JPS63105000A - Acylated casein-derived polypeptide of salt thereof - Google Patents
Acylated casein-derived polypeptide of salt thereofInfo
- Publication number
- JPS63105000A JPS63105000A JP25270286A JP25270286A JPS63105000A JP S63105000 A JPS63105000 A JP S63105000A JP 25270286 A JP25270286 A JP 25270286A JP 25270286 A JP25270286 A JP 25270286A JP S63105000 A JPS63105000 A JP S63105000A
- Authority
- JP
- Japan
- Prior art keywords
- casein
- acid
- derived polypeptide
- amino
- salt
- 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
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical class NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 title claims abstract description 141
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 111
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 105
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 105
- 150000003839 salts Chemical class 0.000 title claims abstract description 14
- 239000005018 casein Substances 0.000 claims abstract description 125
- 235000021240 caseins Nutrition 0.000 claims abstract description 123
- 150000001413 amino acids Chemical class 0.000 claims abstract description 24
- 125000000217 alkyl group Chemical group 0.000 claims abstract description 4
- 229910052783 alkali metal Inorganic materials 0.000 claims abstract description 3
- 150000001340 alkali metals Chemical class 0.000 claims abstract description 3
- 125000004432 carbon atom Chemical group C* 0.000 claims description 9
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 claims description 8
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 claims description 7
- 239000011347 resin Substances 0.000 claims description 6
- 229920005989 resin Polymers 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 4
- 125000003342 alkenyl group Chemical group 0.000 claims description 3
- 229910052739 hydrogen Inorganic materials 0.000 claims description 3
- 239000001257 hydrogen Substances 0.000 claims description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 claims description 2
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 claims description 2
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 claims description 2
- 229910052700 potassium Inorganic materials 0.000 claims description 2
- 239000011591 potassium Substances 0.000 claims description 2
- 229910052708 sodium Inorganic materials 0.000 claims description 2
- 239000011734 sodium Substances 0.000 claims description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 claims 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 claims 1
- 239000007864 aqueous solution Substances 0.000 abstract description 35
- 150000004665 fatty acids Chemical class 0.000 abstract description 29
- 235000014113 dietary fatty acids Nutrition 0.000 abstract description 28
- 229930195729 fatty acid Natural products 0.000 abstract description 28
- 239000000194 fatty acid Substances 0.000 abstract description 28
- 238000003756 stirring Methods 0.000 abstract description 14
- RSWGJHLUYNHPMX-UHFFFAOYSA-N 1,4a-dimethyl-7-propan-2-yl-2,3,4,4b,5,6,10,10a-octahydrophenanthrene-1-carboxylic acid Chemical group C12CCC(C(C)C)=CC2=CCC2C1(C)CCCC2(C)C(O)=O RSWGJHLUYNHPMX-UHFFFAOYSA-N 0.000 abstract description 10
- 239000006210 lotion Substances 0.000 abstract description 10
- 239000002453 shampoo Substances 0.000 abstract description 10
- 150000001875 compounds Chemical class 0.000 abstract description 8
- 108091005804 Peptidases Proteins 0.000 abstract description 7
- 239000002537 cosmetic Substances 0.000 abstract description 7
- 102000035195 Peptidases Human genes 0.000 abstract description 6
- 230000001172 regenerating effect Effects 0.000 abstract description 5
- NGNBDVOYPDDBFK-UHFFFAOYSA-N 2-[2,4-di(pentan-2-yl)phenoxy]acetyl chloride Chemical class CCCC(C)C1=CC=C(OCC(Cl)=O)C(C(C)CCC)=C1 NGNBDVOYPDDBFK-UHFFFAOYSA-N 0.000 abstract description 3
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 abstract description 3
- 239000000654 additive Substances 0.000 abstract description 3
- 230000000996 additive effect Effects 0.000 abstract description 3
- 239000004202 carbamide Substances 0.000 abstract description 3
- 239000000470 constituent Substances 0.000 abstract description 3
- 230000002633 protecting effect Effects 0.000 abstract description 3
- ODIGIKRIUKFKHP-UHFFFAOYSA-N (n-propan-2-yloxycarbonylanilino) acetate Chemical compound CC(C)OC(=O)N(OC(C)=O)C1=CC=CC=C1 ODIGIKRIUKFKHP-UHFFFAOYSA-N 0.000 abstract description 2
- 230000007794 irritation Effects 0.000 abstract description 2
- 239000004615 ingredient Substances 0.000 abstract 1
- 239000000463 material Substances 0.000 abstract 1
- 238000002360 preparation method Methods 0.000 abstract 1
- 102000011632 Caseins Human genes 0.000 description 129
- 108010076119 Caseins Proteins 0.000 description 129
- 239000000047 product Substances 0.000 description 54
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 48
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 40
- 239000002994 raw material Substances 0.000 description 34
- 239000000203 mixture Substances 0.000 description 32
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 27
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 26
- 238000006460 hydrolysis reaction Methods 0.000 description 25
- 238000006243 chemical reaction Methods 0.000 description 23
- 239000002253 acid Substances 0.000 description 22
- 235000001014 amino acid Nutrition 0.000 description 22
- 229940024606 amino acid Drugs 0.000 description 22
- 230000007062 hydrolysis Effects 0.000 description 22
- 238000004458 analytical method Methods 0.000 description 21
- 239000000243 solution Substances 0.000 description 21
- 125000003277 amino group Chemical group 0.000 description 20
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 17
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 17
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 16
- 238000000034 method Methods 0.000 description 16
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 16
- 238000004817 gas chromatography Methods 0.000 description 15
- 230000000694 effects Effects 0.000 description 13
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 13
- XDOFQFKRPWOURC-UHFFFAOYSA-N 16-methylheptadecanoic acid Chemical compound CC(C)CCCCCCCCCCCCCCC(O)=O XDOFQFKRPWOURC-UHFFFAOYSA-N 0.000 description 12
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 12
- 235000013162 Cocos nucifera Nutrition 0.000 description 11
- 244000060011 Cocos nucifera Species 0.000 description 11
- 150000004702 methyl esters Chemical class 0.000 description 11
- 235000013336 milk Nutrition 0.000 description 11
- 239000008267 milk Substances 0.000 description 11
- 210000004080 milk Anatomy 0.000 description 11
- 239000003513 alkali Substances 0.000 description 10
- 235000019441 ethanol Nutrition 0.000 description 10
- UXFQFBNBSPQBJW-UHFFFAOYSA-N 2-amino-2-methylpropane-1,3-diol Chemical compound OCC(N)(C)CO UXFQFBNBSPQBJW-UHFFFAOYSA-N 0.000 description 9
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 239000007788 liquid Substances 0.000 description 9
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 8
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical group N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 238000007796 conventional method Methods 0.000 description 7
- 229910001873 dinitrogen Inorganic materials 0.000 description 7
- 238000000605 extraction Methods 0.000 description 7
- -1 jetanolamine Chemical compound 0.000 description 7
- 230000035484 reaction time Effects 0.000 description 7
- FFKZOUIEAHOBHW-UHFFFAOYSA-N N,4-dimethyl-N-nitrosobenzenesulfonamide Chemical compound O=NN(C)S(=O)(=O)C1=CC=C(C)C=C1 FFKZOUIEAHOBHW-UHFFFAOYSA-N 0.000 description 6
- 238000002523 gelfiltration Methods 0.000 description 6
- 238000006386 neutralization reaction Methods 0.000 description 6
- 239000011541 reaction mixture Substances 0.000 description 6
- 239000004094 surface-active agent Substances 0.000 description 6
- 102000008186 Collagen Human genes 0.000 description 5
- 108010035532 Collagen Proteins 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 235000021120 animal protein Nutrition 0.000 description 5
- 229920001436 collagen Polymers 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 150000002169 ethanolamines Chemical class 0.000 description 5
- 239000003676 hair preparation Substances 0.000 description 5
- 235000018102 proteins Nutrition 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 description 4
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 229960002446 octanoic acid Drugs 0.000 description 4
- 239000003921 oil Substances 0.000 description 4
- 239000008213 purified water Substances 0.000 description 4
- 235000021247 β-casein Nutrition 0.000 description 4
- WRIDQFICGBMAFQ-UHFFFAOYSA-N (E)-8-Octadecenoic acid Natural products CCCCCCCCCC=CCCCCCCC(O)=O WRIDQFICGBMAFQ-UHFFFAOYSA-N 0.000 description 3
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 3
- TWJNQYPJQDRXPH-UHFFFAOYSA-N 2-cyanobenzohydrazide Chemical compound NNC(=O)C1=CC=CC=C1C#N TWJNQYPJQDRXPH-UHFFFAOYSA-N 0.000 description 3
- LQJBNNIYVWPHFW-UHFFFAOYSA-N 20:1omega9c fatty acid Natural products CCCCCCCCCCC=CCCCCCCCC(O)=O LQJBNNIYVWPHFW-UHFFFAOYSA-N 0.000 description 3
- QSBYPNXLFMSGKH-UHFFFAOYSA-N 9-Heptadecensaeure Natural products CCCCCCCC=CCCCCCCCC(O)=O QSBYPNXLFMSGKH-UHFFFAOYSA-N 0.000 description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 3
- 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 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 102000011782 Keratins Human genes 0.000 description 3
- 108010076876 Keratins Proteins 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- 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 3
- 102000004407 Lactalbumin Human genes 0.000 description 3
- 108090000942 Lactalbumin Proteins 0.000 description 3
- 102000008192 Lactoglobulins Human genes 0.000 description 3
- 108010060630 Lactoglobulins Proteins 0.000 description 3
- WMFOQBRAJBCJND-UHFFFAOYSA-M Lithium hydroxide Chemical compound [Li+].[OH-] WMFOQBRAJBCJND-UHFFFAOYSA-M 0.000 description 3
- 235000021360 Myristic acid Nutrition 0.000 description 3
- TUNFSRHWOTWDNC-UHFFFAOYSA-N Myristic acid Natural products CCCCCCCCCCCCCC(O)=O TUNFSRHWOTWDNC-UHFFFAOYSA-N 0.000 description 3
- 239000005642 Oleic acid Substances 0.000 description 3
- ZQPPMHVWECSIRJ-UHFFFAOYSA-N Oleic acid Natural products CCCCCCCCC=CCCCCCCCC(O)=O ZQPPMHVWECSIRJ-UHFFFAOYSA-N 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 238000005904 alkaline hydrolysis reaction Methods 0.000 description 3
- 235000009582 asparagine Nutrition 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 235000003704 aspartic acid Nutrition 0.000 description 3
- 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 3
- 238000009833 condensation Methods 0.000 description 3
- 230000005494 condensation Effects 0.000 description 3
- 239000006071 cream Substances 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 239000000706 filtrate Substances 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
- 150000004820 halides Chemical class 0.000 description 3
- QXJSBBXBKPUZAA-UHFFFAOYSA-N isooleic acid Natural products CCCCCCCC=CCCCCCCCCC(O)=O QXJSBBXBKPUZAA-UHFFFAOYSA-N 0.000 description 3
- 239000002075 main ingredient Substances 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 235000014593 oils and fats Nutrition 0.000 description 3
- ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 3
- 239000003755 preservative agent Substances 0.000 description 3
- 230000002335 preservative effect Effects 0.000 description 3
- 239000008257 shaving cream Substances 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- LPWCRLGKYWVLHQ-UHFFFAOYSA-N tetradecanoyl chloride Chemical compound CCCCCCCCCCCCCC(Cl)=O LPWCRLGKYWVLHQ-UHFFFAOYSA-N 0.000 description 3
- 235000015961 tonic Nutrition 0.000 description 3
- 230000001256 tonic effect Effects 0.000 description 3
- 235000021249 α-casein Nutrition 0.000 description 3
- FRPZMMHWLSIFAZ-UHFFFAOYSA-N 10-undecenoic acid Chemical compound OC(=O)CCCCCCCCC=C FRPZMMHWLSIFAZ-UHFFFAOYSA-N 0.000 description 2
- LFDKQJVNMJFNGG-UHFFFAOYSA-N 16-methylheptadecanoyl chloride Chemical compound CC(C)CCCCCCCCCCCCCCC(Cl)=O LFDKQJVNMJFNGG-UHFFFAOYSA-N 0.000 description 2
- SJIWUNNSRFWATG-UHFFFAOYSA-N 4-[2-(2-hydroxyethoxy)ethoxy]-4-oxobutanoic acid Chemical compound OCCOCCOC(=O)CCC(O)=O SJIWUNNSRFWATG-UHFFFAOYSA-N 0.000 description 2
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- 208000001840 Dandruff Diseases 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
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- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
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- 235000021355 Stearic acid Nutrition 0.000 description 2
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- BXWNKGSJHAJOGX-UHFFFAOYSA-N hexadecan-1-ol Chemical compound CCCCCCCCCCCCCCCCO BXWNKGSJHAJOGX-UHFFFAOYSA-N 0.000 description 2
- VKYKSIONXSXAKP-UHFFFAOYSA-N hexamethylenetetramine Chemical compound C1N(C2)CN3CN1CN2C3 VKYKSIONXSXAKP-UHFFFAOYSA-N 0.000 description 2
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- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 210000004400 mucous membrane Anatomy 0.000 description 2
- OQCDKBAXFALNLD-UHFFFAOYSA-N octadecanoic acid Natural products CCCCCCCC(C)CCCCCCCCC(O)=O OQCDKBAXFALNLD-UHFFFAOYSA-N 0.000 description 2
- REEZZSHJLXOIHL-UHFFFAOYSA-N octanoyl chloride Chemical compound CCCCCCCC(Cl)=O REEZZSHJLXOIHL-UHFFFAOYSA-N 0.000 description 2
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- 239000002304 perfume Substances 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
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- BWHMMNNQKKPAPP-UHFFFAOYSA-L potassium carbonate Chemical compound [K+].[K+].[O-]C([O-])=O BWHMMNNQKKPAPP-UHFFFAOYSA-L 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 239000000376 reactant Substances 0.000 description 2
- 229940108461 rennet Drugs 0.000 description 2
- 108010058314 rennet Proteins 0.000 description 2
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- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 159000000000 sodium salts Chemical class 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000008117 stearic acid Substances 0.000 description 2
- KHPCPRHQVVSZAH-UHFFFAOYSA-N trans-cinnamyl beta-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OCC=CC1=CC=CC=C1 KHPCPRHQVVSZAH-UHFFFAOYSA-N 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- 229960002703 undecylenic acid Drugs 0.000 description 2
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
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Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/74—Biological properties of particular ingredients
- A61K2800/75—Anti-irritant
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/02—Preparations for cleaning the hair
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/04—Preparations for permanent waving or straightening the hair
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/06—Preparations for styling the hair, e.g. by temporary shaping or colouring
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/12—Preparations containing hair conditioners
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明はカゼイン誘導ポリペブタイドのアシル化物また
はその塩に関する。DETAILED DESCRIPTION OF THE INVENTION [Industrial Field of Application] The present invention relates to an acylated casein-derived polypeptide or a salt thereof.
（従来の技術〕
コラーゲンやケラチンなどの動物性蛋白質の加水分解物
が頭髪用化粧品に有効であることは、例えば本出廓人の
出願による特公昭５５−３８３５８号公報などにおいて
も報告されている。これはそれらの動物性蛋白質の加水
分解物が毛髪や皮膚と同様の化学構造を有し、そのアミ
ノ基やカルボキシル基によって、あるいは構成アミノ酸
の側鎖の作用によって毛髪に吸着して、毛髪を保護、再
生する作用を有することによるものと考えられる。(Prior Art) The effectiveness of hydrolysates of animal proteins such as collagen and keratin in hair cosmetics has been reported, for example, in Japanese Patent Publication No. 38358/1983 filed by the present distributor. This is because the hydrolysates of these animal proteins have a chemical structure similar to that of hair and skin, and are adsorbed to the hair by their amino and carboxyl groups, or by the action of the side chains of the constituent amino acids. This is thought to be due to its protective and regenerating effects.
しかしながら、上記コラーゲン、ケラチンなどの動物性
蛋白質は、生体である動物を出発原料とする関係上、そ
の供給に限度があり、上記コラーゲン、ケラチン以外に
も使用できる動物性蛋白質を見出しておかねばならない
という問題がある。However, since animal proteins such as collagen and keratin are used as starting materials from living animals, their supply is limited, and it is necessary to find other animal proteins that can be used in addition to collagen and keratin. There is a problem.
また、それら動物性蛋白質の加水分解物は前述のように
毛髪の保護、再生にを用であるが、そのような頭髪用化
粧品への有用性を保持しながら、加水分解物だけでは到
達しえない領域までへの応用を考えていきたいという要
望がある。In addition, as mentioned above, hydrolysates of animal proteins are used to protect and regenerate hair, but while retaining their usefulness in hair cosmetics, hydrolysates alone cannot achieve this goal. There is a desire to consider applications to areas where there are no existing areas.
本発明はカゼインを加水分解することによって得られる
カゼイン誘導ポリペブタイドを高級脂肪酸または樹脂酸
でアシル化して、カゼイン誘導ポリペブタイドの特性を
生かしながら、カゼイン誘導ポリペブタイドにはない界
面活性能を付与し、頭髪用化粧品の添加剤や皮膚用化粧
品の主剤として有用な新規化合物を提供したものである
。The present invention acylates casein-derived polypeptide obtained by hydrolyzing casein with higher fatty acids or resin acids, and while making use of the properties of casein-derived polypeptide, it imparts surfactant ability that casein-derived polypeptide does not have, and is used for hair. The present invention provides a new compound useful as an additive in cosmetics or as a main ingredient in skin cosmetics.
すなわち、本発明は一般式（［）
（式中、Ｒ１は炭素数８〜２０の長鎖アルキル基、炭素
数８〜２０の長鎖アルケニル基または樹脂酸の側鎖であ
り、Ｒ２はカゼイン誘導ポリペブタイドの構成アミノ酸
の側鎖である。ｎは３〜２０の整数であり、Ｍは水素、
ナトリウム、カリウムなどのアルカリ金属、アンモニウ
ムまたはモノエタノールアミン、ジェタノールアミン、
トリエタノールアミン、２−アミノ−２−メチル−１，
３−プロパンジオールなどの有機アルカノールアミンの
オニウムである）
で示されるカゼイン誘導ポリペブタイドのアシル化物ま
たはその塩に関する。That is, the present invention is based on the general formula ([) (wherein R1 is a long-chain alkyl group with 8 to 20 carbon atoms, a long-chain alkenyl group with 8 to 20 carbon atoms, or a side chain of a resin acid, and R2 is a casein-derived It is the side chain of the constituent amino acid of polypeptide. n is an integer from 3 to 20, M is hydrogen,
Alkali metals such as sodium and potassium, ammonium or monoethanolamine, jetanolamine,
triethanolamine, 2-amino-2-methyl-1,
The present invention relates to an acylated casein-derived polypeptide or a salt thereof, which is an onium of an organic alkanolamine such as 3-propanediol.
上記一般式（１）においてその側鎖がＲ２で示されるア
ミノ酸としては、アラニン、グリシン、バリン、ロイシ
ン、イソロイシン、プロリン、フェニルアラニン、チロ
シン、セリン、トレオニン、メチオニン、アルギニン、
ヒスチジン、リシン、アスパラギン酸、アスパラギン、
グルタミン酸、グルタミン、シスチン、トリプトファン
などがあげられる。そして、これらのアミノ酸の組成比
の分析例を示すと第１表のとおりである。なお、第１表
中にはアスパラギン中グルタミンが示されていないが、
これは分析に先だって行われる加水分解時に（常法では
６Ｎ塩酸により完全加水分解される）それぞれアスパラ
ギン酸とグルタミン酸になったからである。つまり、第
１表中のアスパラギン酸やグルタミン酸にはポリペブタ
イド中ではアスパラギンやグルタミンとして存在したも
のも含まれている。また、トリプトファンもカゼイン中
に約１モル％含まれているが、これも分析に先だって行
われる加水分解時に完全に分解されるため、分析結果を
示す第１表にはトリプトファンは示されていない、そし
て、シスチンはアミノ基とカルボキシル基をそれぞれ２
個ずつ有するので、第１表において組成比を示すにあた
ってはハーフシスチンとして表示されている。In the above general formula (1), the amino acids whose side chain is represented by R2 include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine,
histidine, lysine, aspartic acid, asparagine,
Examples include glutamic acid, glutamine, cystine, and tryptophan. Table 1 shows an analysis example of the composition ratio of these amino acids. Although glutamine in asparagine is not shown in Table 1,
This is because they were converted into aspartic acid and glutamic acid, respectively, during hydrolysis (completely hydrolyzed with 6N hydrochloric acid in the conventional method) prior to analysis. That is, aspartic acid and glutamic acid in Table 1 include those that existed as asparagine and glutamine in polypeptide. In addition, tryptophan is also contained in casein at approximately 1 mol%, but this is also completely decomposed during hydrolysis prior to analysis, so tryptophan is not shown in Table 1 showing the analysis results. Cystine has two amino groups and two carboxyl groups each.
Therefore, when showing the composition ratio in Table 1, it is expressed as half cystine.
第 １ 表
このような一般式（１）で示されるカゼイン誘導ポリペ
ブタイドのアシル化物やその塩は、優れた界面活性能を
有し、一般の界面活性剤が使用される用途に対してすべ
て使用可能であるが、通常の合成界面活性剤とは異なり
、天然の高分子化合物から誘導して得られるものである
ため、皮膚や粘膜への刺激がきわめて少なく、作用が非
常に穏やかである。そして皮膚や毛髪と同じペプチド成
分を含むため、皮膚や毛髪に対しても穏やかに作用し、
皮膚や毛髪に損傷を与えることなく優れた洗浄効果を発
揮することができる。さらに上記一般式（１）で示され
る化合物はカゼイン成分と油脂成分から構成されており
、そのカゼイン成分中のアミノ基やカルボキシル基さら
には各種アミノ酸の側鎖の作用によって毛髪に吸着する
ので、毛髪に必要なペプチド成分と油脂分とを同時に供
給することができる。この一般式（Ｔ）で示される化合
物は、優れた界面活性剤を有する上に、ペプチド成分に
由来する皮膚や毛髪の保護と損傷した毛髪を再生する作
用を有し、かつ油脂成分に由来する艶や光沢の付与、く
し通り性の改善などに対して優れた効果を発揮するので
、シャンプー、リンス、スタイリングフオーム、ヘアー
コンディショナー、ヘアーパック、ヘアーリキッド、ヘ
アートニック、パーマネントウェーブ用剤などの各種頭
髪用化粧品に毛髪の保護、コンディショニング、栄養補
給の目的で添加され、そのすぐれた効果を発揮すること
ができる。また皮膚や粘膜への刺激が少なく、カゼイン
は皮膚に対して親和性が良好なことより、油脂分の親和
性もよくなり、作用の強い界面活性剤などによる皮膚の
油脂分のとれすぎを防ぎ、皮膚に潤いを与え、皮膚を保
護し、乾燥を防ぐので、ローション、クレンジングロー
ション、シェービングローション、各種クリームなどの
主剤として有効に利用できる。Table 1 The acylated casein-derived polypeptide shown by the general formula (1) and its salts have excellent surfactant properties and can be used in all applications where general surfactants are used. However, unlike ordinary synthetic surfactants, it is derived from a natural polymer compound, so it causes very little irritation to the skin and mucous membranes, and its action is very mild. Since it contains the same peptide components as the skin and hair, it has a mild effect on the skin and hair.
It can exhibit excellent cleaning effects without damaging the skin or hair. Furthermore, the compound represented by the above general formula (1) is composed of a casein component and an oil and fat component, and is adsorbed to the hair by the action of the amino groups and carboxyl groups in the casein component as well as the side chains of various amino acids. It is possible to simultaneously supply the peptide components and fats and oils necessary for The compound represented by the general formula (T) not only has an excellent surfactant, but also has the effect of protecting the skin and hair derived from the peptide component and regenerating damaged hair, and has the effect of regenerating damaged hair derived from the oil component. It has excellent effects on adding shine and gloss, and improving combability, so it can be used in various hair products such as shampoos, conditioners, styling foams, hair conditioners, hair packs, hair liquids, hair tonics, and permanent waving agents. It is added to hair cosmetics for the purpose of hair protection, conditioning, and nutritional supplementation, and can demonstrate its excellent effects. In addition, it is less irritating to the skin and mucous membranes, and since casein has a good affinity for the skin, it also has a good affinity for oils and fats, preventing excessive removal of oils and fats from the skin due to strong surfactants. Because it moisturizes the skin, protects it, and prevents dryness, it can be effectively used as a main ingredient in lotions, cleansing lotions, shaving lotions, and various creams.
本発明において使用するカゼイン誘導ポリペブタイドは
カゼインを構成する蛋白質を酸、アルカリ、あるいは蛋
白質分解酵素などを用い加水分解することによって得ら
れる。そして加水分解に際して、添加する酸、アルカリ
、あるいは酵素の量、反応温度、反応時間を適宜選択す
ることによって、得られるカゼイン誘導ポリペブタイド
のｎの値を３〜２０すなわち分子量を約３００〜約２．
０００の好ましいものにすることができる。The casein-derived polypeptide used in the present invention can be obtained by hydrolyzing the protein constituting casein using an acid, an alkali, or a protease. During hydrolysis, by appropriately selecting the amount of acid, alkali, or enzyme to be added, reaction temperature, and reaction time, the value of n of the obtained casein-derived polypeptide can be adjusted to 3 to 20, that is, the molecular weight is approximately 300 to approximately 2.
000 preferred.
なお、カゼイン誘導ポリペブタイドを得るためのカゼイ
ンの加水分解の詳細はつぎの通りである。The details of the hydrolysis of casein to obtain casein-derived polypeptide are as follows.
原料となるカゼインとしては、牛乳カゼイン、ヤギ乳カ
ゼイン、人乳カゼインなどがあり、これらはほぼ同様の
特性を有し、いずれも使用可能であるが、工業的に最も
入手しやすいものは牛乳カゼインで、工業的には牛乳カ
ゼインのことを単にカゼインと呼ぶほどである。Raw material casein includes cow's milk casein, goat's milk casein, human milk casein, etc. These have almost the same characteristics and can all be used, but milk casein is the most easily available industrially. So, industrially, milk casein is simply called casein.
そこで、工業的に最も利用しやすい牛乳カゼインについ
て特に詳しく説明すると、牛乳カゼインは、牛乳を遠心
分離して脂肪分を除去する（脂肪分が浮上するのでそれ
を除去する）ことによって得られる脱脂乳を、酸または
レンネット（ｒｅｎｎｅｔ）と呼ばれる凝乳酵素剤で処
理して得られる凝固成分として工業的に得られている０
通常、このカード（ｃｕｒｄ）と呼ばれる凝固成分を乾
燥して粉末化したものが牛乳カゼインとして容易に入手
できる。Therefore, to explain in detail about milk casein, which is the most industrially available, milk casein is obtained from skimmed milk obtained by centrifuging milk to remove the fat content (remove the fat content as it floats to the surface). It is industrially obtained as a coagulating component obtained by treating milk with an acid or a milk-clotting enzyme agent called rennet.
Usually, this coagulated component called curd is dried and powdered and is easily available as milk casein.
このようにして得られる牛乳カゼインは、単一物質では
なく、似かよった蛋白質の混合物で、少な（ともα−カ
ゼイン、β−カゼイン、Ｔ−カゼインの３種の成分から
なるが、これらを総称して通常は「牛乳カゼイン」と呼
んでいる。ただし、これらのα−カゼイン、β−カゼイ
ン、Ｔ−カゼインなどはそれぞれ等電点、リン含量、分
子量などが異なる。牛乳中にはカゼイン（約７８％）の
ほか、ラクトアルブミン（約１０％）、ラクトグロブリ
ン（約３％）などの蛋白質も含まれている。これらラク
トアルブミン、ラクトグロブリンなどは、酸あるいはレ
ンネット処理の際、凝固せずに乳清（ホエー（ｗｈｅｙ
） ）に溶解するので、除去することができるが、カゼ
イン誘導ポリペブタイドを得るに際し、その原料として
、カゼイン中にこれらラクトアルブミン、ラクトグロブ
リンなどのカゼイン以外の蛋白質を含んでいてもさしつ
かえない。Milk casein obtained in this way is not a single substance, but a mixture of similar proteins, consisting of three components (α-casein, β-casein, and T-casein), but these are collectively called However, these α-casein, β-casein, T-casein, etc. each have different isoelectric points, phosphorus content, molecular weight, etc. Casein (approximately 78% %), it also contains proteins such as lactalbumin (approximately 10%) and lactoglobulin (approximately 3%).These lactalbumin and lactoglobulin do not coagulate when treated with acid or rennet. whey
)), so it can be removed, but when obtaining casein-derived polypeptide, casein may contain proteins other than casein, such as lactalbumin and lactoglobulin, as raw materials.
また、牛乳カゼインは、前述したように、少なくともα
−カゼイン、β−カゼイン、γ−カゼインの３種の成分
からなり、通常、これらの３成分が共存した状筋で使用
されるが、等電点の差などを利用してα−カゼイン、β
−カゼイン、γ−カゼインなどに互いに分離精製してか
ら用いてもよい。In addition, milk casein, as mentioned above, has at least α
- It consists of three components: casein, β-casein, and γ-casein. Usually, these three components are used together in a form, but α-casein and β-casein are used by utilizing the difference in isoelectric point.
- Casein, γ-casein, etc. may be used after being separated and purified from each other.
加水分解を行なう際には、粉末状で直ちに加水分解に用
いてもよいが、牛乳カゼインを一旦溶解させて、その溶
液について酸、アルカリ、あるいは酵素によって加水分
解することもできる。その場合、加水分解の進行が早く
かつ穏やかな条件を選択でき、さらに生成物が均一に加
水分解できる特長がある。カゼインを溶解するには、例
えば尿素、塩酸グアニジンなどの高濃度（３０ｆｆｉ量
％以上、なお、以下において濃度などに関して特にモル
％や容量％である旨を表示しない場合は重量％である）
水溶液を用い、必要に応じて４０〜１００ を程度まで
の加熱を行ないつつ、これにカゼインを加え、攪拌しな
がら溶解する方法を採用することができる。このように
して得られるカゼイン液にっいて、必要に応じて希釈し
、加水分解を行うことができる。When performing hydrolysis, milk casein may be used immediately in powder form, but it is also possible to dissolve milk casein once and then hydrolyze the resulting solution with acid, alkali, or enzyme. In this case, it is possible to select conditions under which hydrolysis proceeds quickly and mildly, and the product has the advantage of being able to be hydrolyzed uniformly. In order to dissolve casein, for example, urea, guanidine hydrochloride, etc. must be used at a high concentration (30ffi% by weight or more; below, if the concentration is not specifically indicated as mol% or volume%, it is expressed as weight%).
A method can be adopted in which casein is added to an aqueous solution, heated to about 40 to 100 °C as necessary, and dissolved while stirring. The casein liquid obtained in this way can be diluted and hydrolyzed if necessary.
カゼインの酸加水分解、アルカリ加水分解、酵素加水分
解はつぎに示すようにして行われる。Acid hydrolysis, alkaline hydrolysis and enzymatic hydrolysis of casein are carried out as follows.
ｆｉｌ 酸による加水分解
酸としては、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、ギ酸などの有機酸があげら
れる。また塩酸と酢酸などを混合して用いてもよい、こ
れらは一般に５〜８５％の濃度で使用されるが、加水分
解の反応が常にｐＨ４以下となるようにするのが望まし
い、酸を必要以上に使用すると、加水分解物溶液の色相
が褐色となるので好ましくない。反応温度は、４０〜１
００℃が好ましいが加圧下では１６０℃まで上げること
もできる０反応時間は２〜２４時間が好適である０反応
物は水酸化ナトリウム、水酸化カリウム、炭酸ナトリウ
ムなどのアルカリで中和し、そのまま使用できるが、反
応物または中和物をゲル濾過、イオン交換樹脂、限外濾
過、透析、電気透析などによって精製して使用すること
もできる。Hydrolysis with fil acid Examples of the acid include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid, and organic acids such as acetic acid and formic acid. Hydrochloric acid and acetic acid may also be used as a mixture. These are generally used at a concentration of 5 to 85%, but it is desirable to ensure that the hydrolysis reaction is always at pH 4 or less. If used for this purpose, the hue of the hydrolyzate solution becomes brown, which is not preferable. The reaction temperature is 40-1
00℃ is preferable, but it can be raised to 160℃ under pressure.The reaction time is preferably 2 to 24 hours.The reactants are neutralized with an alkali such as sodium hydroxide, potassium hydroxide, sodium carbonate, etc. However, the reactant or neutralized product can also be purified and used by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.
（２）アルカリによる加水分解
アルカリとしては、水酸化ナトリウム、水酸化カリウム
、水酸化リチウム、水酸化バリウム、炭酸ナトリウム、
炭酸カリウム、炭酸リチウムなどの無機アルカリが使用
される。これらは一般に１〜２０％の濃度が適切である
。アルカリを必要以上に使用すると、加水分解物溶液の
色相が褐色〜黒色となるので好ましくない０反応は、室
温〜１００℃の温度で３０分〜２４時間行なうのが好ま
しく、必要以上に温度を上げすぎたり、反応時間を長く
しないよう注意する必要がある。アルカリによる加水分
解では反応の進行とともにカゼインの加水分解物が溶出
し、反応の進行状況が目に見えるという利点がある０反
応は反応混合物が均一溶液となった時点で終了させれば
よい０反応後、前出の酸で中和するか、あるいはゲル濾
過、イオン交換樹脂、限外濾過、透析、電気透析などに
より精製を行なうのが好ましい。(2) Hydrolysis with alkali Examples of alkali include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate,
Inorganic alkalis such as potassium carbonate and lithium carbonate are used. A concentration of 1 to 20% is generally suitable for these. If more alkali is used than necessary, the hue of the hydrolyzate solution will turn brown to black, so it is preferable to carry out the undesirable 0 reaction at a temperature of room temperature to 100°C for 30 minutes to 24 hours, and avoid raising the temperature more than necessary. Care must be taken not to overdo it or make the reaction time too long. Hydrolysis with an alkali has the advantage that the casein hydrolyzate is eluted as the reaction progresses, and the progress of the reaction can be seen visually.The reaction can be terminated when the reaction mixture becomes a homogeneous solution. Afterwards, it is preferable to neutralize with the above-mentioned acid or purify by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.
（３）酵素による加水分解
酵素としては、ペプシン、プロクターゼＡ１プロクター
ゼＢなどの酸性蛋白質分解酵素、パパイン、プロメライ
ン、サーモライシン、トリプシン、プロナーゼ、キモト
リプシンなどの中性ないしアルカリ性蛋白質分解酵素が
使用される。またスプチリシン、スタフィロコッカスプ
ロテアーゼなどの国産性の中性ないしアルカリ性蛋白質
分解酵素も使用できる。加水分解時のｐＨはペプシンな
どの酸性蛋白質分解酵素の場合にはｐＨ１〜４の範囲、
パパインその他の中性ないしアルカリ性蛋白質分解酵素
の場合には４〜１０の範囲に調整するのが好ましい、ｐ
Ｈは一般に酢酸／酢酸ナトリウム緩衝液、リンｆＨｉｔ
衡液などのＦｉ街液により、あるいは酸、アルカリなど
の添加によって適切に調整するのが好ましい０反応温度
は３０〜４５℃が好ましく、反応時間としては一般に３
〜２４時間が採用される。(3) As the enzymatic hydrolysis enzyme, acidic proteolytic enzymes such as pepsin, protase A1 and protase B, and neutral or alkaline proteolytic enzymes such as papain, promelain, thermolysin, trypsin, pronase, and chymotrypsin are used. Furthermore, domestically produced neutral or alkaline proteolytic enzymes such as subtilisin and staphylococcal protease can also be used. The pH during hydrolysis is in the range of pH 1 to 4 in the case of acidic proteolytic enzymes such as pepsin,
In the case of papain and other neutral or alkaline proteolytic enzymes, it is preferable to adjust the p
H is generally acetic acid/sodium acetate buffer, phosphorus fHit
The reaction temperature is preferably 30 to 45°C, and the reaction time is generally 30°C to 45°C.
~24 hours is taken.
酵素による加水分解反応では、酵素の使用量、反応温度
、反応時間により加水分解物の分子量は太き（影蓼され
る。従って、目的とする分子量のカゼイン加水分解物を
得るためには、酵素使用量、反応温度、反応時間の各条
件について、得られた加水分解物の分子量分布をゲル濾
過法により調べ、経験的に最適条件を決定する必要があ
る。In hydrolysis reactions using enzymes, the molecular weight of the hydrolyzate is influenced by the amount of enzyme used, reaction temperature, and reaction time. Therefore, in order to obtain a casein hydrolyzate with the desired molecular weight, it is necessary to It is necessary to examine the molecular weight distribution of the obtained hydrolyzate using a gel filtration method for each condition of usage amount, reaction temperature, and reaction time, and to determine the optimum conditions empirically.
酵素による加水分解物は、酸、アルカリによる加水分解
物に比較して分子量分布かせま＜、ｉ離のアミノ酸の生
成も少ないので、化粧品配合用としては非常に好適であ
る。Enzymatic hydrolysates produce fewer amino acids with a molecular weight distribution of less than or equal to 1, compared with acid or alkali hydrolysates, and are therefore very suitable for use in cosmetic formulations.
これら加水分解反応によって得られる加水分解物の平均
分子量は、３００以上２．０００以下であることが望ま
しい。カゼイン分解物の毛髪に対する吸着性はその分子
量によって決まり、分子量３００〜１ 、０００程度の
ものが最も吸着しやすく、かつ水に溶けやす（て取扱い
が容易であり、分子量が２，０００を超えるものは毛髪
に対する吸着性が少なくかつ取扱いにくいからである。The average molecular weight of the hydrolyzate obtained by these hydrolysis reactions is preferably 300 or more and 2.000 or less. The adsorption of casein decomposition products to hair is determined by their molecular weight; those with a molecular weight of about 300 to 1,000 are the most adsorbable, and those with a molecular weight of over 2,000 are most easily adsorbed and soluble in water (and easy to handle). This is because they have low adsorption to hair and are difficult to handle.
この３００〜２，０００という分子量範囲は前記一般式
（１）においてｎが３〜２０に相当する。This molecular weight range of 300 to 2,000 corresponds to n of 3 to 20 in the general formula (1).
一方、カゼイン誘導ポリペブタイドをアシル化するため
の成分としては、炭素数８〜２０の長鎖アルキル基また
は炭素数８〜２０の長鎖アルケニル基を有する高級脂肪
酸、あるいは樹脂酸が用いられるが、これらは従来から
石鹸の酸側成分として用いられていたものである。そし
て、樹脂酸としては、通常ロジン系またはトール油系の
ものが用いられる。なお、以下の説明においては、簡略
化のため、これらを樹脂酸も含めて高級脂肪酸または高
級脂肪酸側成分という表現で説明する。On the other hand, as a component for acylating casein-derived polypeptide, higher fatty acids having a long chain alkyl group having 8 to 20 carbon atoms or a long chain alkenyl group having 8 to 20 carbon atoms, or resin acids are used. has traditionally been used as the acid component of soap. As the resin acid, rosin-based or tall oil-based ones are usually used. In the following description, for the sake of simplicity, these components, including resin acids, will be referred to as higher fatty acids or higher fatty acid side components.
そして、前記のようにして得られたカゼイン誘導ポリペ
ブタイドをアシル化するには、カゼイン誘導ポリペブタ
イドと高級脂肪酸とを縮合させればよいが、その最も一
般的な方法としては、ショツテン−バウマン（Ｓｃｈｏ
ｔｔｅｎ−Ｂａｕｍａｎｎ反応）をあげることができる
。In order to acylate the casein-derived polypeptide obtained as described above, it is sufficient to condense the casein-derived polypeptide and a higher fatty acid.
tten-Baumann reaction).
この反応はカゼイン誘導ポリペブタイドの水溶液に、縮
合させる高級脂肪酸の酸クロライド誘導体をｐＨ８〜１
０のアルカリ条件下に攪拌しながら加える反応であり、
この反応によれば次式に示すように、
ＯＲ２
１（Ｉ
Ｒ＋Ｃ−Ｃｌ＋Ｈ−→ＮＨ−ＣＨ−Ｃｏ←ＯＨＯＲ２
１ｌ
−Ｒ１−Ｃ→ＮＨ−ＣＨ−ＣＯ層ＯＨ＋ＨＣ１塩酸が生
成し、ｐＨが低下するので、酸クロライドを加えながら
、水酸化ナトリウＪ・や水酸カリウムなどのアルカリを
加えてｐＨ８〜１０に維持することが必要である。反応
時間は１〜６時間、反応温度は０〜６０℃、好ましくは
２０〜４０℃が採用される。In this reaction, acid chloride derivatives of higher fatty acids to be condensed are added to an aqueous solution of casein-derived polypeptide at a pH of 8 to 1.
It is a reaction that is added while stirring under alkaline conditions of 0.
According to this reaction, as shown in the following formula, OR2 1(I R+C-Cl+H-→NH-CH-Co←OHOR2 1l -R1-C→NH-CH-CO layer OH+HC1 hydrochloric acid is generated and the pH decreases. Therefore, while adding acid chloride, it is necessary to add an alkali such as sodium hydroxide or potassium hydroxide to maintain the pH at 8 to 10.The reaction time is 1 to 6 hours, and the reaction temperature is 0 to 60°C. , preferably 20 to 40°C.
高級脂肪酸側成分としては上記の酸クロライド以外にも
、臭素（Ｂｒ）、沃素（１）などの高級脂肪酸の酸ハラ
イドが使用できる。ただし、酸クロライドが最も一般的
である。As the higher fatty acid side component, in addition to the above-mentioned acid chlorides, acid halides of higher fatty acids such as bromine (Br) and iodine (1) can be used. However, acid chlorides are the most common.
また炭素数８〜２０の汎用されている脂肪酸では、上記
酸ハライドによる方法以外に、１５０〜２００℃の高温
、高圧下、カゼイン誘導ポリペブタイドと高級脂肪酸ま
たはそのメチルエステル、エチルエステルなどの低級ア
ルコールエステルとを処理し脱水縮合または脱アルコー
ル縮合させる方法も採用できるが、高温処理による方・
法であるため生成物が着色し必ずしも好ましいとはいえ
ない。In addition, for commonly used fatty acids having 8 to 20 carbon atoms, in addition to the method using acid halides, casein-derived polypeptides and lower alcohol esters such as higher fatty acids or their methyl esters and ethyl esters can be used at high temperatures of 150 to 200°C and under high pressure. A method of dehydration condensation or dealcolation condensation by treating with
Since it is a method, the product is colored and is not necessarily preferable.
さらにペプチド合成に使用されている試薬を用い、高級
脂肪酸を例えばＮ−オキシコハク酸イミドエステル、Ｎ
−フタルイミドエステルなどカルボキシル基活性誘導体
とした上でカゼイン誘導ポリペブタイドと反応させる方
法も採用できるが、コスト高になる上に、酸ハライドに
よる反応はど反応性は高くない。Furthermore, using reagents used for peptide synthesis, higher fatty acids such as N-oxysuccinimide ester, N-
Although it is possible to use a method in which a carboxyl group-activated derivative such as -phthalimide ester is made and then reacted with casein-derived polypeptide, the cost is high, and the reaction with an acid halide is not very reactive.
いずれにせよ、得られたアシル化物は、好ましくは塩酸
、硫酸などの強酸の水ｆ６液中に放出して遊離物を浮遊
沈澱として採取し、これを水洗して精製したのち、遊離
のまま、あるいは中和して塩のかたちにして、水または
アルコール、プロピレングリコールなどの溶剤に熔かし
て好ましい濃度（１０〜６０％、特に２０〜４０％）の
溶液状にするか、あるいは乾燥して粉末状にして使用に
供される。In any case, the obtained acylated product is preferably released into a water F6 solution containing a strong acid such as hydrochloric acid or sulfuric acid, and the free product is collected as a suspended sediment, which is purified by washing with water. Alternatively, it can be neutralized in the form of a salt, dissolved in water or a solvent such as alcohol or propylene glycol to form a solution at a desired concentration (10-60%, especially 20-40%), or dried. It is used in powder form.
一般式（Ｉ）で示されるカゼイン誘導ポリペブタイドの
アシル化物またはその塩を用いて頭髪用化粧品を調製す
るには、該一般式（１）で示されるカゼイン誘導ポリペ
ブタイドのアシル化物またはその塩を固形分で、シャン
プーの場合０．１〜３０％程度、ヘアーリンスの場合０
．１〜２０％程度、パーマネントウェーブ用第１剤の場
合０．１〜１０％程度配合すればよい。またローション
、各種クリームなどの皮膚用化粧品には該一般式（１）
で示されるカゼイン誘導ポリペブタイドのアシル化物ま
たはその塩を固形分で０，０５〜１０％程度配合すれば
よい。To prepare hair cosmetics using the acylated casein-derived polypeptide represented by the general formula (I) or its salt, the solid content of the acylated casein-derived polypeptide represented by the general formula (1) or its salt is In the case of shampoo, it is about 0.1 to 30%, and in the case of hair conditioner, it is 0.
．． It may be blended in an amount of about 1 to 20%, and in the case of the first agent for permanent waving, about 0.1 to 10%. In addition, the general formula (1) is used for skin cosmetics such as lotions and various creams.
An acylated casein-derived polypeptide represented by the formula or a salt thereof may be blended in an amount of about 0.05 to 10% in terms of solid content.
つぎに参考例（カゼイン誘導ポリペブタイドの製造例）
および実施例をあげて本発明をさらに詳細に説明する。Next, a reference example (manufacturing example of casein-derived polypeptide)
The present invention will be explained in further detail with reference to Examples.
参考例１
３１ビーカに２Ｎ水酸化ナトリウム２．５βを入れ、こ
れに粉末カゼイン５００ｇの一部を加え、８０℃に加熱
し、攪１ｒを行ないつつ、加水分解により粉末カゼイン
を溶解させ、残部の粉末カゼインを追加して加えた。３
０分間で粉末カゼイン全量を投入後、さらに５時間８０
℃に加熱するとともに攪拌し、加水分解を終了した。反
応生成物に水ＩＩ２を加え希釈ののち減圧濾過した。濾
液を弱酸性カチオン交換樹脂アンバーライトＩＲＣ−５
０（商品名、オルガノ （株） ） ３．２００ ｍ
７！の樹脂塔に通液することにより中和したのち、減圧
濃縮し、濾過して、濃度３０％のカゼイン誘導ポリペブ
タイドの水溶液を得た。このようにして得られたカゼイ
ン８１４ポリペブタイド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６００であった。Reference Example 1 31 Put 2.5β of 2N sodium hydroxide in a beaker, add a part of 500g of powdered casein to it, heat it to 80°C, stir for 1r, dissolve the powdered casein by hydrolysis, and dissolve the remaining part. Additional powdered casein was added. 3
After adding the entire amount of powdered casein for 0 minutes, add 80 minutes for another 5 hours.
The mixture was heated to ℃ and stirred to complete hydrolysis. The reaction product was diluted with water II2 and then filtered under reduced pressure. The filtrate was treated with weakly acidic cation exchange resin Amberlite IRC-5.
0 (Product name, Organo Co., Ltd.) 3.200 m
7! After neutralizing the solution by passing it through a resin tower, the solution was concentrated under reduced pressure and filtered to obtain an aqueous solution of casein-derived polypeptide with a concentration of 30%. The molecular weight of the casein 814 polypeptide thus obtained was measured by gel filtration, and the average molecular weight was 600.
参考例２
６ ｍｏｌ／β尿素水溶液１．０ｋｇに５０℃で粉末カ
ゼイン２００ｇを加え、熔解させたのち、この溶液をイ
オン交換水で計２．０ｋｇに希釈した。この液を２１三
ツロフラスコにて８０°Ｃに加熱するとともに攪拌し、
濃塩酸２５ｇを加え、２時間加水分解した。Reference Example 2 200 g of powdered casein was added to 1.0 kg of a 6 mol/β-urea aqueous solution at 50° C., and after melting, the solution was diluted with ion-exchanged water to a total of 2.0 kg. This liquid was heated to 80°C in a 21 Mitsuro flask and stirred.
25 g of concentrated hydrochloric acid was added and hydrolyzed for 2 hours.
冷却後２０％水酸化ナトリウム水溶液４８ｇを加えて中
和したのち、減圧濾過した。濾液に透析を行ない脱塩の
のち減圧濃縮し濾過して濃度３５％のカゼイン誘導ポリ
ペブタイドの水溶液を得た。このようにして得られたカ
ゼイン誘導ポリペブタイド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 、９００であった。After cooling, 48 g of 20% aqueous sodium hydroxide solution was added to neutralize the mixture, and then filtered under reduced pressure. The filtrate was dialyzed and desalted, concentrated under reduced pressure and filtered to obtain an aqueous solution of casein-derived polypeptide with a concentration of 35%. The molecular weight of the casein-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1.900.
参考例３
粉末カゼイン２００ｇを２２ビーカに入れ、０．ＩＮ酢
酸ナトリウム１！を加え、４０℃とし、アルカリ性蛋白
・質分解酵素スブチリシンＢＰＮ’ （長瀬産業（株
））１００ｍｇを加えて４０℃で５時間加水分解を行な
った。加水分解後、反応混合物を濾過し、濾液を減圧濃
縮して濃度３０％のカゼイン誘導ポリペブタイドの水溶
液を得た。このようにして得られたカゼイン誘導ポリペ
ブタイド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１，２００であった。Reference Example 3 200g of powdered casein was placed in a beaker of 0. IN sodium acetate 1! was added, the temperature was raised to 40°C, 100 mg of an alkaline proteolytic enzyme subtilisin BPN' (Nagase Sangyo Co., Ltd.) was added, and hydrolysis was carried out at 40°C for 5 hours. After hydrolysis, the reaction mixture was filtered, and the filtrate was concentrated under reduced pressure to obtain an aqueous solution of casein-derived polypeptide with a concentration of 30%. The molecular weight of the casein-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1,200.
実施例１
参考例１で得られた濃度３０％のカゼイン誘導ポリペブ
タイド水溶液５００ｇに４０℃恒温下攪ｔ’ｔしながら
ミリスチン酸クロライド４９ｇ （カゼイン誘導ポリペ
ブタイドの０．８当量）を２時間かけて滴下した。その
間、２０％水酸化ナトリウム水溶液を適宜滴下して反応
液のｐＨを９．０に維持した。４０℃で１時間攪拌した
のち、温度を４５℃に上げ１時間攪拌して反応を終了し
た。Example 1 49 g of myristic acid chloride (0.8 equivalent of casein-derived polypeptide) was added dropwise to 500 g of the casein-derived polypeptide aqueous solution with a concentration of 30% obtained in Reference Example 1 over 2 hours while stirring at a constant temperature of 40°C. did. During that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 9.0. After stirring at 40°C for 1 hour, the temperature was raised to 45°C and stirred for 1 hour to complete the reaction.
反応混合物を５％硫酸水溶液５７！中に放出し、生成し
たアシル化物を遊離のかたち（ペプタイドのカルボン酸
が塩でない−ＣＯＯＨのかたち）で浮遊させてから、水
洗したのち、３０％水酸化カリウム溶液を加えて中和し
、カゼイン誘導ポリペブタイドとミリスチン酸との縮合
物のカリウム塩の３０％水溶液５７０ｇを得た。収率は
７９％であった。The reaction mixture was diluted with 5% aqueous sulfuric acid solution57! The resulting acylated product is suspended in a free form (the carboxylic acid of the peptide is not a salt - COOH form), washed with water, and neutralized by adding a 30% potassium hydroxide solution to form casein. 570 g of a 30% aqueous solution of the potassium salt of the condensate of derivatized polypeptide and myristic acid was obtained. The yield was 79%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の３０％水溶液について、ファン・スレ
ータ （Ｖａｎ ５ｌａｋｅ ）法によりアミノ態チッ
素をｆｉ１１定したところ、０．０２３ｍ ｇ ／ ｇ
であった。The amino nitrogen content of a 30% aqueous solution of the obtained product was determined using the Van 5lake method and was found to be 0.023 mg/g.
Met.
原料として用いた参考例１で得られたカゼイン誘導ポリ
ペブタイドの３０％水溶液はアミノ態チノ素７．１０４
ｍ ｇ ／ ｇであり、生成物においてほとんどのアミ
ノ基がアシル化されていることが判明した。The 30% aqueous solution of casein-derived polypeptide obtained in Reference Example 1 used as a raw material was 7.104
mg/g, indicating that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チッ素ガス置換後、試験管を封管し、１１０℃
で２４時間加水分解を行った。開封し、減圧濃縮により
塩酸を除去したのち、水とエーテルを加え分液ロートに
て水層とエーテル層に分離し抽出を行った。水層を試料
とし、これのアミノ酸分析を行ったところ、原料として
用いた参考例１で得られたカゼイン誘導ポリペブタイド
とほぼ同じ組成を有していることが判明した。エーテル
層を常法に従ってＮ−メチル−Ｎ−ニトロソ−ｐ−トル
エンスルホンアミドを用いてメチルエステル化を施した
のち、ガスクロマトグラフィーを行ったところ、同様に
処理しメチルエステル化した原料のミスチリン酸のメチ
ルエステルと全く同じものであることが判明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and the temperature was heated to 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 1, which was used as a raw material. The ether layer was methyl esterified using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, and then gas chromatography was performed. It turned out to be exactly the same as the methyl ester of
以上の結果から、生成物は原料として用いた参考例１で
得られたカゼイン誘導ポリペブタイドのアミン基におけ
るミリスチン酸の縮合物のカリウム塩であることが確認
された。アミノ酸分析の結果を第１図に示す。From the above results, it was confirmed that the product was a potassium salt of a condensate of myristic acid in the amine group of the casein-derived polypeptide obtained in Reference Example 1 used as a raw material. The results of amino acid analysis are shown in FIG.
実施例２
実施例１におけるミリスチン酸クロライドに代えてヤシ
脂肪酸（炭素数８〜１８の混合脂肪酸）クロライド５５
ｇ （カゼイン誘導ポリペブタイドの１．０当量）を用
い、水酸化カリウムに代えてトリエタノールアミンを用
いたほかは実施例１と同様にして濃度３０％のカゼイン
誘導ポリペブタイドのヤシ脂肪酸縮合物のトリエタノー
ルアミン塩水７８液７３０ｇを得た。収率は９６％であ
った。Example 2 Coconut fatty acid (mixed fatty acid having 8 to 18 carbon atoms) chloride 55 instead of myristic acid chloride in Example 1
Triethanol of a coconut fatty acid condensate of casein-derived polypeptide at a concentration of 30% was prepared in the same manner as in Example 1, except that g (1.0 equivalent of casein-derived polypeptide) was used and triethanolamine was used in place of potassium hydroxide. 730 g of 78 liquids of amine brine were obtained. The yield was 96%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の３０％水／８液について、ファン・ス
レーク法によりアミノ態チッ素を求めたところ、０．０
１９ｍ ｇ ／ ｇであった。原料として用いた参考例
１で得られたカゼイン誘導ポリペブタイドの３０％水溶
液はアミノ態チノ素７．１０４ｍ ｇ ／ ｇであり、
生成物においてほとんどのアミノ基がアシル化されてい
ることが判明した。Amino nitrogen was determined by the Van Slake method for the 30% water/8 solution of the obtained product, and it was found to be 0.0.
It was 19 mg/g. The 30% aqueous solution of casein-derived polypeptide obtained in Reference Example 1 used as a raw material contained 7.104 mg/g of amino-form chinoline,
It was found that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チッ素ガス五換後、試験管を封管し、１１０℃
で２４時間加水分解を行った。開封し、減圧濃縮により
塩酸を除去したのち、水とエーテルを加え、分液ロート
にて水層とエーテル層に分離し抽出を行った。水層を試
料とし、これのアミノ酸分析を行ったところ、原料とし
て用いた参考ｕ１１１で得られたカゼイン誘導ポリペブ
タイドとほぼ同じ組成を有していることが判明した。エ
ーテル層を常法に従ってＮ−メチル−Ｎ−ニトロソ−ｐ
−）ルエンスルホンアミドを用いてメチルエステル化し
たところ、同様に処理しメチルエステル化した原料のヤ
シ脂肪酸のメチルエステルと全く同じ組成のものである
ことが判明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after five nitrogen gas exchanges, the test tube was sealed and heated at 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and extraction was performed by separating into an aqueous layer and an ether layer using a separating funnel. When the aqueous layer was used as a sample and amino acid analysis was performed on it, it was found that it had almost the same composition as the casein-derived polypeptide obtained from reference u111 used as a raw material. The ether layer was treated with N-methyl-N-nitroso-p according to a conventional method.
-) When methyl esterified using luenesulfonamide, it was found that it had exactly the same composition as the raw material methyl ester of coconut fatty acid which was similarly treated and methyl esterified.
以上の結果から、生成物は原料として用いた参考例１で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
るヤシ脂肪酸（炭素数８〜１８の混合脂肪酸）の縮合物
のトリエタノールアミン塩であることが＠認された。ア
ミノ酸分析の結果を第２表に、ガスクロマトグラフィー
の結果を第２図に示す。From the above results, it is confirmed that the product is a triethanolamine salt of a condensate of coconut fatty acid (mixed fatty acid having 8 to 18 carbon atoms) in the amino group of the casein-derived polypeptide obtained in Reference Example 1 used as a raw material. @It has been certified. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例３
参考例２で得た濃度３５％のカゼイン誘導ポリペブタイ
ド水溶液５００ｇに３０℃恒温度下攪拌しながらカプリ
ル酸クロライド１５ｇ （カゼイン誘導ポリペブタイド
の１．０当量）を２時間かけて滴下した。Example 3 15 g of caprylic acid chloride (1.0 equivalent of casein-derived polypeptide) was added dropwise to 500 g of the 35% casein-derived polypeptide aqueous solution obtained in Reference Example 2 with stirring at a constant temperature of 30° C. over 2 hours.
その間２０％水酸化ナトリウム水／８液を適宜加えて反
応液のｐＨを９に維持した。さらに３０℃で１時間型１
ヤシたのち、温度を４０℃に上げ１時間攪拌を続けて反
応を終了した。During that time, the pH of the reaction solution was maintained at 9 by appropriately adding 20% aqueous sodium hydroxide/8 solution. Further mold 1 at 30℃ for 1 hour
After heating, the temperature was raised to 40°C and stirring was continued for 1 hour to complete the reaction.
反応混合物を５％硫酸水溶液５１中に放出し、生成した
アシル化物を遊離させ、浮遊物を水洗後、モノエタノー
ルアミンを加えて中和し、カゼイン誘導ポリペブタイド
のカプリル酸縮合物モノエタノールアミン塩の３０％水
溶液６０９ｇを得た。収率は９５％であった。The reaction mixture was discharged into a 5% aqueous sulfuric acid solution 51 to liberate the produced acylated product, and after washing the suspended matter with water, it was neutralized by adding monoethanolamine to form the monoethanolamine salt of the caprylic acid condensation product of casein-derived polypeptide. 609 g of a 30% aqueous solution was obtained. The yield was 95%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
１４られた生成物のモノエタノールアミンにより中和す
る前の浮遊物（乾燥残分３７．２０％）について、ファ
ン・スレーク法によりアミノ態チッ素を求めたところ、
０．０４１ｍ ｇ ／ ｇであった。なおモノエタノー
ルアミンによる中和前のものについてアミノ態チッ素の
測定を行ったのは、中和後はモノエタノールアミンのア
ミノ基を測定してしまうためアミノ態チノ素の測定試料
にできないからである。原料として用いた参考例２で得
られたカゼイン誘導ポリペブタイドの３５％水溶液はア
ミノ態チッ素２．５８０ｍ ｇ ／ ｇであり、生成物
においてほとんどのアミノ基がアシル化されていること
が判明した。Amino nitrogen was determined by the Van Slake method for the suspended solids (dry residue 37.20%) before neutralization with monoethanolamine of the 14-produced product.
It was 0.041 mg/g. The reason why amino nitrogen was measured on the sample before neutralization with monoethanolamine was because after neutralization, the amino group of monoethanolamine would be measured, so it could not be used as a measurement sample for amino chinogen. be. The 35% aqueous solution of casein-derived polypeptide obtained in Reference Example 2 used as a raw material had an amino nitrogen content of 2.580 mg/g, and it was found that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チッ素ガス１換後、試験管を封管し、１１０℃
で２４時間加水分解を行った。開封し、減圧濃縮により
塩酸を除去したのち、水とエーテルを加え、分液ロート
にて水層とエーテル層に分離し抽出を行った。水層を試
料とし、これのアミノ酸分析を行ったところ、原料とし
て用いた参考例２で得られたカゼイン誘導ポリペブタイ
ドとほぼ同じ組成を有していることが判明した。エーテ
ル層を常法に従ってＮ−メチル−Ｎ−ニトロソ−ｐ−ト
ルエンスルホンアミドを用いてメチルエステル化を施し
たのち、ガスクロマトグラフィーを行ったところ、同様
に処理しメチルエステル化した原料のカプリル酸のメチ
ルエステルと全く同じものであることが判明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after one exchange of nitrogen gas, the test tube was sealed and heated at 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and extraction was performed by separating into an aqueous layer and an ether layer using a separating funnel. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 2, which was used as a raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, gas chromatography revealed that caprylic acid, a raw material that had been similarly treated and methyl esterified, was detected. It turned out to be exactly the same as the methyl ester of
以上の結果から、生成物は原料として用いた参考例２で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
るカプリル酸の縮合物のモノエタノールアミン塩である
ことが確認された。アミノ酸分析の結果を第２表に、ガ
スクロマトグラフィーの結果を第３図に示す。From the above results, it was confirmed that the product was a monoethanolamine salt of a condensate of caprylic acid at the amino group of the casein-derived polypeptide obtained in Reference Example 2 used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例４
参考例３におけるカプリル酸クロライドに代えてウンデ
シレン酸クロライド１６．８ｇ （カゼイン誘導ポリ
ペブタイドの０．ｇ当量）を用い、モノエタノールアミ
ンに代えて水酸化カリウムを用いたほかは実施例３と同
様にしてカゼイン誘導ポリペブタイドのウンデシレン酸
縮合物のカリウム塩の３０％水溶液５６２ｇを得た。収
率は８７％であった。Example 4 Same as Example 3 except that 16.8 g of undecylenic acid chloride (0.g equivalent of casein-derived polypeptide) was used in place of caprylic acid chloride in Reference Example 3, and potassium hydroxide was used in place of monoethanolamine. Similarly, 562 g of a 30% aqueous solution of a potassium salt of an undecylenic acid condensate of casein-derived polypeptide was obtained. The yield was 87%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の３０％水溶液について、ファン・スレ
ーク法によりアミノ態チッ素を求めたところ、０．０３
２ｍ ｇ ／ ｇであった。原料として用いた参考例２
で得られたカゼイン誘導ポリペブタイドの４０％水溶液
はアミノ態チッ素２．５８０ｍ ｇ ／ ｇであり、生
成物においてほとんどのアミン基がアシル化されている
ことが判明した。Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.03.
It was 2 mg/g. Reference example 2 used as raw material
The 40% aqueous solution of casein-derived polypeptide obtained in the above contained 2.580 mg/g of amino nitrogen, indicating that most of the amine groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに４Ｎメタ
ルスルホン酸を加え、チッ素ガス置換後、試験管を封管
し、１１０℃で１２時間加水分解を行った。開封し、減
圧濃縮により塩酸を除去したのち、水とエーテルを加え
、分液ロートにて水層とエーテル層に分離し抽出を行っ
た。水層を試料とし、これのアミノ酸分析を行ったとこ
ろ、原料として用いた参考例２で得られたカゼイン誘導
ポリペブタイドとほぼ同じ組成を有していることが判明
した。エーテル層を當法に従ってＮ−メチル−Ｎ−ニト
ロソ−ｐ−）ルエンスルホンアミドを用いてメチルエス
テル化を施したのち、ガスクロマトグラフィーを行った
ところ、同様に処理しメチルエステル化した原料のウン
デシレン酸のメチルエステルと全く同じものであること
が判明した。Next, a small amount of the product was placed in a test tube, 4N metal sulfonic acid was added thereto, the tube was replaced with nitrogen gas, the test tube was sealed, and hydrolysis was performed at 110° C. for 12 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and extraction was performed by separating into an aqueous layer and an ether layer using a separating funnel. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 2, which was used as a raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-)luenesulfonamide according to the method, gas chromatography revealed that undecylene, a raw material that had been similarly treated and methyl esterified, was It turned out to be exactly the same as the methyl ester of the acid.
以上の結果から、生成物は原料として用いた参考例２で
得られたカゼイン誘導ポリペブタイドのアミン基におけ
るウンデシレン酸の縮合物のカリウム塩であることが確
認された。アミノ酸分析の結果を第２表に、ガスクロマ
トグラフィーの結果を第４図に示す。From the above results, it was confirmed that the product was a potassium salt of a condensate of undecylenic acid in the amine group of the casein-derived polypeptide obtained in Reference Example 2 used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例５
参考例３で得た濃度３０％のカゼイン誘導ポリペブタイ
ド水溶液５００ｇに３０℃恒温度下攪崖しながらイソス
テアリン酸クロライド３０ｇ （カゼイン誘導ポリペブ
タイドの０．８当量）を３時間かけて滴下した。その間
、２０％水酸化ナトリウム水溶液を適宜加えて反応液の
ｐＨを９に維持した。さらに３０℃で１時間攪拌したの
ち、温度を４０℃に上げ１時間攪拌を続けて反応を終了
した。Example 5 To 500 g of the casein-derived polypeptide aqueous solution obtained in Reference Example 3 with a concentration of 30%, 30 g of isostearic acid chloride (0.8 equivalent of casein-derived polypeptide) was added dropwise over 3 hours while stirring at a constant temperature of 30°C. During that time, the pH of the reaction solution was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After further stirring at 30°C for 1 hour, the temperature was raised to 40°C and stirring was continued for 1 hour to complete the reaction.
反応混合物を５％硫酸水溶液５１中に放出し、生成した
アシル化物を遊離させ、浮遊物を水洗後２−アミノ−２
−メチル−１，３−プロパンジオールで中和し、エチル
アルコールを加えて、カゼイン誘導ポリペブタイドのイ
ソステアリン酸縮合物の２−アミノ−２−メチル−１，
３−プロパンジオール塩の２５％エチルアルコール水溶
液６０５ｇを得た。エチルアルコールの濃度は５０％で
ある。収率は７７％であった。The reaction mixture was discharged into a 5% aqueous sulfuric acid solution 51 to liberate the produced acylated product, and after washing the suspended matter with water, 2-amino-2
- 2-amino-2-methyl-1, an isostearic acid condensate of casein-derived polypeptide, neutralized with methyl-1,3-propanediol and added with ethyl alcohol.
605 g of a 25% aqueous ethyl alcohol solution of 3-propanediol salt was obtained. The concentration of ethyl alcohol is 50%. The yield was 77%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の２−アミノ−２−メチル−１゜３−プ
ロパンジオールにより中和する前の浮遊物（乾１ｉ残分
５２．７４％）について、ファン・スレーク法によりア
ミノ態チッ素を求めたところ、０．０１７ｍ ｇ ／
ｇであった。なお２−アミノ−２−メチル−１，３−プ
ロパンジオールによる中和前のものについてアミノ態チ
ッ素の測定を行ったのは、中和後は２−アミノ−２−メ
チル−１，３−プロパンジオールのアミノ基を測定して
しまうためアミノ憇チッ素の測定試料にできないからで
ある。原料として用いた参考例３で得られたカゼイン誘
導ポリペブタイドの３０％水溶液はアミノ態チッ素３．
５２４ｍｇ／ｇであり、生成物においてほとんどのアミ
ノ基がアシル化されていることが判明した。Amino nitrogen was removed from the resulting suspended product (dry residue 52.74%) before neutralization with 2-amino-2-methyl-1°3-propanediol by the Van Slake method. When I calculated it, it was 0.017m g/
It was g. Note that the amino nitrogen was measured before neutralization with 2-amino-2-methyl-1,3-propanediol; after neutralization, 2-amino-2-methyl-1,3- This is because the amino group of propanediol is measured, so it cannot be used as a measurement sample for amino nitrogen. The 30% aqueous solution of casein-derived polypeptide obtained in Reference Example 3 used as a raw material contains amino nitrogen 3.
It was found that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チノ素ガス置換後、試験管を封管し、１１０℃
で２４時間加水分解を行った。開封し減圧ａ縮により塩
酸を除去したのち、水とエーテルを加え、分液ロートに
て水層とエーテル層に分離し抽出を行った。水層を試料
とし、これのアミノ酸分析を行ったところ、原料として
用いた参考例３で得られたカゼイン誘導ポリペブタイド
とほぼ同じ組成を有していることが判明した。エーテル
層を常法に従ってＮ−メチル−Ｎ−ニトロソ−ｐ−トル
エンスルホンアミドを用いてメチルエステル化を施した
のち、ガスクロマトグラフィーを行ったところ、同様に
処理しメチルエステル化した原料のイソステアリン酸の
メチルエステルと全く同じものであることが判明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing the chinodine gas, the test tube was sealed and heated at 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by vacuum condensation, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 3, which was used as a raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, gas chromatography revealed that isostearic acid, a raw material that had been similarly treated and methyl esterified. It turned out to be exactly the same as the methyl ester of
以上の結果から、生成物は原料として用いた参考例３で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
るイソステアリン酸の縮合物の２−アミノ−２−メチル
−１，３−プロパンジオール塩であることが確認された
。アミノ酸分析の結果を第２表に、ガスクロマトグラフ
ィーの結果を第５図に示す。From the above results, the product is a 2-amino-2-methyl-1,3-propanediol salt of a condensate of isostearic acid at the amino group of the casein-derived polypeptide obtained in Reference Example 3 used as a raw material. was confirmed. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例６
実施例５におけるイソステアリン酸クロライドに代えて
オレイン酸クロライド３０ｇ （カゼイン誘導ポリペブ
タイドの０．８当量）を用い、２−アミノ−２−メチル
−１，３−プロパンジオールに代えて水酸化ナトリウム
を用い、エチルアルコールを用いなかったほかは実施例
５と同様にしてカゼイン誘導ポリペブタイドのオレイン
酸縮合物のナトリウム塩の３０％水溶液４５８ｇを得た
。収率は７４％であった。Example 6 30 g of oleic acid chloride (0.8 equivalent of casein-derived polypeptide) was used in place of isostearic acid chloride in Example 5, and sodium hydroxide was used in place of 2-amino-2-methyl-1,3-propanediol. 458 g of a 30% aqueous solution of the sodium salt of the oleic acid condensate of casein-derived polypeptide was obtained in the same manner as in Example 5, except that ethyl alcohol was not used. The yield was 74%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の３０％水溶液について、ファン・スレ
ーク法によりアミノ態チッ素を求めたところ、０．０２
９ｍ ｇ ／ ｇであった。原料として用いた参考例３
で得られたカゼイン誘導ポリペブタイドの３０％水溶液
はアミノ態チノ素３．５２４ｍ ｇ ／ ｇであり、生
成物においてほとんどのアミノ基がアシル化されている
ことが判明した。Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.02.
It was 9 mg/g. Reference example 3 used as raw material
The 30% aqueous solution of casein-derived polypeptide obtained in the above contained 3.524 mg/g of amino-form chinogen, indicating that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに４Ｎメタ
ルスルホン酸を加え、チッ素ガス五換後、試験管を封管
し、１１０℃で１２時間加水分解を行った。開封し、減
圧濃縮により塩酸を除去したのち水とエーテルを加え、
分液ロートにて水層とエーテル層に分離し抽出を行った
。水層を試料とし、これのアミノ酸分析を行ったところ
、原料として用いた参考例３で得られたカゼイン誘導ポ
リペブタイドとほぼ同じ組成を有していることが判明し
た。エーテル層を常法に従ってＮ−メチル−Ｎ−ニトロ
ソ−ｐ−トルエンスルホンアミドを用いてメチルエステ
ル化を施したのち、ガスクロマトグラフィーを行ったと
ころ、同様に処理しメチルエステル化した原料のオレイ
ン酸のメチルエステルとまったく同じものであることが
判明した。Next, a small amount of the product was placed in a test tube, 4N metal sulfonic acid was added thereto, and after five nitrogen gas exchanges, the test tube was sealed and hydrolysis was performed at 110° C. for 12 hours. After opening the package and removing hydrochloric acid by concentrating under reduced pressure, water and ether were added.
The mixture was separated into an aqueous layer and an ether layer using a separatory funnel and extracted. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 3, which was used as a raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, gas chromatography revealed that oleic acid, a raw material that had been similarly treated and methyl esterified, was detected. It turned out to be exactly the same as the methyl ester of
以上の結果から、生成物は原料として用いた参考例３で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
るオレイン酸の縮合物のナトリウム塩であることがＲｕ
された。アミノ酸分析の結果を第２表に、ガスクロマト
グラフィーの結果を第６図に示す。From the above results, it is confirmed that the product is a sodium salt of a condensate of oleic acid at the amino group of the casein-derived polypeptide obtained in Reference Example 3 used as a raw material.
It was done. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例７
参考例３で得た濃度３０％のカゼイン誘導ポリペブタイ
ド水７８液５００ｇに３０℃恒温度下攪ｌヤしながらヤ
シ脂肪酸クロライド２７ｇ （カゼイン誘導ポリペブタ
イドの１．０当量）を２時間かけて滴下した。Example 7 27 g of coconut fatty acid chloride (1.0 equivalent of casein-derived polypeptide) was added to 500 g of the casein-derived polypeptide water 78 solution with a concentration of 30% obtained in Reference Example 3 while stirring at a constant temperature of 30°C for 2 hours. dripped.
その間、２０％水酸化カリウム水溶液を適宜加えて反応
液のｐＨを９に維持した。さらに３０°Ｃで１時間攪拌
したのち、温度を４０℃に上げ１時間攪ＩＴを続けて反
応を終了した。During this time, the pH of the reaction solution was maintained at 9 by appropriately adding a 20% aqueous potassium hydroxide solution. After further stirring at 30°C for 1 hour, the temperature was raised to 40°C and stirring was continued for 1 hour to complete the reaction.
反応混合物を５％硫酸水溶液５１中に放出し、生成した
アシル化物を遊離のかたちで浮遊させ、浮遊物を水洗後
プロピレングリコールを加えて溶解してカゼイン誘導ポ
リペブタイドのヤシ脂肪酸縮合物の２５％プロピレング
リコール水ｉ？＆６６５ｇを得た。なおプロピレングリ
コールの濃度は４０％である。収率は９５％であった。The reaction mixture was discharged into a 5% sulfuric acid aqueous solution 51, the produced acylated product was suspended in a free form, and the suspended matter was washed with water and then dissolved by adding propylene glycol to obtain 25% propylene of the coconut fatty acid condensate of casein-derived polypeptide. Glycol water i? &665g was obtained. Note that the concentration of propylene glycol was 40%. The yield was 95%.
なお得られた生成物の確認は以下のようにして行った。The obtained product was confirmed as follows.
得られた生成物の２５％プロピレングリコール水溶液に
ついて、ファン・スレーク法によりアミノ態チッ素を求
めたところ、０．０１０ｍ ｇ ／ ｇであった。原料
として用いた参考例３で得られたカゼイン誘導ポリペブ
タイドの３０％水溶液はアミノ態チッ素３．５２４ｍ
ｇ ／ ｇであり、生成物においてほとんどのアミノ基
がアシル化されていることが１１明した。The amino nitrogen content of a 25% propylene glycol aqueous solution of the obtained product was determined by the Van Slake method and was found to be 0.010 mg/g. The 30% aqueous solution of casein-derived polypeptide obtained in Reference Example 3 used as a raw material contained 3.524 m of amino nitrogen.
g/g, indicating that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チッ素ガス置換後、試験管を封青し、１１０℃
で２４時間加水分解を行った。開封し減圧濃縮により塩
酸を除去したのち、水とエーテルを加え、分液ロートに
て水層とエーテル層に分離し抽出を行った。水層を試料
とし、これのアミノ酸分析を行ったところ、原料として
用いた参考例３で得られたカゼイン誘導ポリペブタイド
とほぼ同じ組成を有していることが判明した。エーテル
層を審決に従ってＮ−メチル−Ｎ−ニトロソ−ｐ−トル
エンスルホンアミドを用いてメチルエステル化を施した
のち、ガスクロマトグラフィーを行ったところ、同様に
処理しメチルエステル化した原料のヤシ脂肪酸のメチル
エステルと全く同じものであることが判明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and the temperature was heated to 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 3, which was used as a raw material. After the ether layer was methyl esterified using N-methyl-N-nitroso-p-toluenesulfonamide in accordance with the trial decision, gas chromatography was performed, and it was found that the raw coconut fatty acid that had been similarly treated and methyl esterified was It turned out to be exactly the same as methyl ester.
以上の結果から、生成物は原料として用いた参考例３で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
るヤシ脂肪酸の縮合物であることが確認された。アミノ
酸分析の結果を第２表に、ガスクロマトグラフィーの結
果を第７図に示す。From the above results, it was confirmed that the product was a condensation product of coconut fatty acid in the amino group of the casein-derived polypeptide obtained in Reference Example 3 used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
実施例８
実施例１におけるミリスチン酸クロライドに代えて樹脂
酸（ロジン系でアビエチン酸を主成分とするもの）クロ
ライド８１ｇ （カゼイン誘導ポリペブタイドの１．０
当量）を用いたほかは実施例１と同様にして１度３０％
のカゼイン誘導ポリペブタイドの…脂酸縮合物のカリウ
ム塩水溶液７３４ｇを得た。収率は９４％であった。Example 8 In place of myristic acid chloride in Example 1, 81 g of resin acid (rosin-based one containing abietic acid as the main component) chloride (1.0 g of casein-derived polypeptide) was used.
30% once in the same manner as in Example 1 except that
734 g of a potassium salt aqueous solution of a fatty acid condensate of casein-derived polypeptide was obtained. The yield was 94%.
なお得られた生成１！ＩＪの確認は以下のようにして行
った。Furthermore, the obtained generation 1! IJ was confirmed as follows.
得られた生成物の３０％水溶液について、ファン・スレ
ーク法によりアミノ態チッ素を求めたところ、０．０２
７ｍ ｇ ／ ｇであった。原料として用いた参考例１
で得られたカゼイン誘導ポリペブタイドの３０％水溶液
はアミノ態チッ素７．１０４ｍ ｇ ／ ｇであり、生
成物においてほとんどのアミノ基がアシル化されている
ことが判明した。Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.02.
It was 7 mg/g. Reference example 1 used as raw material
The 30% aqueous solution of casein-derived polypeptide obtained in the above had an amino nitrogen content of 7.104 mg/g, indicating that most of the amino groups in the product were acylated.
ついで、生成物の少量を試験管にとり、これに６Ｎ塩酸
を加え、チッ素ガス置換後、試験管を封管し、１１０℃
で２４時間加水分解を行った。開封し、減圧ａ縮により
塩酸を除去したのち、水とエーテルを加え、分液ロート
にて水層とエーテル層に分離し抽出を行った。水層を試
料とし、これのアミノ酸分析を行ったところ、原料とし
て用いた参考例１で得られたカゼイン誘導ポリペブタイ
ドとほぼ同じ組成を有していることが判明した。エーテ
ル層を常法に従ってＮ−メチル−Ｎ−ニトロソ−ｐ−ト
ルエンスルホンアミドを用いてメチルエステル化したと
ころ、同様に処理しメチルエステル化した原料の樹脂酸
のメチルエステルと全く同じ組成のものであることが判
明した。Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and the temperature was heated to 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by condensation under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. When the aqueous layer was used as a sample and subjected to amino acid analysis, it was found that it had almost the same composition as the casein-derived polypeptide obtained in Reference Example 1, which was used as a raw material. When the ether layer was methyl esterified using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, it was found that it had exactly the same composition as the methyl ester of the raw resin acid that was similarly treated and methyl esterified. It turns out that there is something.
以上の結果から、生成物は原料として用いた参考例１で
得られたカゼイン誘導ポリペブタイドのアミノ基におけ
る樹脂酸の縮合物のカリウム塩であることが確認された
。アミノ酸分析の結果を第２表に、ガスクロマトグラフ
ィーの結果を第８図に示す。From the above results, it was confirmed that the product was a potassium salt of a condensate of resin acid at the amino group of the casein-derived polypeptide obtained in Reference Example 1 used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.
なお、第２表に含まれるシスティン酸は、カゼインが加
水分解あるいはアシル化される際にシスチンが一部酸化
されたことにより生成したものである。The cystic acid included in Table 2 is produced by partial oxidation of cystine when casein is hydrolyzed or acylated.
そして、ガスクロマトグラフィーの分析条件は以下のと
おりである。The analysis conditions for gas chromatography are as follows.
カラム：ＤＥＧＳ（ジエチレングリコールサクシネート
）＋８３ ＰＯ４（１０： １）、内径３ｍｍＸ長さ２
ｍ（実施例１〜７およびその原料）
シリコン５Ｅ３０、内径３１×長さ２ｍ（実施例８およ
びその原料）
ガ ス：千ノ素（５０ｍ ｌ ７分）
検 出：水素炎イオン化検出法
温度にフいては各図に表示した。図中の各ピークの数字
はピーク検出時間（分）を示す。Column: DEGS (diethylene glycol succinate) + 83 PO4 (10: 1), inner diameter 3 mm x length 2
m (Examples 1 to 7 and their raw materials) Silicon 5E30, inner diameter 31 x length 2 m (Example 8 and its raw materials) Gas: 1,000 ml (50 ml 7 minutes) Detection: Hydrogen flame ionization detection method At temperature The lines are shown in each figure. The number of each peak in the figure indicates the peak detection time (minutes).
応用例１
実施例１で得たカゼイン誘導ポリペブタイドのアシル化
物のカリウム塩（カゼイン誘導ポリペブタイドのミリス
チン酸縮合物のカリウム塩）を用いて第３表に示す組成
のシャンプー（実施品１）を調製した。Application Example 1 A shampoo (Example 1) having the composition shown in Table 3 was prepared using the potassium salt of the acylated casein-derived polypeptide obtained in Example 1 (potassium salt of the myristic acid condensate of casein-derived polypeptide). .
比較対照のため、該カゼイン誘導ポリペブタイドのアシ
ル化物のカリウム塩を含まないシャンプー（対照量１）
を調製し、両シャンプーの使用感を１０人のパネルによ
り官能評価した。その結果を第４表に示す。なお、各成
分の配合量は重量部で示す。以下においても同様である
。For comparison, a shampoo containing no potassium salt of the acylated casein-derived polypeptide (control amount 1)
were prepared, and the feeling of use of both shampoos was sensory evaluated by a panel of 10 people. The results are shown in Table 4. In addition, the compounding amount of each component is shown in parts by weight. The same applies to the following.
第 ３ 表
第 ４ 表
応用例２
実施例５で得たカゼイン誘導ポリペブタイドのアシル化
物の２−アミノ−２−メチル−１，３−プロパンジオー
ル塩（カゼイン誘導ポリペブタイドのイソステアリン酸
縮合物の２−アミノ−２−メチル−１，３−プロパンジ
オール塩）を用いて第５表に示す組成のヘアーリンス（
実施品２）を調製した。Table 3 Table 4 Application example 2 2-amino-2-methyl-1,3-propanediol salt of the acylated casein-derived polypeptide obtained in Example 5 (2-amino-2-methyl-1,3-propanediol salt of the isostearic acid condensate of the casein-derived polypeptide) -2-methyl-1,3-propanediol salt) with the composition shown in Table 5.
Example 2) was prepared.
比較対照のため、該カゼイン誘導ポリペブタイドのアシ
ル化物の２−アミノ−２−メチル−１，３−プロパンジ
オール塩を含まないヘアーリンス（対照量２）を調製し
、両ヘアーリンスを２０倍に希釈して市販のシャンプー
で洗髪後の毛髪に使用し、その使用感を１０人の女性パ
ネルにより官能評価した。その結果を第６表に示す。For comparison, a hair rinse (control amount 2) not containing the 2-amino-2-methyl-1,3-propanediol salt of the acylated casein-derived polypeptide was prepared, and both hair rinses were diluted 20 times. A commercially available shampoo was used on the hair after washing, and the feeling of use was sensory evaluated by a panel of 10 women. The results are shown in Table 6.
第 ５ 表
第 ６ 表
応用例３
実施例３で得たカゼイン誘導ポリペブタイドのアシル化
物のモノエタノールアミン塩（カゼイン誘導ポリペブタ
イドのカプリル酸縮合物のモノエタノールアミン塩）を
用いて第７表に示す組成のパーマネントウェーブ用第１
剤（実施品３）を調製した。Table 5 Table 6 Application Example 3 Using the monoethanolamine salt of the acylated casein-derived polypeptide obtained in Example 3 (monoethanolamine salt of the caprylic acid condensate of casein-derived polypeptide), the composition shown in Table 7 was prepared. 1st for permanent wave
An agent (Example 3) was prepared.
比較対照のため、該カゼイン誘導ポリペブタイドのアシ
ル化物のモノエタノールアミン塩を含まないパーマネン
トウェーブ用第１剤（対照品３）を調製し、それらの第
１剤と６％臭素酸ナトリウム水溶液よりなる第２剤を用
い、常法により１０人の女性パネルにパーマネントウェ
ーブを施術し、その使用怒を官能評価した。その結果を
第８表に示す。For comparison, a first agent for permanent waving (control product 3) that does not contain the monoethanolamine salt of the acylated casein-derived polypeptide was prepared, and a first agent consisting of the first agent and a 6% sodium bromate aqueous solution was prepared. Permanent waving was performed on a panel of 10 women using the two drugs in a conventional manner, and their effects on use were sensually evaluated. The results are shown in Table 8.
第 ７ 表
第 ８ 表
応用例４〜５
実施例で得たカゼイン誘導ポリペブタイドのアシル化物
のトリエタノールアミン塩（カゼイン誘導ポリペブタイ
ドのヤシ脂肪酸縮合物のトリエタノールアミン塩）を用
いて第９表に示す組成のシャンプー（実施品４）を調製
した。Table 7 Table 8 Application Examples 4 to 5 Using the triethanolamine salt of the acylated casein-derived polypeptide obtained in the example (triethanolamine salt of the coconut fatty acid condensate of casein-derived polypeptide), the results are shown in Table 9. A shampoo (implementation product 4) with the following composition was prepared.
また実施例４で得たカゼイン誘導ポリペブタイドのアシ
ル化物のカリウム塩（カゼイン誘導ポリペブタイドのウ
ンデシレン縮合物のカリウム塩）と上記実施例２で得た
カゼイン誘導ポリペブタイドのヤシ脂肪酸縮合物のトリ
エタノールアミン塩を用いて第９表に示す組成のフケ防
止用シャンプー（実施品５）を調製した。In addition, the potassium salt of the acylated casein-derived polypeptide obtained in Example 4 (potassium salt of the undecylene condensate of casein-derived polypeptide) and the triethanolamine salt of the coconut fatty acid condensate of the casein-derived polypeptide obtained in Example 2 above were used. An anti-dandruff shampoo (Example 5) having the composition shown in Table 9 was prepared using the following methods.
第 ９ 表
上記のようにして調製されたシャンプーにより洗髪した
ところ洗髪後の毛髪は柔軟性があり、かつ艶があり、く
し通り性が良好で、しかもフケの発生とかゆみが防止さ
れた。Table 9 When hair was washed with the shampoo prepared as described above, the hair after washing was flexible and shiny, had good combability, and was free from dandruff and itching.
応用例６
実施例５で得たカゼイン誘導ポリペブタイドのアシル化
物の塩（カゼイン誘導ポリペブタイドのイソステアリン
酸縮合物の２−アミノ−２−メチル−１，３−プロパン
ジオール塩）を用いて下記組成のへアートニックをｍ！
した。Application Example 6 Using the salt of the acylated casein-derived polypeptide obtained in Example 5 (2-amino-2-methyl-1,3-propanediol salt of isostearic acid condensate of casein-derived polypeptide), the following composition was prepared. Artonic m!
did.
二に」ニしＬＬ批戊
カゼイン誘導ポリペブタイドのイソ ２．０ステアリ
ン酸槽合物の２−アミノ
＝２−メチル−１，３−プロパンジ
オール塩
（２５％液、アルコール５０％）
ジイソプロピルアジベート１．５
プロピレングリコール １．ＯＬ−メン
トール ０．２エチルアルコー
ル ７０．０殺菌剤 適
量
養毛剤 通量
香 料 通量
精製水 ２５．３
上記のようにして調製されたヘアートニックは頭皮、毛
髪に潤いを与え、毛髪をしなやかにし、かつドライヤー
などによる毛髪の損傷を防ぐ作用を有していた。2-Amino=2-methyl-1,3-propanediol salt of stearic acid compound (25% liquid, 50% alcohol) Diisopropyl adibate 1 .5 Propylene glycol 1. OL-Menthol 0.2 Ethyl alcohol 70.0 Bactericide Appropriate amount Hair tonic Appropriate amount Perfume Percentage Purified water 25.3 The hair tonic prepared as above moisturizes the scalp and hair, makes the hair supple, It also had the effect of preventing hair damage from hair dryers and the like.
応用例７
実施例５で得たカゼイン誘導ポリペブタイドのアシル化
物の塩（カゼイン誘導ポリペブタイドのイソステアリン
酸縮合物の２−アミノ−２−メチル−１，３−プロパン
ジオール塩）を用いて下記組成のローションを調製した
。Application Example 7 A lotion with the following composition was prepared using the acylated salt of casein-derived polypeptide obtained in Example 5 (2-amino-2-methyl-1,3-propanediol salt of isostearic acid condensate of casein-derived polypeptide). was prepared.
一ジニヱ」二〇１戊
カゼイン誘導ポリペブタイドのイソ ２．０ステアリ
ン酸槽合物の２−アミノ
−２−メチル−１，３−プロパンジ
オール塩
（２５％液、アルコール５０％）
エチルアルコール １５．０ＥＤＴ
Ａ Ｏ，１防腐剤
適量
香 料 通
量精製水 ８２．９
上記のように調製されたローションは縮合物の皮膚に対
する親和性が高く、過当な潤いを皮膚に与える作用を有
していた。2-amino-2-methyl-1,3-propanediol salt of iso-2.0 stearic acid compound of casein-derived polypeptide (25% liquid, 50% alcohol) Ethyl alcohol 15.0 EDT
A O,1 preservative
Appropriate amount Perfume Purified water 82.9 The lotion prepared as above had a high affinity for the skin of the condensate and had the effect of imparting excessive moisture to the skin.
応用例８
実施例８で得たカゼイン誘導ポリペブタイドのアシル化
物のトリエタノールアミン塩（カゼイン誘導ポリペブタ
イドの樹脂酸縮合物のカリウム塩）を用いて下記組成の
クレンジングローションを調製した。Application Example 8 A cleansing lotion having the following composition was prepared using the triethanolamine salt of the acylated casein-derived polypeptide obtained in Example 8 (potassium salt of the resin acid condensate of casein-derived polypeptide).
クレンジングローション組成
カゼイン誘導ポリペブタイドの樹脂 ２５．０酸槽合
物のカリウム塩
（３０％水溶液）
コラーゲン誘導ポリペブタイド ５．０（アルカ
リ加水分解による、平均分
子量５００．３０％水溶液）
エチルアルコール ５．０ＥＤＴ
Ａ ０．１防腐剤
適量
香 料 通
量精製水 ６４．９
上記のようにして調製されたクレンジングローションは
皮膚を保護しながらクレンジングを効果的に行い、皮膚
の油脂分をうばわず、乾性の皮膚に対しては油脂分の補
給を行う作用を有していた。Cleansing lotion composition Casein-derived polypeptide resin 25.0 Potassium salt of acid bath compound (30% aqueous solution) Collagen-derived polypeptide 5.0 (average molecular weight 500.30% aqueous solution by alkaline hydrolysis) Ethyl alcohol 5.0 EDT
A 0.1 preservative
Appropriate amount of fragrance Purified water 64.9 The cleansing lotion prepared as above cleanses effectively while protecting the skin, does not remove oils and fats from the skin, and is suitable for dry skin. It had the effect of replenishing the supply of
応用例９
実施例７で得たカゼイン誘導ポリペブタイドのアシル化
物（カゼイン誘導ポリペブタイドのヤシ脂肪酸縮合物）
を用いて下記組成のエアゾールタイプのシェービングク
リームをＵｉＭした。Application example 9 Acylated product of casein-derived polypeptide obtained in Example 7 (coconut fatty acid condensate of casein-derived polypeptide)
An aerosol type shaving cream having the following composition was UiMed using the following.
シェービングクリーム （０）
カゼイン誘導ポリペブタイドのヤシ ２０．０脂肪酸
槽合物（２５％液、溶剤：プ
ロピレングリコール４０％水ｇ 液）
セチルアルコール ０．５イソプロ
ピルイソステアレート １．０バラオキシ安息
香酸メチル（防腐剤）０．１コラーゲン誘導ポリペブタ
イドとヤ １０．０シ脂肪酸との縮合物のカリウム塩
（３５％水溶液）
コラーゲン誘導ポリペブタイド ５．０（アルカ
リ加水分解による、平均分
子量５００．３０％水溶液）
グリセリン ５．０香
料 適量精製水
５８．４
五ＭＵ暉筐
原 液 ９
４．０フレオン１２ ４
．２フレオン１１４ １．
８上記のように調製されたシェービングクリームはひげ
剃りにより失われた皮膚の油脂分を補い、ひげ剃り後の
肌をととのえる作用を有していた。Shaving cream (0) Casein-derived polypeptide palm 20.0 Fatty acid bath compound (25% liquid, solvent: propylene glycol 40% water g liquid) Cetyl alcohol 0.5 Isopropyl isostearate 1.0 Methyl oxybenzoate (preservative) (35% aqueous solution) Collagen-derived polypeptide 5.0 (Aqueous solution with average molecular weight 500.30% by alkaline hydrolysis) Glycerin 5. 0 scent
Adequate amount of purified water
58.4 5 MU Akira Kagohara Liquid 9
4.0 Freon 12 4
．． 2 freon 114 1.
8. The shaving cream prepared as described above had the effect of replenishing the oil and fat content of the skin lost due to shaving and soothing the skin after shaving.
以上説明したように、本発明の一般式（１）で示される
カゼイン誘導ポリペブタイドのアシル化物またはその塩
は、天然の蛋白質から誘導されたものであって、皮膚や
毛髪と同じペプチド成分を含むため、皮膚や毛髪に対し
て穏やかに作用し、皮膚や毛髪に損傷を与えることなく
優れた洗浄効果を発揮することができ、かつペプチド成
分に基づく皮膚や毛髪の保護作用とｔＭ （ｎした毛髪
を再生する作用を有しており、例えば各種頭髪用化粧品
の添加剤として、あるいはクリームなど皮膚用化粧品の
主剤としてきわめて有用なものである。As explained above, the acylated casein-derived polypeptide or its salt represented by the general formula (1) of the present invention is derived from a natural protein and contains the same peptide components as skin and hair. , which acts gently on the skin and hair, can exert an excellent cleaning effect without damaging the skin or hair, and has a protective effect on the skin and hair based on peptide components and tM It has a regenerating effect and is extremely useful, for example, as an additive in various hair cosmetics or as a main ingredient in skin cosmetics such as creams.
第１〜８図は本発明物質の高級脂肪酸部分のメチルエス
テル化物と原料として用いた高級脂肪酸のメチルエステ
ル化物のガスクロマトグラフィー結果を示すものである
。温度と昇温速度は各図に示すとおりであり、図中の各
ピークの数字は検出時間（分）を示す。
特許出願人 株式会社 成 和 化 成７１図
芳２図
芳３図
−Ｅ万改り暑１６
で方丘仔１１３ ／−１／ｊλ糾
芳４図
ア５図
賃６図
着７閏
オ８０Figures 1 to 8 show the results of gas chromatography of the methyl ester of the higher fatty acid moiety of the substance of the present invention and the methyl ester of the higher fatty acid used as the raw material. The temperature and heating rate are as shown in each figure, and the number of each peak in the figure indicates the detection time (minutes). Patent Applicant Seiwa Ka Co., Ltd. Sei 71 Zuho 2 Zuho 3 – Emankairisatsu 16
113 / - 1 / jλ 糾 4 fig.
Claims (1)
素数８〜２０の長鎖アルケニル基または樹脂酸の側鎖で
あり、Ｒ＿２はカゼイン誘導ポリペプタイドの構成アミ
ノ酸の側鎖である。ｎは３〜２０の整数であり、Ｍは水
素、ナトリウム、カリウムなどのアルカリ金属、アンモ
ニウムまたはモノエタノールアミン、ジエタノールアミ
ン、トリエタノールアミン、２−アミノ−２−メチル−
１，３−プロパンジオールなどの有機アルカノールアミ
ンのオニウムである） で示されるカゼイン誘導ポリペプタイドのアシル化物ま
たはその塩。(1) General formula (I) ▲Mathematical formulas, chemical formulas, tables, etc.▼(I) (In the formula, R_1 is a long-chain alkyl group with 8 to 20 carbon atoms, a long-chain alkenyl group with 8 to 20 carbon atoms, or a resin R_2 is the side chain of the amino acid constituting the casein-derived polypeptide. n is an integer from 3 to 20, M is hydrogen, an alkali metal such as sodium or potassium, ammonium or monoethanolamine, Diethanolamine, triethanolamine, 2-amino-2-methyl-
An acylated casein-derived polypeptide or a salt thereof.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP25270286A JPS63105000A (en) | 1986-10-22 | 1986-10-22 | Acylated casein-derived polypeptide of salt thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP25270286A JPS63105000A (en) | 1986-10-22 | 1986-10-22 | Acylated casein-derived polypeptide of salt thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS63105000A true JPS63105000A (en) | 1988-05-10 |
Family
ID=17241063
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP25270286A Pending JPS63105000A (en) | 1986-10-22 | 1986-10-22 | Acylated casein-derived polypeptide of salt thereof |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS63105000A (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2672289A1 (en) * | 1991-02-06 | 1992-08-07 | Oreal | URETHANE GROUPED DIPEPTIDE DERIVATIVES, USEFUL AS MOISTURIZING AGENTS AND AS SURFACTANTS IN COSMETIC, PHARMACEUTICAL OR FOOD COMPOSITIONS. |
| JPH1095726A (en) * | 1996-09-20 | 1998-04-14 | Seiwa Kasei:Kk | Cosmetic base |
| GB2325231A (en) * | 1997-04-28 | 1998-11-18 | Nippon Fine Chemical Co | Acylated polypeptide for use in cosmetic compositions |
| WO1999062935A1 (en) * | 1998-06-01 | 1999-12-09 | Fuji Oil Co., Ltd. | Reaction products between carboxylic acid and amino acid or amino acid condensate and process for producing the same |
| EP1291470A1 (en) | 2001-09-06 | 2003-03-12 | Prolyte Vastgoed B.V. | Truss construction and coupling part, basic element and coupling element for application therein |
| CN105878095A (en) * | 2014-12-05 | 2016-08-24 | 江南大学 | Method for preparing pumpkin seed polypeptide-containing cosmetics |
-
1986
- 1986-10-22 JP JP25270286A patent/JPS63105000A/en active Pending
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2672289A1 (en) * | 1991-02-06 | 1992-08-07 | Oreal | URETHANE GROUPED DIPEPTIDE DERIVATIVES, USEFUL AS MOISTURIZING AGENTS AND AS SURFACTANTS IN COSMETIC, PHARMACEUTICAL OR FOOD COMPOSITIONS. |
| JPH1095726A (en) * | 1996-09-20 | 1998-04-14 | Seiwa Kasei:Kk | Cosmetic base |
| GB2325231A (en) * | 1997-04-28 | 1998-11-18 | Nippon Fine Chemical Co | Acylated polypeptide for use in cosmetic compositions |
| US6183759B1 (en) | 1997-04-28 | 2001-02-06 | Nippon Fine Chemical Co., Ltd. | Cosmetic composition |
| GB2325231B (en) * | 1997-04-28 | 2001-02-21 | Nippon Fine Chemical Co | A cosmetic composition |
| WO1999062935A1 (en) * | 1998-06-01 | 1999-12-09 | Fuji Oil Co., Ltd. | Reaction products between carboxylic acid and amino acid or amino acid condensate and process for producing the same |
| US6743945B1 (en) | 1998-06-01 | 2004-06-01 | Fuji Oil Co., Ltd. | Carboxylic acid and amino acid or amino condensate reactants and manufacturing method therefor |
| EP1291470A1 (en) | 2001-09-06 | 2003-03-12 | Prolyte Vastgoed B.V. | Truss construction and coupling part, basic element and coupling element for application therein |
| CN105878095A (en) * | 2014-12-05 | 2016-08-24 | 江南大学 | Method for preparing pumpkin seed polypeptide-containing cosmetics |
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