JPH0311099A - Hydrolyzed keratin, its production and cosmetic base consisting of hydrolyzed keratin - Google Patents
Hydrolyzed keratin, its production and cosmetic base consisting of hydrolyzed keratinInfo
- Publication number
- JPH0311099A JPH0311099A JP14332289A JP14332289A JPH0311099A JP H0311099 A JPH0311099 A JP H0311099A JP 14332289 A JP14332289 A JP 14332289A JP 14332289 A JP14332289 A JP 14332289A JP H0311099 A JPH0311099 A JP H0311099A
- Authority
- JP
- Japan
- Prior art keywords
- keratin hydrolyzate
- keratin
- hair
- molecular weight
- average molecular
- 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
Links
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- 150000001413 amino acids Chemical class 0.000 claims abstract description 32
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- 238000000034 method Methods 0.000 claims description 8
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- 108090000787 Subtilisin Proteins 0.000 description 1
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- 150000001298 alcohols Chemical class 0.000 description 1
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- 229950010030 dl-alanine Drugs 0.000 description 1
- 125000003438 dodecyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- DDXLVDQZPFLQMZ-UHFFFAOYSA-M dodecyl(trimethyl)azanium;chloride Chemical compound [Cl-].CCCCCCCCCCCC[N+](C)(C)C DDXLVDQZPFLQMZ-UHFFFAOYSA-M 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
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- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
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- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000000834 fixative Substances 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 229960002989 glutamic acid Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 229960002449 glycine Drugs 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 1
- RNYJXPUAFDFIQJ-UHFFFAOYSA-N hydron;octadecan-1-amine;chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCCCC[NH3+] RNYJXPUAFDFIQJ-UHFFFAOYSA-N 0.000 description 1
- 235000019447 hydroxyethyl cellulose Nutrition 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
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- 150000007522 mineralic acids Chemical class 0.000 description 1
- ISTASGAHDLTQRU-UHFFFAOYSA-N n-(2-hydroxyethyl)undec-10-enamide Chemical compound OCCNC(=O)CCCCCCCCC=C ISTASGAHDLTQRU-UHFFFAOYSA-N 0.000 description 1
- KKBOOQDFOWZSDC-UHFFFAOYSA-N n-[2-(diethylamino)ethyl]octadecanamide Chemical compound CCCCCCCCCCCCCCCCCC(=O)NCCN(CC)CC KKBOOQDFOWZSDC-UHFFFAOYSA-N 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- GSGDTSDELPUTKU-UHFFFAOYSA-N nonoxybenzene Chemical compound CCCCCCCCCOC1=CC=CC=C1 GSGDTSDELPUTKU-UHFFFAOYSA-N 0.000 description 1
- HLERILKGMXJNBU-UHFFFAOYSA-N norvaline betaine Chemical compound CCCC(C([O-])=O)[N+](C)(C)C HLERILKGMXJNBU-UHFFFAOYSA-N 0.000 description 1
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- 235000005985 organic acids Nutrition 0.000 description 1
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- 229920001282 polysaccharide Polymers 0.000 description 1
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- 239000002244 precipitate Substances 0.000 description 1
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- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
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- 229910052979 sodium sulfide Inorganic materials 0.000 description 1
- GRVFOGOEDUUMBP-UHFFFAOYSA-N sodium sulfide (anhydrous) Chemical compound [Na+].[Na+].[S-2] GRVFOGOEDUUMBP-UHFFFAOYSA-N 0.000 description 1
- UAJTZZNRJCKXJN-UHFFFAOYSA-M sodium;2-dodecoxy-2-oxoethanesulfonate Chemical compound [Na+].CCCCCCCCCCCCOC(=O)CS([O-])(=O)=O UAJTZZNRJCKXJN-UHFFFAOYSA-M 0.000 description 1
- HFQQZARZPUDIFP-UHFFFAOYSA-M sodium;2-dodecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O HFQQZARZPUDIFP-UHFFFAOYSA-M 0.000 description 1
- RUTSRVMUIGMTHJ-UHFFFAOYSA-M sodium;tetradec-1-ene-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCC=CS([O-])(=O)=O RUTSRVMUIGMTHJ-UHFFFAOYSA-M 0.000 description 1
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- 238000001179 sorption measurement Methods 0.000 description 1
- SFVFIFLLYFPGHH-UHFFFAOYSA-M stearalkonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CC1=CC=CC=C1 SFVFIFLLYFPGHH-UHFFFAOYSA-M 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
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Landscapes
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は分子中にメルカプト基を有するケラチン加水分
解物、その製造方法および上記ケラチン加水分解物から
なる化粧品基剤に関する。DETAILED DESCRIPTION OF THE INVENTION [Industrial Application Field] The present invention relates to a keratin hydrolyzate having a mercapto group in the molecule, a method for producing the same, and a cosmetic base comprising the keratin hydrolyzate.
ケラチンに含まれるシスチンのジスルフィド結合（ＳＳ
結合）をメルカプタン類や硫化物などの還元剤により還
元して、ジスルフィド結合を開裂し、メルカプト基（−
３Ｈ基）を生成させて、シスチンをシスティンに変換し
、ついでタンパク加水分解酵素により、メルカプト基を
保持しつつケラチンを加水分解して、分子中にメルカプ
ト基を有する水溶性のケラチン加水分解物を製造する方
法は、既に特公昭５５−３８３５８号公報において明ら
かにされている。Disulfide bond (SS) of cystine contained in keratin
The mercapto group (-
3H group) to convert cystine to cysteine, and then hydrolyze keratin while retaining the mercapto group using a protein hydrolase to produce a water-soluble keratin hydrolyzate having a mercapto group in the molecule. The manufacturing method has already been disclosed in Japanese Patent Publication No. 55-38358.
しかしながら、ケラチンを還元剤により還元しただけで
は、かなりの不溶成分が残り、水に可溶なケラチン還元
物の収量が少なく、また、還元剤を除去した後、加水分
解などの処理工程が加わると、メルカプト基の空気酸化
が部分的に生じて、ジスルフィド結合を再生し、ケラチ
ン加水分解物中のメルカプト基が減少して、化粧品基剤
としての有用性を欠くことになる。However, if keratin is simply reduced with a reducing agent, a considerable amount of insoluble components will remain, and the yield of water-soluble reduced keratin products will be low.Also, if treatment steps such as hydrolysis are added after removing the reducing agent, , air oxidation of mercapto groups partially occurs, regenerating disulfide bonds, and mercapto groups in the keratin hydrolyzate are reduced, resulting in a lack of utility as a cosmetic base.
しかも、ケラチンを還元するには、ケラチンのジスルフ
ィド結合に対して、化学当量で数１０〜１００倍の大過
剰の還元剤を必要とし、また尿素や塩酸グアニジンなど
のタンパク変性剤を必要とする。Moreover, in order to reduce keratin, it is necessary to use a reducing agent in a large excess of several tens to hundreds of times the chemical equivalent of the disulfide bonds of keratin, and also to use a protein denaturing agent such as urea or guanidine hydrochloride.
さらに、この大量の悪臭を有する還元剤や高ＣＯＤ、Ｂ
ＯＤのタンパク変性剤を含む廃液の処理も、実用上大き
な問題となった。Furthermore, this large amount of foul-smelling reducing agents, high COD,
The treatment of waste liquid containing OD protein denaturing agents has also become a major practical problem.
また、還元に使用したメルカプタン類や硫化物などの還
元剤の奥がケラチン加水分解物に残り、化粧品基剤とし
ての有用性が低下するという問題もあった。There is also the problem that the reducing agents used for reduction, such as mercaptans and sulfides, remain in the keratin hydrolyzate, reducing its usefulness as a cosmetic base.
上記のように、分子中にメルカプト基を有するケラチン
加水分解物を製造する場合には、その還元工程における
ケラチン還元物の収率が低く、その結果、ケラチン加水
分解物の収率が低（なり、しかも大量の還元剤やタンパ
ク変性剤を必要とし、その廃液処理にも問題を有し、さ
らに還元に使用した還元剤の奥がケラチン加水分解物に
残り、化粧品基剤としての有用性を低下させるという問
題があった。As mentioned above, when producing a keratin hydrolyzate having a mercapto group in the molecule, the yield of the reduced keratin product in the reduction step is low; Moreover, it requires a large amount of reducing agent and protein denaturing agent, and there are also problems in waste liquid treatment.Furthermore, the reducing agent used for reduction remains in the keratin hydrolyzate, reducing its usefulness as a cosmetic base. There was a problem with letting it happen.
したがって、本発明は、上記の分子中にメルカプト基を
有するケラチン加水分解物の製造方法において、その還
元工程で生じる諸問題を解決し、高収率でケラチン加水
分解物を得ることができ、しかもケラチン加水分解物に
還元剤の残臭がなく、化粧品基剤として有用性の高いケ
ラチン加水分解物を製造する方法、それによって得られ
る還元剤の残臭がないケラチン加水分解物および上記ケ
ラチン加水分解物からなる化粧品基剤を提供することを
目的とする。Therefore, the present invention solves the problems that occur in the reduction step in the above-mentioned method for producing a keratin hydrolyzate having a mercapto group in its molecule, and is capable of obtaining a keratin hydrolyzate in high yield. A method for producing a keratin hydrolyzate that has no residual odor of a reducing agent and is highly useful as a cosmetic base, a keratin hydrolyzate obtained thereby that has no residual odor of a reducing agent, and the above-mentioned keratin hydrolyzate. The purpose of the present invention is to provide a cosmetic base comprising:
〔課題を解決するための手段］
本発明は、平均分子量３００〜５．０００で、シスチン
量が全アミノ酸中５〜１８モル％のケラチン加水分解物
を、電解還元により還元することによって平均分子量２
００〜３，０００で、システィン量が全アミノ酸中５〜
１８モル％のケラチン加水分解物を得ることにより、上
記目的を達成したものである。[Means for Solving the Problems] The present invention reduces a keratin hydrolyzate with an average molecular weight of 300 to 5.000 and a cystine content of 5 to 18 mol% in all amino acids by electrolytic reduction.
00 to 3,000, the amount of cysteine is 5 to 5 among all amino acids
The above objective was achieved by obtaining a 18 mol% keratin hydrolyzate.
すなわち、本発明によれば、シスチンのジスルフィド結
合を開裂し、メルカプト基を生成させるための還元にあ
たって、メルカプタン類や硫化物などの還元剤を使用し
ないので、得られるケラチン加水分解物に還元剤の悪臭
が残存することがない。したがって、得られるケラチン
加水分解物は、たとえば種々の化粧品に応用することが
でき、化粧品基剤として優れたものとなる。That is, according to the present invention, reducing agents such as mercaptans and sulfides are not used in the reduction to cleave the disulfide bonds of cystine and generate mercapto groups, so the resulting keratin hydrolyzate is free of reducing agents. No odor remains. Therefore, the obtained keratin hydrolyzate can be applied, for example, to various cosmetics and is excellent as a cosmetic base.
また、還元を電解還元により行うので、ケラチン加水分
解物のシスチンのジスルフィド結合をほぼ完全に還元す
ることができ、還元剤を用いる場合に比べて、還元物の
収率が高い。Further, since the reduction is carried out by electrolytic reduction, the disulfide bonds of cystine in the keratin hydrolyzate can be almost completely reduced, and the yield of the reduced product is higher than when a reducing agent is used.
もとより、還元剤を使用しないので、還元剤の無駄が生
じず、また、尿素などのタンパク変性剤を必要とせず、
還元剤やタンパク変性剤を含む廃液の処理問題も生じな
い。Of course, since no reducing agent is used, there is no waste of reducing agent, and there is no need for protein denaturing agents such as urea.
There is no problem with the treatment of waste liquid containing reducing agents or protein denaturing agents.
本発明においては、出発物質として、平均分子量３００
〜５，０００で、シスチン量が全アミノ酸中５〜１８モ
ル％のケラチン加水分解物を用いるが、このケラチン加
水分解物は、羊毛などの獣毛、毛髪、羽毛、蹄、爪、角
などのケラチンを、酸、酵素、あるいは両者の併用によ
り、加水分解することによって得られる。また、酸とし
て２種以上の酸を用いて加水分解を行ってもよい。In the present invention, starting materials with an average molecular weight of 300
A keratin hydrolyzate with a cystine content of 5,000 to 5,000% and a cystine content of 5 to 18 mol% of all amino acids is used. It is obtained by hydrolyzing keratin using an acid, an enzyme, or a combination of both. Moreover, you may perform hydrolysis using two or more types of acids as acids.
本発明において、出発物質として、このような平均分子
量３００〜５，０００で、シスチン量が全アミノ酸中５
〜１８モル％のケラチン加水分解物を用いるのは、次の
理由によるものである。In the present invention, as a starting material, the average molecular weight is 300 to 5,000, and the amount of cystine is 5 out of all the amino acids.
The reason for using ~18 mol % of keratin hydrolyzate is as follows.
すなわち、出発物質のケラチン加水分解物の平均分子量
が３００未満では、ケラチンの加水分解によって生成す
る種々のアミノ酸が遊離状態で存在する量が多くなり、
たとえばシスチンは遊離状態では水溶性が低く、沈殿し
てしまい、ケラチン加水分解物全体中で占めるシスチン
量が少なくなる。That is, when the average molecular weight of the keratin hydrolyzate as a starting material is less than 300, the amount of various amino acids produced by hydrolysis of keratin present in a free state increases,
For example, cystine has low water solubility in its free state and precipitates, reducing the amount of cystine in the entire keratin hydrolyzate.
そのため、電解還元を行う意味も薄れるし、また還元さ
れたケラチン加水分解物としての特有の効果を期待でき
ない、一方、出発物質のケラチン加水分解物の平均分子
量が５，０００を超えると、ケラチン加水分解物の一部
の成分は水不溶性になり、電解還元によっては、容易に
還元されなくなる。Therefore, the meaning of electrolytic reduction is diminished, and the unique effects of the reduced keratin hydrolyzate cannot be expected.On the other hand, if the average molecular weight of the starting keratin hydrolyzate exceeds 5,000, the keratin hydrolyzate Some components of the decomposition product become water-insoluble and cannot be easily reduced by electrolytic reduction.
また、出発物質のケラチン加水分解物のシスチン量が前
アミノ酸中５モル％未満では、シスチン量が少なすぎて
、電解還元を行う意味が薄れるし、また還元されたケラ
チン加水分解物としての特有の効果を充分に期待するこ
とができない。一方、出発物質のケラチン加水分解物の
シスチン量が前アミノ酸中１８モル％を超えると、シス
チンによるジスルフィド結合が多くなりすぎるために、
ケラチン加水分解物の水溶性が著しく低下し、電解還元
によって還元することが実質的に不可能になるからであ
る。Furthermore, if the amount of cystine in the starting keratin hydrolyzate is less than 5 mol% in the pre-amino acid, the amount of cystine will be too small and the purpose of electrolytic reduction will be diminished, and the characteristic characteristics of the reduced keratin hydrolyzate will be reduced. The effect cannot be fully expected. On the other hand, if the amount of cystine in the starting keratin hydrolyzate exceeds 18 mol% in the preamino acid, the number of disulfide bonds due to cystine will be too large.
This is because the water solubility of the keratin hydrolyzate decreases significantly, making it substantially impossible to reduce it by electrolytic reduction.
上記ケラチン加水分解物を得るための酸加水分解では、
酸として、たとえば塩酸、硫酸、リン酸、硝酸、臭化水
素酸などの無機酸、酢酸、メルカプト酢酸、ギ（蟻）酸
などの有機酸が用いられる。In acid hydrolysis to obtain the above keratin hydrolyzate,
Examples of acids used include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid, and organic acids such as acetic acid, mercaptoacetic acid, and formic acid.
これらは一般に５〜８５％（単に％のみで表示する場合
は、重量％であり、以下においても同様である）の濃度
で使用され、加水分解はｐＨ４以下で、反応温度は１０
〜１００°Ｃの範囲で行うのが望ましく、反応時間は通
常２〜１００時間である。These are generally used at a concentration of 5 to 85% (when expressed simply as %, it is % by weight, and the same applies hereinafter), hydrolysis is carried out at a pH of 4 or less, and the reaction temperature is 10%.
It is desirable to carry out the reaction at a temperature in the range of -100°C, and the reaction time is usually 2 to 100 hours.
酵素加水分解による場合、酵素としては、たとえばペプ
チン、プロクターゼＡ１プロクターゼＢなどの酸性タン
パク加水分解酵素、パパイン、ブロメライン、サーモラ
イシン、トリプシン、プロナーゼ、キモトリプリンなど
の中性タンパク加水分解酵素、スブチリシン、ステフィ
ロコカスブロテアーゼなどの国産性の中性タンパク加水
分解酵素などが使用される。In the case of enzymatic hydrolysis, the enzymes include peptin, acidic protein hydrolases such as protase A and protase B, neutral protein hydrolases such as papain, bromelain, thermolysin, trypsin, pronase, and chymotrypurine, subtilisin, and stephylococcus. Domestically produced neutral protein hydrolases such as protease are used.
加水分解時のｐＨは、ベブチンなどの酸性タンパク加水
分解酵素を用いる場合はｐＨ１〜４の範囲、パパインな
どの中性タンパク加水分解酵素を用いる場合はｐＨ４〜
１０の範囲に調整するのが望ましい９反応温度は３０〜
６０°Ｃの範囲が望ましく、反応時間は通常３〜４８時
間である。The pH during hydrolysis is within the range of 1 to 4 when using an acidic protein hydrolase such as bebutin, and between 4 and 4 when using a neutral protein hydrolase such as papain.
It is desirable to adjust the reaction temperature to a range of 10 to 30.
The temperature range is preferably 60°C, and the reaction time is usually 3 to 48 hours.
電解還元は、たとえば湯浅アイオニクス■のＭＡＲＫ−
ＩＬ２室流動型電解装置などの電解還元装置を用いて行
われる。Electrolytic reduction is possible, for example, with Yuasa Ionics' MARK-
This is carried out using an electrolytic reduction device such as an IL two-chamber flow type electrolyzer.
電解還元においては、還元は陰極で生じ、酸化は陽掻で
生じる。したがって、本発明のように還元を目的とする
ときには、陰極槽に前記ケラチン加水分解物の溶液を導
入し、陽極槽には電解質〔たとえば硫酸（濃度３％）〕
を導入し、両者の間をイオン交換膜などで隔離して、電
解還元が行われる。電解還元時の条件は、装置の規模、
特に陰極の実質表面積や流速、装置の規模と液量の関係
、さらには還元によって陰極から発生する水素ガスの泡
による効率の低下などによっても異なるが、通常、０．
５〜３０Ａの電流値で、８〜１００時間程度の条件下で
電解還元が行われる。In electrolytic reduction, reduction occurs at the cathode and oxidation occurs at the anode. Therefore, when the purpose is reduction as in the present invention, a solution of the keratin hydrolyzate is introduced into the cathode tank, and an electrolyte [for example, sulfuric acid (concentration 3%)] is introduced into the anode tank.
electrolytic reduction is carried out by introducing an ion exchange membrane or the like between the two and isolating the two. The conditions during electrolytic reduction depend on the scale of the equipment,
Although it varies depending on the actual surface area of the cathode, the flow rate, the relationship between the scale of the device and the liquid volume, and the reduction in efficiency due to hydrogen gas bubbles generated from the cathode during reduction, it is usually 0.
Electrolytic reduction is performed at a current value of 5 to 30 A for about 8 to 100 hours.
本発明においては、最終物質として平均分子量２００〜
３，０００で、システィン量が全アミノ酸５〜１８モル
％のケラチン加水分解物を得ることを目的とするが、こ
れは次の理由によるものである。In the present invention, the final substance has an average molecular weight of 200 to
The purpose is to obtain a keratin hydrolyzate with a cysteine content of 5 to 18 mol % of total amino acids.
すなわち、最終物質のケラチン加水分解物の平均分子量
が２００未満では、ケラチン加水分解物中のシスティン
量が少なくなり、還元されたケラチン加水分解物として
の特有の効果を期待できない。That is, if the average molecular weight of the keratin hydrolyzate as the final material is less than 200, the amount of cysteine in the keratin hydrolyzate will be small, and the unique effects of a reduced keratin hydrolyzate cannot be expected.
一方、最終物質のケラチン加水分解物の平均分子量が３
．０００を超えると、一部の成分は、水不溶性になり、
取扱いが困難になるとともに、毛髪への吸着性や浸透性
が低下する。On the other hand, the average molecular weight of the final keratin hydrolyzate is 3.
．． 000, some components become water-insoluble,
It becomes difficult to handle, and its adsorption and permeability to hair decreases.
また、最終物質のケラチン加水分解物のシスティン量が
全アミノ酸中５モル％未満では、システィン量が少なす
ぎて、還元されたケラチン加水分解物としての特有の効
果を期待できない、一方、最終物質のケラチン加水分解
物のシスティン量が全アミノ酸中１８モル％を超えると
、水溶性が著しく低下して、取扱いが困難になるからで
ある。In addition, if the amount of cysteine in the keratin hydrolyzate of the final material is less than 5 mol% of the total amino acids, the amount of cysteine is too small and the unique effect of the reduced keratin hydrolyzate cannot be expected. This is because if the amount of cysteine in the keratin hydrolyzate exceeds 18 mol% of the total amino acids, the water solubility will be significantly reduced and handling will become difficult.
上記のような平均分子ｉｉ ２００〜３，０００で、シ
スティン量が全アミノ酸中５〜１８モル％のケラチン加
水分解物は、分子中にメルカプト基を有するので、この
ケラチン加水分解物を希薄水溶液の状態で毛髪上に塗布
または吹きつけ、該毛髪をロンドに巻きつけて水分を乾
燥させると、該加水分解物中のメルカプト基が空気中の
酸素あるいは酸化剤によって酸化され、層状に接してい
るケラチン加水分解物の他の分子のメルカプト基と架橋
してシスチン結合を形成し、毛髪をカールしたままの状
態でそのうえに被膜を形成する。そして、この被膜は、
ケラチン加水分解物の分子量が高い場合、水不溶性とな
る。The above-mentioned keratin hydrolyzate with an average molecular weight of 200 to 3,000 and a cysteine content of 5 to 18 mol% of all amino acids has a mercapto group in the molecule, so this keratin hydrolyzate is diluted in a dilute aqueous solution. When this product is applied or sprayed onto the hair and the hair is wrapped in a ronde to dry the moisture, the mercapto groups in the hydrolyzate are oxidized by oxygen in the air or an oxidizing agent, and the keratin in contact with the layer is oxidized. It crosslinks with the mercapto groups of other molecules of the hydrolyzate to form cystine bonds, forming a film over the hair while it remains curled. And this film is
When the molecular weight of the keratin hydrolyzate is high, it becomes water-insoluble.
しかも上記のケラチン加水分解物は、その分子中にアミ
ノ基およびカルボキシル基を有するので、それらがそれ
ぞれ毛髪を構成するケラチン中のカルボキシル基および
アミノ基と結合して造塩するため、毛髪との結合が強固
になり、水洗しても水不溶性であることと相まって容易
には離脱しない。Moreover, since the above-mentioned keratin hydrolyzate has amino groups and carboxyl groups in its molecules, these combine with the carboxyl groups and amino groups in keratin, which constitutes hair, to form salts. It becomes strong and does not come off easily even when washed with water due to its water insolubility.
このようにして、本発明によって得られるケラチン加水
分解物は、毛髪に損傷を与えることな（、好適なウェー
ブ効果ないしはセント効果を付与し、しかもその効果を
長期間持続する。したがって、このケラチン加水分解物
を水その他の溶剤に溶解して、パーマネントウェーブ用
剤またはセット剤として用いることができるし、また、
このケラチン加水分解物を在来のパーマネントウェーブ
用剤やセット剤に配合して、その効果を高めることがで
きる。In this way, the keratin hydrolyzate obtained according to the present invention imparts a suitable waving effect or centrifugal effect to the hair without damaging the hair, and maintains the effect for a long period of time. The decomposition product can be dissolved in water or other solvent and used as a permanent waving agent or setting agent, and
This keratin hydrolyzate can be added to conventional permanent waving agents and setting agents to enhance their effects.
また本発明のケラチン加水分解物は毛髪に１１１１した
化学構造を有するので、これを毛髪に使用した際に従来
の樹脂系セット剤のような異相窓を感じさせないし、ま
た通気性を有していて毛髪をむれさせることがない。In addition, the keratin hydrolyzate of the present invention has a chemical structure similar to 1111 in hair, so when it is used on hair, it does not give the impression of a foreign phase window unlike conventional resin-based setting agents, and it also has air permeability. It won't make your hair frizzy.
そして、本発明のケラチン加水分解物は、天然のタンパ
ク質であるケラチンから誘導されるものであるから毛髪
や皮膚に対する安全性が高く、また、メルカプト基に基
づく還元性により、たとえばチオグリコール酸などのよ
うに刺激性や悪臭を有する物質が配合されている化粧品
に配合すると、それらの刺激性や悪臭を低減する効果が
ある。Since the keratin hydrolyzate of the present invention is derived from keratin, which is a natural protein, it is highly safe for hair and skin, and due to its reducing properties based on mercapto groups, it is highly resistant to thioglycolic acid, etc. When added to cosmetics that contain irritating and malodorous substances, it has the effect of reducing those irritants and malodors.
もとより、通常のペプチド（タンパク質加水分解物）と
同様に毛髪のコンディショニング効果や毛髪の保護・強
化作用を有していて、毛髪に吸着して、毛髪に艶、柔軟
性、潤いを付与し、毛髪のｔ員傷を防止し、かつ損傷し
た毛髪を回復させる作用を有している。In addition, like regular peptides (protein hydrolysates), they have hair conditioning effects and hair protection/strengthening effects, and are adsorbed to the hair, giving it shine, flexibility, and moisture. It has the effect of preventing hair damage and restoring damaged hair.
また、皮膚に対しても親和性を有していて、皮膚に潤い
と艶を付与し、かつ皮膚をなめらかにする。It also has an affinity for the skin, providing moisture and luster to the skin, and making it smooth.
本発明の分子中にメルカプト基を有するケラチン加水分
解物は、上記のような特性を利用して、化粧品基剤とし
て、コールドまたは加温式パーマネントウェーブ用第１
剤、ストレートパーマ液、セントローシタン、ヘアコン
ディジツナ−、セットまたはコンディショニングを目的
とするムース剤、シェイピングフオーム、シェイピング
ローション、プレシェイピングローション、脱毛・除毛
剤、脱毛、除毛を目的とするムース剤、ジャンプ、リン
ス、ヘアローシコン、ヘアクリーム、美白化粧品、スキ
ンローシゴン、スキンクリーム、洗＃ｉ ＊Ｊ、フェイ
スローション、フェイスクリーム、角質除去剤などに応
用される。The keratin hydrolyzate having a mercapto group in the molecule of the present invention can be used as a cosmetic base by utilizing the above-mentioned properties as a first agent for cold or heated permanent waving.
hair conditioner, straight perm solution, Centrocitan, hair conditioner, mousse for setting or conditioning, shaping foam, shaping lotion, pre-shaping lotion, hair removal/hair removal agent, hair removal, mousse for hair removal It is applied to products such as hair lotion, jump, conditioner, hair lotion, hair cream, whitening cosmetics, skin lotion, skin cream, wash #i*J, face lotion, face cream, and exfoliant.
また、本発明のケラチン加水分解物は、前記のような酸
化による被膜形成能を利用して、たとえば医薬品、生体
物質、着色剤などのマイクロカプセル用の壁材や、織！
ｌ製品の固定化剤などとして使用することができる。In addition, the keratin hydrolyzate of the present invention can be used as a wall material for microcapsules for pharmaceuticals, biological substances, colorants, etc., for example, by making use of the ability to form a film through oxidation as described above, and for fabrics!
It can be used as a fixative for products.
そして、本発明のケラチン加水分解物を用い、化粧品を
調製するにあたって併用できる成分としては、例えばラ
ウリル硫酸アンモニウム、ラウリル硫酸エタノールアミ
ン、ラウリル硫酸ナトリウム、ラウリル硫酸トリエタノ
ールアミンなどのアルキル硫酸塩、ポリオキシエチレン
（２ＥＯ）ラウリルエーテル硫酸トリエタノールアミン
、ポリオキシエチレン（３ＥＯ）アルキル（炭素数１１
〜１５のいずれかまたは２種以上の混合物）エーテル硫
酸ナトリウムなどのポリオキシエチレンアルキルエーテ
ル硫酸塩、ラウリルヘンゼンスルホン酸ナトリウム、ラ
ウリルベンゼンスルホン酸トリエタノールアミンなどの
アルキルベンゼンスルホン酸塩、ポリオキシエチレン（
３ＥＯ））リゾシルエーテル酢酸ナトリウムなどのポリ
オキシエチレンアルキルエーテル酢酸塩、ヤシ油脂肪酸
サルコシンナトリウム、ラウロイルサルコシントリエタ
ノールアミン、ラウロイルメチル−β−アラニンナトリ
ウム、ラウロイル−Ｌ−グルタミン酸ナトリウム、ラウ
ロイル−し−グルタミン酸トリエタノールアミン、ヤシ
油脂肪酸−Ｌ−グルタミン酸ナトリウム、ヤシ油脂肪酸
−Ｌ−グルタミン酸トリエタノールアミン、ヤシ油脂肪
酸メチルタウリンナトリウム、ラウロイルメチルタウリ
ンナトリラムなどのＮ−アシルアミノ酸塩、エーテル硫
酸アルカンスルホン酸ナトリウム、硬化ヤシ油脂肪酸グ
リセリン硫酸ナトリウム、ランデシレノイルアミドエチ
ルスルホコハク酸二ナトリウム、オクチルフェノキシジ
ェトキシエチルスルホン酸ナトリウム、オレイン酸アミ
ドスルホコハク酸二ナトリウム、スルホコハク酸ジオク
チルナトリウム、スルホコハク酸うウリルニナトリウム
、ポリオキシエチレンアルキル（炭素数１２〜１５）エ
ーテルリン酸（８〜ｌ０ＥＯ） 、ポリオキシエチレン
オレイルエーテルリン酸ナトリウム、ポリオキシエチレ
ンセチルエーテルリン酸ナトリウム、ポリオキシエチレ
ンスルホコハク酸うウリルニナトリウム、ポリオキシエ
チレンラウリルエーテルリン酸ナトリウム、ラウリルス
ルホ酢酸ナトリウム、テトラデセンスルホン酸ナトリウ
ムなどのアニオン性界面活性剤、塩化ジステアリルジメ
チルアンモニウム、塩化ジポリオキシエチレンオレイル
メチルアンモニウム、塩化ステアリルジメチルベンジル
アンモニウム、塩化ステアリルトリメチルアンモニウム
、塩化セチルトリメチルアンモニウム、塩化トリ （ポ
リオキシエチレン）ステアリルアンモニウム、塩化ポリ
オキシプロピレンメチルジエチルアンモニウム、塩化ミ
リスチルジメチルベンジルアンモニウム、塩化ラウリル
トリメチルアンモニウムなどのカチオン性界面活性剤、
２−アルキル−Ｎ−カルボキシメチル−Ｎ−ヒドロキシ
エチルイミダゾリニウムベタイン、ウンデシルヒドロキ
シエチルイミダゾリウムベタインナトリウム、ウンデシ
ル−Ｎ−ヒドロキシエチル−Ｎ＝カルボキシメチルイミ
ダゾリニウムベタイン、ステアリルジヒドロキシエチル
ベタイン、ステアリルジメチルアミノ酢酸ベタイン、ヤ
シ油アルキルベタイン、ヤシ油脂肪酸アミドプロピルベ
タイン、ヤシ油アルキルＮ−カルボキシエチル−Ｎ−ヒ
ドロキシエチルイミダゾリニウムベタインナトリウム、
ヤシ油アルキルＮ−カルボキシエトキシエチル−Ｎ−カ
ルボキシエチルイミダゾリニウムジナトリウムヒドロキ
シド、ヤシ油アルキルＮ−カルボキシメトキシエチル−
Ｎ−カルボキシメチルイミダゾリニウムジナトリウムラ
ウリル硫酸、Ｎ−ヤシ油脂肪酸アシルＬ−アルギニンエ
チル・ＤＬ−ピロリドンカルボン酸塩などの両性界面活
性剤、ポリオキシエチレンアルキル（炭素数１２〜１４
）エーテル（７ＥＯ）、ポリオキシエチレンオクチルフ
ェニルエーテル、ポリオキシエチレンオレイルエーテル
、ポリオキシエチレンオレイン酸グリセリル、ポリオキ
シエチレンステアリルエーテル、ポリオキシエチレンセ
チルエーテル、ポリオキシエチレンセチルステアリルジ
エーテル、ポリオキシエチレンソルビトール・ラノリン
（４０ＥＯ）、ポリオキシエチレンノニルフヱニルエー
テル、ポリオキシエチレンポリオキシプロピレンセチル
エーテル、ポリオキシエチレンポリオキシプロピレンテ
トラデシルエーテル、ポリオキシエチレンラノリン、ポ
リオキシエチレンラノリンアルコール、ポリオキシプロ
ピレンステアリルエーテルなどのノニオン性界面活性剤
、カチオン化セルロース、カチオン化ヒドロキシエチル
セルロース、ポリ （塩化ジアリルジメチルアンモニウ
ム）、ジエチル硫酸ビニルピロリドン、Ｎ、Ｎ−ジメチ
ルアミノエチルメタクリル酸共重合体、ポリビニルピリ
ジン、ポリエチレンイミンなどのカチオン性ポリマー、
両性ポリマー、アクリル酸エステル・メタクリル酸エス
テル系共重合体などのアニオン性ポリマーイソステアリ
ン酸ジェタノールアミド、ウンデシレン酸モノエタノー
ルアミド、オレイン酸ジェタノールアミド、牛脂肪酸モ
ノエタノールアミド、硬化牛脂肪酸ジェタノールアミド
、ステアリン酸ジェタノールアミド、ステアリン酸ジエ
チルアミノエチルアミド、ステアリン酸モノエタノール
アミド、ミリスチン酸ジェタノールアミド、ヤシ油脂肪
酸エタノールアミド、ヤシ油脂肪酸ジェタノールアミド
、ラウリン酸イソプロパツールアミド、ラウリン酸エタ
ノールアミドまたはジェタノールアミド、ラノリン脂肪
酸ジェタノールアミドなどの増粘剤、動植物抽出物、ポ
リサッカライドまたはその誘導体、プロピレングリコー
ル、１．３−ブチレングリコール、エチレングリコール
、クリセリン、ポリエチレングリコールなどの湿潤剤、
工タノール、メタノール、プロピルアルコール、イソプ
ロピルアルコールなどの低級アルコール類、Ｌ−アスパ
ラギン酸、Ｌ−アスパラギン酸ナトリウム、ＤＬ−アラ
ニン、Ｌ−アルギニン、グリシン、Ｌ−グルタミン酸、
し−システィン、Ｌ−スレオニンなどのアミノ酸などを
あげられる。Ingredients that can be used in combination when preparing cosmetics using the keratin hydrolyzate of the present invention include, for example, alkyl sulfates such as ammonium lauryl sulfate, ethanolamine lauryl sulfate, sodium lauryl sulfate, triethanolamine lauryl sulfate, and polyoxyethylene. (2EO) lauryl ether sulfate triethanolamine, polyoxyethylene (3EO) alkyl (11 carbon atoms
~15) polyoxyethylene alkyl ether sulfates such as sodium ether sulfate, alkylbenzenesulfonates such as sodium laurylbenzenesulfonate, triethanolamine laurylbenzenesulfonate, polyoxyethylene (
3EO)) Polyoxyethylene alkyl ether acetate such as sodium lysosyl ether acetate, sodium coconut oil sarcosine, lauroyl sarcosine triethanolamine, sodium lauroyl methyl-β-alanine, sodium lauroyl-L-glutamate, lauroyl-glutamic acid N-acyl amino acid salts such as triethanolamine, coconut oil fatty acid-sodium L-glutamate, coconut oil fatty acid-L-glutamate triethanolamine, sodium coconut oil fatty acid methyltaurine, lauroylmethyltaurine natrirum, sodium ether sulfate alkanesulfonate , sodium hydrogenated coconut oil fatty acid glycerol sulfate, disodium randecylenoylamide ethyl sulfosuccinate, sodium octylphenoxyjethoxyethyl sulfonate, disodium oleic acid amide sulfosuccinate, dioctyl sodium sulfosuccinate, disodium uryl sulfosuccinate, polyoxy Ethylene alkyl (12 to 15 carbon atoms) ether phosphoric acid (8 to 10 EO), sodium polyoxyethylene oleyl ether phosphate, sodium polyoxyethylene cetyl ether phosphate, disodium polyoxyethylene uryl sulfosuccinate, polyoxyethylene lauryl Anionic surfactants such as sodium ether phosphate, sodium lauryl sulfoacetate, sodium tetradecene sulfonate, distearyldimethylammonium chloride, dipolyoxyethyleneoleylmethylammonium chloride, stearyldimethylbenzylammonium chloride, stearyltrimethylammonium chloride, chloride Cationic surfactants such as cetyltrimethylammonium, tri(polyoxyethylene)stearylammonium chloride, polyoxypropylenemethyldiethylammonium chloride, myristyldimethylbenzylammonium chloride, lauryltrimethylammonium chloride,
2-Alkyl-N-carboxymethyl-N-hydroxyethylimidazolinium betaine, undecylhydroxyethylimidazolium betaine sodium, undecyl-N-hydroxyethyl-N=carboxymethylimidazolinium betaine, stearyl dihydroxyethyl betaine, stearyl dimethyl Aminoacetic acid betaine, coconut oil alkyl betaine, coconut oil fatty acid amidopropyl betaine, coconut oil alkyl N-carboxyethyl-N-hydroxyethylimidazolinium betaine sodium,
Coco alkyl N-carboxyethoxyethyl-N-carboxyethyl imidazolinium disodium hydroxide, Coco alkyl N-carboxymethoxyethyl-
Ampholytic surfactants such as N-carboxymethylimidazolinium disodium lauryl sulfate, N-coconut oil fatty acid acyl L-arginine ethyl DL-pyrrolidone carboxylate, polyoxyethylene alkyl (carbon number 12-14)
) Ether (7EO), polyoxyethylene octylphenyl ether, polyoxyethylene oleyl ether, polyoxyethylene glyceryl oleate, polyoxyethylene stearyl ether, polyoxyethylene cetyl ether, polyoxyethylene cetyl stearyl diether, polyoxyethylene sorbitol・Lanolin (40EO), polyoxyethylene nonylphenyl ether, polyoxyethylene polyoxypropylene cetyl ether, polyoxyethylene polyoxypropylene tetradecyl ether, polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, polyoxypropylene stearyl ether Nonionic surfactants such as cationized cellulose, cationized hydroxyethyl cellulose, poly(diallyldimethylammonium chloride), vinylpyrrolidone diethyl sulfate, N,N-dimethylaminoethyl methacrylic acid copolymer, polyvinylpyridine, polyethyleneimine, etc. cationic polymer,
Ampholytic polymers, anionic polymers such as acrylic acid ester/methacrylic acid ester copolymers, isostearic acid jetanolamide, undecylenic acid monoethanolamide, oleic acid jetanolamide, bovine fatty acid monoethanolamide, hydrogenated bovine fatty acid jetanolamide, Stearic acid jetanolamide, stearic acid diethylaminoethylamide, stearic acid monoethanolamide, myristic acid jetanolamide, coconut oil fatty acid ethanolamide, coconut oil fatty acid jetanolamide, lauric acid isopropanolamide, lauric acid ethanolamide or Thickeners such as tanolamide, lanolin fatty acid jetanolamide, animal and plant extracts, polysaccharides or derivatives thereof, wetting agents such as propylene glycol, 1,3-butylene glycol, ethylene glycol, chrycerin, polyethylene glycol,
Lower alcohols such as ethanol, methanol, propyl alcohol, isopropyl alcohol, L-aspartic acid, sodium L-aspartate, DL-alanine, L-arginine, glycine, L-glutamic acid,
Examples include amino acids such as cysteine and L-threonine.
また、本発明のケラチン加水分解物は、それ以外のペプ
チド、さらにはペプチドの誘導体（たとえば、ペプチド
のアシル化物またはその塩、ペプチドの第４級アンモニ
ウム誘導体、ペプチドのエステルなど）とも併用できる
。また、上記以外にも、それぞれの化粧品に通常配合さ
れる成分とも併用できる。Furthermore, the keratin hydrolyzate of the present invention can be used in combination with other peptides and even peptide derivatives (eg, acylated peptides or salts thereof, quaternary ammonium derivatives of peptides, esters of peptides, etc.). In addition to the above, it can also be used in combination with other ingredients that are normally included in each cosmetic product.
つぎに本発明の実施例をあげるが、本発明は実施例のみ
に限定されるものではない。Next, examples of the present invention will be given, but the present invention is not limited only to the examples.
実施例１
三ツロフラスコ中で羊毛５００ｇに３５％塩酸４５０ｇ
を加え、８０゛Ｃで１８時間攪拌下に加水分解を行った
。加水分解後、反応混合物を濾過し、濾液を弱塩基性ア
ニオン交換樹脂ダイヤイオンＷＡ２０（商品名、三菱化
成■製） １，４００ ｍ １．により中和したのち、
濃縮し、濾過してイオン交換樹脂を除去し、濃度４０％
のケラチン加水分解物の水溶液を得た。Example 1 450 g of 35% hydrochloric acid to 500 g of wool in a Mitsuro flask
was added, and hydrolysis was carried out under stirring at 80°C for 18 hours. After hydrolysis, the reaction mixture was filtered and the filtrate was treated with a weakly basic anion exchange resin Diaion WA20 (trade name, manufactured by Mitsubishi Kasei ■) 1,400 m 1. After being neutralized by
Concentrate and filter to remove ion exchange resin to a concentration of 40%
An aqueous solution of keratin hydrolyzate was obtained.
このようにして得られたケラチン加水分解物の分子量を
ゲル濾過法により測定したところ、平均分子量４００で
あった。また、得られたケラチン加水分解物中のシスチ
ン量をアミノ酸自動分析計〔日本電子■ＪＬＣ−３００
型〕によって測定したところ、シスチン量は全アミノ酸
中８．７モル％であった。The molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration and found to be an average molecular weight of 400. In addition, the amount of cystine in the obtained keratin hydrolyzate was measured using an automatic amino acid analyzer [JEOL JLC-300].
The amount of cystine was 8.7 mol% of the total amino acids.
つぎに、この濃度４０％のケラチン加水分解物を電解還
元装置に通液して、電流２Ａで１０時間電解還元を行っ
た。Next, this keratin hydrolyzate having a concentration of 40% was passed through an electrolytic reduction device, and electrolytic reduction was performed at a current of 2 A for 10 hours.
使用された電解還元装置は、次のとおりである。The electrolytic reduction device used is as follows.
装置名：湯浅アイオニクス■製、ＭＡＲＫ−ＩＬ２室流
動型電解装置
電 極：陽極−Ｔｉ−Ｐｔほか、
陰極−Ｐｂほか
電極面積：各１．８ｄｒｒｒ
上記のようにして電解還元されたケラチン加水分解物の
分子量をゲル濾過法により測定したところ、平均分子ｆ
２７０であった。また、得られたケラチン加水分解物
のう・スティン量を測定したところ、システィン量は全
アミノ酸中８．４モル％であった。なお、システィン量
の測定は、ケラチン加水分解物のメルカプト基をヨード
酢酸によりＳ−カルボキシメチル化したのち、６Ｎ塩酸
で完全加水分解し、アミノ酸自動分析計（前出）で上記
加水分解物中のＳ−カルボキシメチルシスティン量を測
定することにより行った。Equipment name: Manufactured by Yuasa Ionics ■, MARK-IL 2-chamber flow type electrolyzer Electrodes: Anode - Ti-Pt, etc., Cathode - Pb, etc. Electrode area: 1.8 drrr each Keratin hydrolyzed electrolytically reduced as above When the molecular weight of the substance was measured by gel filtration method, the average molecular weight f
It was 270. Further, when the amount of cysteine in the obtained keratin hydrolyzate was measured, the amount of cysteine was 8.4 mol % in the total amino acids. To measure the amount of cysteine, the mercapto group in the keratin hydrolyzate is S-carboxymethylated with iodoacetic acid, then completely hydrolyzed with 6N hydrochloric acid, and the amount of cysteine in the hydrolyzate is measured using an automatic amino acid analyzer (mentioned above). This was done by measuring the amount of S-carboxymethylcysteine.
電解還元前のケラチン加水分解物に対する電解還元後の
ケラチン加水分解物の収率は９８％であつた。The yield of the keratin hydrolyzate after electrolytic reduction relative to the keratin hydrolyzate before electrolytic reduction was 98%.
実施例２
粉砕した羊毛５００ｇに３０％塩酸７５０ｇを加え、２
０℃で７２時間攪拌して加水分解を行った。加水分解後
、反応液を冷却攪拌しながらアンモニアガスを反応液に
通じてＰＨ７に中和した。つぎに、反応液を濾過したの
ち、電気透析によって脱塩し、濃縮して濃度３０％のケ
ラチン加水分解液の水溶液を得た。Example 2 Add 750 g of 30% hydrochloric acid to 500 g of crushed wool,
Hydrolysis was carried out by stirring at 0°C for 72 hours. After the hydrolysis, ammonia gas was passed through the reaction solution while cooling and stirring to neutralize the reaction solution to pH 7. Next, the reaction solution was filtered, desalted by electrodialysis, and concentrated to obtain an aqueous solution of keratin hydrolyzate having a concentration of 30%.
使用された電気透析装置は下記のとおりである。The electrodialysis equipment used is as follows.
型式： Ｄｏ−Ｃｂ Ｃ奇人エンジニアリング■製〕膜
名称：セレミオンＣＭＶおよびＡＭＶ （旭硝子■製、
商品名〕
膜寸法： １８ＣＩ Ｘ １２ＣＩ
組込膜数＝１０対
電圧：３０■
陽極液：硫酸ナトリウム水溶ＷＬ（無水硫酸ナトリウム
として約５％）
陰極液：硫酸ナトリウム水溶液（無水硫酸ナトリウムと
して約５％）
このようにして得られたケラチン加水分解物の分子量を
ゲル濾過法により測定したところ、平均分子３１３，８
００であった。また、得られたケラチン加水分解物中の
シスチン量を実施例１と同様のアミノ酸自動分析計で測
定したところ、シスチン量は全アミノ酸中１２．２モル
％であった。Model: Do-Cb Made by C Kijin Engineering ■ Membrane name: Selemion CMV and AMV (made by Asahi Glass ■,
Product name] Membrane dimensions: 18CI ) The molecular weight of the keratin hydrolyzate thus obtained was measured by a gel filtration method, and the average molecular weight was 313.8.
It was 00. Further, when the amount of cystine in the obtained keratin hydrolyzate was measured using the same automatic amino acid analyzer as in Example 1, the amount of cystine was 12.2 mol% of the total amino acids.
つぎに、この濃度３０％のケラチン加水分解物の水溶液
を実施例１と同様の電解還元装置に通液し、電流２Ａで
１４時間電解還元を行った。Next, this aqueous solution of keratin hydrolyzate having a concentration of 30% was passed through an electrolytic reduction device similar to that in Example 1, and electrolytic reduction was performed at a current of 2 A for 14 hours.
電解還元されたケラチン加水分解物の分子量をゲル濾過
法により測定したところ、平均分子量は２．９００であ
った。また、得られたケラチン加水分解物のシスティン
量を実施例１と同様の方法で測定したところ、システィ
ン量は全アミノ酸中１０．２モル％であった。When the molecular weight of the electrolytically reduced keratin hydrolyzate was measured by a gel filtration method, the average molecular weight was 2.900. Further, when the amount of cysteine in the obtained keratin hydrolyzate was measured in the same manner as in Example 1, the amount of cysteine was 10.2 mol% of the total amino acids.
電解還元前のケラチン加水分解物に対する電解還元後の
ケラチン加水分解物の収率は９７％であった。The yield of the keratin hydrolyzate after electrolytic reduction relative to the keratin hydrolyzate before electrolytic reduction was 97%.
実施例３
粉砕した羊毛５００ｇに３２％塩酸ｓｏｏ ｇを加え、
２５℃で７２時間攪拌して加水分解を行った。加水分解
後、反応液に２０％水酸化ナトリウム水溶液を加えてｐ
Ｈ５にした。この反応液にタンパク加水分解酵素パパイ
ンを０．５ｇ加え、４２°Ｃで攪拌しながら２４時間加
水分解を行った。加水分解途中、２０％水酸化ナトリウ
ム水溶液を加えて反応液のｐＨを５に保った。パパイン
による加水分解後、反応液を７５°Ｃで１時間加熱して
パパインを失活させた。Example 3 Add soo g of 32% hydrochloric acid to 500 g of crushed wool,
Hydrolysis was carried out by stirring at 25° C. for 72 hours. After hydrolysis, add 20% aqueous sodium hydroxide solution to the reaction solution and
I set it to H5. 0.5 g of protein hydrolase papain was added to this reaction solution, and hydrolysis was carried out at 42°C for 24 hours with stirring. During the hydrolysis, a 20% aqueous sodium hydroxide solution was added to maintain the pH of the reaction solution at 5. After hydrolysis with papain, the reaction solution was heated at 75°C for 1 hour to inactivate papain.
反応液に２０％水酸化ナトリウム溶液を加えてｐＨ６に
したのち、濾過し、濾液を実施例２と同様の電気透析装
置により電気透析して脱塩し、濃度調整を行い、濃度２
５％のケラチン加水分解物の水溶液を得た。After adjusting the pH to 6 by adding 20% sodium hydroxide solution to the reaction solution, it was filtered, and the filtrate was desalted by electrodialysis using the same electrodialysis apparatus as in Example 2, and the concentration was adjusted to a concentration of 2.
A 5% aqueous solution of keratin hydrolyzate was obtained.
このようにして得られたケラチン加水分解物の分子量を
ゲル濾過法により測定したところ、平均分子量１ 、２
００であった。また、得られたケラチン加水分解物中の
シスチン量を実施例１と同様のアミノ酸自動分析計で測
定したところ、シスチン量は全アミノ酸中７．２モル％
であった。When the molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration, the average molecular weight was 1, 2.
It was 00. Furthermore, when the amount of cystine in the obtained keratin hydrolyzate was measured using an automatic amino acid analyzer similar to that used in Example 1, the amount of cystine was 7.2 mol% of the total amino acids.
Met.
つぎに、この濃度２５％のケラチン加水分解物の水溶液
を実施例１と同様の電解還元装置に通液し、電流２人で
１０時間電解還元を行った。Next, this aqueous solution of the keratin hydrolyzate having a concentration of 25% was passed through an electrolytic reduction apparatus similar to that in Example 1, and electrolytic reduction was performed for 10 hours using electric current by two people.
電解還元されたケラチン加水分解物の分子量をゲル濾過
法により測定したところ、平均分子量は８００であった
。また、得られたケラチン加水分解物のシスティン量を
実施例１と同様の方法で測定したところ、システィン量
は全アミノ酸中５．８モル％であった。When the molecular weight of the electrolytically reduced keratin hydrolyzate was measured by a gel filtration method, the average molecular weight was 800. Further, when the amount of cysteine in the obtained keratin hydrolyzate was measured in the same manner as in Example 1, the amount of cysteine was 5.8 mol % in the total amino acids.
電解還元前のケラチン加水分解物に対する電解還元後の
ケラチン加水分解物の収率は９７％であった。The yield of the keratin hydrolyzate after electrolytic reduction relative to the keratin hydrolyzate before electrolytic reduction was 97%.
比較例１
１ｆｆｉのビーカーに尿素３６０ｇ、 トリス−（ヒ
ドロキシメチル）−アミノメタン２４ｇおよびＥＤＴＡ
ｌｇを入れ、蒸留水を加えて全容を約８００ｍｆとし、
撹拌して加えた試薬をほどんど熔解させたのち、２−メ
ルカプトエタノール２０ｇを加えた。Comparative Example 1 360 g of urea, 24 g of tris-(hydroxymethyl)-aminomethane and EDTA in a 1ffi beaker.
1g, add distilled water to make the total volume about 800mf,
After stirring to almost dissolve the added reagent, 20 g of 2-mercaptoethanol was added.
つぎに２０％水酸化ナトリウム水溶液を加えて溶液をｐ
Ｈ１０に調整し、蒸留水を追加してこの溶液の全容を１
１とした。Next, add 20% aqueous sodium hydroxide solution to make the solution p
Adjust to H10 and add distilled water to bring the total volume of this solution to 1.
It was set to 1.
この溶液に脱脂された羊毛２０ｇを加え、攪拌して発生
する泡を除去したのち、容器に上蓋をし、ときどき攪拌
しながら室温で３日間放置した。After adding 20 g of defatted wool to this solution and stirring to remove generated bubbles, the container was covered with a top lid and left at room temperature for 3 days with occasional stirring.
つぎに得られた反応混合物を減圧濾過して、未反応の羊
毛を除去した。The resulting reaction mixture was then filtered under reduced pressure to remove unreacted wool.
得られた濾液約８２０ｍｊ！を限外濾過器〔アミコン社
製、４０２型セル、ダイアフローメンプランＵＭ１０（
分画分子量１０，０００） ）を使用して限外濾過する
ことによって、反応生成物の濃度を高くするとともに、
尿素と還元剤などを含む溶媒を濾去した。４００ｍ１に
まで濃縮し、得られた濃縮液をセロファン透析チューブ
に詰め、０．１Ｎギ酸５１で８時間透析し、さらに０．
１Ｎギ酸５１で８時間ずつ透析を２回繰り返し、ついで
蒸留水３１で３時間透析した。The obtained filtrate was about 820mj! Ultrafilter [manufactured by Amicon, 402 type cell, Diaflow Menplan UM10 (
The concentration of the reaction product is increased by ultrafiltration using a molecular weight cutoff of 10,000).
The solvent containing urea, reducing agent, etc. was filtered off. It was concentrated to 400 ml, and the resulting concentrate was packed in a cellophane dialysis tube, dialyzed against 0.1N formic acid 51 for 8 hours, and further 0.1N.
Dialysis was repeated twice with 1N formic acid 51 for 8 hours each time, and then with distilled water 31 for 3 hours.
透析後の濃縮液を５００ｍ！！、のビーカーに移し、こ
れにペプシン５０ｍｇを０．ＩＮ酢酸５ｍ２に溶解させ
た溶液を加えた。湯浴で反応溶液を３７°Ｃに保ちなが
ら、電磁式攪拌器によって反応溶液を充分に攪拌しつつ
、２０時間かけてケラチンを加水分解した。500m of concentrated liquid after dialysis! ! , and add 50 mg of pepsin to it. A solution in 5 m2 of IN acetic acid was added. The keratin was hydrolyzed over a period of 20 hours while the reaction solution was kept at 37°C in a hot water bath and sufficiently stirred using an electromagnetic stirrer.
反応終了後、２０％水酸化ナトリウム水溶液を加えて反
応液をｐＨ７にし、これを湯浴で７０℃に保ち３０分間
放置してペプシンを不活性化させた。After the reaction was completed, the reaction solution was adjusted to pH 7 by adding a 20% aqueous sodium hydroxide solution, and kept at 70° C. in a hot water bath for 30 minutes to inactivate pepsin.
冷却後、得られた反応液を減圧濾過し、濾液を５００ｍ
ｊ！の共栓付ナス型コルベンに移し、ロータリーエバポ
レーターにより減圧１１１１１Ｌ乾燥残分が２０％のケ
ラチン加水分解物を得た。収率は４８％であった。After cooling, the obtained reaction solution was filtered under reduced pressure, and the filtrate was filtered at 500 m
j! The mixture was transferred to an eggplant type kolben with a stopper, and a rotary evaporator was used to obtain a keratin hydrolyzate having a reduced pressure of 11111L and a dry residue of 20%. The yield was 48%.
得られたケラチン加水分解物の分子量をゲル濾過法によ
り測定したところ、平均分子量は１ 、６００であった
。また、得られたケラチン加水分解物のシスティン量を
実施例１と同様の方法で測定したところ、システィン量
は全アミノ酸中７．５モル％であった。When the molecular weight of the obtained keratin hydrolyzate was measured by gel filtration method, the average molecular weight was 1,600. Further, when the amount of cysteine in the obtained keratin hydrolyzate was measured in the same manner as in Example 1, the amount of cysteine was 7.5 mol % in the total amino acids.
比較例２
羊毛３５ｇを０゜５モル／ｌ硫化ナトリウム１Ｎ（０゜
１％ＥＤＴＡを含む）に加え、発生する泡を除いたのち
、ときどき攪拌しながら２４時間放置した。Comparative Example 2 35 g of wool was added to 0.5 mol/l sodium sulfide 1N (containing 0.1% EDTA), and after removing generated bubbles, the mixture was allowed to stand for 24 hours with occasional stirring.
つぎに得られた反応混合物を減圧濾過して未反応物を除
去し、得られた濾液を比較例１と同様に限外濾過して反
応液が１／３容になるまで濃縮した。Next, the obtained reaction mixture was filtered under reduced pressure to remove unreacted substances, and the obtained filtrate was subjected to ultrafiltration in the same manner as in Comparative Example 1, and the reaction solution was concentrated to 1/3 volume.
得られた１４１１液をセロファン透析チューブに詰め、
蒸留水３２で６時間ずつ透析を３回繰り返した。The obtained 1411 liquid was packed into a cellophane dialysis tube,
Dialysis was repeated three times for 6 hours each with distilled water.
透析後の濃縮液をビーカーに移し、ｐＨメーターを用い
酢酸を加えてｐＨ５に調整した。これにプロメライン（
５０万単位／ｇ）５００ｍｇを加え、湯浴で反応液を４
０’Ｃに保ちながら攪拌して２４時間加水分解した０反
応終了後、反応液を７０°Ｃに昇温し、３０分間放置し
てブロメラインを不活性化させた。The concentrated solution after dialysis was transferred to a beaker, and the pH was adjusted to 5 by adding acetic acid using a pH meter. Add this to Promeline (
500,000 units/g) was added, and the reaction solution was heated in a hot water bath for 4 hours.
After the completion of the 24-hour hydrolysis reaction while maintaining the temperature at 0'C, the reaction solution was heated to 70C and left to stand for 30 minutes to inactivate the bromelain.
得られた反応液を減圧濾過し、以後比較例１と同様にし
て、乾燥残分が２０％のケラチン加水分解物を得た。収
率は４３％であった。The obtained reaction solution was filtered under reduced pressure, and the same procedure as in Comparative Example 1 was carried out to obtain a keratin hydrolyzate with a dry residue of 20%. The yield was 43%.
得られたケラチン加水分解物の分子量をゲル濾過法によ
り測定したところ、平均分子量は８２０であった。また
、得られたケラチン加水分解物のシスティン量を実施例
１と同様の方法で測定したところ、システィン量は全ア
ミノ酸中７．３モル％であった。When the molecular weight of the obtained keratin hydrolyzate was measured by gel filtration method, the average molecular weight was 820. Further, when the amount of cysteine in the obtained keratin hydrolyzate was measured in the same manner as in Example 1, the amount of cysteine was 7.3 mol % in the total amino acids.
上記のようにして得られた実施例１〜３および比較例１
〜２のケラチン加水分解物を濃度調整して、いずれも５
％水溶液にし、１０名の女性パネラ−により、奥の判定
を行ったところ、比較例１のケラチン加水分解物にはメ
ルカプタン臭が、比較例２のケラチン加水分解物には硫
化水素臭がはっきりと認められるが、実施例１〜３のケ
ラチン加水分解物には奥が認められないとのことであっ
た。Examples 1 to 3 and Comparative Example 1 obtained as above
The concentration of the keratin hydrolyzate of ~2 was adjusted, and both were 5.
% aqueous solution and was evaluated by 10 female panelists, the keratin hydrolyzate of Comparative Example 1 had a mercaptan odor, and the keratin hydrolyzate of Comparative Example 2 had a distinct hydrogen sulfide odor. However, in the keratin hydrolyzates of Examples 1 to 3, no depth was observed.
つぎに、本発明のケラチン加水分解物の応用例について
説明する。Next, application examples of the keratin hydrolyzate of the present invention will be explained.
応用例１
本発明のケラチン加水分解物を配合した下記組成のパー
マネントウェーブ用第１剤を調製し、これを本発明の実
施品ｌとした。Application Example 1 A first agent for permanent waving having the following composition containing the keratin hydrolyzate of the present invention was prepared, and this was designated as Example 1 of the present invention.
実施例１のケラチン加水分解物 ２．５％（平
均分子量２７０、システィンＭ８，４モル％）チオグリ
コール酸アンモニウム ６．０％ポリオキシ
エチレン（ｌＯ）ノニルフェニルエーテル
０，５％塩化セチルトリメチルアンモ
ニウム ０．２％モノエタノールアミン
０．８％アンモニア水（２５％）
ＰＨ９，２とするＥＤＴＡ
Ｏ，１％香料 通量
計１００．０％
また、上記実施品１のパーマネントウェーブ用第１剤か
ら、実施例１のケラチン加水分解物を除き、そのぶん精
製水を増量したパーマネントウェーブ用第１剤を調製し
、これを比較品１とした。Keratin hydrolyzate of Example 1 2.5% (average molecular weight 270, cysteine M8, 4 mol%) Ammonium thioglycolate 6.0% polyoxyethylene (lO) nonylphenyl ether
0.5% Cetyltrimethylammonium chloride 0.2% Monoethanolamine
0.8% ammonia water (25%)
EDTA to pH 9.2
O, 1% Fragrance Meter: 100.0% In addition, from the first agent for permanent waves of Example 1, the keratin hydrolyzate of Example 1 was removed, and the amount of purified water was increased accordingly. A preparation was prepared, and this was designated as Comparative Product 1.
つぎに、上記実施品１および比較品１のパーマネントウ
ェーブ用第１剤を用い、パーマネントウェーブ用第２剤
には６％臭素酸ナトリウム水溶液を用いて、下記に示す
試験（試験例１〜４）により、パーマネントウェーブ用
第１剤の評価をした。Next, the following tests (Test Examples 1 to 4) were carried out using the first agent for permanent waving of the above-mentioned implementation product 1 and comparative product 1, and using a 6% aqueous sodium bromate solution as the second agent for permanent waving. The first agent for permanent waves was evaluated.
く試験例１〉
（１）試料の調整
パーマネントウェーブや染毛などを行ったことのない女
性の毛髪（長さ約１８１）を１０本ずつたばねて毛束と
し、これらの毛束を事前にポリオキシエチレンノニルフ
ェニルエーテルの２％水溶液で洗浄し、室温で自然乾燥
して、試験用毛束とした。Test Example 1 (1) Sample preparation 10 hairs (length approximately 181cm) from a woman who has never had her hair permanently waved or dyed are tied together into hair bundles. It was washed with a 2% aqueous solution of oxyethylene nonylphenyl ether and air-dried at room temperature to obtain a test hair bundle.
（２）試験操作
上記試験用毛束を直径１ｃ嘗のプラスチック製口ラドに
巻き付け、この毛束に前記実施品１および比較品１のパ
ーマネントウェーブ用第１剤をそれぞれ充分に塗付し、
室温で１５分間放置し、水洗した後、パーマネントウェ
ーブ用第２剤を充分に塗付し、常温で１０分間放置した
のちロンドから毛束をはずし、水洗後自然乾燥した。こ
の毛束をつり下げて、そのカールの直径を測定した。こ
のカール処理した毛束をポリオキシエチレンノニルフェ
ニルエーテルの２％水溶液で２４時間おきに軽く手での
ばしながら５回洗浄し、毎洗浄直後に自然乾燥し、カー
ルの直径を測定した。その結果を第１表に示す。(2) Test procedure Wrap the above test hair bundle around a plastic rad with a diameter of 1 cm, sufficiently apply the first agent for permanent waves of the above-mentioned Example Product 1 and Comparative Product 1 to the hair bundle,
After being left at room temperature for 15 minutes and washed with water, a second agent for permanent waving was sufficiently applied, and after being left at room temperature for 10 minutes, the hair bundle was removed from the ronde, washed with water, and air-dried. This hair bundle was hung and the diameter of the curl was measured. The curled hair bundles were washed five times with a 2% aqueous solution of polyoxyethylene nonylphenyl ether while being gently stretched by hand every 24 hours, air-dried immediately after each wash, and the diameter of the curls was measured. The results are shown in Table 1.
第 １ 表
第１表に示すように、実施品１のパーマネントウェーブ
用第１剤は、比較品１のパーマネントウェーブ用第１剤
に比べて、カールの直径が小さく、毛髪に持続性のある
強力なウェーブを付与することができた。Table 1 As shown in Table 1, the first agent for permanent waving of Example Product 1 has a smaller curl diameter than the first agent for permanent waving of Comparative Product 1, and has a strong and long-lasting effect on the hair. I was able to give a nice wave.
〈試験例２〉
試験例１でカール処理した毛束を試料とし、カールの保
持性を調べた。その結果を第２表に示す。<Test Example 2> The hair bundles curled in Test Example 1 were used as samples to examine curl retention. The results are shown in Table 2.
試験操作
試験例１でそれぞれカール処理した毛束を、水洗後直径
２０＋ｍｓのローラーに巻き付けて固定し、自然乾燥後
、ローラーからはずし、つり下げて室内に放置したとき
のカールリテンション％の経時変化を求めた。なお、カ
ールリテンション％は次式で算出した。Test procedure After washing the hair bundles curled in Test Example 1, they were wrapped around a roller with a diameter of 20+ ms and fixed, and after air drying, they were removed from the roller, hung, and left indoors. I asked for it. Note that curl retention % was calculated using the following formula.
Ｌ−Ｌ。L-L.
Ｌ＝毛束を充分のばした時の長さ （Ｌ＝１８ｃｍ）Ｌ
、−毛束を自然乾燥後ローラーからはずした時のカール
先端の長さ
り、＝一定時間つり下げた時のカール先端の長さ
第 ２ 表
第２表に示すように、実施品１のパーマネントウェーブ
用第１剤は、比較品１のパーマネントウェーブ用第１剤
に比べて、カールリテンション％が大き（、この結果か
ら、ウェーブの保持性が優れていることが明らかにされ
た。L = Length when the hair bundle is fully stretched (L = 18cm) L
, - Length of the tip of the curl when the hair bundle is removed from the roller after air drying, = Length of the tip of the curl when it is hung for a certain period of time Table 2 As shown in Table 2, the permanent wave of Product 1 The first agent for permanent waves had a higher curl retention% than the first agent for permanent waves (comparative product 1) (from this result, it was revealed that the wave retention was excellent).
〈試験例３〉
前記実施品１および比較品１のパーマネントウェーブ用
第１剤ならびに６％臭素酸ナトリウム水溶液からなるパ
ーマネントウェーブ用第２剤により、通常の手法で毛髪
にパーマネントウェーブをかけ、それぞれ１０人の女性
パネラ−により、パーマネントウェーブ処理後の毛髪の
状態（艶、柔軟性および潤い）ならびに不快臭の少なさ
（パーマネントウェーブ処理の直後および洗髪１回後の
毛髪の不快臭）について調べた。その結果は第３表に示
すとおりである。なお、評価は５段階評価で行い、結果
は１０人の平均値で示した。毛髪の状態に関しては、点
数が高いほど毛髪の状態が良好であることを示しており
、不快臭の少なさに関しては、点数が高いぼどチオグリ
コール酸アンモニウムに基づく不快臭が少ないことを示
している。<Test Example 3> Hair was permanently waved in the usual manner using the first agent for permanent waving of the above-mentioned Example Product 1 and Comparative Product 1 and the second agent for permanent wave consisting of a 6% aqueous sodium bromate solution. A female panelist examined the condition of the hair after the permanent wave treatment (shininess, flexibility, and moisture) and the lack of unpleasant odor (unpleasant odor of the hair immediately after the permanent wave treatment and after one hair wash). The results are shown in Table 3. The evaluation was performed on a 5-level scale, and the results are shown as the average value of 10 people. Regarding hair condition, a higher score indicates better hair condition, and regarding less unpleasant odor, a higher score indicates less unpleasant odor caused by ammonium thioglycolate. There is.
第 ３ 表
第３表に示す結果から明らかなように、実施品１のパー
マネントウェーブ用第１剤の場合は、比較品１のパーマ
ネントウェーブ用第１剤に比べて、不快臭が少なく、ま
たパーマネントウェーブ処理後の毛髪の状態も良好であ
った。Table 3 As is clear from the results shown in Table 3, the first agent for permanent waves of Example Product 1 has less unpleasant odor than the first agent for permanent waves of Comparative Product 1. The condition of the hair after waving was also good.
く試験例４）
試験例３においてパーマネントウェーブ処理を行った毛
髪の一部を採取してアミノ酸分析を行い毛髪中のシステ
ィン酸の定量をした。このシスティン酸の生成は毛髪の
損傷と関連性を有しており、毛髪中のシスティン酸量が
多いほど、パーマネントウェーブ処理による毛髪の損傷
が大きいことを示している。システィン酸の測定結果（
１０人の平均値）を第４表に示す。Test Example 4) A portion of the hair that had been subjected to the permanent wave treatment in Test Example 3 was collected and subjected to amino acid analysis to determine the amount of cystic acid in the hair. The production of cystic acid is associated with hair damage, and the greater the amount of cystic acid in hair, the greater the hair damage caused by permanent waving. Cystic acid measurement results (
The average values of 10 people) are shown in Table 4.
第 ４ 表
ウェーブ用第１剤は、比較品１のパーマネントウェーブ
用第２剤に比べて、パーマネントウェーブ処理後の毛髪
中のシスティン酸量が少なく、パーマネントウェーブ処
理による毛髪の損傷が少ないことが明らかにされた。Table 4 It is clear that the first agent for waving has a lower amount of cystic acid in the hair after the permanent waving treatment than the second agent for permanent waving of Comparative Product 1, and there is less damage to the hair due to the permanent waving treatment. was made into
応用例２
本発明のケラチン加水分解物を配合した下記組成のセッ
トローションを調製し、これを本発明の実施品２とした
。Application Example 2 A setting lotion with the following composition containing the keratin hydrolyzate of the present invention was prepared, and this was designated as Example 2 of the present invention.
実施例２のケラチン加水分解物
（平均分子量２，９００、システィン量１０．２）カチ
オン化セルロース
ヤシ油アルキルアミドプロピルベタインエタノール
ＤＴＡ
防腐剤
香料
４．０％
０．３％
０．５％
１２．０％
０．１％
適量
適量
第４表に示すように、実施品１のパーマネント計１００
．０％
また、上記実施品２のセットローションから、実施例２
のケラチン加水分解物を除き、そのぶん精製水を増量し
たセットローションを調製し、これを比較品２とした。Keratin hydrolyzate of Example 2 (average molecular weight 2,900, cysteine content 10.2) cationized cellulose coconut oil alkylamide propyl betaine ethanol DTA preservative fragrance 4.0% 0.3% 0.5% 12.0 % 0.1% Appropriate amount Appropriate amount As shown in Table 4, the permanent total of product 1 is 100
．． 0% Also, from the set lotion of Example 2 above, Example 2
A setting lotion was prepared in which the keratin hydrolyzate was removed and the amount of purified water was increased accordingly, and this was designated as Comparative Product 2.
これら実施品２および比較品２のセットローションを１
０人の女性パネラ−に、洗髪後、頭の中央から毛髪を左
右に分けてカーラ−に巻き付け、本人には知らせずに、
実施品２および比較例２のセンドローションをカーラ−
に巻き付けた毛髪上に塗付し、ドライヤーで１５分間乾
燥して、セット性、柔軟性、潤い、艶を比較した。その
結果を第５表に示す。なお、第５表には、実施品２が良
いと答えた人数、どちらが良いかわからないと答えた人
数、比較品２が良いと答えた人数で示す。1 set lotion of these implementation product 2 and comparison product 2
After washing the hair, 0 female panelists were asked to separate their hair from the center of their head to the left and right and wrap it around curlers without letting them know.
Apply the send lotions of Example 2 and Comparative Example 2 to the curler.
It was applied onto hair wrapped around the hair, dried for 15 minutes with a hair dryer, and the set properties, flexibility, moisture, and shine were compared. The results are shown in Table 5. Table 5 shows the number of people who answered that the experimental product 2 was better, the number of people who answered that they did not know which one was better, and the number of people who said that the comparison product 2 was better.
第 ５ 表
上記第５表に示すように、本発明のケラチン加水分解物
を配合した実施品２のセットローションは、上記ケラチ
ン加水分解物を配合していない比較品２のセットローシ
ョンに比べて、毛髪のセント性、柔軟性、潤い、艷のい
ずれもが優れていた。Table 5 As shown in Table 5 above, the setting lotion of Example 2 containing the keratin hydrolyzate of the present invention had the following effects compared to the setting lotion of Comparative Product 2 which did not contain the keratin hydrolyzate. The hair's stiffness, flexibility, moisture, and silkiness were all excellent.
特にセット性に関しては、明らかな優位性を示していた
。In particular, it showed clear superiority in terms of set performance.
応用例３
本発明のケラチン加水分解物を配合した下記組成のフェ
イスクリームを調製し、これを本発明の実施品３とした
。Application Example 3 A face cream containing the keratin hydrolyzate of the present invention and having the following composition was prepared and designated as Example 3 of the present invention.
５．０％
実施例３のケラチン加水分解物
（平均分子ｆｆｉ ８００、システィン量５．８モル％
）乳化剤〔アヤコールＬＣ−ＷＡＸ
（商品名）、■成和化成製〕
乳化剤〔アヤコールＧＴＩＳＳ
（商品名）、■成和化成製］
オクチルイソパルミテート
イソプロビルイソステアレート
グリセリンモノステアレート
シリコンオイル（ポリジメチル
シロキサン）
メチルパラベン
プロピルパラベン
トリエタノールアミン
１．３−ブチレングリコール
グリセリン
ＤＴＡ
香料
６．０％
６．０％
３．５％
２．０％
４．５％
０．２％
０．２％
０．１％
０．２％
１０．０％
４．１％
０．１％
適量
計ｉｏｏ、ｏ％
また、上記実施品３のフェイスクリームから実施例３の
ケラチン加水分解物を除き、そのぶん精製水を増量した
フェイスクリームを調製し、これを比較品３とした。5.0% Keratin hydrolyzate of Example 3 (average molecular ffi 800, cysteine content 5.8 mol%
) Emulsifier [Ayacol LC-WAX (product name), Seiwa Kasei] Emulsifier [Ayacol GTISS (product name), Seiwa Kasei] Octyl isopalmitate isoprobyl isostearate glycerin monostearate silicone oil (polymer) Dimethylsiloxane) Methylparabenpropylparabentriethanolamine 1.3-butylene glycol glycerin DTA Fragrance 6.0% 6.0% 3.5% 2.0% 4.5% 0.2% 0.2% 0.1% 0.2% 10.0% 4.1% 0.1% Adequate amount ioo, o% In addition, the keratin hydrolyzate of Example 3 was removed from the face cream of Example 3, and the amount of purified water was increased accordingly. A face cream was prepared and designated as Comparative Product 3.
上記実施品３、比較品３のフェイスクリームを、１０人
の女性パネラ−に、石鹸で洗顔、水洗後の顔に使用し、
３時間後の皮膚の潤い、艶、なめらかさについて、どち
らが良いかを評価させた。その結果を第６表に示す。The face creams of Implementation Product 3 and Comparison Product 3 were applied to 10 female panelists after washing their faces with soap and water.
After 3 hours, participants were asked to evaluate the moisture, luster, and smoothness of their skin. The results are shown in Table 6.
第 ６ 表
上記第６表に示すように、本発明のケラチン加水分解物
を配合した実施品３のフェイスクリームは、上記ケラチ
ン加水分解物を配合していない比較品３のフェイスクリ
ームに比べて、皮膚に潤いと艶を付与し、かつ皮膚をな
めらかにする効果が優れていた。これは本発明のケラチ
ン加水分解物が皮膚と親和性を有していて、皮膚になじ
みやすく、他の配合成分と共に長時間皮膚上に残ること
によるものと考えられる。Table 6 As shown in Table 6 above, the face cream of Example 3 containing the keratin hydrolyzate of the present invention had the following effects compared to the face cream of Comparative Product 3 that did not contain the keratin hydrolyzate. It had an excellent effect of imparting moisture and luster to the skin and smoothing the skin. This is considered to be because the keratin hydrolyzate of the present invention has an affinity for the skin, easily blends into the skin, and remains on the skin for a long time together with other ingredients.
以上説明したように、本発明では、シスチンのジスルフ
ィド結合を開裂し、メルカプト基を生成させるための還
元にあたって、メルカプタン類や硫化物などの還元剤を
使用しないで、電解還元により行うので、得られるケラ
チン加水分解物に還元剤の悪臭が残存することがない。As explained above, in the present invention, the reduction to cleave the disulfide bonds of cystine and generate mercapto groups is carried out by electrolytic reduction without using reducing agents such as mercaptans or sulfides. No odor from the reducing agent remains in the keratin hydrolyzate.
また、還元を電解還元により行うので、ケラチン加水分
解物のシスチンのジスルフィド結合をほぼ完全に還元す
ることができるので、還元剤を用いる場合に比べて、還
元物の収率が高い。Further, since the reduction is performed by electrolytic reduction, the disulfide bonds of cystine in the keratin hydrolyzate can be almost completely reduced, so the yield of the reduced product is higher than when a reducing agent is used.
もとより、還元剤を使用しないので、還元剤の無駄が生
じず、また、尿素などのタンパク変性剤を必要とせず、
還元剤やタンパク変性剤を含む廃液の処理問題も生じな
い。Of course, since no reducing agent is used, there is no waste of reducing agent, and there is no need for protein denaturing agents such as urea.
There is no problem with the treatment of waste liquid containing reducing agents or protein denaturing agents.
本発明によって得られるケラチン加水分解物は、分子中
にメルカプト基を有するものであるが、前記のように還
元剤に基づく悪、奥を有しないので、種々の化粧品に応
用することができる。Although the keratin hydrolyzate obtained by the present invention has a mercapto group in its molecule, it does not have the disadvantages caused by reducing agents as described above, and therefore can be applied to various cosmetics.
また、メルカプト基に基づく還元作用により、たとえば
チオグリコールなどのように刺激性や悪臭を有する物質
が配合されている化粧品に配合すると、それらの刺激性
や悪臭を低減する効果がある。Further, due to the reducing action based on the mercapto group, when it is added to cosmetics that contain irritating and malodorous substances such as thioglycol, it has the effect of reducing the irritation and malodor of these substances.
さらに、メルカプト基が空気中の酸素や酸化剤によって
酸化され、毛髪上で被膜を形成する作用があるので、そ
れ自身でウェーブ効果ないしはセット効果を有し、また
在来のパーマネントウェーブ用剤やセット剤に配合され
たときは、その効果を高める作用がある。Furthermore, since the mercapto group is oxidized by oxygen and oxidizing agents in the air and forms a film on the hair, it has a waving effect or setting effect by itself, and it also has a waving effect or a setting effect. When added to a drug, it has the effect of enhancing its effect.
また、天然のタンパク質であるケラチンから誘導される
ものであるため、毛髪や皮膚に対して安全であり、その
分子中に有するアミノ基やカルボキシル基の作用により
、毛髪にコンディショニング効果と毛髪の保護・強化作
用を有していて、毛髪に吸着して、毛髪に艶、柔軟性、
潤いを付与し、毛髪のｔ員傷を防止し、かつ損傷した毛
髪を回復させ、皮膚に対しても親和性を有していて、皮
膚に潤いと艶を付し、かつ皮膚をなめらかにする。In addition, since it is derived from keratin, a natural protein, it is safe for hair and skin, and the amino and carboxyl groups in its molecules have a conditioning effect on the hair and protect and protect the hair. It has a strengthening effect and is adsorbed to the hair, giving it shine, flexibility,
Provides moisture, prevents hair damage, restores damaged hair, and has an affinity for the skin, adding moisture and luster to the skin, and smoothing the skin. .
手続補正書（自発） 平成２年２月１６日Procedural amendment (voluntary) February 16, 1990
Claims (3)
全アミノ酸中５〜１８モル％のケラチン加水分解物を、
電解還元することによって得られた平均分子量２００〜
３，０００で、システイン量が全アミノ酸中５〜１８モ
ル％のケラチン加水分解物。(1) A keratin hydrolyzate with an average molecular weight of 300 to 5,000 and a cystine content of 5 to 18 mol% of all amino acids,
Average molecular weight obtained by electrolytic reduction: 200~
3,000, and the amount of cysteine is 5 to 18 mol% of the total amino acids.
全アミノ酸中５〜１８モル％のケラチン加水分解物を、
電解還元によって還元し、平均分子量２００〜３，００
０で、システイン量が全アミノ酸中５〜１８モル％のケ
ラチン加水分解物を得ることを特徴とするケラチン加水
分解物の製造方法。(2) A keratin hydrolyzate with an average molecular weight of 300 to 5,000 and a cystine content of 5 to 18 mol% among all amino acids,
Reduced by electrolytic reduction, average molecular weight 200-3,00
A method for producing a keratin hydrolyzate, the method comprising obtaining a keratin hydrolyzate with a cysteine content of 0 and a cysteine content of 5 to 18 mol% based on all amino acids.
品基剤。(3) A cosmetic base comprising the keratin hydrolyzate according to claim 1.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP14332289A JPH0311099A (en) | 1989-06-06 | 1989-06-06 | Hydrolyzed keratin, its production and cosmetic base consisting of hydrolyzed keratin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP14332289A JPH0311099A (en) | 1989-06-06 | 1989-06-06 | Hydrolyzed keratin, its production and cosmetic base consisting of hydrolyzed keratin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH0311099A true JPH0311099A (en) | 1991-01-18 |
Family
ID=15336093
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP14332289A Pending JPH0311099A (en) | 1989-06-06 | 1989-06-06 | Hydrolyzed keratin, its production and cosmetic base consisting of hydrolyzed keratin |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0311099A (en) |
Cited By (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH05222100A (en) * | 1992-02-14 | 1993-08-31 | San Orient Kagaku Kk | Production of reduced-type keratin peptide |
| US6544548B1 (en) | 1999-09-13 | 2003-04-08 | Keraplast Technologies, Ltd. | Keratin-based powders and hydrogel for pharmaceutical applications |
| JP2004347405A (en) * | 2003-05-21 | 2004-12-09 | Umeda Jimusho:Kk | Medical/histological evaluation method of ultraviolet disorder and anti-ultraviolet skin care composition |
| JP2006151940A (en) * | 2004-10-29 | 2006-06-15 | Dainichiseika Color & Chem Mfg Co Ltd | Cell activator |
| WO2007023816A1 (en) | 2005-08-23 | 2007-03-01 | Seiwa Kasei Company, Limited | Method for preparation of reduced keratin, reduced cuticle protein or mixture thereof |
| US8258093B2 (en) | 2006-02-17 | 2012-09-04 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
| US8299013B2 (en) | 2006-02-17 | 2012-10-30 | Wake Forest University Health Sciences | Clotting and healing compositions containing keratin biomaterials |
| US8324346B2 (en) | 2002-01-28 | 2012-12-04 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
| US8637231B2 (en) | 2004-08-17 | 2014-01-28 | Wake Forest University Health Sciences | Method for increasing the volume of a blood substitute with an expander comprising basic alpha keratose |
| US8920827B2 (en) | 2005-10-21 | 2014-12-30 | Wake Forest University Health Sciences | Keratin bioceramic compositions |
| US8968764B2 (en) | 2006-02-10 | 2015-03-03 | Wake Forest University Health Sciences | Nerve regeneration employing keratin biomaterials |
| US9045600B2 (en) | 2009-05-13 | 2015-06-02 | Keraplast Technologies, Ltd. | Biopolymer materials |
| US9068162B2 (en) | 2007-08-17 | 2015-06-30 | Wake Forest University Health Sciences | Keratin biomaterials for cell culture and methods of use |
| US9220754B2 (en) | 2010-11-17 | 2015-12-29 | Wake Forest University Health Sciences | Keratin compositions for treatment of bone deficiency or injury |
| US10434213B2 (en) | 2010-03-05 | 2019-10-08 | Wake Forest University Health Sciences | Controlled delivery system |
| EP3701802A1 (en) | 2019-02-28 | 2020-09-02 | Bretagne Chimie Fine | Composition with high free amino acid content and use as raw material and complete food for animal nutrition |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5630909A (en) * | 1979-08-22 | 1981-03-28 | Seiwa Kasei:Kk | Preparation of keratin hydrolyzate |
| JPS57109797A (en) * | 1980-12-26 | 1982-07-08 | Kao Corp | Preparation of low-molecular weight keratinous substance |
| JPS59192056A (en) * | 1983-04-13 | 1984-10-31 | Teijin Eng Kk | Modification of bean protein |
| JPS61236795A (en) * | 1985-04-11 | 1986-10-22 | Fuji Oil Co Ltd | Method for fractionating protein |
-
1989
- 1989-06-06 JP JP14332289A patent/JPH0311099A/en active Pending
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5630909A (en) * | 1979-08-22 | 1981-03-28 | Seiwa Kasei:Kk | Preparation of keratin hydrolyzate |
| JPS57109797A (en) * | 1980-12-26 | 1982-07-08 | Kao Corp | Preparation of low-molecular weight keratinous substance |
| JPS59192056A (en) * | 1983-04-13 | 1984-10-31 | Teijin Eng Kk | Modification of bean protein |
| JPS61236795A (en) * | 1985-04-11 | 1986-10-22 | Fuji Oil Co Ltd | Method for fractionating protein |
Cited By (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH05222100A (en) * | 1992-02-14 | 1993-08-31 | San Orient Kagaku Kk | Production of reduced-type keratin peptide |
| US6544548B1 (en) | 1999-09-13 | 2003-04-08 | Keraplast Technologies, Ltd. | Keratin-based powders and hydrogel for pharmaceutical applications |
| US8324346B2 (en) | 2002-01-28 | 2012-12-04 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
| JP2004347405A (en) * | 2003-05-21 | 2004-12-09 | Umeda Jimusho:Kk | Medical/histological evaluation method of ultraviolet disorder and anti-ultraviolet skin care composition |
| JP4538202B2 (en) * | 2003-05-21 | 2010-09-08 | 有限会社梅田事務所 | Anti-ultraviolet skin care composition |
| US8637231B2 (en) | 2004-08-17 | 2014-01-28 | Wake Forest University Health Sciences | Method for increasing the volume of a blood substitute with an expander comprising basic alpha keratose |
| JP2006151940A (en) * | 2004-10-29 | 2006-06-15 | Dainichiseika Color & Chem Mfg Co Ltd | Cell activator |
| WO2007023816A1 (en) | 2005-08-23 | 2007-03-01 | Seiwa Kasei Company, Limited | Method for preparation of reduced keratin, reduced cuticle protein or mixture thereof |
| US11173233B2 (en) | 2005-10-21 | 2021-11-16 | Wake Forest University Health Sciences | Keratin bioceramic compositions |
| US8920827B2 (en) | 2005-10-21 | 2014-12-30 | Wake Forest University Health Sciences | Keratin bioceramic compositions |
| US8968764B2 (en) | 2006-02-10 | 2015-03-03 | Wake Forest University Health Sciences | Nerve regeneration employing keratin biomaterials |
| US9968706B2 (en) | 2006-02-10 | 2018-05-15 | Wake Forest University Health Sciences | Nerve regeneration employing keratin biomaterials |
| US8258093B2 (en) | 2006-02-17 | 2012-09-04 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
| US9149566B2 (en) | 2006-02-17 | 2015-10-06 | Wake Forest University Health Sciences | Coatings and biomedical implants formed from keratin biomaterials |
| US8299013B2 (en) | 2006-02-17 | 2012-10-30 | Wake Forest University Health Sciences | Clotting and healing compositions containing keratin biomaterials |
| US10821211B2 (en) | 2006-02-17 | 2020-11-03 | Wake Forest University Health Sciences | Coatings and biomedical implants formed from keratin biomaterials |
| US8273702B2 (en) | 2006-02-17 | 2012-09-25 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
| US9068162B2 (en) | 2007-08-17 | 2015-06-30 | Wake Forest University Health Sciences | Keratin biomaterials for cell culture and methods of use |
| US9045600B2 (en) | 2009-05-13 | 2015-06-02 | Keraplast Technologies, Ltd. | Biopolymer materials |
| US10434213B2 (en) | 2010-03-05 | 2019-10-08 | Wake Forest University Health Sciences | Controlled delivery system |
| US9220754B2 (en) | 2010-11-17 | 2015-12-29 | Wake Forest University Health Sciences | Keratin compositions for treatment of bone deficiency or injury |
| EP3701802A1 (en) | 2019-02-28 | 2020-09-02 | Bretagne Chimie Fine | Composition with high free amino acid content and use as raw material and complete food for animal nutrition |
| FR3093275A1 (en) * | 2019-02-28 | 2020-09-04 | Bretagne Chimie Fine | Composition with high contents of free amino acids and use as raw material and complete feed for animal feed. |
| US11678680B2 (en) | 2019-02-28 | 2023-06-20 | Bretagne Chimie Fine | Composition with high free amino acid contents and use as a starting material and complete feed for animal feed |
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