JPH0229092B2 - SS * BEETAAHIDOROKISHIIGANMAATORIMECHIRUANMONIOPUROPIRU * KERATEIN - Google Patents
SS * BEETAAHIDOROKISHIIGANMAATORIMECHIRUANMONIOPUROPIRU * KERATEINInfo
- Publication number
- JPH0229092B2 JPH0229092B2 JP9825580A JP9825580A JPH0229092B2 JP H0229092 B2 JPH0229092 B2 JP H0229092B2 JP 9825580 A JP9825580 A JP 9825580A JP 9825580 A JP9825580 A JP 9825580A JP H0229092 B2 JPH0229092 B2 JP H0229092B2
- Authority
- JP
- Japan
- Prior art keywords
- keratein
- trimethylammoniopropyl
- hydroxy
- reaction
- keratin
- 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.)
- Expired - Lifetime
Links
- 229910052736 halogen Inorganic materials 0.000 claims description 3
- 125000005843 halogen group Chemical group 0.000 claims description 3
- 102000011782 Keratins Human genes 0.000 description 10
- 108010076876 Keratins Proteins 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- 238000006722 reduction reaction Methods 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 7
- 229940024606 amino acid Drugs 0.000 description 7
- 150000001413 amino acids Chemical class 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 125000003396 thiol group Chemical group [H]S* 0.000 description 6
- 210000002268 wool Anatomy 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 5
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 239000003638 chemical reducing agent Substances 0.000 description 4
- 229960003067 cystine Drugs 0.000 description 4
- 239000012046 mixed solvent Substances 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 4
- PUVAFTRIIUSGLK-UHFFFAOYSA-M trimethyl(oxiran-2-ylmethyl)azanium;chloride Chemical compound [Cl-].C[N+](C)(C)CC1CO1 PUVAFTRIIUSGLK-UHFFFAOYSA-M 0.000 description 4
- ZWEHNKRNPOVVGH-UHFFFAOYSA-N 2-Butanone Chemical compound CCC(C)=O ZWEHNKRNPOVVGH-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
- 238000007259 addition reaction Methods 0.000 description 3
- -1 for example Substances 0.000 description 3
- 210000004209 hair Anatomy 0.000 description 3
- 239000012535 impurity Substances 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108010038807 Oligopeptides Proteins 0.000 description 2
- 102000015636 Oligopeptides Human genes 0.000 description 2
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 210000003746 feather Anatomy 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 239000012429 reaction media Substances 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
- TUQOTMZNTHZOKS-UHFFFAOYSA-N tributylphosphine Chemical compound CCCCP(CCCC)CCCC TUQOTMZNTHZOKS-UHFFFAOYSA-N 0.000 description 2
- RIOQSEWOXXDEQQ-UHFFFAOYSA-N triphenylphosphine Chemical compound C1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1 RIOQSEWOXXDEQQ-UHFFFAOYSA-N 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 101800004419 Cleaved form Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 206010020649 Hyperkeratosis Diseases 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- GNOIPBMMFNIUFM-UHFFFAOYSA-N hexamethylphosphoric triamide Chemical compound CN(C)P(=O)(N(C)C)N(C)C GNOIPBMMFNIUFM-UHFFFAOYSA-N 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 210000003284 horn Anatomy 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000006011 modification reaction Methods 0.000 description 1
- 210000000282 nail Anatomy 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000002798 polar solvent Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- 235000010265 sodium sulphite Nutrition 0.000 description 1
- 125000000542 sulfonic acid group Chemical group 0.000 description 1
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
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- 239000004474 valine Substances 0.000 description 1
Description
本発明は一般式〔〕で表わされるＳ−（β−
ヒドロキシ−γ−トリメチルアンモニオプロピ
ル）ケラテインに関する。
（式中、Kerは分子量１万〜10万のケラテイン主
鎖を示し、Ｘはハロゲンを示す。）
ケラテインとは、ケラチン中のジスルフイド結
合（−Ｓ−Ｓ−）を還元によりスルフヒドリル基
（−SH）に開裂した形をいう。ケラチンとは、高
等動物の表皮に分布し、生体保護の機能を行なう
繊維状蛋白質の総称であり、例えば羊毛、羽毛、
毛髪、爪、角などである。ケラチンを構成するア
ミノ酸は18種類（アラリン、アルギニン、アスパ
ラギン酸、シスチン、グルタミン酸、グリシン、
ヒスチヂン、イソロイシン、ロイシン、リジン、
メチオニン、フエニルアラニン、プロリン、セリ
ン、スレオニン、トリプトフアン、チロシン、バ
リン）であり、その特徴はシスチン含量が多く、
平均で10〜20アミノ酸残基当り一つのジスルフイ
ド結合（−Ｓ−Ｓ−）が存在し、架橋構造をとつ
ている点である。
ケラチンを工業的に利用しようとする場合何ら
かの溶媒、例えば水などに溶解させる事がまず必
要となるが、その為には架橋ジスルフイド結合を
開裂しなければならない。開裂の方法としては還
元及び酸化があり、還元によつてジスルフイド結
合はスルフヒドリル基（−SH）となり生成物は
ケラテイン（Ker−SH）と呼ばれる。一方、酸
化によつてはジスルフイド結合はスルホン酸基
（−SO3H）となり、生成物はケラトーズ（Ker−
SO3H）と呼ばれる。このようにして得られる直
鎖状蛋白質は本質的には水に可溶性の筈である
が、蛋白質同志の水素結合、イオン結合、疎水結
合などの為に水や有機極性溶媒に対して難溶性で
あり、溶解したとしても極めて希薄な溶液しか得
られない。
本発明者は鋭意検討した結果、ケラテイン中の
スルフヒドリル基をＳ−β−ヒドロキシ−γ−ト
リメチルアンモニオプロピル基
The present invention relates to S-(β-
Hydroxy-γ-trimethylammoniopropyl)keratein. (In the formula, Ker represents a keratein main chain with a molecular weight of 10,000 to 100,000, and X represents a halogen.) Keratein is a keratein that has a sulfhydryl group (-SH ) is the cleaved form. Keratin is a general term for fibrous proteins that are distributed in the epidermis of higher animals and perform biological protection functions, such as wool, feathers,
Hair, nails, horns, etc. There are 18 amino acids that make up keratin (ararin, arginine, aspartic acid, cystine, glutamic acid, glycine,
histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, valine), and its characteristics include a high cystine content,
On average, there is one disulfide bond (-S-S-) per 10 to 20 amino acid residues, forming a cross-linked structure. In order to use keratin industrially, it is first necessary to dissolve it in some kind of solvent, such as water, and to do so, the crosslinked disulfide bonds must be cleaved. Methods of cleavage include reduction and oxidation, and upon reduction, the disulfide bond becomes a sulfhydryl group (-SH) and the product is called keratein (Ker-SH). On the other hand, by oxidation, the disulfide bond becomes a sulfonic acid group (-SO 3 H), and the product is keratose (Ker-
SO 3 H). The linear protein obtained in this way should essentially be soluble in water, but it is poorly soluble in water and organic polar solvents due to hydrogen bonds, ionic bonds, hydrophobic bonds, etc. between proteins. Even if it is dissolved, only an extremely dilute solution can be obtained. As a result of extensive studies, the present inventors found that the sulfhydryl group in keratein was replaced by an S-β-hydroxy-γ-trimethylammoniopropyl group.
【式】に変え
る事により、水及び水と親水性有機溶媒との混合
溶媒に易溶性のケラテイン誘導体が得られる事を
見い出し、本発明に到達した。
即ち本発明は一般式
（式中、Kerは分子量１万〜10万のケラテイン主
鎖を示し、Ｘはハロゲンを示す。）で表わされる
Ｓ−（β−ヒドロキシ−γ−トリメチルアンモニ
オプロピル）ケラテインを提供するものである。
なお、本発明でいうケラテインとは、ケラチン
を加水分解して得られる、一般に分子量が数千以
下のオリゴペプチドではなく、ケラチンのジスル
フイド結合が開裂した分子量１万〜10万のものを
いい、通常のケラチンから得られるものは２万〜
５万のものが多い。
Ｓ−（β−ヒドロキシ−γ−トリメチルアンモ
ニオプロピル）ケラテインは、例えば次の機構に
よる方法でつくられる。
原料であるケラチンは天然の羊毛、羽毛、毛髪
などを洗浄し、挟雑物を除去したものがそのまま
使用される。
第１段階のケラチンの還元反応は、従来公知の
方法により行なえる。即ち溶媒として水或いは水
と親水性有機溶媒との混合溶媒を用いる。そのよ
うな親水性有機溶媒としては、例えばメタノー
ル、エタノール、ｎ−プロパノール、アセトン、
メチルエチルケトン、ジオキサン、テトラヒドロ
フラン、ジメチルホルムアミド、ジメチルスルホ
キシド、ヘキサメチルホスホリツクトリアミドな
どが挙げられる。また還元剤としては、例えば２
−メルカプトエタノール、チオグリコール酸、ト
リｎ−ブチルホスフイン、トリフエニルホスフイ
ン、アスコルビン酸、亜硫酸水素ナトリウム、亜
硫酸ナトリウムなどが用いられる。反応温度は通
常室温で充分であるが、必要に応じて加熱し還元
時間を短縮することが出来る。反応時間について
は普通２〜３時間或いはそれ以上を要する。さら
に反応系のPHであるが、一般には６〜11の範囲で
還元反応を行なう。
次に第２段階のケラテインの変性反応である
が、ケラテインに付加させる試薬としては例えば
式(2)中に示した様なグリシジルトリメチルアンモ
ニウムクロリドがある。付加反応は還元反応終了
後還元反応媒体中へ還元により生成したスルフヒ
ドリル基と当量のグリシジルトリメチルアンモニ
ウムクロリドを添加する事により行なわれる。反
応温度は室温から90℃迄任意の温度を選べるが、
高温にする程付加反応は促進される。付加反応が
進むにつれ、Ｓ−（β−ヒドロキシ−γ−トリメ
チルアンモニオプロピル）ケラテインが反応媒体
中に溶出し、最終的な不溶部は原料のケラチンに
対して30％以下になる。不溶部を過、遠心分離
などの手段により除き、Ｓ−（β−ヒドロキシ−
γ−トリメチルアンモニオプロピル）ケラテイン
の溶液を得る。
このようにして得られるＳ−（β−ヒドロキシ
−γ−トリメチルアンモニオプロピル）ケラテイ
ンの溶液は限外過法や透析法などにより、還元
剤などの低分子不純物を除き、そのまま溶液とし
て用いる事も出来るが、凍結乾燥法などによりＳ
−（β−ヒドロキシ−γ−トリメチルアンモニオ
プロピル）ケラテインを固体として回収する方が
利用する上でも、また保存輸送などの面でも便利
である。
本発明のＳ−（β−ヒドロキシ−γ−トリメチ
ルアンモニオプロピル）ケラテインは高分子量で
あるにもかかわらず、水及び水と親水性有機溶媒
との混合溶媒に対する溶解性が極めて優れてい
る。そして、それら溶媒から均一透明なフイルム
が製膜でき、この性質を利用して、例えば水とエ
タノールとの混合溶媒に溶解し毛髪用のセツトロ
ーシヨンなどとして用いる事ができる。
次に実施例により本発明を更に詳細に説明す
る。
実施例
羊毛繊維10ｇを0.02Mのトリス緩衝剤を加えた
50％ｎ−プロパノール水溶液700ｇに浸漬し、還
元剤として４mlのトリ−ｎ−ブチルホスフインを
加えた後、1Nの塩酸でPH8.0に調整し、窒素気流
下、室温で24時間還元反応を行なう。次に反応系
にグリシジルトリメチルアンモニウムクロリド
1.5ｇを加え、70℃で５時間攪拌を行なうと、羊
毛繊維の約85％が反応液中に可溶化する。不溶部
を過により除き、得られた液を限外過（分
画分子量1000の膜を使用）にかけ、還元剤などの
低分子不純物を除くと共に、全系を約150mlに濃
縮した。これを凍結乾燥する事により8.1ｇの粉
末固体を得た。得られた粉末固体の分子量をゲル
過法（セフアデツクスＧ−75を使用）により求
めたところ39000であつた。また該粉末固体を6N
塩酸中、110℃で24時間加水分解をし、分解物の
アミノ酸分析（Hitachi Automatic Amino
Acid Analyser Type KLA−５を使用）を行な
い、原料羊毛のアミノ酸分析結果と比較したとこ
ろ表−１に示すようにシスチン以外のアミノ酸組
成及び含量は両者で殆んど同一であるが、シスチ
ンに関しては羊毛には100モルのアミノ酸中5.5モ
ルのシスチンが認められるが、該粉末固体には全
く認められず、グリシジルトリメチルアンモニウ
ムクロリドの付加を受けた事を示している。従つ
て得られた粉末固体はその分子量及びアミノ酸分
析結果よりケラチン蛋白質の主鎖ペプチド結合に
は加水分解などの変化を受けていず、ジスルフイ
ド結合が開裂し、β−ヒドロキシ−γ−トリメチ
ルアンモニオプロピル基が付加したもの、即ちＳ
−（β−ヒドロキシ−γ−トリメチルアンモニオ
プロピル）ケラテインである事がわかる。It was discovered that a keratein derivative that is easily soluble in water and a mixed solvent of water and a hydrophilic organic solvent can be obtained by changing the formula to [Formula], and the present invention was achieved based on this finding. That is, the present invention is based on the general formula (In the formula, Ker represents a keratein main chain with a molecular weight of 10,000 to 100,000, and X represents a halogen.) . Note that keratein in the present invention does not refer to oligopeptides obtained by hydrolyzing keratin, which generally have a molecular weight of several thousand or less, but refers to oligopeptides with a molecular weight of 10,000 to 100,000 obtained by cleavage of the disulfide bonds of keratin, and usually The amount obtained from keratin is 20,000~
Many are priced at 50,000. S-(β-hydroxy-γ-trimethylammoniopropyl)keratein is produced, for example, by the following mechanism. The raw material, keratin, is made from natural wool, feathers, hair, etc., which has been washed to remove impurities and then used as is. The first step of the keratin reduction reaction can be carried out by a conventionally known method. That is, water or a mixed solvent of water and a hydrophilic organic solvent is used as the solvent. Examples of such hydrophilic organic solvents include methanol, ethanol, n-propanol, acetone,
Examples include methyl ethyl ketone, dioxane, tetrahydrofuran, dimethylformamide, dimethyl sulfoxide, and hexamethylphosphoric triamide. In addition, as a reducing agent, for example, 2
-Mercaptoethanol, thioglycolic acid, tri-n-butylphosphine, triphenylphosphine, ascorbic acid, sodium bisulfite, sodium sulfite, etc. are used. Although room temperature is usually sufficient for the reaction temperature, the reduction time can be shortened by heating if necessary. The reaction time usually takes 2 to 3 hours or more. Furthermore, regarding the pH of the reaction system, the reduction reaction is generally carried out within the range of 6 to 11. Next, in the second step of the keratein modification reaction, the reagent added to keratein includes, for example, glycidyltrimethylammonium chloride as shown in formula (2). The addition reaction is carried out by adding glycidyltrimethylammonium chloride in an amount equivalent to the sulfhydryl group produced by the reduction to the reduction reaction medium after the completion of the reduction reaction. Any reaction temperature can be selected from room temperature to 90℃, but
The addition reaction is accelerated as the temperature increases. As the addition reaction progresses, S-(β-hydroxy-γ-trimethylammoniopropyl)keratein dissolves into the reaction medium, and the final insoluble portion becomes 30% or less based on the starting keratin. The insoluble portion is removed by means such as filtration or centrifugation, and S-(β-hydroxy-
A solution of γ-trimethylammoniopropyl)keratein is obtained. The solution of S-(β-hydroxy-γ-trimethylammoniopropyl)keratein thus obtained can be used as a solution after removing low-molecular impurities such as reducing agents by ultrafiltration or dialysis. It is possible, but S
-(β-Hydroxy-γ-trimethylammoniopropyl)keratein is more convenient to collect as a solid in terms of utilization and storage and transportation. Although the S-(β-hydroxy-γ-trimethylammoniopropyl)keratein of the present invention has a high molecular weight, it has extremely excellent solubility in water and a mixed solvent of water and a hydrophilic organic solvent. A uniform transparent film can be formed from these solvents, and by utilizing this property, it can be dissolved in a mixed solvent of water and ethanol and used as a setting lotion for hair. Next, the present invention will be explained in more detail with reference to Examples. Example 10g of wool fiber added with 0.02M Tris buffer
After immersing in 700 g of 50% n-propanol aqueous solution and adding 4 ml of tri-n-butylphosphine as a reducing agent, the pH was adjusted to 8.0 with 1N hydrochloric acid, and the reduction reaction was carried out at room temperature for 24 hours under a nitrogen stream. Let's do it. Next, add glycidyltrimethylammonium chloride to the reaction system.
When 1.5 g is added and stirred at 70°C for 5 hours, about 85% of the wool fibers are solubilized in the reaction solution. Insoluble portions were removed by filtration, and the resulting solution was subjected to ultrafiltration (using a membrane with a molecular weight cutoff of 1000) to remove low-molecular impurities such as reducing agents, and the entire system was concentrated to about 150 ml. By freeze-drying this, 8.1 g of solid powder was obtained. The molecular weight of the obtained powder solid was determined to be 39,000 by gel filtration method (using Sephadex G-75). In addition, the powder solid is 6N
Hydrolysis was carried out in hydrochloric acid at 110℃ for 24 hours, and amino acid analysis of the decomposed product (Hitachi Automatic Amino
Acid Analyzer Type KLA-5) was used to compare the amino acid analysis results of raw wool, and as shown in Table 1, the composition and content of amino acids other than cystine were almost the same. Although 5.5 moles of cystine in 100 moles of amino acids are found in the wool, none was found in the powdered solid, indicating that glycidyltrimethylammonium chloride was added thereto. Therefore, the molecular weight and amino acid analysis results of the obtained solid powder show that the main chain peptide bonds of the keratin protein have not undergone any changes such as hydrolysis, and the disulfide bonds have been cleaved to form β-hydroxy-γ-trimethylammoniopropyl. A group is added, that is, S
-(β-hydroxy-γ-trimethylammoniopropyl)keratein.
Claims (1)
シ−γ−トリメチルアンモニオプロピル）ケラテ
イン。 （式中、Kerは分子量１万〜10万のケラテイン主
鎖を示し、Ｘはハロゲンを示す。）[Claims] 1 S-(β-hydroxy-γ-trimethylammoniopropyl)keratein represented by the general formula []. (In the formula, Ker represents a keratein main chain with a molecular weight of 10,000 to 100,000, and X represents a halogen.)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9825580A JPH0229092B2 (en) | 1980-07-18 | 1980-07-18 | SS * BEETAAHIDOROKISHIIGANMAATORIMECHIRUANMONIOPUROPIRU * KERATEIN |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9825580A JPH0229092B2 (en) | 1980-07-18 | 1980-07-18 | SS * BEETAAHIDOROKISHIIGANMAATORIMECHIRUANMONIOPUROPIRU * KERATEIN |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS5723630A JPS5723630A (en) | 1982-02-06 |
| JPH0229092B2 true JPH0229092B2 (en) | 1990-06-27 |
Family
ID=14214843
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9825580A Expired - Lifetime JPH0229092B2 (en) | 1980-07-18 | 1980-07-18 | SS * BEETAAHIDOROKISHIIGANMAATORIMECHIRUANMONIOPUROPIRU * KERATEIN |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0229092B2 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2609997B2 (en) * | 1994-06-02 | 1997-05-14 | 合同インキ株式会社 | Filling and packaging method and apparatus for printing ink and container for filling and packaging |
| JP2017008436A (en) * | 2015-06-19 | 2017-01-12 | 日本毛織株式会社 | Moisture absorptive heat generating feather product and manufacturing method therefor |
-
1980
- 1980-07-18 JP JP9825580A patent/JPH0229092B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPS5723630A (en) | 1982-02-06 |
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