JPH093773A - Fiber structure and its production - Google Patents

Fiber structure and its production

Info

Publication number
JPH093773A
JPH093773A JP7150363A JP15036395A JPH093773A JP H093773 A JPH093773 A JP H093773A JP 7150363 A JP7150363 A JP 7150363A JP 15036395 A JP15036395 A JP 15036395A JP H093773 A JPH093773 A JP H093773A
Authority
JP
Japan
Prior art keywords
protein
fiber structure
cross
producing
fiber
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.)
Pending
Application number
JP7150363A
Other languages
Japanese (ja)
Inventor
Keiji Takeda
恵司 竹田
Toshinori Hara
稔典 原
Jiro Amano
慈朗 天野
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Toray Industries Inc
Original Assignee
Toray Industries 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 Toray Industries Inc filed Critical Toray Industries Inc
Priority to JP7150363A priority Critical patent/JPH093773A/en
Publication of JPH093773A publication Critical patent/JPH093773A/en
Pending legal-status Critical Current

Links

Abstract

PURPOSE: To produce a simple and inexpensive fiber structure excellent in a mass feeling and moisture permeable performance, having durability, not damaging characteristics of a synthetic fiber itself constituting the fiber structure. CONSTITUTION: This fiber structure is impregnated with a resin. The resin is a cross-linked product of a protein. The fiber structure is obtained by impregnating a fiber structure, in which the cross-linking bond of the cross-linked product is a bond between a γ-carboxamide group as the glutamine reside of an amino acid constituting the protein and an ε-amino group as the lysine residue, with the protein and transglutaminase and heat-treating the fiber structure to form an insolubilized product as the cross-linked protein in the fiber structure.

Description

【発明の詳細な説明】Detailed Description of the Invention

【0001】[0001]

【産業上の利用分野】本発明は、繊維構造物に関する。
より詳細には、優れた吸湿性を具備した繊維構造物およ
びその製造方法に関する。
FIELD OF THE INVENTION The present invention relates to a fiber structure.
More specifically, it relates to a fiber structure having excellent hygroscopicity and a method for producing the same.

【0002】[0002]

【従来の技術】従来、合成繊維布帛の快適性はその衣服
内気候により検討され、快適性向上における大きなファ
クターとして吸湿性能の向上が必須であるとされてい
る。
2. Description of the Related Art Conventionally, the comfort of a synthetic fiber cloth has been examined depending on the climate in the clothes, and it has been said that the improvement of the moisture absorption performance is essential as a major factor in improving the comfort.

【0003】合成繊維に吸湿性能を付与する方法とし
て、後加工による方法では、とりわけポリエステルにア
クリル酸をグラフト共重合した後、中和処理を行ない、
−COONa基を導入する方法などが提案されている
が、グラフト率を高くすることが困難であること、グラ
フト率を高くすると力学的特性が低下するなどといった
問題点がある。
As a method for imparting hygroscopicity to synthetic fibers, a post-processing method is, in particular, a graft copolymerization of polyester with acrylic acid, followed by a neutralization treatment.
Although a method of introducing a —COONa group and the like have been proposed, there are problems that it is difficult to increase the graft ratio and that the mechanical properties decrease when the graft ratio is increased.

【0004】これに対して、紡糸時に合成繊維自体を親
水化する試みも行なわれており、ポリオキシアルキレン
エーテルなどを共重合する方法などが提案されている
が、かかる方法で十分な吸湿性を得るためには共重合比
率を高くする必要性があり、吸湿性と力学特性を両立し
た繊維は得られていないのが現状である。
On the other hand, attempts have been made to hydrophilize the synthetic fiber itself at the time of spinning, and a method of copolymerizing polyoxyalkylene ether or the like has been proposed, but such a method provides sufficient hygroscopicity. In order to obtain it, it is necessary to increase the copolymerization ratio, and it is the current situation that fibers having both hygroscopicity and mechanical properties have not been obtained.

【0005】また、これらの方法では加工工程が複雑と
なるなどの問題点もある。
Further, these methods also have a problem that the processing steps are complicated.

【0006】[0006]

【発明が解決しようとする課題】本発明の目的は、前記
従来技術の欠点を解消し、天然由来の蛋白質を利用する
ことから質感、吸湿性能に優れ、耐久性を有する繊維構
造物および水系で酵素反応を利用するため合成繊維自身
の特性を損わず、簡便かつ低コストの繊維構造物の製造
方法を提供することにある。
The object of the present invention is to solve the above-mentioned drawbacks of the prior art and to utilize a naturally-derived protein, so that it is possible to provide a fiber structure and an aqueous system which are excellent in texture, moisture absorption performance and durability. It is an object of the present invention to provide a simple and low-cost method for producing a fiber structure, which does not impair the properties of the synthetic fiber itself because it utilizes an enzymatic reaction.

【0007】[0007]

【課題を解決するための手段】本発明の繊維構造物は前
記課題を解決するため以下の構成を有する。
The fiber structure of the present invention has the following constitution in order to solve the above problems.

【0008】すなわち、樹脂が含浸せしめられた繊維構
造物であって、該樹脂が蛋白質の架橋生成物であり、該
架橋生成物の架橋結合が蛋白質を構成するアミノ酸のグ
ルタミン残基であるγ−カルボキシアミド基とリジン残
基であるε−アミノ基間での結合であることを特徴とす
る繊維構造物である。
That is, a fibrous structure impregnated with a resin, wherein the resin is a cross-linked product of a protein, and the cross-linked bond of the cross-linked product is a glutamine residue of amino acids constituting the protein γ- It is a fiber structure characterized by a bond between a carboxamide group and an ε-amino group which is a lysine residue.

【0009】また、本発明の繊維構造物の製造方法は前
記課題を解決するため以下の構成を有する。
Further, the method for producing a fiber structure of the present invention has the following constitution in order to solve the above problems.

【0010】すなわち、繊維構造物に蛋白質とトランス
グルタミナーゼを含浸せしめ、熱処理することにより、
該繊維構造物中に架橋された蛋白質である不溶化生成物
を形成させることを特徴とする繊維構造物の製造方法で
ある。
That is, by impregnating the fiber structure with protein and transglutaminase and heat-treating,
A method for producing a fiber structure, which comprises forming an insolubilized product which is a crosslinked protein in the fiber structure.

【0011】[0011]

【作用】以下、本発明の繊維構造物を詳細に説明する。The fiber structure of the present invention will be described in detail below.

【0012】本発明において繊維構造物に樹脂を含浸せ
しめてなるとは、繊維構造物を樹脂溶液中に浸漬するこ
とで、樹脂が繊維構造物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
に少なくとも存在することをいい、樹脂が糸束の単繊維
フィラメントあるいはステープルに固着もしくは被覆し
ていることをいう。
In the present invention, the term "impregnating a fiber structure with a resin" means that the resin is soaked in a resin solution so that the resin forms a fiber structure. It means that it is present on at least one of the surfaces, and that the resin is fixed or coated on the monofilament filaments or staples of the yarn bundle.

【0013】該樹脂が蛋白質の架橋生成物であるとは、
含浸せしめた樹脂が蛋白質であり、製造過程によってそ
の蛋白質の分子鎖同志が架橋され、不溶化、3次元構造
となったものをいう。
The fact that the resin is a cross-linked product of protein means that
The impregnated resin is a protein, and the molecular chains of the protein are cross-linked by the production process to insolubilize it to form a three-dimensional structure.

【0014】架橋生成物の架橋結合が蛋白質を構成する
アミノ酸のグルタミン残基であるγ−カルボキシアミド
基とリジン残基であるε−アミノ基間での結合とは、本
発明に使用される酵素(トランスグルタミナーゼ)の反
応形式によるものであり、酵素反応の基質特異性によっ
て形成される結合のことをいう。
The cross-linking of the cross-linking product is a bond between the γ-carboxamide group, which is a glutamine residue of amino acids constituting a protein, and the ε-amino group, which is a lysine residue, of the enzyme used in the present invention. (Transglutaminase) depending on the reaction type, and refers to the bond formed by the substrate specificity of the enzymatic reaction.

【0015】本発明においては酵素反応によって架橋さ
れた蛋白質が布帛を構成する繊維構造中に存在すること
により高い吸湿性を発現することが可能となるのであ
る。
In the present invention, the presence of the protein cross-linked by the enzymatic reaction in the fiber structure constituting the cloth makes it possible to exhibit high hygroscopicity.

【0016】次に、本発明の繊維構造物の製造方法につ
いて説明する。
Next, the method for producing the fiber structure of the present invention will be described.

【0017】本発明の製造方法は繊維構造物を蛋白質と
トランスグルタミナーゼの混合水溶液に含浸し、加熱し
て、酵素反応を促進することにより、蛋白質の不溶化生
成物を形成させるものである。
In the production method of the present invention, a fiber structure is impregnated with a mixed aqueous solution of a protein and transglutaminase and heated to promote an enzymatic reaction to form an insolubilized product of the protein.

【0018】本発明に使用される被架橋蛋白質は、その
起源に制約されず、植物性蛋白質、動物性蛋白質などい
かなるものでも使用できる。
The cross-linked protein used in the present invention is not limited to its origin, and any protein such as plant protein or animal protein can be used.

【0019】植物性蛋白質としては植物種子の脱脂物お
よびそれらから分離した蛋白質、すなわち大豆蛋白質、
小麦蛋白質などを用いることができる。
The vegetable protein includes defatted plant seeds and proteins separated therefrom, that is, soybean protein,
Wheat protein or the like can be used.

【0020】また、動物性蛋白質としては、乳蛋白質
(カゼインなど)、ゼラチン、コラーゲン、ケラチン、
フィブロインなどの水溶液を用いることができる。
Animal proteins include milk proteins (casein etc.), gelatin, collagen, keratin,
An aqueous solution such as fibroin can be used.

【0021】本発明に使用されるトランスグルタミナー
ゼはEC2.3.2.13に属するアシル転移酵素であ
り、動物由来のCa2+依存性のもの、植物や菌体由来
のCa2+依存性が必要とされないものなどが利用でき
る。
The transglutaminase used in the present invention is an acyl transferase belonging to EC 2.3.2.13 and is dependent on Ca 2+ derived from animals, and does not require Ca 2+ dependence derived from plants or fungi. Etc. can be used.

【0022】本発明において、繊維構造物に蛋白質とト
ランスグルタミナーゼを含浸せしめるとは、被架橋蛋白
質とトランスグルタミナーゼの混合水溶液を酵素反応に
適したpHおよび蛋白質濃度に調整し、蛋白質水溶液に
蛋白質の架橋に必要な量のトランスグルタミナーゼを添
加、調整した水溶液中に浸漬することをいう。
In the present invention, impregnating a fiber structure with a protein and transglutaminase means adjusting a mixed aqueous solution of a protein to be crosslinked and transglutaminase to a pH and a protein concentration suitable for an enzymatic reaction, and crosslinking the protein with the aqueous protein solution. It means that the required amount of transglutaminase is added and immersed in the prepared aqueous solution.

【0023】酵素反応速度と製膜性の観点から、pHは
4〜11が好ましく、5〜8がより好ましい。
From the viewpoint of enzyme reaction rate and film forming property, the pH is preferably 4 to 11, and more preferably 5 to 8.

【0024】蛋白質濃度は酵素反応の場合、基質である
蛋白質濃度が低いと進行しにくいが、本発明の場合、後
で述べる熱処理により蛋白質が濃縮されることが理由と
なり、反応の進行が促進される。このため、混合水溶液
中の蛋白質濃度は0.5重量%%以上が好ましく、繊維
構造物の加工性を考慮した濃度であればよい。
In the case of an enzymatic reaction, the protein concentration is less likely to proceed if the concentration of the protein that is the substrate is low, but in the case of the present invention, the progress of the reaction is promoted because the protein is concentrated by the heat treatment described later. It For this reason, the protein concentration in the mixed aqueous solution is preferably 0.5% by weight or more, and may be any concentration considering the processability of the fiber structure.

【0025】蛋白質の架橋に必要な量のトランスグルタ
ミナーゼは、被架橋蛋白質1.0gに対して、0.1ユ
ニット以上添加するのが好ましい。
The amount of transglutaminase required for protein crosslinking is preferably 0.1 unit or more per 1.0 g of the protein to be crosslinked.

【0026】また、酵素の安定性から、水溶液に適宜、
ジチオスレイトール、グルタチオンなどのSH保護作用
物質を添加するのも好ましい。
From the stability of the enzyme, an aqueous solution may be used as appropriate.
It is also preferable to add an SH protective substance such as dithiothreitol or glutathione.

【0027】使用する酵素がCa2+依存性のものであ
れば、混合水溶液中のCa2+濃度が通常10mMにな
るように添加すれば十分である。
If the enzyme used is Ca 2+ -dependent, it is sufficient to add it so that the Ca 2+ concentration in the mixed aqueous solution is usually 10 mM.

【0028】また、熱処理は浸漬により繊維構造物中に
含浸された混合水溶液中での酵素反応の促進と混合水溶
液の水分率を下げて行くことによる蛋白質濃度の上昇に
よる反応の促進を進行させると同時に、最終的には固着
された架橋蛋白質の水分を蒸発させることを目的とする
ものである。
Further, the heat treatment promotes the promotion of the enzymatic reaction in the mixed aqueous solution impregnated in the fiber structure by immersion and the promotion of the reaction due to the increase of the protein concentration by decreasing the water content of the mixed aqueous solution. At the same time, finally, the purpose is to evaporate the water content of the fixed crosslinked protein.

【0029】熱処理方法は従来法における乾熱空気を利
用した乾熱処理、乾熱空気と水蒸気を湿熱処理のいずれ
の方法も利用できる。
As the heat treatment method, any of the conventional methods of dry heat treatment using dry heat air and wet heat treatment of dry heat air and steam can be used.

【0030】熱処理温度は酵素反応の進行、酵素の失
活、水分の蒸発および工程通過性の観点から、10℃以
上が好ましく、30℃以上がより好ましい。被架橋蛋白
質濃度、添加酵素量あるいは熱処理温度にもよるが通常
1分から2時間、熱処理することにより本発明の繊維構
造物が得られる。
The heat treatment temperature is preferably 10 ° C. or higher, more preferably 30 ° C. or higher, from the viewpoints of the progress of enzyme reaction, enzyme deactivation, water evaporation and process passability. The fiber structure of the present invention can be obtained by heat treatment for 1 minute to 2 hours, although it depends on the concentration of the protein to be crosslinked, the amount of added enzyme or the heat treatment temperature.

【0031】以上のように処理液が水系であり、基質特
異性のある酵素反応を利用するため合成繊維への作用が
小さく、繊維特性の変化がない。
As described above, since the treatment liquid is an aqueous system and utilizes an enzyme reaction with substrate specificity, the action on the synthetic fiber is small and the fiber characteristics do not change.

【0032】また、水系の酵素反応であるため薬品の回
収、廃棄といった問題点も解決できるようになるのであ
る。
Further, since it is an aqueous enzymatic reaction, problems such as collection and disposal of chemicals can be solved.

【0033】本発明における繊維構造物とは、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
より作製されたものをいい、具体的には布帛等のことで
ある。
The fiber structure in the present invention means wool,
A natural fiber such as silk or cotton, a synthetic fiber such as nylon, polyester, or acrylic, and a material produced by blended spinning, blended knitting, or blended fiber of these, specifically, a cloth or the like.

【0034】羊毛、絹などのタンパク系繊維、ナイロン
などのポリアミド系繊維では酵素反応により、その末端
アミノ基も架橋結合に関与するため繊維と蛋白質との接
着性がさらに向上する。
In the case of protein fibers such as wool and silk, and polyamide fibers such as nylon, the terminal amino group also participates in the cross-linking due to the enzymatic reaction, so that the adhesion between the fiber and the protein is further improved.

【0035】[0035]

【実施例】以下、本発明をさらに実施例および比較例に
より、さらに詳細に説明する。
The present invention will be described in more detail below with reference to Examples and Comparative Examples.

【0036】実施例中の吸湿度の評価、架橋蛋白質の耐
久性については次の方法にしたがって行なった。
Evaluation of moisture absorption and durability of crosslinked protein in Examples were carried out according to the following methods.

【0037】[吸湿度] 秤量ビンに試験片を入れ、蓋を半分開いたかたちで乗
せた。
[Hygroscopicity] A test piece was put in a weighing bottle, and the lid was placed with the lid half opened.

【0038】秤量ビンを温度20±2℃、相対湿度6
5±2%の恒温恒湿槽の中に入れ、4時間放置後、蓋を
直ちに閉じ、重量を測定した。
The weighing bottle is placed at a temperature of 20 ± 2 ° C. and a relative humidity of 6
The sample was placed in a constant temperature and humidity chamber of 5 ± 2% and left for 4 hours, then the lid was immediately closed and the weight was measured.

【0039】再び容器の蓋を半分開け、110℃で1
時間絶乾後、蓋を直ちに閉じ、重量を測定した。
Open the lid of the container half again, and at 110 ° C.,
After drying for an hour, the lid was immediately closed and the weight was measured.

【0040】上記で求めた重量より秤量ビンの重量を差
し引いた重量から、次式によって吸湿度を算出した。
Moisture absorption was calculated by the following formula from the weight obtained by subtracting the weight of the weighing bottle from the weight obtained above.

【0041】吸湿度(%)=〔(吸湿時の試験片重量−
絶乾時の重量)×100〕/絶乾時の重量 [架橋蛋白質の耐久性] 秤量ビンに試験片を入れ、蓋を半分開いたかたちで乗
せた。
Moisture absorption (%) = [(weight of test piece when absorbing moisture-
Absolutely dry weight) × 100] / absolutely dry weight [Durability of crosslinked protein] A test piece was put in a weighing bottle and placed with the lid half opened.

【0042】秤量ビンを温度110℃で1時間絶乾
後、蓋を直ちに閉じ、重量を測定した。
The weighing bottle was completely dried at a temperature of 110 ° C. for 1 hour, then the lid was immediately closed, and the weight was measured.

【0043】試料を熱湯(90℃)に10分間浸漬し
た。
The sample was immersed in boiling water (90 ° C.) for 10 minutes.

【0044】浸漬後、試料を風乾し、ふたたび秤量ビ
ンに入れ、温度110℃で1時間絶乾後、蓋を直ちに閉
じ、重量を測定した。
After the immersion, the sample was air-dried, put in a weighing bottle again, and completely dried at a temperature of 110 ° C. for 1 hour, then the lid was immediately closed and the weight was measured.

【0045】浸漬前の絶乾重量から浸漬後の絶乾重量
をひき、試料への蛋白固着率に対する重量変化率が5%
以下のものを耐久性がある架橋皮膜であるとした。
The absolute dry weight before the immersion was subtracted from the absolute dry weight after the immersion to obtain a weight change rate of 5% with respect to the protein adhesion rate to the sample.
The following was defined as a durable crosslinked film.

【0046】また、実施例中に用いた蛋白質および酵素
は次のものを使用した。
The following proteins and enzymes were used in the examples.

【0047】蛋白質:ゼラチン精製粉末(ナカライテス
ク株式会社製) 酵素:トランスグルタミナーゼ(EC2.3.2.1
3) 酵素起源:放線菌ストレプトバートシリウム由来 酵素活性:1000ユニット/g [実施例1]ゼラチン精製粉末をイオン交換水に溶解
し、3重量%の水溶液を調整、pH6とした。この水溶
液に蛋白質1g当たり1.25ユニットとなるようにト
ランスグルタミナーゼを添加し含浸処理液を作製した。
Protein: Gelatin purified powder (manufactured by Nacalai Tesque, Inc.) Enzyme: Transglutaminase (EC 2.3.2.1)
3) Enzyme origin: Streptobert silium actinomycete enzyme activity: 1000 units / g [Example 1] The purified gelatin powder was dissolved in ion-exchanged water to prepare a 3 wt% aqueous solution, and the pH was adjusted to 6. To this aqueous solution, transglutaminase was added so that 1.25 units per 1 g of protein were added to prepare an impregnation treatment liquid.

【0048】基布にたて糸、よこ糸が共に75デニール
のポリエステルフィラメント糸使いの平織物を使用し、
前記に作製した含浸処理液に浸漬し、浸漬、絞りを3回
繰り返した後、37℃で2時間インキュベートを行なっ
た。インキュベート後、100℃で乾燥し、酵素を失活
させることで目的の繊維構造物を得た。蛋白の固着量は
布帛重量に対して3.26%であった。
A plain woven fabric using polyester filament yarn with both warp and weft of 75 denier for the base fabric,
It was immersed in the impregnating solution prepared as described above, immersed and squeezed three times, and then incubated at 37 ° C. for 2 hours. After the incubation, the target fiber structure was obtained by drying at 100 ° C. and deactivating the enzyme. The amount of protein fixed was 3.26% based on the weight of the fabric.

【0049】表1に示すように、吸湿性に優れ、また、
皮膜耐久性に優れた繊維構造物が得られた。
As shown in Table 1, it has excellent hygroscopicity, and
A fiber structure having excellent film durability was obtained.

【0050】[0050]

【表1】 [実施例2]基布がたて糸、よこ糸が共に70デニール
のナイロンフィラメント糸使いの平織物である以外は実
施例1と同じ方法で目的の繊維構造物を得た。蛋白の固
着量は布帛重量に対して4.08%であった。
[Table 1] [Example 2] A target fiber structure was obtained in the same manner as in Example 1 except that the base fabric was a plain woven fabric using 70 denier nylon filament yarn for both warp and weft. The amount of protein fixed was 4.08% based on the weight of the fabric.

【0051】表1に示すように、吸湿性に優れ、また、
皮膜耐久性に優れた繊維構造物が得られた。
As shown in Table 1, it has excellent hygroscopicity, and
A fiber structure having excellent film durability was obtained.

【0052】[比較例1]酵素を添加しないこと以外は
実施例1と同じ方法で繊維構造物を作製した。蛋白の固
着量は布帛重量に対して3.18%であった。
Comparative Example 1 A fiber structure was prepared in the same manner as in Example 1 except that the enzyme was not added. The amount of protein fixed was 3.18% based on the weight of the fabric.

【0053】表1に示すように、吸湿性はあるが、酵素
添加を行なわなかったため、皮膜耐久性に劣った繊維構
造物が得られた。
As shown in Table 1, a fibrous structure having hygroscopicity but inferior film durability was obtained because no enzyme was added.

【0054】[0054]

【発明の効果】本発明によれば、質感が良好で、かつ、
吸湿性能に優れ、耐久性を有する繊維構造物および構成
する合成繊維自身の特性を損わない、簡便かつ低コスト
の繊維構造物の製造方法を得ることができる。
According to the present invention, the texture is good, and
It is possible to obtain a simple and low-cost method for producing a fiber structure that does not impair the characteristics of the fiber structure having excellent moisture absorption performance and durability and the synthetic fiber itself that constitutes the fiber structure.

Claims (7)

【特許請求の範囲】[Claims] 【請求項1】樹脂が含浸せしめられた繊維構造物であっ
て、該樹脂が蛋白質の架橋生成物であり、該架橋生成物
の架橋結合が蛋白質を構成するアミノ酸のグルタミン残
基であるγ−カルボキシアミド基とリジン残基であるε
−アミノ基間での結合であることを特徴とする繊維構造
物。
1. A fibrous structure impregnated with a resin, wherein the resin is a cross-linked product of a protein, and the cross-linked bond of the cross-linked product is a glutamine residue of amino acids constituting the protein. Carboxamide group and lysine residue ε
-A fibrous structure characterized in that it is a bond between amino groups.
【請求項2】蛋白質が植物性蛋白質または動物性蛋白質
であることを特徴とする請求項1記載の繊維構造物。
2. The fiber structure according to claim 1, wherein the protein is a vegetable protein or an animal protein.
【請求項3】繊維構造物に蛋白質とトランスグルタミナ
ーゼを含浸せしめ、熱処理することにより、該繊維構造
物中に架橋された蛋白質である不溶化生成物を形成させ
ることを特徴とする繊維構造物の製造方法。
3. A method for producing a fiber structure, which comprises impregnating a fiber structure with a protein and transglutaminase and heat-treating the same to form an insolubilized product which is a crosslinked protein in the fiber structure. Method.
【請求項4】トランスグルタミナーゼがEC2.3.
2.13に属するアシル転移酵素であることを特徴とす
る請求項3記載の繊維構造物の製造方法。
4. A transglutaminase is EC2.3.
The method for producing a fiber structure according to claim 3, which is an acyltransferase belonging to 2.13.
【請求項5】混合水溶液のpHが4〜11であることを
特徴とする請求項3記載の繊維構造物の製造方法。
5. The method for producing a fiber structure according to claim 3, wherein the pH of the mixed aqueous solution is 4 to 11.
【請求項6】混合水溶液における蛋白質濃度が0.5重
量%以上であることを特徴とする請求項3記載の繊維構
造物の製造方法。
6. The method for producing a fiber structure according to claim 3, wherein the protein concentration in the mixed aqueous solution is 0.5% by weight or more.
【請求項7】熱処理温度が10℃以上であることを特徴
とする請求項3記載の繊維構造物の製造方法。
7. The method for producing a fiber structure according to claim 3, wherein the heat treatment temperature is 10 ° C. or higher.
JP7150363A 1995-06-16 1995-06-16 Fiber structure and its production Pending JPH093773A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP7150363A JPH093773A (en) 1995-06-16 1995-06-16 Fiber structure and its production

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP7150363A JPH093773A (en) 1995-06-16 1995-06-16 Fiber structure and its production

Publications (1)

Publication Number Publication Date
JPH093773A true JPH093773A (en) 1997-01-07

Family

ID=15495363

Family Applications (1)

Application Number Title Priority Date Filing Date
JP7150363A Pending JPH093773A (en) 1995-06-16 1995-06-16 Fiber structure and its production

Country Status (1)

Country Link
JP (1) JPH093773A (en)

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2002004739A1 (en) * 2000-07-10 2002-01-17 The Nottingham Trent University A method for enzymatic treatment of textiles such as wool
JP2003041484A (en) * 2001-07-31 2003-02-13 Seiren Co Ltd Textile product and method for producing the same
WO2009066785A1 (en) 2007-11-19 2009-05-28 Ajinomoto Co., Inc. Processed fiber product, and method for production thereof
CN104631109A (en) * 2015-02-02 2015-05-20 浙江理工大学 Method for catalytic reinforcement of fragile silk fabric by employing aminoacidase
CN104631119A (en) * 2015-02-02 2015-05-20 浙江理工大学 Catalytic reinforcement method for fragile silk fabric employing fibroinase
WO2022149306A1 (en) * 2021-01-07 2022-07-14 ミテジマ化学株式会社 Animal hair modification method

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2002004739A1 (en) * 2000-07-10 2002-01-17 The Nottingham Trent University A method for enzymatic treatment of textiles such as wool
JP2003041484A (en) * 2001-07-31 2003-02-13 Seiren Co Ltd Textile product and method for producing the same
WO2009066785A1 (en) 2007-11-19 2009-05-28 Ajinomoto Co., Inc. Processed fiber product, and method for production thereof
CN104631109A (en) * 2015-02-02 2015-05-20 浙江理工大学 Method for catalytic reinforcement of fragile silk fabric by employing aminoacidase
CN104631119A (en) * 2015-02-02 2015-05-20 浙江理工大学 Catalytic reinforcement method for fragile silk fabric employing fibroinase
WO2022149306A1 (en) * 2021-01-07 2022-07-14 ミテジマ化学株式会社 Animal hair modification method

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