ング処理液がゲル化したり、 塗布に用いるナイフ コ一夕一上で固まる恐れが高く、 高濃度のゼラチン水溶液をコーティング するのは実用的な方法でないと考えられる。 また、 皮膜耐久性も 9 0での 熱湯中での溶解の有無を確認しているだけで、 洗濯などの実用的な処理を 行なった後でも効果が保持されるかどうか開示されていない。  Even if a synthetic fiber substrate such as nylon is used, if there is a reactive residue that can be a substrate for transdal ligase, the addition of the third component causes the residue of the synthetic fiber substrate to react with the third component. As in the case of silk, a cross-linking reaction via the third component and efficient introduction of functional substances may be possible. From such a point of view, a method of coating the surface of gelatin ^ polyester (JP-A-Hei 9 37 7 2) has been proposed, and it is disclosed that fibers with high moisture permeability and moisture absorption can be obtained by coating gelatin. Has been. In this method, from the viewpoint of film-forming properties, a high concentration (30 wt%) gelatin aqueous solution containing transdalinase is coated on the polyester surface. The knives used are likely to harden overnight, and it is not considered practical to coat a highly concentrated aqueous gelatin solution. Moreover, only whether or not the film durability is dissolved in hot water at 90 is confirmed, and it is not disclosed whether or not the effect is maintained even after practical treatment such as washing.

高濃度ゼラチン水溶液を使う弊害を回避するため、 トランスダル夕ミナ —ゼを含む 3 w t %ゼラチン水溶液をポリエステルに浸漬する方法 (特開 平 9 一 3 7 7 3号公報) が提案されているが、 皮膜耐久性も 9 0での熱湯 中での溶解の有無を確認しているだけで、 洗濯などの実用的な処理を行な つた後でも効果が保持されるかどうか開示されていない。  In order to avoid the harmful effects of using high-concentration gelatin aqueous solution, a method of immersing 3 wt% gelatin aqueous solution containing transdal yuminase in polyester (Japanese Patent Laid-Open No. Hei 9 3 7 7 3) has been proposed. The film durability is 90% only by confirming the presence or absence of dissolution in hot water, and it is not disclosed whether the effect is maintained even after practical treatment such as washing.

これらの方法により、 繊維を高濃度のゼラチンで被覆することが、 繊維 の透湿度、 吸湿度を向上させる効果があることは示されているが、 洗濯耐 久性に乏しく、 吸水性や吸湿性が持続しないというのが実情であつた。 発明の開示 Although it has been shown that coating the fiber with high-concentration gelatin by these methods has the effect of improving the moisture permeability and moisture absorption of the fiber, it has poor washing durability, water absorption and moisture absorption. The fact was that it did not last. Disclosure of the invention

本発明は、 このような現状に鑑みて行なわれたものであり、 前記背景技 術の欠点を解消し、 強度、 吸水性に優れ、 洗濯耐久性を有する繊維を、 簡 便かつ低コス 卜で製造する方法を提供することを目的とするものである。 本発明者らは上記課題を解決すべく鋭意研究を重ねた結果、 小麦タンパ ク質部分加水分解物を使用する方法を見出し、 本発明に到達した。 即ち、 本発明は以下の通りである。  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. As a result of intensive studies to solve the above-mentioned problems, 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.

( 1 ) 小麦タンパク質部分加水分解物を繊維表面に付着させた後、 トランス ダルタミナーゼを作用させて得られる繊維加工物。  (1) A processed fiber product obtained by allowing trans-daltaminase to act after attaching a wheat protein partial hydrolyzate to the fiber surface.

(2) 小麦タンパク質部分加水分解物が、 小麦タンパク質を酵素処理又は 酸処理又はアル力リ処理して得られたものである( 1 )記載の繊維加工物。  (2) The processed fiber product according to (1), wherein the wheat protein partial hydrolyzate is obtained by subjecting wheat protein to an enzyme treatment, an acid treatment, or an alkaline treatment.

( 3 ) 小麦夕ンパク質部分加水分解物が、 平均分子量が 7 0 0〜 5 0 0 0 0のものである ( 1 ) 又は (2) 記載の繊維加工物。  (3) The processed fiber product according to (1) or (2), wherein the partial hydrolyzate of wheat protein has an average molecular weight of from 70 to 500.000.

(4) 小麦タンパク質部分加水分解物を繊維表面に付着させた後、 卜ラン スグル夕ミナーゼを作用させることを特徴とする繊維加工物の製造法。 (4) 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.

(5) 小麦タンパク質部分加水分解物が、 小麦タンパク質を酵素処理又は 酸処理又はアルカリ処理して得られたものである (4) 記載の製造法。 (5) The production method according to (4), wherein the wheat protein partial hydrolyzate is obtained by subjecting wheat protein to enzyme treatment, acid treatment or alkali treatment.

( 6 ) 小麦タンパク質部分加水分解物が、 平均分子量が 7 0 0〜 5 0 0 0 0のものである (4) 又は (5) 記載の製造法。  (6) The production method according to (4) or (5), wherein the wheat protein partial hydrolyzate has an average molecular weight of from 700 to 500.000.

本発明において、 小麦タンパク質部分加水分解物とは、 小麦ダルテン夕 ンパク質を、 酵素、 酸、 アルカリなどで適度に部分的に加水分解したもの を意味し、 加水分解処理されていない小麦タンパク質や、 アミノ酸まで過 度に加水分解が進んだ夕ンパク質加水分解物は含まれない。 市販の酵素部 分加水分解小麦グルテンタンパク質(例えば、 DMV社製 WG E80G P U) をそのまま用いてもよいし、 小麦グルテンを適切なタンパク質加水分解酵 素で分解することで調製することも可能である。 また、 酸部分加水分解小 麦ダルテンタンパク質、 アル力リ部分加水分解小麦グルテンタンパク質も 用いることができる。 小麦タンパク質部分加水分解物の平均分子量は 7 0 0〜 5 0, 0 0 0 D aが好ましく、 3 , 0 0 0〜 4 0 , O O O D aがより 好ましく、 5, 0 0 0〜 3 0 , 0 0 0 D a程度が特に好ましい。 In the present invention, 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) can be used as it is, or it can be prepared by degrading wheat gluten with an appropriate proteolytic enzyme. . In addition, 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.

小麦夕ンパク質部分加水分解物を繊維表面に付着させる方法は特に限 定されないが、 例えば、 小麦タンパク質部分加水分解物を水等の溶媒に溶 解又は分散させた溶液に繊維を浸漬する、 あるいは、 繊維に小麦タンパク 質部分加水分解物を塗布あるいは噴霧する等が一例である。 小麦タンパク 質部分加水分解物が繊維を形成する糸束の単繊維フィ ラメントあるいは ステープルの間隙および表面のいずれかに少なく と.も存在していればよ く、 小麦タンパク質部分加水分解物が、 糸束の単繊維フィラメントあるい はステ一プルに固着もしくは被覆していればよい。 - 小麦タンパク質部分加水分解物を水等の溶媒に溶解又は分散させた溶 液に繊維を浸漬する、 あるいは、 繊維に小麦タンパク質部分加水分解物を 塗布あるいは噴霧する際に用いる、 小麦タンパク質部分加水分解物溶液の 濃度は 1〜 3 0 g Z Lが好ましく、 コス ト、 作業性の点で 3〜 1 0 g Z L がより好ましい。  The method for attaching the wheat protein partial hydrolyzate to the fiber surface is not particularly limited. For example, the fiber is immersed in a solution obtained by dissolving or dispersing the wheat protein partial hydrolyzate in a solvent such as water, or An example is application or spraying of a wheat protein partial hydrolyzate to the fiber. 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. -Wheat protein partial hydrolyzate used when dipping the fiber in a solution in which the wheat protein partial hydrolyzate is dissolved or dispersed in a solvent such as water, or when applying or spraying the wheat protein partial hydrolyzate on the fiber 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.

繊維表面に付着させる小麦タンパク質部分加水分解物の量は、 繊維 1 g 当り 0 . 1〜 3 gが好ましく、 コスト、 作業性の点で 0 . 3〜 l gがより 好ましい。  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.

本発明に使用される トランスダル夕ミナーゼ (以下、 T Gと表記する場 合がある) は、 E C 2 . 3 . 2 . 1 3に属するァシル転移酵素であり、 夕 ンパク質やべプチド中のダルタミン残基を供与体、 リジン残基を受容体と するァシル転移反応を触媒する活性を有する酵素である。 哺乳動物由来め もの、 魚類由来のもの、 微生物由来のものなど、 種々の起源のものが知ら れている。 本発明で用いる酵素はこの活性を有している酵素であれば構わ ず、 その起源としてはいずれのものでも構わない。 また、 組み換え酵素で あっても構わない。 例えば、 放線菌由来 (特許第 2 5 7 2 7 1 6号公報参 照)、 枯草菌由来 (特許第 3 8 7 3 4 0 8号公報参照) 等の微生物由来の ものをあげることができる。 また、 モルモッ ト肝臓由来のもの (特許第 1 6 8 9 6 1 4号公報参照)、微生物由来のもの(W0 9 6 / 0 6 9 3 1参照)、 牛血液、 豚血液等の動物由来のもの、 サケ、 マダイ等の魚由来のもの (関 ら、 日本水産学会誌, 1990, 56, 125- 132)、 カキ由来のもの (米国特許 第 5 7 3 6 3 5 6号公報参照) 等をあげることができる。 この他、 遺伝子 組み換えにより製造されるもの (例えば、 特許第 3 0 1 0 5 8 9号公報、 特開平 1 1一 7 5 8 7 6号公報、 WO 0 1 2 3 5 9 1号公報、 WO 0 2 / 0 8 1 6 94公報、 WO 2 0 04Z0 7 8 9 7 3号公報参照)、 耐熱性 の向上したジスルフィ ド結合導入トランスダル夕ミナーゼ (WO 2 0 0 8 / 0 9 9 8 9 8 ) 等をあげることができる。 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. A variety of sources are known, 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. 2 5 7 2 7 16) and Bacillus subtilis (see Japanese Patent No. 3 8 7 3 4 8). Also derived from guinea pig liver (see Patent No. 1 6 8 9 6 14), from microorganisms (see W0 9 6/0 6 9 3 1), bovine blood, pork blood and other animal-derived Derived from fish, salmon, red sea bream, etc. (Seki et al., Journal of the Japanese Fisheries Society, 1990, 56, 125-132), derived from oysters (US patent) No. 5 7 3 6 3 5 6)). In addition, those produced by gene recombination (for example, Japanese Patent No. 3 0 1 0 5 89, Japanese Patent Application Laid-Open No. 1 1 1 7 5 8 7 6, WO 0 1 2 3 5 9 1, WO 0 2/0 8 1 6 94 publication, WO 2 0 04Z0 7 8 9 7 3 publication), disulfide bond-introduced transdal junction minase with improved heat resistance (WO 2 0 0 8/0 9 9 8 9 8 ) Etc.

味の素㈱より 「ァクティバ」 TG という商品名で市販されている微生物 由来のトランスダル夕ミナーゼが本発明で用いる トランスグル夕ミナー ゼの一例である。  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.

トランスダルタミナーゼを作用させる方法は、 繊維を小麦タンパク質部 分加水分解物と TGを含む溶液に浸漬する方法、 あるいは、 繊維を小麦夕 ンパク質部分加水分解物溶液に浸潰した後、 T G溶液に浸漬する方法が例 として挙げられる。 小麦タンパク質部分加水分解物と TGを含む溶液、 あ るいは、 TG溶液は、 T Gの酵素反応性と安定性の観点から ρ Ηは 4〜 1 2が好ましく、 5〜 8がより好ましい。  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, ρ 含 む 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.

酵素の反応時間は、 酵素が基質物質に作用することが可能な時間であれ ば特に構わなく、 非常に短い時間でも逆に長時間作用させても構わないが、 現実的な作用時間としては 5分〜 24時間が好ましい。 また、 反応温度に 関しても酵素が活性を保つ範囲であればどの温度であっても構わないが、 現実的な温度としては 0〜 8 0ででの作用させることが好ましい。  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. In addition, 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.

T Gの最適な添加量は小麦タンパク質部分加水分解物と T Gを含む溶 液、 あるいは、 T G溶液における T G濃度は、 1 0〜 3 0 0 0 UZL、 好 ましくは 1 0 0〜 3 0 0 0 UZL 、より好ましくは 1 0 0 0〜 3 0 0 0 U ZLが適正であるが、 繊維の種類、 TG反応時間、 TG 反応温度等により 適宜調整することができる。 尚、 3 0 0 0 UZLを超える場合も効果はあ るが、 コス トに見合うほどではない。  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.

TGの添加量は繊維 1 gに対して 1〜 3 0 0 Uが好ましく、 小麦タンパ ク質部分加水分解物 1 gに対して 1〜 3 0 0 Uが好ましいが、 繊維の種類、 T G反応温度等により適宜調整することができる。  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.

尚、酵素活性についてはベンジルォキシカルボニル -L-ダル夕ミニルグリ シンとヒ ドロキシルアミンを基質として反応を行い、 生成したヒドロキサ ム酸を トリクロロ酢酸存在下で鉄錯体を形成させた後 5 2 5 nmの吸光 度を測定し、 ヒ ドロキサム酸の量を検量線より求め活性を算出する。 3 7 、 p H 6. 0で 1分間に 1 molのヒ ドロキサム酸を生成する酵素量 を 1 Uと定義した。 As for enzyme activity, 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.

本発明による繊維加工物とは、 羊毛、絹、 綿などの天然繊維、 ナイロン、 ポリエステル、 アクリルなどの合成繊維およびこれらの混紡、 混編、 混繊 により作成されたものをいう。 羊毛、 絹などのタンパク質系繊維、 ナイ口 ンなどのポリアミ ド系の繊維ではトランスグル夕ミナ一ゼ反応により、 そ の末端アミノ基も架橋結合に関与するため繊維とタンパク質との接着性 がさらに向上する。 発明を実施するための最良の形態  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. BEST MODE FOR CARRYING OUT THE INVENTION

以下に実施例を挙げ、 本発明をさらに詳しく説明する。 本発明は、 これ らの実施例により何ら限定されない。 実施例 1  The following examples further illustrate the present invention. The present invention is not limited in any way by these examples. Example 1

.実施例中に用いたタンパク質および酵素は次のものを使用した。  The following proteins and enzymes were used in the examples.

夕ンパク質  Evening protein

グルタミンペプチド A: 小麦ダルテンタンパク質部分加水分解物、 DM V社製 WG E 8 0 G P U (平均分子量 9, 6 5 0 D)  Glutamine peptide A: Wheat dartene protein partial hydrolyzate, DM V WG E 80 G P U (average molecular weight 9, 65 50 D)

ダルタミンぺプチド B : 小麦ダルテンタンパク質部分加水分解物 B : D MV社製 WGE 8 0 GPA (平均分子量 6 6 0 D)  Dartamine peptide B: Wheat dartene protein partial hydrolyzate B: D MV WGE 80 GPA (average molecular weight 6 60 0 D)

ゼラチン A : キシダ化学製牛由来アル力リ処理ゼラチン  Gelatin A: Kishida Chemical's cow-derived Al-powered gelatin

酵素  Enzyme

トランスグル夕ミナーゼ (E C 2. 3. 2. 1 3)  Transglutaminase (E C 2. 3. 2. 1 3)

酵素起源 : 放線菌ストレプトマイセス , モバラェンシス由来  Enzyme origin: Actinomycetes Streptomyces, Mobaraensis

酵素活性 : 1 0 0 0ユニッ ト/ g 絹布帛 UIS L 0803絹 2-1号添付白布、 平羽二重) を lg程度とり、 グ ル夕ミンペプチド (A、 B 2種類)、 ゼラチン Aを、 それぞれ布帛の重量 と同量 (l g) 含む水溶液 100m l 中で 40 において、 それぞれ 1時間、 吸尽 処理を行った。 そして、 グルタミンペプチド、 ゼラチン吸尽処理後の絹布 帛を乾燥後" トランスグル夕ミナーゼ 10mg を含む 100m l のトリス塩酸緩 衝液 (p H 7 ) 中で (100 U / L )、 40t:、 1時間、 酵素処理を実施し、 乾燥 した (コントロールとして、 夕ンパク質吸尽処理をしていない絹布帛にも T G処理を実施した)。 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).

処理後の絹布帛の引き裂き強度の測定は、 J I S L 1096 に準拠し、 ペン ジュラム法で行い、 縦糸を切断する方向の引き裂き強度 (単位 : 二ユート ン N) を測定した。 さらに、 上記処理による絹布帛の強度が繰り返しの水 洗いによってどの程度影響を受けるかを調べるために、 上記処理後の絹布 帛を蒸留水 1 リッ トル、 40でにおいて、 スターラーで 10 分間の攪拌を 3 回繰り返して水洗い処理を行った。 そして、 その布帛を乾燥後、 すでに述 ベた方法と同様の方法で引き裂き強度を測定した。  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.

表 1に示すように、 グルタミンペプチド A、 B、 ゼラチン Aを吸尽処理 した全てにおいて、 絹繊維の強度増加が見られたが、 洗濯後にも強度が保 持され、 強度増加が最も大きかったのはダルタミンぺプチド Aであった。 このことより、 グルタミンペプチド Aは、 トランスダル夕ミナ一ゼ反応に よって、 絹布帛表面に強固に付着していることが明らかとなった。 一方、 ゼラチンを用いた場合は、 十分な引裂強度が得られず、 特開平 9 - 3 7 7 3に開示されている方法と比較し、 小麦タンパク質部分加水分解物を用い る本発明の方法は顕著な効果を示した。 表 1 各種タンパク質処理後の絹繊維の強度  As shown in Table 1, all of the glutamine peptides A, B, and gelatin A that had been exhausted showed an increase in the strength of the silk fibers, but the strength was maintained after washing and the increase in strength was the largest. Was dartamine peptide A. From this, it was clarified that glutamine peptide A was firmly attached to the surface of the silk fabric by the transdal reaction. On the other hand, when gelatin is used, sufficient tear strength cannot be obtained, and the method of the present invention using a wheat protein partial hydrolyzate is compared with the method disclosed in JP-A-9-3773. It showed a remarkable effect. Table 1 Strength of silk fibers after various protein treatments

Figure imgf000009_0001
. 実施例 2
Figure imgf000009_0001
Example 2

タンパク質の種類、 分子量の影響を検討するため、 実施例 1に用いた以 外の下記のタンパク質を使用して実験を行った。  In order to examine the effects of protein type and molecular weight, experiments were conducted using the following proteins other than those used in Example 1.

タンパク質  Protein

グルタミンぺプチド C : 小麦ダルテンタンパク質部分加水物、 アミラム 社製 SWP 5 0 0 (S D S— P AGEから推定した分子量 5 , 0 0 0〜 3 0 , 0 0 0 D)  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)

ダルタミンぺプチド D : 小麦ダルテンタンパク質部分分解物、 自作 (平 均分子量 3 , 0 0 0 D)  Daltamin peptide D: Wheat dartene protein partial degradation product, self-made (average molecular weight 3, 0 0 0 D)

グルタミンペプチド E : 小麦ダルテンタンパク質部分分解物、 片山化学 工業研究所社製ダルパール 3 0 (酸、 アルカリ加水分解、 分子量 4 0, 0 0 0〜 5 0, 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)

グルタミンペプチド Dに関しては、 小麦ダルテンをプロテアーゼ (バチ ルス · アミ口リキファシエンス MR Pタンパク) にて、 部分加水分解し、 平均分子量 3 0 0 0 Dまで分解した。 反応終了後、 不溶物を除き、 スプレ 一ドライで乾燥することによって粉末を調製した。  For glutamine peptide 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.

絹布帛 (JIS L 0803絹 2-1号添付白布、 平羽二重) を lg程度とり、 グ ル夕ミンペプチド (3種類) それぞれ布帛の重量と同量 (lg) 含む水溶液 100ml 中で 40でにおいて、 それぞれ 1 時間、 吸尽処理を行った。 そして、 グルタミンペプチド吸尽処理後の絹布帛を乾燥後、 トランスダル夕ミナ一 ゼ 40mgを含む 400mlのトリス塩酸緩衝液( p H 7 )中で( 100UZ L )、 40 :、 1 時間、 酵素処理を実施し、 乾燥した。 処理後の絹布帛の引き裂き強度の 測定は、 JIS L 1096 に準拠し、 ペンジュラム法で行い、 縦糸を切断する 方向の引き裂き強度 (単位 : ニュートン N) を測定した。  Take about 1 lg of silk cloth (JIS L 0803 silk 2-1 attached white cloth, Hiraha double) and gluten-min peptide (3 types) each in 40 ml in 100 ml of aqueous solution containing the same amount (lg) as the weight of the cloth. In each case, exhaustion treatment was performed for 1 hour. Then, after drying the silk fabric after the glutamine peptide exhaustion treatment, the enzyme treatment was performed in 400 ml of Tris-HCl buffer (pH 7) containing 40 mg of Transdal Yuminase (100 UZ L), 40: for 1 hour. And dried. The tear strength of the silk fabric after the treatment was measured by the pendulum method according to JIS L 1096, and the tear strength (unit: Newton N) in the direction of cutting the warp was measured.

実施例 1の結果と合わせて、 表 2に結果を示す。 グルタミンペプチドに 関しては、 平均分子量の増加に伴い、 引裂き強度の上昇が見られた。 グル 夕ミンペプチド Cに関しては、 手触りがなめらかになるという効果も見ら れた。 グルタミンペプチド Eに関しては、 酸、 アルカリ加水分解物である が、 引裂き強度の上昇が見られた。 表 2 絹繊維の強度へのタンパク質の分子量の影響 The results are shown in Table 2 together with the results of Example 1. For glutamine peptides, an increase in tear strength was observed with an increase in average molecular weight. With regard to glutamine peptide C, an effect of smooth touch was also observed. Regarding glutamine peptide E, although it was an acid or alkaline hydrolyzate, an increase in tear strength was observed. Table 2 Effect of protein molecular weight on silk fiber strength

Figure imgf000011_0001
実施例 3
Figure imgf000011_0001
Example 3

タンパク質の濃度、 トランスダルタミナーゼの濃度の影響を検討するた め、 実施例 2で用いたグルタミンぺプチド Cを使用して実験を行った。 絹布帛 (JIS L 0803絹 2-1号添付白布、 平羽二重) を lg程度とり、 グ ル夕ミンペプチド, Cを含む水溶液 100ml 中で 40でにおいて、 それぞれ 1 時間、 吸尽処理を行った。 そして、 グルタミンペプチド C吸尽処理後の絹 布帛を乾燥後、 トランスダル夕ミナーゼを含む 100ml のトリス塩酸緩衝液 (pH7 ) 中で、 40 、 1時間、 酵素処理を実施し、 乾燥した。 処理した夕 ンパク質濃度、 トランスダル夕ミナーゼ濃度は表 3に記載した。 処理後の 絹布帛の引き裂き強度の測定は、 JIS L 1096 に準拠し、 ペンジュラム法 で行い、 縦糸を切断する方向の引き裂き強度 (単位 : ニュートン N) を測 定した。  In order to examine the effects of the protein concentration and the transdaltaminase concentration, experiments were performed using glutamine peptide C used in Example 2. Take about 1 lg of silk fabric (JIS L 0803 silk 2-1 attached white cloth, Hiraha double) and perform exhaustion treatment for 1 hour each at 40 in 100 ml of aqueous solution containing glutamine peptide and C. It was. The silk fabric after the glutamine peptide C exhaustion treatment was dried, and then subjected to an enzyme treatment in 100 ml of Tris-HCl buffer (pH 7) containing transdalinase for 40 hours for 1 hour, followed by drying. Table 3 shows the concentrations of processed protein and transdal protein. The tear strength of the silk fabric after the treatment was measured by the pendulum method according to JIS L 1096, and the tear strength (unit: Newton N) in the direction of cutting the warp was measured.

表 3に結果を示す。 タンパク質濃度に関しては、 l gZL以上で顕著な 効果が得られ、 濃度が増えるに従い、 引裂き強度が大幅に上昇した。 トラ ンスダル夕ミナーゼ濃度に関しては、 実験を行なった全ての濃度で引裂き 強度の大幅な上昇が確認された。 表 3 絹繊維強度へのタンパク質の濃度、 トランスダル夕ミナーゼの 濃度の影響 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

タンパク質濃度  Protein concentration

0.1 0.3 1 3 10 30  0.1 0.3 1 3 10 30

(g/L)  (g / L)

酵素活性  Enzyme activity

1,000 1,000 1,000 1,000 1,000 1,000  1,000 1,000 1,000 1,000 1,000 1,000

(UZL)  (UZL)

引き裂き強度  Tear strength

4.67 4.55 6.08 8.88 11.46 12.91  4.67 4.55 6.08 8.88 11.46 12.91

(N)  (N)

タンパク質濃度 Protein concentration

10 10 10 10 0 0  10 10 10 10 0 0

(gZL)  (gZL)

酵素活性  Enzyme activity

10 30 100 3,000 3,000 0  10 30 100 3,000 3,000 0

(UZL)  (UZL)

引き裂き強度  Tear strength

12.39 10.56 11.39 11.90 4.33 4.10  12.39 10.56 11.39 11.90 4.33 4.10

(N) 実施例 4  (N) Example 4

ポリエステル布帛 (JIS L 0803'ポリエステル添付白布) lg をそれぞれ 採取し、 グルタミンペプチド A、 あるいはゼラチン Aを、 それぞれ布帛の 重量と同量 (lg) 含む水溶液 100ml 中で 40°Cにおいて、 それぞれ 1時間、 吸尽処理を行った。 そして、 グルタミンペプチド A、 ゼラチン A吸尽処理 後のポリエステル布帛を乾燥後、 トランスダルタミナーゼ 10mg を含む 100mlのトリス塩酸緩衝液 (pH7 ) 中で ( 1 0 0 UZL)、 40で、 1時間、 TG処理を実施し、 乾燥した (コントロールとして、 タンパク質吸尽処理 をしていないポリエステル布帛にも酵素処理を実施レた)。  Polyester fabric (JIS L 0803 'white fabric with polyester) lg was collected, and 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).

処理後のポリエステル布帛の引き裂き強度の測定は、 HS L 1096 に準 拠し、 ペンジュラム法で行い、縦糸を切断する方向の引き裂き強度(単位 : ニュートン N) を測定した。 また、 処理後の布帛の表面親水性の変化を評 価するために、 HS L 1907滴下法に基づく吸水性試験を行った。 この滴下 法では、 水滴下 1分後の水滴浸透面積 (単位: cm2) を計測した。 さらに、 上記処理によるポリエステル布帛の表面親水性が、 繰り返しの洗濯によつ てどの程度影響を受けるかを調べるために、 上記処理後の布帛を J I S L 0844 A-2法 (40t:、 洗剤 5 g /し 攪拌 42 rpm、 30分) の条件に従って、 繰 り返しの洗濯試験を行った。 繰り返し洗濯は、 1回目は洗剤を加えた条件 で、 また 2回目は洗剤なしの条件で行った。 そして、 その洗濯後の布帛を 乾燥後、 すでに述べた方法と同様の方法で表面親水性を測定した。 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.

表 4に示すように、 ダルタミンぺプチド Aを吸尽処理したポリエステル 布帛は、 引き裂き強度が向上した。 また、 グルタミンペプチド A、 ゼラチ ン Aを吸尽処理したポリエステル布帛は、 表面親水性が大幅に向上するが、 洗濯試験後も表面親水性を保持しているものは、 グルタミンぺプチドのみ であった。 グルタミンペプチド Aをポリエステル表面に付着させ、 T Gを 作用させることにより、 洗濯後であっても表面親水性が向上することが確 認された。 .ポリエステルの唯一とも言える欠点は、 水 (汗) を吸わないこ とであり、 この欠点を補うために、 綿との混紡にすることが多いのである が、 本発明によると表面浸水性を高めることができるので、 ポリエステル の欠点が改善されることが示唆された。  As shown in Table 4, the tear resistance of the polyester fabric exhausted with dartamine peptide A was improved. In addition, 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.

一方、 ゼラチンを用いた場合は、 十分な引裂強度、 水滴浸透面積が得ら れず、 特開平 9 一 3 7 7 3に開示されている方法と比較し、 小麦タンパク 質部分加水分解物を用いる本発明の方法は顕著な効果を示した。 On the other hand, when gelatin is used, sufficient tear strength and water droplet infiltration area cannot be obtained. Compared with the method disclosed in Japanese Patent Laid-Open No. Hei 9 37 7 3 The method of the invention showed a significant effect.

表 4 各種タンパク質処理後のポリエステルの強度、 水滴浸透面積 Table 4 Strength of polyester after various protein treatments, water drop penetration area

Figure imgf000014_0001
実施例 5
Figure imgf000014_0001
Example 5

ナイロン布帛 (JIS L 0803 ナイロン添付白布) lg をそれぞれ採取し、 グルタミンペプチド A、 あるいはゼラチン Aを、 それぞれ布帛の重量と同 量 (lg) 含む水溶液 100ml 中で 40 において、 それぞれ 1時間、 吸尽処理 を行った。 そして、 グルタミンペプチド A、 ゼラチン A吸尽処理後のナイ 口ン布帛を乾燥後、 トランスダルタミナーゼ 10mg を含む 100ml の卜リス. 塩酸緩衝液 (PH7 ) 中で (100UZL)、 40で、 1時間、 TG処理を実施し、 乾燥した (コントロールとして、 タンパク質吸尽処理をしていないナイ口 ン布帛にも酵素処理を実施した)。  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).

処理後のナイロン布帛の引き裂き強度の測定は、 nSL 1096 に準拠し、 ペンジュラム法で行い、 縦糸を切断する方向の引き裂き強度 (単位 : ニュ 一トン N) を測定した。 また、 処理後の布帛の表面親水性の変化を評価す るために、 HS L 1907滴下法に基づく吸水性試験を行った。 この滴下法で は、 水滴下 1 分後の水滴浸透面積 (単位 : cm2) を計測した。 さらに、 上 記処理によるナイロン布帛の表面親水性が、 繰り返しの洗濯によってどの 程度影響を受けるかを調べるために、 上記処理後の布帛を JIS L 0844 A-2 法 (40で、 洗剤 5g /し 攪拌 42rpm、 30分) の条件に従って、 繰り返しの 洗濯試験を行った。 繰り返し洗濯は、 1回目は洗剤を加えた条件で、 また 2回目は洗剤なしの条件で行った。 そして、 その洗濯後の布帛を乾燥後、 すでに述べた方法と同様の方法で表面親水性を測定した。 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.

表 5に示すように、 グルタミンペプチド A、 ゼラチン Aを吸尽処理した ナイロン布帛は、引き裂き強度が向上した。また、 グルタミンペプチド A、 ゼラチン Aを吸尽処理したポリエステル布帛は、 表面親水性が向上する力 グルタミンペプチド Aの方が 4倍以上の水滴浸透面積を示した。 また、 洗 濯試験後も表面親水性を保持しているものは、 グルタミンぺプチドのみで あった。 グルタミンペプチド Aをナイロン表面に付着させ、 T Gを作用さ せることにより、 洗濯後であっても表面親水性が向上することが確認され た。 一方、 ゼラチンを用いた場合は、 十分な水滴浸透面積が得られず、 特 開平 9— 3 7 7 3に開示されている方法と比較し、 小麦タンパク質部分加 水分解物を用いる本発明の方法は顕著な効果を示した。 表 5 各種タンパク質処理後のナイロンの強度、 水滴浸透面積  As shown in Table 5, the nylon fabric that was exhausted with glutamine peptide A and gelatin A had improved tear strength. In addition, 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. In addition, 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. On the other hand, when gelatin is used, a sufficient water droplet permeation area cannot be obtained, and the method of the present invention using a partially hydrolyzed product of wheat protein as compared with the method disclosed in JP 9-37 7 3 Showed a remarkable effect. Table 5 Nylon strength and water drop penetration area after various protein treatments

Figure imgf000015_0001
実施例 6
Figure imgf000015_0001
Example 6

ポリエステル布帛 (J I S L 0803ポリエステル添付白布) 1. 25gをそれぞ れ採取し、 グルタミンペプチド Aを、 布帛の重量と同量 (1. 25g) 含む水 溶液 200m l 中で 40でにおいて、 それぞれ 1時間、 吸尽処理を行った。 そし て、 ペプチド吸尽処理後のポリエステル布帛を乾燥後、 トランスダルタミ ナ一ゼ 200mg を含む 200ml のトリス塩酸緩衝液 ( pH7 ) 中で ( 1000U/ L)、 40で、 1 時間、 T G処理を実施し、 乾燥した (コントロールとして、 タンパク質吸尽処理、 酵素処理をしていないもの、 タンパク質吸尽処理の み行なったものも実施した)。 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).

上記処理後の布帛を JISL 0844 A- 2法(40で、 洗剤 5g/ l 、 攪拌 42rpm、 30分) の条件に従って、 繰り返しの洗濯試験を行った。 洗濯は、 洗剤を加 えた条件で行なった後、 洗剤なしの条件で洗浄を行い、 自然乾燥させるェ 程を 1回とした。 洗濯前、 洗濯 1回後、 洗濯 5回後、 洗濯 1 0回後に、 JIS L 1907 滴下法に基づく吸水性試験を行った。 この滴下法では、 水滴下 1 分後の水滴浸透面積 (単位 : cm2) を計測した。  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.

表 6に結果を示す。 ダルタミンぺプチド Aのみでトランスグル夕ミナ一 ゼ処理をしていないものは、 洗濯 5回後には効果がなくなつていた。 それ に対して、 ダルタミンペプチド Aと トランスダル夕ミナーゼで処理を行な つたものは、 洗濯 1 0回後も効果を保持していた。 表 6 TG処理ポリエステルの水滴表面面積への洗濯回数の影響  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

水滴浸透面積 TK.濯 洗濯  Water drop penetration area TK.

(cm2) 前 1 回後 5回後 10回後  (cm2) 1 time before 5 times after 10 times

― 0.94 0.94 0.94 0.94  ― 0.94 0.94 0.94 0.94

ク'ルタミンへ。フ。チド A 8.75 2.81 0.94 0.94  To Ku'Lutamin. Huh. Tide A 8.75 2.81 0.94 0.94

ク'ルタミンへ。フ。チド A + TG 9.06 5.31 4.69 3.75  To Ku'Lutamin. Huh. Chido A + TG 9.06 5.31 4.69 3.75

実施例 7 Example 7

夕ンパク質の濃度、 トランスダルタミナーゼの濃度の影響を検討するた め、 グルタミンペプチド Aを使用して実験を行った。  In order to investigate the effects of the concentration of protein and the concentration of transdaltaminase, experiments were conducted using glutamine peptide A.

ポリエステル布帛 UIS L 0803ポリエステル添付白布) 1.25gを採取し、 グルタミンペプチド Aを、 布帛の重量と同量 (1.25g)、 あるいは、 1 0分 の 1 (0.125g) 含む水溶液 200ml 中で 40 において、 それぞれ 1時間、 吸 尽処理を行った。 そして、 ペプチド吸尽処理後のポリエステル布帛を乾燥 後、 トランスグル夕ミナーゼ それぞれ、 2000rag、 あるいは、 200mg を含 む 200ml のトリス塩酸緩衝液 ( PH7 ) 中で (それぞれ、 10000UZL、 1000 U/L)、 40で、 1時間、 T G処理を実施し、 乾燥した (コントロールとし て、 夕ンパク質吸尽処理のみで酵素処理していないものも実施した)。 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).

上記処理後の布帛を L 0844 A-2法 (40で、 洗剤 5g /し 攪拌 42rpm、 30分) の条件に従って、 繰り返しの洗濯試験を行った。 洗濯は、 洗剤を加 えた条件で行なった後、 洗剤なしの条件で洗浄を行い、 自然乾燥させるェ 程を 1回とした。 洗濯前、 洗濯 1回後、 洗濯 5回後、 洗濯 1 0回後に、 JIS L 1907 滴下法に基づく吸水性試験を行った。 この滴下法では、 水滴下 1 分後の水滴浸透面積 (単位 : cm2) を計測した。  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.

表 7に結果を示す。 酵素濃度を 1 0倍にした場合、 ペプチド濃度を 1 0 分の 1にした場合、 どちらの場合も洗濯 1 0回後まで効果を保持していた。 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.

表 7 TG処理ポリエステルの水滴表面面積への洗濯回数の影響 Table 7 Effect of number of washings on water drop surface area of TG treated polyester

Figure imgf000018_0001
実施例 8
Figure imgf000018_0001
Example 8

ポリエステル布帛( J IS L 0803ポリエステル添付白布) 1.25gを採取し、 布帛の重量と同量 (1.25g) のグルタミンペプチド Aと トランスダルタミ ナ一ゼ lOOOmg を含む 100ml のトリス塩酸緩衝液 (pH7 ) 中で ( 10000U ZL)、 40t:、 1時間、 グルタミンペプチドの吸尽処理と トランスグルタミ ナーゼ処理を同時に行った。  Polyester fabric (J IS L 0803 white fabric with polyester) 1.25g was collected and 100ml of Tris-HCl buffer (pH7) containing glutamine peptide A and transdaltaminase lOOOmg in the same amount (1.25g) as the weight of the fabric. Inside (10000U ZL), 40t: 1 hour, glutamine peptide exhaustion treatment and transglutaminase treatment were performed simultaneously.

上記処理後の布帛を JISL 0844 A- 2法 (40°C、 洗剤 5g /し 攪拌 42rpm、 30分) の条件に従って、 繰り返しの洗濯試験を行った。 洗濯は、 洗剤を加 えた条件で行なった後、 洗剤なしの条件で洗浄を行い、 自然乾燥させるェ 程を 1回とした。 洗濯前、 洗濯 1回後、 洗濯 5回後、 洗濯 1 0回後に、 JIS L 1907 滴下法に基づく吸水性試験を行った。 この滴下法では、 水滴下 1 分後の水滴浸透面積 (単位 : cm2) を計測した。 表 8に結果を示す。 ダルタミンぺプチド Aの吸尽処理と トランスダル夕 ミナーゼ処理を同時に行なっても、 洗濯 1 0回後も効果を保持していた。 表 8 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

水滴浸透面積 洗 |1 li濯  Water drop penetration area Washing | 1 li rinsing

¾t濯前  ¾t before rinsing

(cm2) 1 回後 5回後 1 0回後  (cm2) After 1 time After 5 times After 10 times

ク'ルタミンへ。フ。チド A  To Ku'Lutamin. Huh. Chido A

1 2.50 6.25 4.40 2.1 0  1 2.50 6.25 4.40 2.1 0

+ TG  + TG

産業上の利用可能性 Industrial applicability

本発明によると、 強度が向上し、 吸水性が優れた繊維加工物が簡便かつ 低コストで得ることができるので、 繊維工業分野において極めて有用であ る。  According to the present invention, 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.

Claims

請 求 の 範 囲 The scope of the claims 1 . 小麦タンパク質部分加水分解物を繊維表面に付着させた後、 トランスグ ル夕ミナ一ゼを作用させて得られる繊維加工物。 1. A processed fiber product obtained by applying a transglutaminase after attaching a wheat protein partial hydrolyzate to the fiber surface. 2 . 小麦タンパク質部分加水分解物が、 小麦タンパク質を酵素処理又は酸 処理又はアルカリ処理して得られたものである請求の範囲第 1項記載の 繊維加工物。  2. The processed fiber product according to claim 1, wherein the wheat protein partial hydrolyzate is obtained by subjecting wheat protein to an enzyme treatment, an acid treatment or an alkali treatment. 3 . 小麦タンパク質部分加水分解物が、 平均分子量が 7 0 0〜 5 0 0 0 0 のものである請求の範囲第 1項又は第 2項記載の繊維加工物。  3. The processed fiber product according to claim 1 or 2, wherein the wheat protein partial hydrolyzate has an average molecular weight of from 70 to 500.000. 4 . 小麦タンパク質部分加水分解物を繊維表面に付着させた後、 トランス ダル夕ミナーゼを作用させることを特徴とする繊維加工物の製造法。  4. A method for producing a processed fiber product, characterized in that after a wheat protein partial hydrolyzate is adhered to a fiber surface, transdalinase is allowed to act. 5 . 小麦タンパク質部分加水分解物が、 小麦タンパク質を酵素処理又は酸 処理又はアルカリ処理して得られたものである請求の範囲第 4項記載の 製造法。  5. The method according to claim 4, wherein the wheat protein partial hydrolyzate is obtained by subjecting wheat protein to enzyme treatment, acid treatment or alkali treatment. 6 . 小麦タンパク質部分加水分解物が、 平均分子量が 7 0 0〜 5 0 0 0 0 のものである請求の範囲第 4項又は第 5項記載の製造法。  6. The method according to claim 4 or 5, wherein the wheat protein partial hydrolyzate has an average molecular weight of from 70 to 500.000.
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