JPS6257319B2 - - Google Patents

Info

Publication number: JPS6257319B2
Authority: JP; Japan
Prior art keywords: keratin; oligokeratin; reduction; reaction; acid
Prior art date: 1980-12-26
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

Application number

JP18719080A

Other languages

English (en)

Japanese (ja)

Other versions

JPS57109797A (en

Inventor

Takeaki Myamoto

Rikio Tsushima

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Kao Corp

Original Assignee

Kao Corp

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1980-12-26

Filing date

1980-12-26

Publication date

1987-11-30

1980-12-26 Application filed by Kao Corp filed Critical Kao Corp

1980-12-26 Priority to JP18719080A priority Critical patent/JPS57109797A/ja

1982-07-08 Publication of JPS57109797A publication Critical patent/JPS57109797A/ja

1987-11-30 Publication of JPS6257319B2 publication Critical patent/JPS6257319B2/ja

Status Granted legal-status Critical Current

Links

102000011782 Keratins Human genes 0.000 claims description 46
108010076876 Keratins Proteins 0.000 claims description 46
239000000463 material Substances 0.000 claims description 32
238000006722 reduction reaction Methods 0.000 claims description 26
239000002994 raw material Substances 0.000 claims description 14
238000006460 hydrolysis reaction Methods 0.000 claims description 9
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
230000003301 hydrolyzing effect Effects 0.000 claims description 5
239000012429 reaction media Substances 0.000 claims description 5
238000004519 manufacturing process Methods 0.000 claims description 3
230000009467 reduction Effects 0.000 description 15
102000004190 Enzymes Human genes 0.000 description 14
108090000790 Enzymes Proteins 0.000 description 14
229940088598 enzyme Drugs 0.000 description 14
238000000034 method Methods 0.000 description 14
239000003638 chemical reducing agent Substances 0.000 description 13
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 12
239000002609 medium Substances 0.000 description 11
210000002268 wool Anatomy 0.000 description 11
239000007864 aqueous solution Substances 0.000 description 10
BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 10
102000004157 Hydrolases Human genes 0.000 description 9
108090000604 Hydrolases Proteins 0.000 description 9
239000007788 liquid Substances 0.000 description 8
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 7
102000057297 Pepsin A Human genes 0.000 description 7
108090000284 Pepsin A Proteins 0.000 description 7
229940111202 pepsin Drugs 0.000 description 7
239000000843 powder Substances 0.000 description 7
238000000926 separation method Methods 0.000 description 7
238000005063 solubilization Methods 0.000 description 7
230000007928 solubilization Effects 0.000 description 7
239000000126 substance Substances 0.000 description 7
150000003573 thiols Chemical group 0.000 description 6
239000002253 acid Substances 0.000 description 5
239000002537 cosmetic Substances 0.000 description 5
238000006047 enzymatic hydrolysis reaction Methods 0.000 description 5
210000004209 hair Anatomy 0.000 description 5
102000004169 proteins and genes Human genes 0.000 description 5
108090000623 proteins and genes Proteins 0.000 description 5
230000002378 acidificating effect Effects 0.000 description 4
239000002585 base Substances 0.000 description 4
230000007071 enzymatic hydrolysis Effects 0.000 description 4
239000000835 fiber Substances 0.000 description 4
238000001914 filtration Methods 0.000 description 4
239000002904 solvent Substances 0.000 description 4
CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 4
TUQOTMZNTHZOKS-UHFFFAOYSA-N tributylphosphine Chemical compound CCCCP(CCCC)CCCC TUQOTMZNTHZOKS-UHFFFAOYSA-N 0.000 description 4
238000005406 washing Methods 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
102000015636 Oligopeptides Human genes 0.000 description 3
108010038807 Oligopeptides Proteins 0.000 description 3
108010059712 Pronase Proteins 0.000 description 3
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 3
239000003513 alkali Substances 0.000 description 3
239000004202 carbamide Substances 0.000 description 3
238000000502 dialysis Methods 0.000 description 3
239000002612 dispersion medium Substances 0.000 description 3
210000003746 feather Anatomy 0.000 description 3
230000007062 hydrolysis Effects 0.000 description 3
-1 phosphorus compound Chemical class 0.000 description 3
238000011084 recovery Methods 0.000 description 3
238000000108 ultra-filtration Methods 0.000 description 3
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 3
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
108090000526 Papain Proteins 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
239000004365 Protease Substances 0.000 description 2
DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 2
QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
108090000631 Trypsin Proteins 0.000 description 2
102000004142 Trypsin Human genes 0.000 description 2
241000251539 Vertebrata <Metazoa> Species 0.000 description 2
150000001298 alcohols Chemical class 0.000 description 2
125000003277 amino group Chemical group 0.000 description 2
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
239000007810 chemical reaction solvent Substances 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
238000003776 cleavage reaction Methods 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
238000000354 decomposition reaction Methods 0.000 description 2
XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
230000000694 effects Effects 0.000 description 2
239000011261 inert gas Substances 0.000 description 2
239000000203 mixture Substances 0.000 description 2
230000007935 neutral effect Effects 0.000 description 2
229940055729 papain Drugs 0.000 description 2
235000019834 papain Nutrition 0.000 description 2
229910052698 phosphorus Inorganic materials 0.000 description 2
239000011574 phosphorus Substances 0.000 description 2
229920001184 polypeptide Polymers 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
108090000765 processed proteins & peptides Proteins 0.000 description 2
238000000746 purification Methods 0.000 description 2
230000007017 scission Effects 0.000 description 2
239000000243 solution Substances 0.000 description 2
230000008961 swelling Effects 0.000 description 2
JOXIMZWYDAKGHI-UHFFFAOYSA-N toluene-4-sulfonic acid Chemical compound CC1=CC=C(S(O)(=O)=O)C=C1 JOXIMZWYDAKGHI-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
239000012588 trypsin Substances 0.000 description 2
102000008186 Collagen Human genes 0.000 description 1
108010035532 Collagen Proteins 0.000 description 1
VCUFZILGIRCDQQ-KRWDZBQOSA-N N-[[(5S)-2-oxo-3-(2-oxo-3H-1,3-benzoxazol-6-yl)-1,3-oxazolidin-5-yl]methyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C1O[C@H](CN1C1=CC2=C(NC(O2)=O)C=C1)CNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F VCUFZILGIRCDQQ-KRWDZBQOSA-N 0.000 description 1
GRYLNZFGIOXLOG-UHFFFAOYSA-N Nitric acid Chemical compound O[N+]([O-])=O GRYLNZFGIOXLOG-UHFFFAOYSA-N 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
101710172711 Structural protein Proteins 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
230000009471 action Effects 0.000 description 1
230000001476 alcoholic effect Effects 0.000 description 1
229910000147 aluminium phosphate Inorganic materials 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
239000012736 aqueous medium Substances 0.000 description 1
DLIJPAHLBJIQHE-UHFFFAOYSA-N butylphosphane Chemical compound CCCCP DLIJPAHLBJIQHE-UHFFFAOYSA-N 0.000 description 1
210000000078 claw Anatomy 0.000 description 1
238000004140 cleaning Methods 0.000 description 1
229920001436 collagen Polymers 0.000 description 1
238000005238 degreasing Methods 0.000 description 1
229910001873 dinitrogen Inorganic materials 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
238000000605 extraction Methods 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
125000000524 functional group Chemical group 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
210000000003 hoof Anatomy 0.000 description 1
210000003284 horn Anatomy 0.000 description 1
239000001257 hydrogen Substances 0.000 description 1
229910052739 hydrogen Inorganic materials 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
230000003993 interaction Effects 0.000 description 1
JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
150000007522 mineralic acids Chemical class 0.000 description 1
IHYNKGRWCDKNEG-UHFFFAOYSA-N n-(4-bromophenyl)-2,6-dihydroxybenzamide Chemical compound OC1=CC=CC(O)=C1C(=O)NC1=CC=C(Br)C=C1 IHYNKGRWCDKNEG-UHFFFAOYSA-N 0.000 description 1
239000005445 natural material Substances 0.000 description 1
229910017604 nitric acid Inorganic materials 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
150000007524 organic acids Chemical class 0.000 description 1
150000002898 organic sulfur compounds Chemical class 0.000 description 1
230000003647 oxidation Effects 0.000 description 1
238000007254 oxidation reaction Methods 0.000 description 1
238000010979 pH adjustment Methods 0.000 description 1
ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
150000003018 phosphorus compounds Chemical class 0.000 description 1
239000002798 polar solvent Substances 0.000 description 1
230000008569 process Effects 0.000 description 1
235000019260 propionic acid Nutrition 0.000 description 1
238000000197 pyrolysis Methods 0.000 description 1
IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
230000035484 reaction time Effects 0.000 description 1
238000010992 reflux Methods 0.000 description 1
229940079827 sodium hydrogen sulfite Drugs 0.000 description 1
235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
239000007787 solid Substances 0.000 description 1
239000004753 textile Substances 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1

Landscapes

Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)

JP18719080A 1980-12-26 1980-12-26 Preparation of low-molecular weight keratinous substance Granted JPS57109797A (en)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP18719080A JPS57109797A (en)	1980-12-26	1980-12-26	Preparation of low-molecular weight keratinous substance

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP18719080A JPS57109797A (en)	1980-12-26	1980-12-26	Preparation of low-molecular weight keratinous substance

Publications (2)

Publication Number	Publication Date
JPS57109797A JPS57109797A (en)	1982-07-08
JPS6257319B2 true JPS6257319B2 (it)	1987-11-30

Family

ID=16201675

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP18719080A Granted JPS57109797A (en)	1980-12-26	1980-12-26	Preparation of low-molecular weight keratinous substance

Country Status (1)

Country	Link
JP (1)	JPS57109797A (it)

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPH0311099A (ja) *	1989-06-06	1991-01-18	Seiwa Kasei:Kk	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
US6544548B1 (en)	1999-09-13	2003-04-08	Keraplast Technologies, Ltd.	Keratin-based powders and hydrogel for pharmaceutical applications
JP2005516072A (ja)	2002-01-28	2005-06-02	ケラプラストテクノロジーズ，リミテッド	生物活性ケラチンタンパク質
US7439012B2 (en)	2004-08-17	2008-10-21	Wake Forest University Health Sciences	Ambient stored blood plasma expanders containing keratose
US8920827B2 (en)	2005-10-21	2014-12-30	Wake Forest University Health Sciences	Keratin bioceramic compositions
EP1991253B1 (en)	2006-02-10	2013-07-31	Wake Forest University Health Sciences	Nerve regeneration employing keratin biomaterials
US9149566B2 (en)	2006-02-17	2015-10-06	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
CN102482319B (zh)	2009-05-13	2015-07-29	凯拉普雷斯特技术有限公司	生物聚合物材料
EP2542564B1 (en)	2010-03-05	2018-05-09	Wake Forest University Health Sciences	Controlled delivery system
WO2011112575A1 (en)	2010-03-08	2011-09-15	Wake Forest University Health Sciences	Keratin biomaterials for treatment of ischemia
CA2818166C (en)	2010-11-17	2019-04-30	Wake Forest University Health Sciences	Keratin compositions for treatment of bone deficiency or injury

1980
- 1980-12-26 JP JP18719080A patent/JPS57109797A/ja active Granted

Also Published As

Publication number	Publication date
JPS57109797A (en)	1982-07-08

Publication	Publication Date	Title
EP0628573A1 (en)	1994-12-14	Process for producing solubilized protein
JPS6257319B2 (it)	1987-11-30
EP0052441B1 (en)	1985-08-28	Hair rinse composition
KR100923326B1 (ko)	2009-10-22	케라틴 유도체의 제조방법
JP3094181B2 (ja)	2000-10-03	再生天然ケラチンを壁材とするマイクロカプセル及びその製造方法
US4390525A (en)	1983-06-28	Keratin hydrolyzate useful as hair fixatives
EP0081440B1 (fr)	1986-08-27	Procédé de préparation de formes nouvelles de collagène natif ou déréticulé, à structure hélicoidale préservée, associées à des mucopolysaccharides et leurs applications notamment dans les domaines cosmétologiques, pharmaceutiques, analytiques et autres
JP2004534137A (ja)	2004-11-11	ケラチン系製品およびその製造方法
JP3283302B2 (ja)	2002-05-20	還元ケラチンの製造方法
JPS6160804B2 (it)	1986-12-23
JPH0591893A (ja)	1993-04-16	ケラチンの加水分解方法
JPH06116300A (ja)	1994-04-26	ケラチンフラグメントおよびその製造方法
FR2499412A1 (fr)	1982-08-13	Production de vaccin antivirus
JPS638205B2 (it)	1988-02-22
JP3891509B2 (ja)	2007-03-14	高等動物体毛由来の還元タンパク質またはその水性媒体分散物およびその製造方法
EP0454600A1 (fr)	1991-10-30	Produit à base de kératines modifiées, son procédé de préparation et les applications notamment en médecine humaine ou vétérinaire
JP3094182B2 (ja)	2000-10-03	ケラチンｓ−スルフォ塩を壁構成原料として用いるマイクロカプセル及びその製造方法
JPH07126296A (ja)	1995-05-16	可溶化蛋白質
JPS609531B2 (ja)	1985-03-11	多孔質膜状物の製造方法
JP3891508B2 (ja)	2007-03-14	還元クチクルタンパクまたはその水性媒体分散液およびその製造方法
JPS6027680B2 (ja)	1985-06-29	ケラチン加水分解物の製造方法
CN101087802A (zh)	2007-12-12	从原料中分离角蛋白的方法
JP2009298737A (ja)	2009-12-24	可溶性羽毛ケラチン蛋白質の製造方法
JP2946491B2 (ja)	1999-09-06	ケラチンのミセル水溶液の製造法
FR2643909A1 (fr)	1990-09-07	Composition de base pour la preparation d'une composition cosmetique formant composition capillaire et composition cosmetique formant composition capillaire ainsi preparee, contenant de l'heparine ou de l'heparane sulfate