JP3283302B2 - Method for producing reduced keratin - Google Patents
Method for producing reduced keratinInfo
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- JP3283302B2 JP3283302B2 JP27783092A JP27783092A JP3283302B2 JP 3283302 B2 JP3283302 B2 JP 3283302B2 JP 27783092 A JP27783092 A JP 27783092A JP 27783092 A JP27783092 A JP 27783092A JP 3283302 B2 JP3283302 B2 JP 3283302B2
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- Prior art keywords
- keratin
- reduced
- reduced keratin
- molecular weight
- aqueous solution
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Description
【０００１】[0001]
【産業上の利用分野】本発明は、高分子量成分が多く、
かつ架橋可能なチオール基を有する還元ケラチンの製造
方法に関する。本発明によって得られる還元ケラチン
は、架橋可能なチオール基を有することと、高分子量成
分が多いという特性を利用して、たとえば膜、フィル
ム、繊維、スポンジなどの製造に好適に使用される。BACKGROUND OF THE INVENTION The present invention relates to a high-molecular weight component,
The present invention relates to a method for producing reduced keratin having a crosslinkable thiol group. The reduced keratin obtained by the present invention is suitably used for production of, for example, membranes, films, fibers, sponges, etc. by utilizing the property of having a crosslinkable thiol group and having a high molecular weight component.
【０００２】[0002]
【従来の技術】毛髪、獣毛、羽毛などの動物組織中に構
造タンパクとして存在するケラチンは、従来から、フィ
ルム、繊維などの産業素材原料として注目されてきた。
しかしながら、ケラチンは、通常の溶媒に対して不溶も
しくは難溶であるため、溶液状態を経て二次加工に利用
するには、加水分解により大幅に短分子量化するか、ま
たはケラチンのジスルフィド結合の還元処理をするか、
あるいは生成したチオール基の化学処理（アルキル化反
応など）による不可逆的修飾を施さなければ利用するこ
とができなかった。2. Description of the Related Art Keratin, which is present as a structural protein in animal tissues such as hair, animal hair, and feathers, has been attracting attention as a raw material for industrial materials such as films and fibers.
However, since keratin is insoluble or hardly soluble in ordinary solvents, it can be used for secondary processing via a solution state by significantly shortening the molecular weight by hydrolysis or reducing the disulfide bond of keratin. To process or
Alternatively, the thiol group could not be used without irreversible modification by chemical treatment (such as an alkylation reaction).
【０００３】すなわち、これまで、ケラチンを溶液状態
を経て二次加工に利用するには、上記のケラチン含有物
質を酸、アルカリまたは酵素により加水分解して短分子
量化したケラチン加水分解物の水溶液として利用する
か、あるいは還元剤と尿素などの蛋白質変成剤との共用
によりケラチンのジスルフィド結合をチオール基に還元
して生成した還元ケラチンの水溶液として利用するか、
あるいは上記の還元ケラチンのチオール基の再結合防止
のためにモノヨード酢酸によりアルキル化誘導体とする
か、あるいは亜硫酸ナトリウム／テトラチオン酸ナトリ
ウムによりＳ−ＳＯ3 - Ｎａ+ 化することによって不可
逆的に化学修飾したケラチン誘導体の水溶液として利用
されてきた。[0003] In other words, in order to utilize keratin in a secondary process through a solution state, a keratin hydrolyzate obtained by hydrolyzing the above keratin-containing substance with an acid, an alkali or an enzyme to shorten the molecular weight has been used. Whether to use as an aqueous solution of reduced keratin generated by reducing the disulfide bond of keratin to a thiol group by sharing a reducing agent and a protein denaturing agent such as urea,
Alternatively S-SO 3 or an alkylated derivative, or by sodium sulfite / sodium tetrathionate by monoiodoacetic acid for recombination prevention of thiol groups of the reducing keratin - irreversibly chemically modified by Na + of It has been used as an aqueous solution of keratin derivatives.
【０００４】[0004]
【発明が解決しようとする課題】しかしながら、加水分
解により短分子量化したケラチン加水分解物は、分子量
が小さいためにフィルムなどに加工したときに強度が劣
り、また水中ではすぐ崩壊するなどの問題があった。However, the keratin hydrolyzate whose molecular weight has been shortened by hydrolysis has a problem that it has poor strength when processed into a film or the like due to its small molecular weight, and also collapses quickly in water. there were.
【０００５】一方、ケラチン含有物質から還元ケラチン
を得るための還元処理においては、ケラチン含有物質に
チオグリコール酸などの還元剤と尿素などの蛋白質変成
剤とからなる可溶化剤を加えて還元抽出した後、透析、
限外濾過などによって可溶化剤を除去することが行われ
ているが、この透析や限外濾過は、大量の水、還元剤、
蛋白質変成剤などの浪費を引き起こす上に、製造時間と
製造費用の増大を引き起こし、しかも過剰の還元剤や蛋
白質変成剤の廃棄に伴い公害を引き起こすという問題が
あった。On the other hand, in a reduction treatment for obtaining reduced keratin from a keratin-containing substance, the keratin-containing substance is reduced and extracted by adding a solubilizing agent comprising a reducing agent such as thioglycolic acid and a protein denaturing agent such as urea. After, dialysis,
Removal of the solubilizing agent by ultrafiltration or the like has been performed, but this dialysis or ultrafiltration requires a large amount of water, a reducing agent,
In addition to the waste of the protein denaturing agent and the like, there is a problem that the production time and the production cost are increased, and moreover, the disposal of the excess reducing agent and the protein denaturant causes pollution.
【０００６】さらに、透析や限外濾過は長時間を要する
ため、還元により生成したチオール基がそれらの間に酸
化されて再結合し、架橋可能なチオール基が失われると
いう問題があり、また、透析や限外濾過による場合は、
還元抽出された還元ケラチンに分子量の低いものが相当
量含まれるため、強度面などで天然高分子原料としての
特長が損なわれてしまうという問題もあった。In addition, since dialysis and ultrafiltration require a long time, thiol groups generated by reduction are oxidized and recombined between them, resulting in a loss of crosslinkable thiol groups. If using dialysis or ultrafiltration,
Since the reduced and extracted keratin contains a considerable amount of low-molecular-weight keratin, there is also a problem that the characteristics as a natural polymer raw material are impaired in terms of strength and the like.
【０００７】[0007]
【課題を解決するための手段】本発明者は、上記事情に
鑑み、ケラチン含有物質から還元抽出された還元ケラチ
ンの単離法の効率化と該還元ケラチン中の高分子量成分
の増加について鋭意検討を重ねた結果、ケラチン含有物
質を水性媒体中、蛋白質変成剤の存在下、または蛋白質
変成剤と界面活性剤の存在下で、還元剤で還元し、不溶
物を遠心または濾過により除去した後、得られた水溶液
に塩化ナトリウムや硫酸アンモニウムなどの無機塩を添
加して塩析するときは、抽出された還元ケラチンがその
還元状態を保持したまま短時間で単離され、高分子量成
分が多く、かつ架橋可能なチオール基を有する還元ケラ
チンが容易に得られることを見出し、本発明を完成する
にいたった。Means for Solving the Problems In view of the above circumstances, the present inventors diligently studied the efficiency of the method for isolating reduced keratin extracted and reduced from keratin-containing substances and the increase in high molecular weight components in the reduced keratin. As a result, the keratin-containing substance is reduced with a reducing agent in an aqueous medium, in the presence of a protein denaturing agent, or in the presence of a protein denaturing agent and a surfactant, and insolubles are removed by centrifugation or filtration. When salting out by adding an inorganic salt such as sodium chloride or ammonium sulfate to the obtained aqueous solution, the extracted reduced keratin is isolated in a short time while maintaining its reduced state, and has a high molecular weight component, and The inventors have found that reduced keratin having a crosslinkable thiol group can be easily obtained, and have completed the present invention.
【０００８】すなわち、ケラチン含有物質を上記のよう
に水性媒体中で還元すると、還元された還元ケラチンは
水性媒体中に溶解し、ケラチンを包んでいたキューティ
クルなどは不溶物として水性媒体中に存在する。That is, when a keratin-containing substance is reduced in an aqueous medium as described above, the reduced reduced keratin dissolves in the aqueous medium, and the cuticle or the like encapsulating keratin exists as an insoluble substance in the aqueous medium. .
【０００９】そこで、この不溶物を遠心または濾過によ
り除去した後、塩化ナトリウムや硫酸アンモニウムなど
の無機塩を添加して溶液のイオン化強度を上げると塩析
が生じ、水性媒体中に溶解していた還元ケラチンが還元
された状態を保持したまま、つまりケラチンを還元した
ときに生成したチオール基がほぼ保持された状態で、溶
液中から高収率で沈殿する。Therefore, after removing the insoluble matter by centrifugation or filtration, if the ionization strength of the solution is increased by adding an inorganic salt such as sodium chloride or ammonium sulfate, salting out occurs, and the reduction dissolved in the aqueous medium is reduced. The keratin precipitates from the solution in a high yield while maintaining the reduced state of keratin, that is, while substantially retaining the thiol group generated when keratin is reduced.
【００１０】一方、還元剤、蛋白質変成剤、界面活性剤
などは、水性媒体中に溶解して水性媒体中に残るので、
濾過、遠心分離などにより還元ケラチンを反応液から単
離することができる。On the other hand, a reducing agent, a protein denaturing agent, a surfactant and the like dissolve in an aqueous medium and remain in the aqueous medium.
Reduced keratin can be isolated from the reaction solution by filtration, centrifugation, or the like.
【００１１】この際、低分子量の蛋白質は水性媒体中に
溶解しやすいため、単離された還元ケラチン中には低分
子量のものがほとんど含まれず、したがって、高分子量
成分の多い還元ケラチンが得られる。At this time, since the low molecular weight protein is easily dissolved in the aqueous medium, the isolated reduced keratin hardly contains the low molecular weight keratin, and thus reduced keratin having a high molecular weight component is obtained. .
【００１２】また、水性媒体中から還元ケラチンが短時
間で沈殿するので、長時間を要する透析や限外濾過によ
る場合のように還元ケラチン中のチオール基が酸化を受
けることが少なく、したがってチオール基がほとんど損
なわれることなく保持される。Further, since reduced keratin precipitates from the aqueous medium in a short time, the thiol group in the reduced keratin is less likely to be oxidized as in the case of dialysis or ultrafiltration requiring a long time. Is retained with little loss.
【００１３】上記方法によれば、分子量が３０，０００
〜１３０，０００のものを主成分とし、アミノ酸１００
残基当り４〜１６個のシステインを有する還元ケラチン
が得られる。そして、その収率は人間の毛髪や羊毛を出
発原料とする場合３５〜５０％程度であり、羽毛を出発
原料とするときは収率が約８０％に達する。According to the above method, the molecular weight is 30,000.
~ 130,000 as the main component, 100 amino acids
Reduced keratins with 4 to 16 cysteines per residue are obtained. The yield is about 35 to 50% when human hair or wool is used as a starting material, and the yield reaches about 80% when feathers are used as a starting material.
【００１４】ここで、上記の還元ケラチンがアミノ酸１
００残基当り４〜１６個のシステインを有することと、
還元ケラチンがその還元状態をほぼ保持したまま、つま
り還元により生成したチオール基をほぼ保持した状態で
得られることとの関係について説明すると、次の通りで
ある。Here, the above reduced keratin is amino acid 1
Having 4-16 cysteines per 00 residues;
The relationship between reduced keratin obtained while substantially maintaining its reduced state, that is, obtained while substantially maintaining thiol groups generated by reduction, will be described as follows.
【００１５】ケラチンは、その含有物質の種類によって
多少異なるが、アミノ酸分析すると、一般にアミノ酸１
００残基当り２〜８個のシスチン（ハーフシスチンとし
ては４〜１６個）を含んでいる。[0015] Keratin differs somewhat depending on the type of the substance contained therein.
It contains 2 to 8 cystine (4 to 16 half cystine) per 00 residues.
【００１６】そこで、このケラチンを還元すると、シス
チン中のジスルフィド結合（−Ｓ−Ｓ−結合）が開裂し
てチオール基（−ＳＨ基）になり、シスチンはシステイ
ンになる。Thus, when this keratin is reduced, the disulfide bond (-SS-bond) in cystine is cleaved to form a thiol group (-SH group), and cystine becomes cysteine.
【００１７】したがって、還元されたケラチンはチオー
ル基を有しているが、従来は長時間を要する透析や限外
濾過により還元剤や蛋白質変成剤などの可溶化剤を除去
していたため、それらの間にチオール基が酸化を受けて
失われていたが、本発明では塩析により還元ケラチンを
反応液中から短時間で沈殿させて単離するので、チオー
ル基が酸化を受けることが少なく、還元状態をほぼ保持
したまま還元ケラチンが得られる。Therefore, although reduced keratin has a thiol group, conventionally, dialysis or ultrafiltration, which requires a long time, removes a solubilizing agent such as a reducing agent or a protein denaturing agent. In the meantime, the thiol group was lost due to oxidation, but in the present invention, the reduced keratin is precipitated and isolated from the reaction solution in a short time by salting out, so that the thiol group is less likely to be oxidized and reduced. Reduced keratin can be obtained while maintaining almost the same state.
【００１８】したがって、本発明により得られる還元ケ
ラチンは、その出発物質のケラチン含有物質中のケラチ
ンに応じて、アミノ酸１００残基当り４〜１６個のシス
テインを有しており、これは還元ケラチンが還元により
生成したチオール基をほぼ保持した状態で得られたこと
に相当する。Therefore, the reduced keratin obtained according to the present invention has 4 to 16 cysteines per 100 amino acid residues, depending on the keratin in the keratin-containing starting material, which is This corresponds to that the thiol group generated by the reduction was obtained in a state where it was substantially retained.
【００１９】また、ケラチンの分子量は、その含有物質
によって多少異なるが、一般に１０，０００〜１３０，
０００である。本発明では塩析により還元ケラチンを反
応液中から沈殿させて単離するので、水に溶解しやすい
低分子量の蛋白質（この中には低分子量の還元ケラチン
も含まれる）がほとんど含まれず、分子量３０，０００
〜１３０，０００のものを主成分とする高分子量成分の
多い還元ケラチンが得られる。The molecular weight of keratin varies somewhat depending on the substance contained therein.
000. In the present invention, reduced keratin is precipitated from the reaction solution by salting out and isolated, so that low-molecular-weight proteins that are easily soluble in water (including low-molecular-weight reduced keratin) are hardly contained. 30,000
~ 130,000 reduced keratin having a large amount of high molecular weight components as a main component is obtained.
【００２０】本発明において還元ケラチンとは、還元工
程を経て得られたものをいうが、その還元によりケラチ
ン中のシスチンのすべてが還元されているということを
意味するものではなく、ケラチン中のシスチンの一部が
還元されることなく残存しているものであってもよい。In the present invention, reduced keratin refers to one obtained through a reduction step, but does not mean that all cystine in keratin has been reduced by the reduction, and it does not mean that cystine in keratin is reduced. May remain without being reduced.
【００２１】そして、上記のようにして得られた還元ケ
ラチンは凍結乾燥法などの手段により粉末にしたり、あ
るいは必要に応じ少量の界面活性剤と酸化防止のための
還元剤を添加した水に溶解することによって、還元ケラ
チンの水溶液とすることができる。The reduced keratin obtained as described above is powdered by a method such as freeze-drying, or dissolved in water to which a small amount of a surfactant and a reducing agent for preventing oxidation are added as required. By doing so, an aqueous solution of reduced keratin can be obtained.
【００２２】本発明において、還元ケラチンを得るにあ
たり、出発原料として用いるケラチン含有物質として
は、ケラチンを含むものであればよく、たとえば人間の
毛髪、羊毛、馬毛、牛毛などの獣毛や、鶏などの鳥類の
羽毛、牛などの動物の爪や角、ひずめ（蹄）、魚のうろ
こ（鱗）などを用いることができる。In the present invention, in order to obtain reduced keratin, the keratin-containing substance used as a starting material may be any substance containing keratin, such as animal hair such as human hair, wool, horse hair, and cow hair, and chicken hair. For example, feathers of birds such as birds, claws and horns of animals such as cows, hooves (hoofs), and fish scales (scales) can be used.
【００２３】上記の水性媒体は、水単独、または水と水
混和性の有機溶媒との混合物であってもよく、含水率が
５０重量％以上、好ましくは８０重量％以上の溶媒を用
いる。水混和性の有機溶媒としては、たとえばメタノー
ル、エタノールなどの低級脂肪族アルコールなどが挙げ
られる。The aqueous medium may be water alone or a mixture of water and a water-miscible organic solvent. A solvent having a water content of 50% by weight or more, preferably 80% by weight or more is used. Examples of the water-miscible organic solvent include lower aliphatic alcohols such as methanol and ethanol.
【００２４】還元剤は、ケラチン含有物質中のケラチン
のジスルフィド結合を還元してチオール基に変換する作
用をするものであり、この還元剤としては、たとえば２
−メルカプトエタノール、チオグリコール酸、ジチオス
レイトール、ジチオエリトリトールなどのチオール化合
物；トリプロピルホスフィン、トリブチルホスフィンな
どの有機リン化合物；亜硫酸水素ナトリウムなどの還元
能力を持つ無機化合物などが挙げられる。The reducing agent acts to reduce the disulfide bond of keratin in the keratin-containing substance to convert it into a thiol group.
Thiol compounds such as mercaptoethanol, thioglycolic acid, dithiothreitol and dithioerythritol; organic phosphorus compounds such as tripropylphosphine and tributylphosphine; and inorganic compounds having a reducing ability such as sodium bisulfite.
【００２５】これらの還元剤の使用量は、通常、ケラチ
ン含有物質１０ｇに対して０．０５〜０．５０モルであ
り、還元反応の効率と経済性を考慮すると、ケラチン含
有物質１０ｇに対して０．０５〜０．２０モルが好まし
い。The amount of the reducing agent used is usually 0.05 to 0.50 mol per 10 g of the keratin-containing substance, and considering the efficiency and economy of the reduction reaction, 10 g of the keratin-containing substance is used. 0.05 to 0.20 mol is preferred.
【００２６】蛋白質変成剤は、ケラチン中の水素結合を
切断する作用を有するもので、その具体例としては、た
とえば尿素、チオ尿素などが好適なものとして挙げられ
る。そして、爪、ひずめ、うろこなどのように堅い組織
のケラチン含有物質を使用する場合には、粉砕した後、
蛋白質に対して溶解作用を有する水酸化ナトリウム、ア
ンモニアなどのアルカリを溶解助剤として用いることが
好ましい。The protein denaturing agent has an action of breaking a hydrogen bond in keratin, and specific examples thereof include urea and thiourea. And when using keratin-containing substances with hard tissues such as nails, hooves, scales, etc., after crushing,
It is preferable to use an alkali having a dissolving effect on proteins, such as sodium hydroxide and ammonia, as a dissolution aid.
【００２７】こらの蛋白質変成剤の濃度と使用量は、ケ
ラチン含有物質の溶解性などを考慮して決定するのが適
しているが、通常、ケラチン含有物質に対して３〜１０
ｍｏｌ／ｌ濃度のものを５〜４０倍重量、好ましくは５
〜８ｍｏｌ／ｌ濃度のものを１０〜３０倍重量である。The concentration and the amount of the protein denaturing agent are suitably determined in consideration of the solubility of the keratin-containing substance and the like.
mol / l concentration 5 to 40 times the weight, preferably 5
The concentration of ８8 mol / l is 10 to 30 times the weight.
【００２８】本発明において、還元工程は、上記のよう
な蛋白質変成剤の存在下、または蛋白質変成剤と界面活
性剤の存在下で行われるが、後者のように界面活性剤を
共存させた場合は、還元速度が速くなり、ケラチン含有
物質からの還元ケラチンの抽出速度が向上する。ただ
し、界面活性剤は還元ケラチンを可溶化する作用がある
ので、塩析のために添加する無機塩を多くする必要があ
る。In the present invention, the reduction step is carried out in the presence of a protein denaturing agent as described above, or in the presence of a protein denaturing agent and a surfactant. In the method, the reduction rate is increased, and the extraction rate of reduced keratin from the keratin-containing substance is improved. However, since the surfactant has an action of solubilizing the reduced keratin, it is necessary to increase the amount of the inorganic salt added for salting out.
【００２９】上記界面活性剤としては、下記のアニオン
界面活性剤、カチオン界面活性剤、両性界面活性剤、ノ
ニオン界面活性剤のいずれも用いることができる。As the above-mentioned surfactant, any of the following anionic surfactants, cationic surfactants, amphoteric surfactants and nonionic surfactants can be used.
【００３０】アニオン界面活性剤としては、たとえばド
デシル硫酸ナトリウムなどのアルキル硫酸塩、アルキル
硫酸エステル塩、脂肪酸アルコールリン酸エステル塩、
スルホコハク酸エステル塩などのアニオン界面活性剤が
挙げられる。Examples of the anionic surfactant include alkyl sulfates such as sodium dodecyl sulfate, alkyl sulfates, fatty acid alcohol phosphates, and the like.
Anionic surfactants such as sulfosuccinate salts are exemplified.
【００３１】カチオン界面活性剤としては、たとえば次
式で示されるカチオン界面活性剤などが挙げられる。 〔Ｒ1 ・Ｒ2 ・Ｒ3 ・Ｒ4 Ｎ〕+ Ｘ- 〔式中、Ｒ1 、Ｒ2 、Ｒ3 およびＲ4 の１個または２個
は直鎖もしくは分岐鎖を有する炭素数８〜２０のアルキ
ル基またはヒドロキシアルキル基であり、残余は水素原
子、炭素数１〜３のアルキル基もしくはヒドロキシアル
キル基またはベンジル基である。Ｘはハロゲン原子、炭
素数１〜２個のアルキル硫酸基またはアルキルピリジニ
ウムハライドなどの芳香族四級アミン塩などである〕。Examples of the cationic surfactant include a cationic surfactant represented by the following formula. [R 1 · R 2 · R 3 · R 4 N ] + X - wherein, R 1, R 2, 1 or 2 R 3 and R 4 8 carbon atoms having a linear or branched 20 alkyl groups or hydroxyalkyl groups, the remainder being a hydrogen atom, an alkyl group having 1 to 3 carbon atoms, a hydroxyalkyl group or a benzyl group. X is a halogen atom, an alkyl sulphate group having 1 to 2 carbon atoms or an aromatic quaternary amine salt such as an alkylpyridinium halide.
【００３２】両性界面活性剤としては、たとえば脂肪族
アミンのＮ−カルボキシメチル体、Ｎ−スルホアルキル
化体、イミダゾリンスルホン酸などのベタイン系の両性
界面活性剤（疎水基は主として炭素数１２〜１４のアル
キル基またはアシル基、対イオンはアルカリ金属などで
ある）などが挙げられる。The amphoteric surfactants include, for example, betaine amphoteric surfactants such as N-carboxymethyl, N-sulfoalkylated aliphatic amines and imidazoline sulfonic acid (hydrophobic groups mainly having 12 to 14 carbon atoms). And the counter ion is an alkali metal or the like).
【００３３】ノニオン界面活性剤としては、たとえばポ
リオキシエチレンアルキルエーテル型、脂肪酸エステル
型、ポリエチレンイミン型、ポリグリセリンエーテル
型、ポリグリセリンエステル型などのノニオン界面活性
剤（疎水基は主として炭素数１２〜１４のアルキル基も
しくはアシル基である）などが挙げられる。The nonionic surfactants include, for example, nonionic surfactants such as polyoxyethylene alkyl ether type, fatty acid ester type, polyethyleneimine type, polyglycerin ether type and polyglycerin ester type (hydrophobic group mainly has 12 to carbon atoms). 14 alkyl groups or acyl groups).
【００３４】そして、この界面活性剤の還元工程での使
用量はケラチン含有物質の５〜５０重量％が好ましい。The amount of the surfactant used in the reduction step is preferably 5 to 50% by weight of the keratin-containing substance.
【００３５】界面活性剤としては、前記したように、ア
ニオン界面活性剤、カチオン界面活性剤、両性界面活性
剤、ノニオン界面活性剤のいずれも使用することができ
るが、なかでもアニオン界面活性剤、たとえばアルキル
硫酸塩やポリオキシエチレンアルキルエーテル硫酸塩な
どが特に好ましい。As described above, any of anionic surfactants, cationic surfactants, amphoteric surfactants and nonionic surfactants can be used as described above. For example, alkyl sulfates and polyoxyethylene alkyl ether sulfates are particularly preferred.
【００３６】還元工程の具体的操作は、たとえば次のよ
うにして行われる。すなわち、ケラチン含有物質をその
全量が浸るに充分な５〜４０重量倍の３〜１０Ｍ（ｍｏ
ｌ／ｌ）の蛋白質変成剤水溶液、たとえば尿素の場合に
は、５〜８Ｍの尿素水溶液に浸漬し、還元剤または還元
剤と界面活性剤を加えてから容器を密栓し、室温〜１０
０℃で１〜２４時間加熱攪拌する。The specific operation of the reduction step is performed, for example, as follows. That is, 3 to 10 M (mo.) Of 5 to 40 times by weight that is sufficient to immerse the whole amount of the keratin-containing substance.
1 / l) of a protein denaturing agent aqueous solution, for example, in the case of urea, is immersed in a 5-8M urea aqueous solution, a reducing agent or a reducing agent and a surfactant are added thereto, and the container is tightly sealed.
Heat and stir at 0 ° C. for 1-24 hours.
【００３７】上記還元工程において、反応系に超音波を
照射すると、還元抽出作用を促進することができ、還元
工程に要する時間を短縮することができる。超音波照射
はプローブ型、浴槽型などの公知の超音波照射装置を用
いることができる。超音波照射の強さは反応系の大きさ
により異なるが、たとえば反応系の大きさが１リットル
以下のときは出力５０〜２００Ｗで充分である。In the above reduction step, when the reaction system is irradiated with ultrasonic waves, the reduction extraction action can be promoted and the time required for the reduction step can be shortened. For the ultrasonic irradiation, a known ultrasonic irradiation device such as a probe type or a bathtub type can be used. The intensity of ultrasonic irradiation varies depending on the size of the reaction system. For example, when the size of the reaction system is 1 liter or less, an output of 50 to 200 W is sufficient.
【００３８】上記の還元工程を経て得られた反応液は、
不溶物を含むので、これを遠心分離や濾過により除去し
た後、塩析により還元ケラチンを沈殿させる。The reaction solution obtained through the above reduction step is
Since it contains insolubles, it is removed by centrifugation or filtration, and then reduced keratin is precipitated by salting out.
【００３９】塩析は、塩化ナトリウム、硫酸アンモニウ
ム、硫酸ナトリウムなどの無機塩を上記不溶物除去後の
水溶液に加えることによって行われる。この塩析にあた
っては、上記水溶液を塩酸などの酸を加えて弱酸性（ｐ
Ｈ３〜５、特に３．５付近が好適）にしておくことが好
ましい。また、アセトンやメタノール、エタノールなど
の極性有機溶媒を併用添加し、塩析効果を上げてもよ
い。The salting out is carried out by adding an inorganic salt such as sodium chloride, ammonium sulfate, sodium sulfate or the like to the aqueous solution after removing the insolubles. In this salting-out, the aqueous solution is acidified by adding an acid such as hydrochloric acid (p.
H3 to 5, particularly preferably around 3.5). In addition, a polar organic solvent such as acetone, methanol or ethanol may be added in combination to enhance the salting out effect.
【００４０】この塩析にあたっての無機塩の添加量は、
ケラチン素抽出液（キューティクルなどの不溶物を除去
したもの）に対して無機塩が０．１〜２Ｍの濃度になる
ようにすることが適しており、特に０．５〜０．７Ｍの
濃度になるようにすることが好ましい。The amount of the inorganic salt to be added for the salting out is as follows.
It is suitable that the concentration of the inorganic salt is adjusted to 0.1 to 2 M with respect to the keratin element extract solution (one from which insoluble substances such as cuticles are removed), and particularly to a concentration of 0.5 to 0.7 M. Preferably.
【００４１】塩析時の温度は０℃近辺から４０℃の範囲
が適しており、塩析に要する時間は短時間で、長くても
１０分間程度をみておけば充分である。The temperature at the time of salting out is preferably in the range of around 0 ° C. to 40 ° C., and the time required for salting out is short, and it is sufficient to allow about 10 minutes at most.
【００４２】上記のようにして固形物として得られた還
元ケラチンは、水洗後、必要に応じ凍結乾燥法などによ
り粉末とするか、あるいはアンモニアなどで弱アルカリ
（ｐＨ８〜９）としつつ還元ケラチンに対して５〜５０
重量％の界面活性剤を含んだ水溶液（酸化防止のために
還元剤を少量含有させてもよい）を加えて可溶化して透
明な水溶液とすることができる。The reduced keratin obtained as a solid as described above may be washed with water and then powdered by freeze-drying or the like, if necessary, or reduced keratin while being made weakly alkaline (pH 8 to 9) with ammonia or the like. 5 to 50
An aqueous solution containing a surfactant by weight (which may contain a small amount of a reducing agent to prevent oxidation) is added to solubilize the solution, and a transparent aqueous solution can be obtained.
【００４３】この水溶液中での還元ケラチンの濃度は、
使用した界面活性剤を含んだ水溶液の量で０．１〜１０
重量％程度に制御することができるが、抽出と塩析の操
作工程を簡便化するため、特に１〜５重量％程度にして
おくことが好ましい。この水溶液は薄いミルク状になっ
ている場合があるが、この場合はさらに濾過処理するこ
とにより、透明度を上げることができる。The concentration of reduced keratin in this aqueous solution is
0.1 to 10 in the amount of the aqueous solution containing the used surfactant
Although it can be controlled to about weight%, it is particularly preferable to keep it at about 1 to 5 weight% in order to simplify the operation steps of extraction and salting out. This aqueous solution may be in the form of a thin milk. In this case, the transparency can be increased by further filtering.
【００４４】上記のようにして得られた還元ケラチン
は、ポリアクリルアミド電気泳動法で分子量を測定する
と、原料として用いたケラチン含有物質によって若干異
なるが、分子量３０，０００〜１３０，０００のものを
８０％以上含んでおり、分子量１５，０００以下のもの
は実質上含んでいない。The molecular weight of the reduced keratin obtained as described above is slightly different depending on the keratin-containing substance used as a raw material when the molecular weight is measured by polyacrylamide electrophoresis, but the reduced keratin has a molecular weight of 30,000 to 130,000. %, And those having a molecular weight of 15,000 or less are not substantially contained.
【００４５】同じ条件下で抽出された還元ケラチンを透
析や限外濾過処理で水溶液として得る方法では、分子量
１５，０００〜１３０，０００のものを主成分としてい
るものの、分子量１５，０００以下のものが０．５〜１
割程度混在している。そのため、後記の試験例で明らか
にするように、フィルム化した時の強度は本発明の還元
ケラチンをフィルム化したものに比べて低い。In a method of obtaining reduced keratin extracted under the same conditions as an aqueous solution by dialysis or ultrafiltration, a method mainly comprising one having a molecular weight of 15,000 to 130,000, but one having a molecular weight of 15,000 or less Is 0.5-1
They are mixed at about 30%. Therefore, as clarified in the test examples described later, the strength when formed into a film is lower than that when the reduced keratin of the present invention is formed into a film.
【００４６】また、本発明で得られた還元ケラチンをア
ミノ酸分析すると、原料として使用したケラチン含有物
質によって若干変動するものの、アミノ酸１００残基当
りシステインを４〜１６個有している。When the reduced keratin obtained in the present invention is subjected to amino acid analysis, the reduced keratin has 4 to 16 cysteines per 100 amino acid residues, depending on the keratin-containing substance used as a raw material.
【００４７】本発明の方法により還元ケラチンの製造に
要する時間は、透析や限外濾過処理による既知の方法に
比べて、大幅に短縮することができる。たとえば、上記
既知の方法では、１００ｍｌのケラチン抽出液につき透
析や限外濾過に１０〜５０時間程度要するが、本発明の
方法による場合、塩析は短時間で行われるので、大幅な
時間短縮を達成できる。The time required for the production of reduced keratin according to the method of the present invention can be greatly reduced as compared with known methods employing dialysis or ultrafiltration. For example, in the above-mentioned known method, dialysis and ultrafiltration require about 10 to 50 hours for 100 ml of keratin extract. However, according to the method of the present invention, salting out is performed in a short time, so that the time is greatly reduced. Can be achieved.
【００４８】また、本発明により還元ケラチンを製造す
る場合は、尿素などの蛋白質変成剤の回収と再使用が容
易である。すなわち、従来の透析や限外濾過では、還元
ケラチンと蛋白質変成剤や残余の還元剤などを大量（単
離還元ケラチン１ｇ当り１〜２リットル）のしかもイオ
ン交換水や蒸留水などの清浄な水を使用して分離するた
め、蛋白質変成剤などは大量の水に溶解しており、その
回収、再使用がきわめて困難であり、また、その廃水処
理にあたって大規模な公害対策も必要になる。In the case of producing reduced keratin according to the present invention, it is easy to recover and reuse a protein denaturant such as urea. That is, in conventional dialysis or ultrafiltration, reduced keratin, protein denaturing agent, residual reducing agent, and the like are used in large amounts (1-2 liters per gram of isolated reduced keratin) and in clean water such as ion-exchanged water or distilled water. Since the protein denaturant is dissolved in a large amount of water, it is extremely difficult to recover and reuse it, and large-scale pollution countermeasures are required for wastewater treatment.
【００４９】これに対して、本発明では水道水を使用す
ることができ、しかもその消費量は単離還元ケラチン１
ｇ当り約０．２リットルと格段と少なく、蛋白質変成剤
などの回収と再使用が容易である。もとより、本発明に
よれば、水の大量使用の必要がなく、水の浪費がない。On the other hand, in the present invention, tap water can be used, and the amount of consumption of the isolated reduced keratin 1
The amount is extremely small at about 0.2 liter per g, and the recovery and reuse of the protein denaturant and the like are easy. Of course, according to the present invention, there is no need to use a large amount of water and no waste of water.
【００５０】[0050]
【実施例】つぎに、実施例を挙げて本発明をさらに詳し
く説明するが、本発明はそれらの実施例のみに限定され
るものではない。EXAMPLES Next, the present invention will be described in more detail with reference to examples, but the present invention is not limited to these examples.
【００５１】実施例１ 羊毛（Ｃｏｌｌｉｄａｌｅ種より採取）２０ｇを５Ｍ尿
素水溶液５５０ｇに浸漬し、２−メルカプトエタノール
２５ｍｌを添加した後、容器を密栓し、６０℃にて２４
時間振盪攪拌した。反応液を室温に戻し、不溶物を濾過
により除去した後、濾液を塩酸でｐＨ５に調整し、その
後、硫酸ナトリウム５５ｇを添加して塩析し、密栓、攪
拌した後、遠心分離した。Example 1 20 g of wool (collected from Collidale species) was immersed in 550 g of a 5M aqueous urea solution, 25 ml of 2-mercaptoethanol was added, the container was capped and sealed at 60 ° C. for 24 hours.
Shake for hours. After the reaction solution was returned to room temperature and insolubles were removed by filtration, the filtrate was adjusted to pH 5 with hydrochloric acid, and then 55 g of sodium sulfate was added thereto for salting out, sealed, stirred, and centrifuged.
【００５２】得られた白色沈殿物を２−メルカプトエタ
ノールを０．３重量％含む水で洗浄し、ドデシル硫酸ナ
トリウム（ＳＤＳ）３ｇと２−メルカプトエタノール
０．６ｇを添加した水２００ｍｌを加え、アンモニアで
ｐＨ８〜９に調整しつつ、溶解した。The obtained white precipitate was washed with water containing 0.3% by weight of 2-mercaptoethanol, and 200 ml of water to which 3 g of sodium dodecyl sulfate (SDS) and 0.6 g of 2-mercaptoethanol were added, and ammonia was added. While adjusting the pH to 8-9 with.
【００５３】この水溶液１０ｇをＬｏｗｒｙ法により蛋
白定量したところ、０．３５ｇの還元ケラチンを含んで
おり、この水溶液中の還元ケラチン濃度は３．５重量％
であって、収率は３５％であった。また上記水溶液を凍
結乾燥して得た還元ケラチン粉末のアミノ酸分析を行っ
たところ、アミノ酸１００残基当りシステインが８．４
個、シスチンが１．５個であった。When the protein content of 10 g of this aqueous solution was determined by the Lowry method, it contained 0.35 g of reduced keratin, and the reduced keratin concentration in this aqueous solution was 3.5% by weight.
And the yield was 35%. Amino acid analysis of the reduced keratin powder obtained by freeze-drying the above aqueous solution revealed that cysteine was found to be 8.4 per 100 amino acid residues.
And 1.5 cystine.
【００５４】また、上記還元ケラチン粉末の分子量をポ
リアクリルアミド電気泳動法で調べたところ、分子量４
０，０００から６０，０００のものが約９０％であり、
分子量３０，０００未満のものは５％以下であった。The molecular weight of the reduced keratin powder was determined by polyacrylamide electrophoresis.
Approximately 90% are from 000 to 60,000,
Those having a molecular weight of less than 30,000 were 5% or less.
【００５５】実施例２ 羊毛（Ｃｏｌｌｉｄａｌｅ種より採取）４ｇを５Ｍ尿素
水溶液１３０ｍｌに浸漬し、２−メルカプトエタノール
６ｍｌを添加した後、容器を密栓、攪拌し、約５０℃で
５時間、２００Ｗの出力にて超音波照射した。反応液を
室温に戻し、不溶物を濾過により除去した後、濾液を塩
酸で弱酸性（ｐＨ５）にし、硫酸ナトリウム１３ｇを添
加すると共に攪拌すると、塩析により還元ケラチンが沈
殿した。Example 2 4 g of wool (collected from Collidale species) was immersed in 130 ml of a 5M aqueous urea solution, 6 ml of 2-mercaptoethanol was added, the container was tightly stoppered and stirred, and a power of 200 W was output at about 50 ° C. for 5 hours for 5 hours. Was irradiated with ultrasonic waves. After the reaction solution was returned to room temperature and insolubles were removed by filtration, the filtrate was made weakly acidic (pH 5) with hydrochloric acid, and 13 g of sodium sulfate was added and stirred. Then, reduced keratin was precipitated by salting out.
【００５６】沈殿物を遠心分離で液から分離し、得られ
た還元ケラチンを２−メルカプトエタノールを０．３重
量％含む水で水洗した後、ドデシル硫酸ナトリウム（Ｓ
ＤＳ）０．７５ｇと２−メルカプトエタノール０．６ｇ
を添加した水１００ｍｌに溶解した。The precipitate was separated from the liquid by centrifugation, and the obtained reduced keratin was washed with water containing 0.3% by weight of 2-mercaptoethanol, and then sodium dodecyl sulfate (S
DS) 0.75 g and 2-mercaptoethanol 0.6 g
Was dissolved in 100 ml of water.
【００５７】この水溶液１０ｇをＬｏｗｒｙ法により蛋
白定量したところ、０．２ｇの還元ケラチンを含んでお
り、水溶液中の還元ケラチン濃度は２重量％であって、
収率は約５０％であった。また上記水溶液を凍結乾燥し
て得た還元ケラチン粉末のアミノ酸分析を行ったとこ
ろ、アミノ酸１００残基当りシステインが８．５個であ
った。When 10 g of this aqueous solution was subjected to protein quantification by the Lowry method, it contained 0.2 g of reduced keratin, and the concentration of reduced keratin in the aqueous solution was 2% by weight.
The yield was about 50%. Amino acid analysis of the reduced keratin powder obtained by freeze-drying the above aqueous solution revealed that cysteine was 8.5 per 100 amino acid residues.
【００５８】また、上記還元ケラチン粉末の分子量をポ
リアクリルアミド電気泳動法で調べたところ、分子量３
０，０００から１２０，０００のものが９０％以上であ
り、分子量３０，０００未満のものは５％以下であっ
た。The molecular weight of the reduced keratin powder was determined by polyacrylamide gel electrophoresis.
Those having a molecular weight of from 000 to 120,000 were 90% or more, and those having a molecular weight of less than 30,000 were 5% or less.
【００５９】比較例１ 羊毛（Ｃｏｌｌｉｄａｌｅ種より採取）２０ｇを８Ｍ尿
素水溶液３７０ｇに浸漬し、ドデシル硫酸ナトリウム１
２ｇと２−メルカプトエタノール３５ｍｌを添加した。
ついで容器を密栓し、６０℃にて２４時間振盪攪拌し
た。反応物を室温に戻し、不溶物を濾過により除去し
た。濾液をセロファンチューブに入れ、２−メルカプト
エタノールを０．２重量％溶解させたイオン交換水７リ
ットルに対してそれぞれ２４時間ずつかけて２回透析し
た。Comparative Example 1 20 g of wool (collected from Collidale species) was immersed in 370 g of an 8M aqueous urea solution, and sodium dodecyl sulfate 1
2 g and 35 ml of 2-mercaptoethanol were added.
Then, the vessel was sealed and shaken and stirred at 60 ° C. for 24 hours. The reaction was returned to room temperature and insolubles were removed by filtration. The filtrate was put into a cellophane tube, and dialyzed twice for 24 hours each against 7 liters of ion-exchanged water in which 0.2% by weight of 2-mercaptoethanol was dissolved.
【００６０】得られた無色透明の透析液の蛋白定量をＬ
ｏｗｒｙ法により行ったところ、透析液１０ｇにつき
０．２３ｇの還元ケラチンを含んでおり、液中の還元ケ
ラチンの濃度は２．３重量％であった。The protein content of the obtained colorless and transparent dialysate was determined by L
According to the owry method, 0.23 g of reduced keratin was contained per 10 g of dialysate, and the concentration of reduced keratin in the solution was 2.3% by weight.
【００６１】また、上記水溶液を凍結乾燥して得た還元
ケラチン粉末の分子量をポリアクリルアミド電気泳動法
で調べたところ、分子量１５，０００〜７０，０００の
ものが主成分であって全体の約８０％を占めていたが、
分子量２４，０００以下のものを約２０％含有してい
た。また、還元ケラチン粉末のアミノ酸分析を行ったと
ころ、アミノ酸１００残基当りシステインが５．２個で
あった。The molecular weight of the reduced keratin powder obtained by freeze-drying the above aqueous solution was examined by polyacrylamide gel electrophoresis. The molecular weight of the powder was 15,000 to 70,000, which was about 80% of the total. Accounted for
It contained about 20% of those having a molecular weight of 24,000 or less. Amino acid analysis of the reduced keratin powder showed 5.2 cysteines per 100 amino acid residues.
【００６２】試験例１ 実施例１〜２および比較例１で得られた還元ケラチンの
水溶液それぞれ６ｍｌに７５重量％グリセリン水溶液
０．２ｍｌを加え、それらをそれぞれ別々に水平な底面
を持つ円形ガラス容器（直径６ｃｍ）に流し、室温、大
気中で乾燥した。その後、８０〜９０℃で１５分間加熱
処理した後、水中に入れ、ガラス容器から剥離してきた
還元ケラチンのフィルムを取り出した。Test Example 1 0.2 ml of a 75% by weight glycerin aqueous solution was added to 6 ml of each of the aqueous solutions of reduced keratin obtained in Examples 1 and 2 and Comparative Example 1, and each of them was separately placed in a circular glass container having a horizontal bottom surface. (6 cm in diameter) and dried in the air at room temperature. Thereafter, after a heat treatment at 80 to 90 ° C. for 15 minutes, the film was put into water, and the reduced keratin film peeled off from the glass container was taken out.
【００６３】得られたフィルムの強伸度をオートグラフ
により測定した。その結果を表１に示す。なお、測定に
あたっての試料の調整および測定条件は次の通りであ
る。The strength and elongation of the obtained film were measured by an autograph. Table 1 shows the results. The adjustment of the sample and the measurement conditions for the measurement are as follows.
【００６４】試料：得られたフィルムを風乾した後、８
０℃で２０分間熱処理し、その後、室温まで戻す。Sample: After air-drying the obtained film, 8
Heat treat at 0 ° C. for 20 minutes, then return to room temperature.
【００６５】測定条件：相対湿度６５％の雰囲気中、引
張速度２００ｍｍ／ｍｉｎで測定する。Measurement conditions: Measurement is performed in an atmosphere with a relative humidity of 65% at a tensile speed of 200 mm / min.
【００６６】[0066]
【表１】 [Table 1]
【００６７】表１に示すように、実施例１〜２で製造し
た還元ケラチンから作製したフィルムは、比較例１で製
造した還元ケラチンから作製したフィルムに比べて、強
伸度が大きい。As shown in Table 1, the film produced from reduced keratin produced in Examples 1 and 2 has a higher elongation than the film produced from reduced keratin produced in Comparative Example 1.
【００６８】[0068]
【発明の効果】本発明によれば、高分子量成分が多く、
かつ架橋可能なチオール基を有する還元ケラチンを短時
間で製造することができる。According to the present invention, the high molecular weight component is large,
In addition, reduced keratin having a crosslinkable thiol group can be produced in a short time.
【００６９】そして、得られた還元ケラチンは、架橋可
能なチオール基を有することと、高分子量成分が多いと
いう特性を利用して、たとえば膜、フィルム、繊維、ス
ポンジなどの産業用品の製造に好適に使用できる。The obtained reduced keratin is suitable for the production of industrial products such as membranes, films, fibers, sponges, etc. by utilizing the property of having a crosslinkable thiol group and having a high molecular weight component. Can be used for
Claims (3)
変成剤の存在下で、還元剤により還元し、不溶物を除去
した後、塩析することを特徴とする還元ケラチンの製造
方法。1. A method for producing reduced keratin, comprising reducing a keratin-containing substance in an aqueous medium with a reducing agent in the presence of a protein denaturing agent, removing insolubles, and salting out.
変成剤と界面活性剤の存在下で、還元剤により還元し、
不溶物を除去した後、塩析することを特徴とする還元ケ
ラチンの製造方法。2. A keratin-containing substance is reduced by a reducing agent in an aqueous medium in the presence of a protein denaturing agent and a surfactant,
A method for producing reduced keratin, comprising removing insolubles and salting out.
または２記載の還元ケラチンの製造方法。3. The method according to claim 1, wherein the reduction is performed under ultrasonic irradiation.
Or the method for producing reduced keratin according to 2 above.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP27783092A JP3283302B2 (en) | 1992-09-22 | 1992-09-22 | Method for producing reduced keratin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP27783092A JP3283302B2 (en) | 1992-09-22 | 1992-09-22 | Method for producing reduced keratin |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH06100600A JPH06100600A (en) | 1994-04-12 |
| JP3283302B2 true JP3283302B2 (en) | 2002-05-20 |
Family
ID=17588864
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP27783092A Expired - Fee Related JP3283302B2 (en) | 1992-09-22 | 1992-09-22 | Method for producing reduced keratin |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP3283302B2 (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007023816A1 (en) | 2005-08-23 | 2007-03-01 | Seiwa Kasei Company, Limited | Method for preparation of reduced keratin, reduced cuticle protein or mixture thereof |
| CN1314732C (en) * | 2004-07-16 | 2007-05-09 | 东华大学 | Process for preparing wool keratin protein and its products |
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1314732C (en) * | 2004-07-16 | 2007-05-09 | 东华大学 | Process for preparing wool keratin protein and its products |
| WO2007023816A1 (en) | 2005-08-23 | 2007-03-01 | Seiwa Kasei Company, Limited | Method for preparation of reduced keratin, reduced cuticle protein or mixture thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH06100600A (en) | 1994-04-12 |
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