JPH02207017A - Deodorant composition - Google Patents
Deodorant compositionInfo
- Publication number
- JPH02207017A JPH02207017A JP1027925A JP2792589A JPH02207017A JP H02207017 A JPH02207017 A JP H02207017A JP 1027925 A JP1027925 A JP 1027925A JP 2792589 A JP2792589 A JP 2792589A JP H02207017 A JPH02207017 A JP H02207017A
- Authority
- JP
- Japan
- Prior art keywords
- deodorizing
- keratin peptide
- acid
- keratin
- reaction
- 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.)
- Granted
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 48
- 239000002781 deodorant agent Substances 0.000 title abstract description 15
- 230000001877 deodorizing effect Effects 0.000 claims abstract description 95
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 90
- 102000011782 Keratins Human genes 0.000 claims abstract description 87
- 108010076876 Keratins Proteins 0.000 claims abstract description 87
- 150000001732 carboxylic acid derivatives Chemical class 0.000 claims abstract description 21
- 229960003067 cystine Drugs 0.000 claims abstract description 18
- 150000001413 amino acids Chemical group 0.000 claims abstract description 17
- 229910052708 sodium Inorganic materials 0.000 claims abstract description 13
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims abstract description 11
- 229910052739 hydrogen Inorganic materials 0.000 claims abstract description 3
- 229910052700 potassium Inorganic materials 0.000 claims abstract 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 claims abstract 3
- -1 Ca/2 Chemical class 0.000 claims description 52
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims description 26
- 239000000126 substance Substances 0.000 claims description 20
- GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 claims description 18
- 229910021529 ammonia Inorganic materials 0.000 claims description 13
- 239000002585 base Substances 0.000 claims description 8
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 claims description 6
- 125000004432 carbon atom Chemical group C* 0.000 claims description 4
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 claims description 3
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 claims description 3
- 229910052783 alkali metal Inorganic materials 0.000 claims description 2
- 150000001340 alkali metals Chemical class 0.000 claims description 2
- 229910052784 alkaline earth metal Inorganic materials 0.000 claims description 2
- 150000001342 alkaline earth metals Chemical class 0.000 claims description 2
- YBRBMKDOPFTVDT-UHFFFAOYSA-N tert-butylamine Chemical compound CC(C)(C)N YBRBMKDOPFTVDT-UHFFFAOYSA-N 0.000 claims description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 claims 1
- 150000002430 hydrocarbons Chemical group 0.000 claims 1
- 229910052744 lithium Inorganic materials 0.000 claims 1
- 229910052749 magnesium Inorganic materials 0.000 claims 1
- 150000001412 amines Chemical class 0.000 abstract description 22
- 210000004209 hair Anatomy 0.000 abstract description 22
- PXQLVRUNWNTZOS-UHFFFAOYSA-N sulfanyl Chemical class [SH] PXQLVRUNWNTZOS-UHFFFAOYSA-N 0.000 abstract description 21
- 125000001183 hydrocarbyl group Chemical group 0.000 abstract description 6
- 125000003396 thiol group Chemical group [H]S* 0.000 abstract description 3
- 150000001875 compounds Chemical class 0.000 abstract 3
- 208000019901 Anxiety disease Diseases 0.000 abstract 1
- 230000036506 anxiety Effects 0.000 abstract 1
- 238000006243 chemical reaction Methods 0.000 description 52
- 235000019645 odor Nutrition 0.000 description 40
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethanethiol Chemical compound CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 24
- 239000003795 chemical substances by application Substances 0.000 description 22
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 20
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 18
- 239000000243 solution Substances 0.000 description 17
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 17
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 15
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 15
- 239000013065 commercial product Substances 0.000 description 14
- KWIUHFFTVRNATP-UHFFFAOYSA-N glycine betaine Chemical compound C[N+](C)(C)CC([O-])=O KWIUHFFTVRNATP-UHFFFAOYSA-N 0.000 description 14
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 14
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 13
- 230000002378 acidificating effect Effects 0.000 description 13
- 229940024606 amino acid Drugs 0.000 description 13
- 235000001014 amino acid Nutrition 0.000 description 13
- 239000000047 product Substances 0.000 description 13
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 12
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 12
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 150000001244 carboxylic acid anhydrides Chemical class 0.000 description 12
- 230000000052 comparative effect Effects 0.000 description 12
- 235000019864 coconut oil Nutrition 0.000 description 11
- 239000003240 coconut oil Substances 0.000 description 11
- 239000011734 sodium Substances 0.000 description 11
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 10
- 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 description 10
- 239000007864 aqueous solution Substances 0.000 description 10
- 230000007062 hydrolysis Effects 0.000 description 10
- 238000006460 hydrolysis reaction Methods 0.000 description 10
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 9
- 235000014113 dietary fatty acids Nutrition 0.000 description 9
- 239000000194 fatty acid Substances 0.000 description 9
- 229930195729 fatty acid Natural products 0.000 description 9
- 238000000034 method Methods 0.000 description 9
- 239000002253 acid Substances 0.000 description 8
- 229960003237 betaine Drugs 0.000 description 8
- 102000004196 processed proteins & peptides Human genes 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 150000004665 fatty acids Chemical class 0.000 description 7
- 238000003756 stirring Methods 0.000 description 7
- WMFOQBRAJBCJND-UHFFFAOYSA-M Lithium hydroxide Chemical compound [Li+].[OH-] WMFOQBRAJBCJND-UHFFFAOYSA-M 0.000 description 6
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 6
- 125000003277 amino group Chemical group 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 235000010323 ascorbic acid Nutrition 0.000 description 6
- 239000011668 ascorbic acid Substances 0.000 description 6
- 239000007795 chemical reaction product Substances 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 239000000284 extract Substances 0.000 description 6
- 229910052742 iron Inorganic materials 0.000 description 6
- 159000000000 sodium salts Chemical class 0.000 description 6
- JPVYNHNXODAKFH-UHFFFAOYSA-N Cu2+ Chemical compound [Cu+2] JPVYNHNXODAKFH-UHFFFAOYSA-N 0.000 description 5
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 5
- 229960005070 ascorbic acid Drugs 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 5
- 229910001431 copper ion Inorganic materials 0.000 description 5
- 229960002989 glutamic acid Drugs 0.000 description 5
- 229910001385 heavy metal Inorganic materials 0.000 description 5
- 150000002500 ions Chemical class 0.000 description 5
- 210000004400 mucous membrane Anatomy 0.000 description 5
- FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- 239000004166 Lanolin Substances 0.000 description 4
- 108091005804 Peptidases Proteins 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- LGRFSURHDFAFJT-UHFFFAOYSA-N Phthalic anhydride Natural products C1=CC=C2C(=O)OC(=O)C2=C1 LGRFSURHDFAFJT-UHFFFAOYSA-N 0.000 description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 4
- 125000000217 alkyl group Chemical group 0.000 description 4
- 229960005261 aspartic acid Drugs 0.000 description 4
- JHIWVOJDXOSYLW-UHFFFAOYSA-N butyl 2,2-difluorocyclopropane-1-carboxylate Chemical compound CCCCOC(=O)C1CC1(F)F JHIWVOJDXOSYLW-UHFFFAOYSA-N 0.000 description 4
- 238000004332 deodorization Methods 0.000 description 4
- POULHZVOKOAJMA-UHFFFAOYSA-N dodecanoic acid Chemical compound CCCCCCCCCCCC(O)=O POULHZVOKOAJMA-UHFFFAOYSA-N 0.000 description 4
- 238000000909 electrodialysis Methods 0.000 description 4
- 229940039717 lanolin Drugs 0.000 description 4
- 235000019388 lanolin Nutrition 0.000 description 4
- FPYJFEHAWHCUMM-UHFFFAOYSA-N maleic anhydride Chemical compound O=C1OC(=O)C=C1 FPYJFEHAWHCUMM-UHFFFAOYSA-N 0.000 description 4
- 230000007935 neutral effect Effects 0.000 description 4
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 239000000741 silica gel Substances 0.000 description 4
- 229910002027 silica gel Inorganic materials 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 229940014800 succinic anhydride Drugs 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-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
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-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
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 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
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 230000010933 acylation Effects 0.000 description 3
- 238000005917 acylation reaction Methods 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 235000009582 asparagine Nutrition 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
- 235000013922 glutamic acid Nutrition 0.000 description 3
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- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
- 235000004554 glutamine Nutrition 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 210000002268 wool Anatomy 0.000 description 3
- FFJCNSLCJOQHKM-CLFAGFIQSA-N (z)-1-[(z)-octadec-9-enoxy]octadec-9-ene Chemical compound CCCCCCCC\C=C/CCCCCCCCOCCCCCCCC\C=C/CCCCCCCC FFJCNSLCJOQHKM-CLFAGFIQSA-N 0.000 description 2
- XDOFQFKRPWOURC-UHFFFAOYSA-N 16-methylheptadecanoic acid Chemical compound CC(C)CCCCCCCCCCCCCCC(O)=O XDOFQFKRPWOURC-UHFFFAOYSA-N 0.000 description 2
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N Alanine Chemical compound CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- 102000008186 Collagen Human genes 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical compound [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 description 2
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 2
- 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 2
- 239000005639 Lauric acid Substances 0.000 description 2
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- 241001465754 Metazoa Species 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- OFOBLEOULBTSOW-UHFFFAOYSA-N Propanedioic acid Natural products OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 description 2
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- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 244000269722 Thea sinensis Species 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
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- 238000005904 alkaline hydrolysis reaction Methods 0.000 description 2
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- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
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- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
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- 235000018977 lysine Nutrition 0.000 description 2
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- 239000011976 maleic acid Substances 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
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- 238000007254 oxidation reaction Methods 0.000 description 2
- XNGIFLGASWRNHJ-UHFFFAOYSA-N phthalic acid Chemical compound OC(=O)C1=CC=CC=C1C(O)=O XNGIFLGASWRNHJ-UHFFFAOYSA-N 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 229920002503 polyoxyethylene-polyoxypropylene Polymers 0.000 description 2
- BWHMMNNQKKPAPP-UHFFFAOYSA-L potassium carbonate Chemical compound [K+].[K+].[O-]C([O-])=O BWHMMNNQKKPAPP-UHFFFAOYSA-L 0.000 description 2
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 229930195734 saturated hydrocarbon Natural products 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- KDYFGRWQOYBRFD-UHFFFAOYSA-N succinic acid Chemical compound OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 229920001059 synthetic polymer Polymers 0.000 description 2
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- ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000000419 plant extract Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000166 polytrimethylene carbonate Polymers 0.000 description 1
- 229920002717 polyvinylpyridine Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 229910000027 potassium carbonate Inorganic materials 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 239000003380 propellant Substances 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 229940045944 sodium lauroyl glutamate Drugs 0.000 description 1
- 229940075560 sodium lauryl sulfoacetate Drugs 0.000 description 1
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- CAVXVRQDZKMZDB-UHFFFAOYSA-M sodium;2-[dodecanoyl(methyl)amino]ethanesulfonate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CCS([O-])(=O)=O CAVXVRQDZKMZDB-UHFFFAOYSA-M 0.000 description 1
- UAJTZZNRJCKXJN-UHFFFAOYSA-M sodium;2-dodecoxy-2-oxoethanesulfonate Chemical compound [Na+].CCCCCCCCCCCCOC(=O)CS([O-])(=O)=O UAJTZZNRJCKXJN-UHFFFAOYSA-M 0.000 description 1
- HFQQZARZPUDIFP-UHFFFAOYSA-M sodium;2-dodecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O HFQQZARZPUDIFP-UHFFFAOYSA-M 0.000 description 1
- RUTSRVMUIGMTHJ-UHFFFAOYSA-M sodium;tetradec-1-ene-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCC=CS([O-])(=O)=O RUTSRVMUIGMTHJ-UHFFFAOYSA-M 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- SFVFIFLLYFPGHH-UHFFFAOYSA-M stearalkonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CC1=CC=CC=C1 SFVFIFLLYFPGHH-UHFFFAOYSA-M 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
- 239000001384 succinic acid Substances 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000000057 synthetic resin Substances 0.000 description 1
- 229920003002 synthetic resin Polymers 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- WHNFPRLDDSXQCL-UAZQEYIDSA-N α-msh Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(N)=O)NC(=O)[C@H](CO)NC(C)=O)C1=CC=C(O)C=C1 WHNFPRLDDSXQCL-UAZQEYIDSA-N 0.000 description 1
Landscapes
- Cosmetics (AREA)
- Disinfection, Sterilisation Or Deodorisation Of Air (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分４〕
本発明は、アミン臭およびメルカプト臭のいずれに対し
ても優れた脱臭効果を発揮し、かつ水溶性で、しかも皮
膚、粘膜などに対する刺激性が少なく、安全性が高い脱
臭剤組成物に関する。Detailed Description of the Invention [Industrial Application 4] The present invention exhibits an excellent deodorizing effect against both amine odor and mercapto odor, is water-soluble, and is non-irritating to the skin, mucous membranes, etc. The present invention relates to a deodorizing composition that has low toxicity and high safety.
悪臭を発生する主たる物質としては、トリメチルアミン
やアンモニアなどの低分子のアミン類とエチルメルカプ
タンや硫化水素などの低分子のメルカプト化合物が挙げ
られる。The main substances that generate bad odors include low-molecular amines such as trimethylamine and ammonia, and low-molecular mercapto compounds such as ethyl mercaptan and hydrogen sulfide.
しかしながら、これら低分子のアミン類から発生する悪
臭（アミン臭）と低分子のメルカプト化合物から発生す
る悪臭（メルカプト臭）の両方に対して優れた脱臭効果
を発揮する脱臭剤は少ない。However, there are few deodorizing agents that exhibit excellent deodorizing effects against both the bad odor (amine odor) generated from these low-molecular amines and the bad odor (mercapto odor) generated from low-molecular mercapto compounds.
すなわち、従来の脱臭剤は、塩基性物質から発生する悪
臭に対しては酸性物質を施して中和し、酸性物質から発
生する悪臭に対しては塩基性物質を施して中和すること
により、脱臭するものであるが、このような化学的な中
和反応を利用した脱臭剤では、メルカプト化合物のよう
に中性物質から発生する悪臭に対して、はとんど効果を
発揮できない、また、上記のような化学的中和反応を利
用した脱臭剤以外に、活性炭やシリカゲルのように吸着
作用を利用した脱臭剤もあるが、活性炭の場合、物質に
よっては、アミン臭、メルカプト臭のいずれに対しても
脱臭効果を発揮するものの、アンモニアや硫化水素など
のように分子が小さいものに対しては脱臭効果が悪いと
いうように、脱臭能力に選択性があり、一方、シリカゲ
ルの場合は総じて脱臭能力が小さく、これらも充分に満
足すべきものとはいえなかった。In other words, conventional deodorizers neutralize bad odors generated by basic substances by applying acidic substances, and neutralize bad odors generated by acidic substances by applying basic substances. However, deodorizing agents that utilize such chemical neutralization reactions are rarely effective against bad odors generated from neutral substances such as mercapto compounds; In addition to deodorizing agents that utilize chemical neutralization reactions as described above, there are also deodorizing agents that utilize adsorption, such as activated carbon and silica gel. Although silica gel has a deodorizing effect against substances with small molecules such as ammonia and hydrogen sulfide, its deodorizing ability is selective, such as having a poor deodorizing effect against substances with small molecules such as ammonia and hydrogen sulfide. Its capabilities were small, and these could not be said to be fully satisfactory.
また、水に容易に溶解し、かつ人体に対して悪影響を及
ぼさず、しかもアミン臭およびメルカプト臭の両方に対
して有効に作用し、例えばパーマネントウェーブ処理後
の毛髪の脱臭にも使用できるような脱臭剤はさらに少な
い、つまり、パーマネントウェーブ用第１剤には、チオ
グリコール酸、チオグリコール酸アンモニウムなどのメ
ルカプト化合物とｐＨ調整のためのアンモニア、モノエ
タノールアミンなどが含まれているので、パーマネント
ウェーブ処理後の毛髪はメルカプト臭とアミン臭が入り
混じっており、この脱臭にはメルカプト臭とアミン臭の
両方に対して有効に作用し、しかも水に容易に溶解して
水溶液状で毛髪に使用することができ、かつ安全性の高
いものでなければならない、したがって、このパーマネ
ントウェーブ処理後の毛髪の脱臭に際しては、たとえア
ミン臭およびメルカプト臭に対する脱臭効果が優れてい
ても、水に溶けないものや皮膚や粘膜に対して刺激性が
あって安全性に欠けるものは使用することができず、こ
のようなパーマネントウェーブ処理後の毛髪の脱臭に使
用できるような脱臭剤で効果の優れたものはほとんど見
当たらない。In addition, it easily dissolves in water, has no adverse effects on the human body, and is effective against both amine and mercapto odors, and can be used, for example, to deodorize hair after permanent waving. The number of deodorizers is even less; in other words, the first agent for permanent wave contains mercapto compounds such as thioglycolic acid and ammonium thioglycolate, as well as ammonia and monoethanolamine for pH adjustment, so it is difficult to use for permanent wave. After treatment, hair contains a mixture of mercapto and amine odors, and this deodorizing agent is effective against both mercapto and amine odors, and it dissolves easily in water and can be used on hair in the form of an aqueous solution. Therefore, when deodorizing hair after this permanent wave treatment, even if the deodorizing effect against amine odor and mercapto odor is excellent, it is necessary to use products that are insoluble in water or Products that are irritating to the skin and mucous membranes and lack safety cannot be used, and there are very few highly effective deodorizers that can be used to deodorize hair after permanent waving. Not found.
例えば、これまでに提案された脱臭剤では、特公昭６１
−４８３７９号公報に示される脱臭剤が、平均分子Ｉｔ
２００〜５，０００のケラチン加水分解物を脱臭基剤
として含有したもので、比較的上記のような制約された
条件下でも使用できるものであるが、それでも、効果が
充分といえず、より効果の優れた脱臭剤の出現が望まれ
ている。For example, in the deodorizing agents proposed so far,
The deodorizer disclosed in Japanese Patent No. 48379 has an average molecular weight of It
It contains keratin hydrolyzate of 200 to 5,000 as a deodorizing base, and can be used even under relatively restricted conditions as mentioned above, but even so, it cannot be said to be sufficiently effective, and more effective It is hoped that an excellent deodorizing agent will emerge.
本発明は、上記したように、従来の脱臭剤が、たとえア
ミン臭の脱臭に対しては有効に作用しても、メルカプト
臭の脱臭に際しては有効でなく、また、アミン臭および
メルカプト臭の両方の脱臭に作用するものも、その性能
面において必ずしも満足すべき結果が得られなかったと
いう問題点を解決し、アミン臭およびメルカプト臭のい
ずれに対しても優れた脱臭効果を発揮し、しかも水に容
易に溶解し、かつ皮膚や粘膜に対する刺激性が少なく、
安全性の高い脱臭剤組成物を提供することを目的とする
。As described above, the present invention provides a method of deodorizing agents that, even if they are effective in deodorizing amine odor, they are not effective in deodorizing mercapto odor, and that they are effective in deodorizing both amine odor and mercapto odor. This solution solves the problem of not always achieving satisfactory results in terms of performance with deodorizing products that act on deodorizing products. It dissolves easily in water and is less irritating to the skin and mucous membranes.
The purpose is to provide a highly safe deodorant composition.
本発明は、上記目的を達成するために種々研究を重ねた
結果、脱臭基剤としてケラチンペプチドのＮ−二塩基カ
ルボン酸モノアシル化誘導体を用いるときは、上記目的
が容易に達成されることを見出すことによって、完成さ
れたものである。As a result of various studies to achieve the above object, the present invention has found that the above object can be easily achieved when an N-dibasic carboxylic acid monoacylated derivative of keratin peptide is used as a deodorizing base. As a result, it has been completed.
すなわち、本発明は、一般式（ｆ） Ｍ、０ＯＣ−Ａ−Ｇｏ−ｆＮＨ−ＣＨ−Ｃｏ蹟ＯＭ。That is, the present invention provides general formula (f) M, 0OC-A-Go-fNH-CH-Co OM.
（式中、Ａは炭素数２〜６の炭化水素骨格を示し、Ｒは
ケラチンペプチドを構成するアミノ酸の側鎖を示す０Ｍ
、およびＭ２は、ＨまたはＮａ、Ｋ、Ｌｌ、Ｍｇ／２、
Ｃａ／２などのアルカリ金属あるいはアルカリ土類金属
、またはアンモニア、トリノチルアミン、トリエチルア
ミン、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−メチルプロパン
、２−アミノ−２−メチル−１，３−プロパンジオール
などの無機アミンあるいは有機アミン、またはアルギニ
ン、リジンなどの塩基性アミノ酸のオニウムを示し、Ｍ
ｌおよびＭ２は同一でもよく、また異なっていてもよい
、ｎは２〜３０である）で示されるＮ−二塩基カルボン
酸モノアシル化ケラチンペプチドを脱臭基剤として含有
することを特徴とする脱臭剤組成物に関する。(In the formula, A represents a hydrocarbon skeleton having 2 to 6 carbon atoms, and R represents the side chain of the amino acid constituting the keratin peptide.
, and M2 is H or Na, K, Ll, Mg/2,
Alkali metals or alkaline earth metals such as Ca/2, or ammonia, trinotylamine, triethylamine, monoethanolamine, jetanolamine, triethanolamine, 2-amino-2-methylpropane, 2-amino-2-methyl Indicates onium of inorganic amines or organic amines such as -1,3-propanediol, or basic amino acids such as arginine and lysine, and M
l and M2 may be the same or different, and n is 2 to 30) A deodorizing agent containing an N-dibasic carboxylic acid monoacylated keratin peptide as a deodorizing base. Regarding the composition.
上記一般式（１）で示されるＮ−二塩基カルボン酸モノ
アシル化ケラチンペプチドにおけるケラチンペプチド部
分は、その分子構造中にアミノ基などの塩基性基やカル
ボキシル基などの酸性基を有しており、またその各種ア
ミノ酸の側鎖も同様に塩基性基や酸性基を存していて、
これらの塩基性基や酸性基が悪臭物質と造塩して酸性物
質に基づく悪臭や塩基性物質に基づくアミン臭などを脱
臭する。そして、メルカプタンや硫化水素などのように
中性でメルカプト臭を発生する物質に対しては、ケラチ
ンペプチドを構成するシスチン（シスチンのジスルフィ
ド結合部分）が上記メルカプト臭を発生する物質のメル
カプト基と反応してメルカプト臭を脱臭する。したがっ
て、メルカプト臭の脱臭には、ケラチンペプチド中のシ
スチンが多い方が好ましく、本発明においては、上記一
般式（夏）で示される二塩基カルボン酸モノアシル化ケ
ラチンペプチドのケラチンペプチドを構成するアミノ酸
のうち、シスチンがハーフシスチンとして６．０モル％
以上含まれていることが望ましい。The keratin peptide moiety in the N-dibasic carboxylic acid monoacylated keratin peptide represented by the above general formula (1) has a basic group such as an amino group or an acidic group such as a carboxyl group in its molecular structure, In addition, the side chains of various amino acids similarly have basic groups and acidic groups.
These basic groups and acidic groups form salts with malodorous substances to deodorize malodors originating from acidic substances and amine odors originating from basic substances. For substances that are neutral and generate a mercapto odor, such as mercaptan and hydrogen sulfide, cystine (the disulfide bond of cystine) that constitutes the keratin peptide reacts with the mercapto group of the substance that generates the mercapto odor. to deodorize the mercapto odor. Therefore, for deodorizing mercapto odor, it is preferable that the keratin peptide contains more cystine, and in the present invention, the amino acids constituting the keratin peptide of the dibasic carboxylic acid monoacylated keratin peptide represented by the above general formula (summer) are Of this, cystine is 6.0 mol% as half cystine.
It is desirable to include the above.
そして、上記一般式（１）で示されるＮ−二塩基カルボ
ン酸モノアシル化ケラチンペプチドは、上記のようにア
ミン臭、メルカプト臭の脱臭に有用なケラチンペプチド
をアシル化したものであって、そのアシル化によって導
入されたカルボン酸（カルボキシル基）が、トリメチル
アミンやアンモニアなどのアミン臭を発生する低分子の
アミン類と造塩するので、これらアミン類から発生する
アミン臭に対する脱臭効果がさらに高まるとともに、そ
のアシル化によって導入された炭化水素骨格がエチルメ
ルカプタンや硫化水素などのメルカプト臭を発生する低
分子のメルカプト化合物に対して親和性を発揮し、ケラ
チンペプチドの有するメルカプト臭の脱臭効果をさらに
高めている。したがって、この一般式（Ｉ）で示される
Ｎ−二塩基カルボン酸モノアシル化ケラチンペプチドの
脱臭効果は、ケラチンペプチドそのものの脱臭効果より
さらに優れている。しかも、上記一般式（１）で示され
るＮ−二塩基カルボン酸モノアシル化ケラチンペプチド
は、そのケラチンペプチド部分が天然の蛋白質から誘導
されるものであって、皮膚、粘膜などに対する刺激が少
なく安全である。さらに、この一般式（１）で示される
Ｎ−二塩基カルボン酸モノアシル化ケラチンペプチドは
、そのケラチンペプチド部分がもともと水溶性であり、
それに加えて、アシル化によりさらに水溶性が高められ
ているので、水に容易に溶解する。したがって、水に溶
解させた水溶液状で使用することができる。The N-dibasic carboxylic acid monoacylated keratin peptide represented by the above general formula (1) is an acylated keratin peptide useful for deodorizing amine odor and mercapto odor as described above. The carboxylic acid (carboxyl group) introduced by the chemical reaction forms salts with low-molecular amines that generate amine odors such as trimethylamine and ammonia, which further enhances the deodorizing effect on amine odors generated from these amines. The hydrocarbon skeleton introduced by the acylation exhibits affinity for low-molecular-weight mercapto compounds that generate mercapto odor, such as ethyl mercaptan and hydrogen sulfide, further enhancing the deodorizing effect of mercapto odor possessed by keratin peptides. There is. Therefore, the deodorizing effect of the N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (I) is even better than that of the keratin peptide itself. In addition, the N-dibasic carboxylic acid monoacylated keratin peptide represented by the above general formula (1) is safe because its keratin peptide moiety is derived from natural protein, and it is less irritating to the skin, mucous membranes, etc. be. Furthermore, the N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (1) has a keratin peptide moiety that is originally water-soluble,
In addition, its water solubility is further enhanced by acylation, so it easily dissolves in water. Therefore, it can be used in the form of an aqueous solution dissolved in water.
しかも、パーマネントウェーブ処理時の毛髪の脱臭には
、この一般式（１）で示されるＮ−二塩基力ルボン酸モ
ノアシル化ケラチンペプチドは、そのケラチンペプチド
が毛髪の構成蛋白質であるケラチンと同様の化学構造を
有していて、両者の有するアミノ基やカルボキシル基が
互いに吸着するので、こ（Ｄ−ａ式（１）で示されるＮ
−二塩基力ルポン酸モノアシル化ケラチンペプチドは、
水溶解性ではあるが、水洗によって全部が毛髪上から洗
い流されるのではなく、一部が毛髪に吸着して毛髪上に
残って、毛髪を保護する。Moreover, the N-dibasic acid monoacylated keratin peptide represented by the general formula (1) is suitable for deodorizing hair during permanent waving. structure, and the amino groups and carboxyl groups of both adsorb to each other, so this (N represented by the D-a formula (1))
-Dibasic acid monoacylated keratin peptides are
Although it is water-soluble, not all of it is washed away from the hair by washing with water, but a portion of it is adsorbed to the hair and remains on the hair, protecting the hair.
上記一般式（１）で示されるＮ−二塩基カルボン酸モノ
アシル化ケラチンペプチドは、ケラチンペプチドと、下
記の一般式（ＩＩ）
し
（式中のＡは炭素数２〜６の炭化水素骨格を示す）で示
される二塩基カルボン酸無水物とを反応させることによ
って得られる。The N-dibasic carboxylic acid monoacylated keratin peptide represented by the above general formula (1) is composed of a keratin peptide and the following general formula (II) (where A represents a hydrocarbon skeleton having 2 to 6 carbon atoms). ) with dibasic carboxylic acid anhydride.
上記ケラチンペプチドは、羊毛、ヤギ毛、モヘア毛、ウ
サギ毛、カシミア毛などの獣毛、入毛、ニワトリ、ガチ
ツウ、アヒルなどの羽毛、羽根、爪、角、蹄、鱗のケラ
チン蛋白質などを、酸、アルカリまたは酵素で加水分解
することによって得られる。このようなケラチンペプチ
ドを得るための加水分解の詳細は、例えば特開昭５９−
８４８９８号公報に記載されている。The above-mentioned keratin peptides include animal hair such as wool, goat hair, mohair hair, rabbit hair, and cashmere hair; Obtained by hydrolysis with acids, alkalis or enzymes. Details of the hydrolysis to obtain such keratin peptides can be found in, for example, Japanese Patent Application Laid-Open No.
It is described in No. 84898.
上記一般式（１）において、ケラチンペプチド部分の側
鎖がＲ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、インロイシン、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、リジン、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、システィン、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結果の一例を示
すと第１表のとおりである。なお、第１表中にはアスパ
ラギンや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ケラチン中ではアスパ
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
。In the above general formula (1), the amino acids whose side chain of the keratin peptide moiety is represented by R include alanine, glycine, valine, leucine, inleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, Examples include lysine, aspartic acid, asparagine, glutamic acid, glutamine, cystine, cysteine, and tryptophan. Table 1 shows an example of the analysis results of the composition ratios of these amino acids. Note that asparagine and glutamine are not shown in Table 1, but this is because they were converted to aspartic acid and glutamic acid, respectively, during hydrolysis (completely hydrolyzed with 6N hydrochloric acid in the conventional method) prior to analysis. It is. In other words, aspartic acid and glutamic acid in Table 1 include those that existed as asparagine and glutamine in keratin.
また、シスチンはアミノ基およびカルボキシル基を２個
ずつ持っているので、第１表ではハーフシスチンとして
モル％を示している。また、トリプトファンは分析に先
だって行われる６Ｎ塩酸による完全加水分解の時に失わ
れるので、第１表中には示されていないが、ケラチン中
には約１モル％程度含まれている。Furthermore, since cystine has two amino groups and two carboxyl groups, Table 1 shows the mole % as half cystine. Also, tryptophan is lost during complete hydrolysis with 6N hydrochloric acid prior to analysis, so although it is not shown in Table 1, it is contained in keratin at about 1 mol%.
第
表
上記ケラチンペプチドを得るためのケラチンの加水分解
は、前記のように、酸、アルカリまたは酵素によって行
われる。The hydrolysis of keratin to obtain the above keratin peptides is carried out with acids, alkalis or enzymes as described above.
酸加水分解に際しては、塩酸、硫酸、リン酸、硝酸、臭
化水素酸などの無機酸、酢酸、ギ（蟻）酸などの有機酸
が用いられる。For acid hydrolysis, 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 are used.
アルカリ加水分解に際しては、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、炭酸リチウムなどが用いられ
る。ただし、アルカリ加水分解は、その加水分解時の条
件によって、シスチンが破壊されるおそれがあるため、
本発明においては、好ましい方法とはいえない。For alkaline hydrolysis, sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, etc. are used. However, alkaline hydrolysis may destroy cystine depending on the conditions during the hydrolysis, so
In the present invention, this method cannot be said to be a preferable method.
また、酵素による加水分解に際しては、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蛋白質分解
酵素などが使用される。また、スブチリシン、スタフィ
ロコッカスプロテアーゼなどの国産性の中性蛋白質分解
酵素も使用できる。酵素の使用に際しては、それらの菌
属性蛋白質分解酵素を含む菌体、あるいは酵素または酵
素を含む菌体を固定化した膜、粒体などの状態で使用に
供することもできる。For hydrolysis by enzymes, acidic proteolytic enzymes such as pepsin, proctase A and protase B, and neutral proteolytic enzymes such as papain, promelain, thermolysin, trypsin, pronase, and chymotrypsin are used. Additionally, domestically produced neutral proteolytic enzymes such as subtilisin and staphylococcal protease can also be used. When using enzymes, they can be used in the form of bacterial cells containing these fungal proteolytic enzymes, or in the form of membranes, granules, etc. in which enzymes or bacterial cells containing enzymes are immobilized.
上記のような酸、アルカリまたは酵素による加水分解に
よって得られるケラチンペプチドは、−般式＜１）にお
けるｎが２〜３０（ただし、ｎの値は平均値であり、ｎ
が２〜３０ということは平均分子量で約１５０〜約ｓ、
ｏｏｏに相当する）になるようにされる、これはｎが２
未満では脱臭効果、特にメルカプト臭に対する脱臭効果
が低下し、また、ｎが３０を超えると水溶性が低下して
取り扱いにくくなり、また脱臭効果も低下するからであ
る。The keratin peptide obtained by hydrolysis with an acid, alkali or an enzyme as described above has n in the general formula <1) of 2 to 30 (however, the value of n is an average value, and n
is 2 to 30, which means the average molecular weight is about 150 to about s,
ooo), which means that n is 2
If n is less than 30, the deodorizing effect, especially against mercapto odor, will be reduced, and if n exceeds 30, the water solubility will be reduced, making it difficult to handle, and the deodorizing effect will also be reduced.
一般式（１）で示されるＮ−二塩基カルボン酸モノアシ
ル化ケラチンペプチドは、前記のように、ケラチンペプ
チドと一般式（ＩＩ）で示される二塩基カルボン酸無水
物との反応によって得られるが、それらの反応式を示す
と次のとおりである。なお、反応式を示すにあたって、
ケラチンペプチドは、次の一般式（Ｉ［Ｉ）で示す。The N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (1) can be obtained by the reaction of the keratin peptide and the dibasic carboxylic acid anhydride represented by the general formula (II), as described above. Their reaction formulas are shown below. In addition, in showing the reaction formula,
The keratin peptide is represented by the following general formula (I[I).
Ｈ−４ＮＨ−ＣＨ−Ｃｏ籍ＯＨ
反応式：
上記ケラチンペプチドと、一般式（ｆｆ）で示される二
塩基カルボン酸無水物との反応は、通常、ケラチンペプ
チドの水溶液に一般式（ＩＩ）で示される二塩基カルボ
ン酸無水物の結晶を投入し、水中で両者を接触させるこ
とによって行われる０反応に際して反応系内のＰＨを８
〜１２、特に９〜１１に保つことが好ましく、そのため
に水酸化ナトリウム、水酸化カリウム、水酸化リチウム
などのアルカリ溶液を必要に応じて反応液中に滴下する
ことが行われる０反応時、反応系内のｐＨを前記の範囲
に維持するのは、ケラチンペプチドのアミノ基が一般式
（ＩＩ）で示される二塩基カルボン酸無水物と反応する
ためには、Ｊ）Ｈ８以上のアルカリ側であることが望ま
しく、またＰＨが１２を超えるとケラチンペプチドや一
般式（Ｉｔ）で示される二塩基カルボン酸無水物が加水
分解を起こすからである。反応は常温でも進行するが、
温度が高いほど反応は速くなる。しかし、ｐＨが高い状
態で温度が高くなると、一般式（Ｉｆ）で示される二塩
基カルボン酸無水物の加水分解も促進されるため、高く
ても８０’Ｃ以下にするのが好ましい、一般式（Ｉｔ）
で示される二塩基カルボン酸無水物は、通常、結晶で用
いるのが好ましい、結晶は細かい方がよいので砕いてか
ら用いてもよい、ケラチンペプチド溶液への一般式（Ｉ
Ｉ）で示される二塩基カルボン酸無水物の投入は、３０
分間〜６時間で終わるのが好ましい、そして、その一般
式（ＩＩ）で示される二塩基カルボン酸無水物の投入後
、さらに１〜２４時間反応を継続させるのが好ましい。H-4NH-CH-Co-based OH Reaction formula: The reaction between the above keratin peptide and the dibasic carboxylic acid anhydride represented by the general formula (ff) is usually carried out by adding an aqueous solution of the keratin peptide to the dibasic carboxylic acid anhydride represented by the general formula (II). During the zero reaction, the pH in the reaction system was set to 8 by adding crystals of dibasic carboxylic acid anhydride and bringing them into contact in water.
-12, especially 9-11, and for this purpose, an alkaline solution such as sodium hydroxide, potassium hydroxide, lithium hydroxide, etc. is added dropwise into the reaction solution as necessary. The pH within the system is maintained within the above range in order for the amino group of the keratin peptide to react with the dibasic carboxylic acid anhydride represented by the general formula (II). This is desirable, and also because if the pH exceeds 12, keratin peptides and dibasic carboxylic acid anhydrides represented by general formula (It) will undergo hydrolysis. The reaction proceeds even at room temperature, but
The higher the temperature, the faster the reaction. However, when the temperature is high under a high pH state, the hydrolysis of the dibasic carboxylic acid anhydride represented by the general formula (If) is also promoted, so it is preferable to keep the temperature at most 80'C or less, the general formula (It)
It is usually preferable to use the dibasic carboxylic acid anhydride represented by the formula (I) in the keratin peptide solution.
The input of the dibasic carboxylic acid anhydride represented by I) is 30
The reaction is preferably completed within minutes to 6 hours, and the reaction is preferably continued for an additional 1 to 24 hours after the addition of the dibasic carboxylic acid anhydride represented by general formula (II).
上記反応においては、反応によってカルボキシル基が生
成して反応液のｐＨが低下するので、アルカリを反応の
開始と同時に滴下し、攪拌して液中のｐＨを反応に適す
る範囲に維持することが必要である。In the above reaction, carboxyl groups are generated by the reaction and the pH of the reaction solution decreases, so it is necessary to drop an alkali at the same time as the reaction starts and stir to maintain the pH in the solution within a range suitable for the reaction. It is.
反応の進行と終了は、アミノ基への反応についてファン
・スレータ（Ｖａｎ ５ｌｙｋｅ）法により、反応液中
のケラチンペプチドのアミノ態チッ素を測定することに
よって確認することができる０反応が終了したのち、反
応液は、適宜、濃縮あるいはイオン交換樹脂、ゲル濾過
、電気透析などによって精製した上で、濃縮して、反応
生成物を固体あるいは濃縮液の状態で得ることができる
。The progress and completion of the reaction can be confirmed by measuring the amino nitrogen of the keratin peptide in the reaction solution using the Van Slater method for the reaction to amino groups. The reaction solution can be appropriately concentrated or purified by ion exchange resin, gel filtration, electrodialysis, etc., and then concentrated to obtain a reaction product in the form of a solid or a concentrated liquid.
上記のように、ケラチンペプチドとの反応に使用される
一般式（ｎ）で示される二塩基カルボン酸無水物につい
て、その具体例を示すと、例えば、無水コハク酸、無水
マレイン酸、無水フタル酸、シス−１，２−シクロヘキ
サンジカルボン酸無水物、シス−４−シクロヘキセン−
１，２−ジカルボン酸無水物などである。なお、一般式
（１）および一般式（■）中の炭化水素骨格を示すＡは
、飽和炭化水素、不飽和炭化水素、芳香族炭化水素、環
式不飽和炭化水素、環式飽和炭化水素のいずれであって
もよい。As mentioned above, specific examples of the dibasic carboxylic anhydride represented by the general formula (n) used in the reaction with the keratin peptide include succinic anhydride, maleic anhydride, phthalic anhydride, etc. , cis-1,2-cyclohexanedicarboxylic anhydride, cis-4-cyclohexene-
1,2-dicarboxylic acid anhydride and the like. In addition, A indicating a hydrocarbon skeleton in the general formula (1) and the general formula (■) is a saturated hydrocarbon, an unsaturated hydrocarbon, an aromatic hydrocarbon, a cyclic unsaturated hydrocarbon, or a cyclic saturated hydrocarbon. It may be either.
本発明の脱臭剤組成物は、脱臭基剤、つまり脱臭にあた
って有効に作用する一般式（１）で示されるＮ−二塩基
カルボン酸モノアシル化ケラチンペプチドを、脱臭剤組
成物に通常採用されている形態、例えば、水、有機溶剤
などに溶解するか、または界面活性剤、乳化剤などによ
って乳化させた液状脱臭剤、上記液状脱臭剤を噴射剤と
ともにスプレー容器に充填したエアゾール型脱臭剤、ゲ
ル状条ｍ類、ポリエチレングリコールなどの天然または
合成高分子からなるゲル化剤に添加してゲル状にしたゲ
ル状脱臭剤、布状、粉末状、粒状などの多孔性物質に吸
着させ、または合成樹脂とともに固体状にした固体状脱
臭剤などの形態に調製される。また、一般式（１）で示
されるＮ−二塩基カルボン酸モノアシル化ケラチンペプ
チドをそのまま固体状で用いることもできる。The deodorizing composition of the present invention uses a deodorizing base, that is, an N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (1) which acts effectively in deodorizing, which is usually employed in deodorant compositions. For example, liquid deodorizers dissolved in water, organic solvents, etc., or emulsified with surfactants, emulsifiers, etc., aerosol type deodorizers filled with the above liquid deodorizers together with a propellant in a spray container, and gel-like strips. Gel-like deodorizers made by adding gelling agents made of natural or synthetic polymers such as Class M, polyethylene glycol, adsorbed onto porous materials such as cloth, powder, and granules, or together with synthetic resins. It is prepared in the form of a solid deodorizer. Further, the N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (1) can also be used as it is in solid form.
そして、上記組成物には、必要に応じて、水、溶剤、ｐ
Ｈ調整剤、香料、防腐剤、着色料などを適宜添加するこ
とができる。また、パーマネントウェーブ時など、毛髪
に関連した脱臭に応用する場合には、通常の毛髪用化粧
品に配合される種々の成分を添加することができる。こ
のような成分としては、例えば、ラウリル硫酸アンモニ
ウム、ラウリル硫酸エタノールアミン、ラウリル硫酸ナ
トリウム、ラウリル硫酸トリエタノールアミンなどのア
ルキル硫酸塩、ポリオキシエチレン（２ＥＯ）ラウリル
−チル硫酸トリエタノールアミン（なお、ＥＯはエチレ
ンオキサイドで、ＥＯの前の数値はエチレンオキサイド
の付加モル数を示す）、ポリオキシエチレン（３ＥＯ）
アルキル（炭素数１１〜１５のいずれかまたは２種以上
の混合物）エーテル硫酸ナトリウムなどのポリオキシエ
チレンアルキルエーテル硫酸塩、ラウリルベンゼンスル
ホン酸ナトリウム、ラウリルベンゼンスルホン酸トリエ
タノールアミンなどのアルキルベンゼンスルホン酸塩、
ポリオキシエチレン（３ＥＯ）トリデシルエーテル酢酸
ナトリウムなどのポリオキシエチレンアルキルエーテル
酢酸塩、ヤシ油脂肪酸サルコシンナトリウム、ラウロイ
ルサルコシントリエタノールアミン、ラウロイルメチル
−β−アラニンナトリウム、ラウロイル−し−グルタミ
ン酸ナトリウム、ラウロイル−Ｌ−グルタミン酸トリエ
タノールアミン、ヤシ油脂肪酸−Ｌ−グルタミン酸ナト
リウム、ヤシ油脂肪酸−Ｌ−グルタミン酸トリエタノー
ルアミン、ヤシ油脂肪酸メチルタウリンナトリウム、ラ
ウロイルメチルタウリンナトリウムなどのＮ−アシルア
ミノ酸塩、エーテル硫酸アルカンスルホン酸ナトリウム
、硬化ヤシ油脂肪酸グリセリン硫酸ナトリウム、ランデ
シレノイルアミドエチルスルホコハク酸二ナトリウム、
オクチルフェノキシジェトキシエチルスルホン酸ナトリ
ウム、オレイン酸アミドスルホコハク酸ニナトリウム、
スルホコハク酸ジオクチルナトリウム、スルホコハク酸
うウリルニナトリウム、ポリオキシエチレンアルキル（
炭素数１２〜１５）エーテルリン酸（８〜１０Ｅ）、ポ
リオキシエチレンオレイルエーテルリン酸ナトリウム、
ポリオキシエチレンセチルエーテルリン酸ナトリウム、
ポリオキシエチレンスルホコハク酸うウリルニナトリウ
ム、ポリオキシエチレンラウリルエーテルリン酸ナトリ
ウム、ラウリルスルホ酢酸ナトリウム、テトラデセンス
ルホン酸ナトリウムなどのアニオン性界面活性剤、塩化
ジステアリルジメチルアンモニウム、塩化ジポリオキシ
エチレンオレイルメチルアンモニウム、塩化ステアリル
ジメチルベンジルアンモニウム、塩化ステアリルトリメ
チルアンモニウム、塩化セチルトリメチルアンモニウム
、塩化トリ （ポリオキシエチレン）ステアリルアンモ
ニウム、塩化ポリオキシプロピレンメチルジエチルアン
モニウム、塩化ミリスチルジメチルベンジルアンモニウ
ム、塩化ラウリルトリメチルアンモニウムなどのカチオ
ン性界面活性剤、２−アルキル−Ｎ−カルボキシメチル
−Ｎ−ヒドロキシエチルイミダゾリニウムベタイン、ウ
ンデシルヒドロキシエチルイミダゾリウムベタインナト
リウム、ウンデシル−Ｎ−ヒドロキシエチル−Ｎ−カル
ポキシメヂルイミダプリニウムベタイン、ステアリルジ
ヒドロキシエチルベタイン、ステアリルジメチルアミノ
酢酸ベタイン、ヤシ油アルキルベタイン、ヤシ油脂肪酸
アミドプロピルベタイン、ヤシ油アルキルＮ−カルボキ
シエチル−Ｎ−ヒドロキシエチルイミダゾリニウムベタ
インナトリウム、ヤシ油アルキルＮ−カルボキシエトキ
シエチル−Ｎ−カルボキシエチルイミダゾリニウムジナ
トリウムヒドロキシド、ヤシ油アルキルＮ−カルボキシ
メトキシエチル−Ｎ−力ルボキシメチルイミダゾリニウ
ムジナトリウムラウリル硫酸、Ｎ−ヤシ油脂肪酸アシル
し一アルギニンエチル・ＤＬ−ピロＩＪ Ｆンカルボン
酸塩などの両性界面活性剤、ポリオキシエチレンアルキ
ル（炭素数１２〜１４）エーテル（７ＥＯ）、ポリオキ
エチレンオクチルフェニルエーテル、ポリオキシエチレ
ンオレイルエーテル、ポリオキシエチレンオレイン酸グ
リセリル、ポリオキシエチレンステアリルエーテル、ポ
リオキシエチレンセチルエーテル、ポリオキシエチレン
セチルステアリルジエーテル、ポリオキシエチレンソル
ビトール・ラノリン（４０ＥＯ）、ポリオキシエチレン
ノニルフェニルエーテル、ポリオキシエチレンポリオキ
シプロピレンセチルエーテル、ポリオキシエチレンポリ
オキシプロピレンデシルテトラデシルエーテル、ポリオ
キシエチレンラノリン、ポリオキシエチレンラノリンア
ルコール、ポリオキシプロピレンステアリルエーテルな
どのノニオン性界面活性剤、カチオン化セルロース、カ
チオン化ヒドロキシエチルセルロース、ポリ （塩化シ
アリルジメチルアンモニウム）、ポリビニルピリジン、
ポリエチレンイミンなどのカチオン性ポリマー、両性ポ
リマー、アニオン性ポリマーなどの合成ポリマー、イソ
ステアリン酸ジェタノールアミド、ウンデシレン酸モノ
エタノールアミド、オレイン酸ジェタノールアミド、牛
脂肪酸モノエタノールアミド、硬化牛脂肪酸ジェタノー
ルアミド、ステアリン酸ジェタノールアミド、ステアリ
ン酸ジエチルアミノエチルアミド、ステアリン酸モノエ
タノールアミド、ミリスチン酸ジェタノールアミド、ヤ
シ油脂肪酸エタノールアミド、ヤシ油脂肪酸ジェタノー
ルアミド、ラウリン酸インプロパツールアミド、ラウリ
ン酸エタノールアミド、ラウリン酸ジェタノールアミド
、ラノリン脂肪酸ジェタノールアミドなどの増粘剤、動
植物抽出物、ポリサッカライドまたはその誘導体、プロ
ピレングリコール、■、３−ブチレングリコール、エチ
レングリコール、グリセリン、ポリエチレングリコール
などの湿潤剤、エタノール、メタノール、プロピルアル
コール、イソプロピルアルコールなどの低級アルコール
類、Ｌ−アスパラギン酸、Ｌアスパラギン酸ナトリウム
、ＤＬ−アラニン、Ｌアルギニン、グリシン、Ｌ−グル
タミン酸、Ｌシスティン、Ｌ−スレオニンなどのアミノ
酸などをあげることができる。The above composition may contain water, a solvent, p
H regulators, fragrances, preservatives, colorants, etc. can be added as appropriate. Furthermore, when applied to hair-related deodorization such as during permanent waving, various ingredients that are included in ordinary hair cosmetics can be added. Examples of such components include alkyl sulfates such as ammonium lauryl sulfate, ethanolamine lauryl sulfate, sodium lauryl sulfate, triethanolamine lauryl sulfate, polyoxyethylene (2EO) lauryl-triethanolamine sulfate (EO is (In ethylene oxide, the number before EO indicates the number of added moles of ethylene oxide), polyoxyethylene (3EO)
Alkyl (having 11 to 15 carbon atoms or a mixture of two or more) polyoxyethylene alkyl ether sulfates such as sodium ether sulfate; alkylbenzenesulfonates such as sodium laurylbenzenesulfonate and triethanolamine laurylbenzenesulfonate;
Polyoxyethylene alkyl ether acetate such as polyoxyethylene (3EO) sodium tridecyl ether acetate, sodium coconut oil sarcosine, lauroyl sarcosine triethanolamine, sodium lauroyl methyl-β-alanine, sodium lauroyl-glutamate, lauroyl- N-acylamino acid salts such as L-glutamic acid triethanolamine, coconut oil fatty acid-sodium L-glutamate, coconut oil fatty acid-L-glutamic acid triethanolamine, sodium coconut oil fatty acid methyltaurate, sodium lauroylmethyltaurate, alkanesulfone ether sulfate acid sodium, hydrogenated coconut fatty acid glycerol sodium sulfate, disodium landecylenoylamide ethyl sulfosuccinate,
Sodium octylphenoxyjethoxyethyl sulfonate, disodium oleic acid amide sulfosuccinate,
Dioctyl sodium sulfosuccinate, uryl disodium sulfosuccinate, polyoxyethylene alkyl (
carbon number 12-15) ether phosphoric acid (8-10E), polyoxyethylene oleyl ether sodium phosphate,
Sodium polyoxyethylene cetyl ether phosphate,
Anionic surfactants such as uryl disodium polyoxyethylene sulfosuccinate, sodium polyoxyethylene lauryl ether phosphate, sodium lauryl sulfoacetate, sodium tetradecene sulfonate, distearyl dimethyl ammonium chloride, dipolyoxyethylene oleyl methyl chloride Cationic compounds such as ammonium, stearyldimethylbenzylammonium chloride, stearyltrimethylammonium chloride, cetyltrimethylammonium chloride, tri(polyoxyethylene)stearylammonium chloride, polyoxypropylenemethyldiethylammonium chloride, myristyldimethylbenzylammonium chloride, lauryltrimethylammonium chloride Surfactant, 2-alkyl-N-carboxymethyl-N-hydroxyethylimidazolinium betaine, undecylhydroxyethylimidazolium betaine sodium, undecyl-N-hydroxyethyl-N-carpoxymedylimidapurinium betaine, stearyl Dihydroxyethyl betaine, stearyldimethylaminoacetic acid betaine, coconut oil alkyl betaine, coconut oil fatty acid amidopropyl betaine, coconut oil alkyl N-carboxyethyl-N-hydroxyethylimidazolinium betaine sodium, coconut oil alkyl N-carboxyethoxyethyl-N -Carboxyethyl imidazolinium disodium hydroxide, coconut oil alkyl N-carboxymethoxyethyl-N-carboxymethyl imidazolinium disodium lauryl sulfate, N-coco fatty acid acyl monoarginine ethyl DL-pyro IJ F amphoteric surfactants such as carboxylic acid salts, polyoxyethylene alkyl (C12-14) ether (7EO), polyoxyethylene octylphenyl ether, polyoxyethylene oleyl ether, polyoxyethylene glyceryl oleate, polyoxyethylene stearyl Ether, polyoxyethylene cetyl ether, polyoxyethylene cetyl stearyl diether, polyoxyethylene sorbitol lanolin (40EO), polyoxyethylene nonylphenyl ether, polyoxyethylene polyoxypropylene cetyl ether, polyoxyethylene polyoxypropylene decyl tetra Nonionic surfactants such as decyl ether, polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, polyoxypropylene stearyl ether, cationized cellulose, cationized hydroxyethyl cellulose, poly(sialyldimethylammonium chloride), polyvinylpyridine,
Cationic polymers such as polyethyleneimine, amphoteric polymers, synthetic polymers such as anionic polymers, isostearic acid jetanolamide, undecylenic acid monoethanolamide, oleic acid jetanolamide, bovine fatty acid monoethanolamide, hydrogenated bovine fatty acid jetanolamide, Stearic acid jetanolamide, stearic acid diethylaminoethylamide, stearic acid monoethanolamide, myristic acid jetanolamide, coconut oil fatty acid ethanolamide, coconut oil fatty acid jetanolamide, lauric acid impropaturamide, lauric acid ethanolamide, lauric acid Thickeners such as acid jetanolamide, lanolin fatty acid jetanolamide, animal and plant extracts, polysaccharides or their derivatives, wetting agents such as propylene glycol, 3-butylene glycol, ethylene glycol, glycerin, polyethylene glycol, ethanol, Examples include lower alcohols such as methanol, propyl alcohol, and isopropyl alcohol, and amino acids such as L-aspartic acid, sodium L-aspartate, DL-alanine, L-arginine, glycine, L-glutamic acid, L-cysteine, and L-threonine. can.
本発明の脱臭剤組成物を使用する場合、その使用量は悪
臭の強さおよび種類によって異なり、脱臭基剤としての
一般式（１）で示されるＮ−二基基カルボン酸モノアシ
ル化ケラチンペプチドの濃度が被処理系中、通常、０．
０１重量％、特に０．１重量％以上となるようにするの
が好ましい、したがって、脱臭剤組成物中における一般
式（１）で示されるＮ−二基基カルボン酸モノアシル化
ケラチンペプチドの含有量は、０．１〜１００重量％、
特に１−３０重重量とするのが好ましい。When using the deodorizing composition of the present invention, the amount used varies depending on the strength and type of malodor, and the amount of the deodorizing composition differs depending on the strength and type of malodor. The concentration in the treated system is usually 0.
Therefore, the content of the N-di-group carboxylic acid monoacylated keratin peptide represented by the general formula (1) in the deodorant composition is preferably set to 0.01% by weight, particularly 0.1% by weight or more. is 0.1 to 100% by weight,
In particular, it is preferable to set it as 1-30 weight.
本発明の脱臭剤組成物は、酸性またはアルカリ性のｐＨ
調整剤を用いて、広いｐＨ？＋Ｉ域、例えばｐＨ０，５
〜１０、好ましくはｐＨ１〜６に調整し、使用すること
ができる１本発明の脱臭剤組成物の使用にあたって、上
記のように、ｐＨを１〜６の範囲に調整するのが好まし
いというのは、そのように酸性側に調整することによっ
てアミノ臭に対する脱臭効果がより向上するからである
。The deodorizing composition of the present invention has an acidic or alkaline pH.
Wide range of pH using adjusting agent? +I range, e.g. pH 0.5
~10, preferably adjusted to pH 1 to 6, and used 1. When using the deodorizing composition of the present invention, as mentioned above, it is preferable to adjust the pH to a range of 1 to 6. This is because the deodorizing effect on amino odor is further improved by adjusting the acidity in this way.
また、本発明の脱臭剤組成物中に、掻く少量の銅イオン
などの重金属イオンが含有されるようにしておくと、メ
ルカプタン類に対する脱臭効果がさらに向上する。すな
わち、銅などの２種以上のイオン価をとり得る金属は、
メルカプタン類のメルカプト基が空気酸化してジチオ化
合物となる過程に触媒として働く作用がある。そのため
、本発明の脱臭剤組成物中に銅イオンなどの重金属イオ
ンが微量でも存在すると、脱臭すべき対象であるメルカ
プタン類と該メルカプタン類に反応して生成したＮ−二
塩基カルボン酸モノアシル化ケラチンペブチドの還元体
との酸化が促進され、脱臭効果がさらに向上する。これ
ら銅イオンなどの重金属イオンは脱臭剤組成物中に０．
１〜１００ｐｐ＋ｓ程度存在していればよい、これら銅
イオンなどの重金属イオンは、０． ｌｐｐｍ程度であ
れば、通常、脱臭剤組成物を調製する際に自然に混入す
るが、効果を上げるためには、例えば硫酸銅などの塩の
形で銅イオンなどの重金属イオンを添加して濃度を高め
るようにすればよい、しかし、濃度が１００ｐｐ■を超
えるようになるとそれ以上の効果の増加は期待できない
、なお、本発明の脱臭剤組成物によって悪臭を脱臭した
結果、悪臭が消失するので、「消臭」という表現の方が
適切な場合もあるが、本明細書では、「脱臭」という表
現で統一した。また、本発明の脱臭剤組成物は悪臭を脱
臭するので、当然、防臭効果も有している。Further, when the deodorizing composition of the present invention contains a small amount of heavy metal ions such as copper ions, the deodorizing effect on mercaptans is further improved. In other words, metals such as copper that can have two or more ionic valences are
It acts as a catalyst in the process of air oxidation of the mercapto group of mercaptans to form dithio compounds. Therefore, if even trace amounts of heavy metal ions such as copper ions are present in the deodorizing composition of the present invention, the mercaptans to be deodorized and the N-dibasic carboxylic acid monoacylated keratin peptides produced by the reaction with the mercaptans. oxidation with the reduced form is promoted, further improving the deodorizing effect. These heavy metal ions such as copper ions are contained in the deodorizing composition at 0.0%.
These heavy metal ions such as copper ions only need to exist in an amount of about 1 to 100 pp+s. If it is about lppm, it is usually mixed naturally when preparing a deodorizing composition, but in order to increase the effect, it is necessary to add heavy metal ions such as copper ions in the form of a salt such as copper sulfate to increase the concentration. However, if the concentration exceeds 100 pp■, no further increase in effectiveness can be expected. Note that as a result of deodorizing the malodor with the deodorant composition of the present invention, the malodor disappears. In some cases, the expression "deodorization" is more appropriate, but in this specification, the expression "deodorization" is unified. Further, since the deodorizing composition of the present invention deodorizes bad odors, it naturally also has a deodorizing effect.
〔実施例〕
以下、実施例をあげて本発明を説明するが、本発明は実
施例のみに限定されるものではない、なお、実施例に先
立って実施例で用いるＮ−二塩基カルボン酸モノアシル
化ケラチンペプチドの合成例を参考例として示す。[Examples] Hereinafter, the present invention will be explained with reference to Examples, but the present invention is not limited only to the Examples. An example of synthesis of a chemically modified keratin peptide is shown as a reference example.
参考例１
羊毛を塩酸で加水分解することによって得たケラチンペ
プチド（ｎ（一般式（ＩＩＩ）におけるｎ）−５ただし
、ｎは平均値であり、以下においてもｎはいずれも平均
値である。なお、このケラチンペプチドのシスチン含有
量はハーフシスチンとして１０００モル％である。〕の
２５％水溶液ｓｏｏ ｇを攪拌下で加温して５０℃に保
ち、その中に無水マレイン酸１００ ｇを１時間で投入
した。この間、反応液のｐＨを２０％水酸化ナトリウム
水溶液を用いてｐＨ９゜５に保った。５０°Ｃで３時間
攪拌したのち、５０°Ｃに保ったまま２４時間静置して
反応を終了した。反応液をｐＨ７に中和し、電気透析に
よって、副生じたマレイン酸のナトリウム塩を除去した
のち、減圧濃縮し、Ｎ−二塩基カルボン酸モノアシル化
ケラチンペプチドとしてのＮ−マレオイルケラチンペプ
チドの３０％水溶液を得た。このＮ−マレオイルケラチ
ンペプチドのアミノ酸分析を行ったところ、ケラチンペ
プチドを構成するアミノ酸中のシスチン含有量はハーフ
シスチンとして９．８モル％であった。Reference Example 1 Keratin peptide (n (n in general formula (III))-5 obtained by hydrolyzing wool with hydrochloric acid. However, n is an average value, and in the following, all n are average values. The cystine content of this keratin peptide is 1000 mol% as half-cystine.] A 25% aqueous solution of soo g was heated under stirring and kept at 50°C, and 100 g of maleic anhydride was added thereto for 1 hour. During this time, the pH of the reaction solution was maintained at 9.5 using a 20% aqueous sodium hydroxide solution.After stirring at 50°C for 3 hours, the reaction solution was left standing at 50°C for 24 hours. The reaction was completed.The reaction solution was neutralized to pH 7, the by-produced sodium salt of maleic acid was removed by electrodialysis, and then concentrated under reduced pressure to obtain N-male as an N-dibasic carboxylic acid monoacylated keratin peptide. A 30% aqueous solution of oil keratin peptide was obtained. Amino acid analysis of this N-maleoyl keratin peptide revealed that the cystine content in the amino acids constituting the keratin peptide was 9.8 mol % as half cystine.
得られた生成物がＮ−マレオイルケラチンペプチドであ
ることは、次の（１）および（２）によって１１！！し
た。The obtained product is an N-maleoyl keratin peptide based on the following (1) and (2) 11! ! did.
（１）反応前のケラチンペプチドのアミノ態チッ素の総
量と反応生成物のアミノ態チッ素の総量をファンスレー
ク法（Ｖａｎ ５ｌｙｋｅ）によって測定したところ、
反応前のケラチンペプチドのアミノ態チッ素の総量は４
２１ミリモルで、反応生成物のアミノ態チッ素の総量は
３４ミリモルであり、反応によってアミノ態チッ素が減
少していた。このアミノ態チッ素の減少は、ケラチンペ
プチド中のアミノ基が無水マレイン酸と反応したことを
示しており、そのアミノ態チッ素の減少量から、ケラチ
ンペプチドのアミノ態チッ素の９２％が反応しているこ
とがわかる。(1) The total amount of amino nitrogen in the keratin peptide before the reaction and the total amount of amino nitrogen in the reaction product were measured by the Van 5lyke method.
The total amount of amino nitrogen in keratin peptide before reaction is 4
At 21 mmol, the total amount of amino nitrogen in the reaction product was 34 mmol, and the amount of amino nitrogen was reduced by the reaction. This decrease in amino nitrogen indicates that the amino groups in the keratin peptide have reacted with maleic anhydride, and the amount of decrease in amino nitrogen indicates that 92% of the amino nitrogen in the keratin peptide has reacted. I know what you're doing.
（２） 以下の条件でゲル濾過を行い、反応前のケラ
チンペプチドと反応後の生成物の平均分子量を測定した
。(2) Gel filtration was performed under the following conditions, and the average molecular weights of the keratin peptide before reaction and the product after reaction were measured.
反応前の平均分子量 ７７０
反応後の平均分子ｉ１ ９５０
測定条件：
カラム： Ｔ Ｓ Ｋ ｇｅｌ Ｇ３０００Ｐ ＷＩＬ
Ｌ直径７．８−霧×長さ３０ｃ曹
溶 媒： Ｏ，ＯＳ％トリフロロ酢酸、４５％アセトニ
トリル−水
流速： ０．３ｍ Ｉｌ ／分
検 出；紫外吸光度検出器（波長２１０ｎｍ）標準物質
：アプロチニン（ＭＷ６５００）α−ＭＳＨ（ＭＷ１６
６５）
ブラジキニン（ＭＷ１０６０）
グルタチオン（ＭＷ３０７）
上記のような分子量増加は、ケラチンペプチドが反応し
たときのマレイン酸の導入による分子量増加によるもの
と考えられ、この分子量増加とアミノ態チッ素量の減少
から、ケラチンペプチドと無水マレイン酸とが反応して
、反応生成物としてＮ−マレオイルケラチンペプチドが
生成していることがわかる、なお、このようにして得ら
れたＮ−マレオイルケラチンペプチドは、ＰＨ７となっ
ているため、部分的にナトリウム塩として存在している
ものと考えられる。Average molecular weight before reaction 770 Average molecular weight after reaction i1 950 Measurement conditions: Column: T S K gel G3000P WIL
L Diameter 7.8 - Fog x Length 30c Solvent: O,OS% trifluoroacetic acid, 45% acetonitrile - Water Flow rate: 0.3m Il/min Detection: Ultraviolet absorbance detector (wavelength 210nm) Standard substance: Aprotinin (MW6500) α-MSH (MW16
65) Bradykinin (MW1060) Glutathione (MW307) The above molecular weight increase is thought to be due to the increase in molecular weight due to the introduction of maleic acid when the keratin peptide reacts, and from this molecular weight increase and the decrease in the amount of amino nitrogen. It can be seen that keratin peptide and maleic anhydride react to produce N-maleoyl keratin peptide as a reaction product.The N-maleoyl keratin peptide thus obtained has a pH of 7. Therefore, it is thought that it exists partially as a sodium salt.
参考例２
羊毛を塩酸で加水分解することによつて得たケラチンペ
プチド（ｎ−８、シスチン含有量：ハーフシスチンとし
て８．４モル％）の４０％水溶液９００ｇ （アミノ態
チッ素の総量５０４ ミリモル）を反応容器に入れ、４
０’Ｃに加熱して撹拌しながら無水コハク酸１５０ｇを
１時間かけて投入し、かつその間、２０％水酸化す）
ＩＪウム水溶液を適宜滴下して反応液のＰＨを１０．０
に維持した。無水コハク酸の投入終了後、ｐＨを１０．
０に維持しながら２時間攪拌を続け、ついで２４時間放
置したのち、アミノ態チッ素を測定したところ、アミノ
態チッ素の総量は２８ミリモルであり、アミノ態チッ素
の９４％が反応していた。つぎに反応液をｐＨ７に中和
し、電気透析によって、副生じたコハク酸のナトリウム
塩を除去したのち、減圧濃縮して、濃度３０％のＮ−二
塩基カルボン酸モノアシル化ケラチンペプチドとしての
Ｎ−サクシノイルケラチンペプチドの水溶液を得た。こ
のＮ−サクシノイルケラチンペプチドのアミノ酸分析を
行ったところ、ケラチンペプチドを構成するアミノ酸中
のシスチン含有量はハーフシスチンとして８．２モル％
であった。Reference Example 2 900 g of a 40% aqueous solution of keratin peptide (n-8, cystine content: 8.4 mol% as half cystine) obtained by hydrolyzing wool with hydrochloric acid (total amount of amino nitrogen 504 mmol) ) into a reaction vessel, and
While heating to 0'C and stirring, 150 g of succinic anhydride was added over 1 hour, during which time 20% hydroxylation was carried out)
The pH of the reaction solution was adjusted to 10.0 by adding an appropriate amount of IJum aqueous solution.
maintained. After adding succinic anhydride, the pH was adjusted to 10.
Stirring was continued for 2 hours while maintaining the temperature at 0, and then the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 28 mmol, and 94% of the amino nitrogen had reacted. Ta. Next, the reaction solution was neutralized to pH 7, the sodium salt of succinic acid produced as a by-product was removed by electrodialysis, and then concentrated under reduced pressure to obtain N-dibasic carboxylic acid monoacylated keratin peptide with a concentration of 30%. - An aqueous solution of succinoyl keratin peptide was obtained. Amino acid analysis of this N-succinoyl keratin peptide revealed that the cystine content in the amino acids constituting the keratin peptide was 8.2 mol% as half cystine.
Met.
反応前のケラチンペプチドと反応後の生成物の平均分子
量を参考例１と同様の方法により測定したところ、反応
前のケラチンペプチドの平均分子量は１ 、２００で、
反応後の生成物の平均分子量は１．３５０であった。こ
のようにして求めた反応前後の平均分子量変化とアミノ
態チッ素の減少量から、反応生成物がケラチンペプチド
と無水コハク酸との反応によるＮ−サクシノイルケラチ
ンペプチドであることがｎ認された。なお、このように
して得られたＮ−サクシノイルケラチンペプチドはｐＨ
７となっているため、部分的にナトリウム塩として存在
しているものと考えられる。The average molecular weight of the keratin peptide before the reaction and the product after the reaction was measured in the same manner as in Reference Example 1, and the average molecular weight of the keratin peptide before the reaction was 1.200.
The average molecular weight of the product after the reaction was 1.350. Based on the average molecular weight change before and after the reaction determined in this manner and the amount of decrease in amino nitrogen, it was confirmed that the reaction product was an N-succinoylkeratin peptide produced by the reaction of keratin peptide and succinic anhydride. . In addition, the N-succinoylkeratin peptide obtained in this way has a pH of
7, it is thought that it exists partially as a sodium salt.
参考例３
羽毛を酵素で分解することによって得たケラチンペプチ
ド（ｎ−２５、シスチン含有量：ハーフシスチンとして
７．０モル％）の４０％水溶液７００ｇ （アミノ態
チッ素の総量１７８ミリモル）を反応容器に入れ、３０
℃で攪拌しながら無水フタル酸８０ｇを３時間かけて投
入し、かつその間、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１１．０に維持した。無水フ
タル酸の投入終了後、ｐＨを１１．０に維持しながら２
時間攪拌を続け、ついで２４時間放置したのち、アミノ
態チッ素を測定したところ、アミノ態チッ素の総量は１
８ミリモルであり、アミノ態チッ素の９０％が反応して
いた。つぎに反応液をｐＨ７に中和し、電気透析によっ
て、副生じたフタル酸のナトリウム塩を除去したのち、
減圧濃縮して濃度３０％のＮ−二塩基カルボン酸モノア
シル化ケラチンペプチドとしてのＮ−フタロイルケラチ
ンペプチドの水溶液を得た。このＮ−フタロイルケラチ
ンペプチドのアミノ酸分析を行ったところ、ケラチンペ
プチドを構成するアミノ酸中のシスチン含有量はハーフ
シスチンとして６゜１モル％であった。Reference Example 3 700 g of a 40% aqueous solution (total amount of amino nitrogen: 178 mmol) of keratin peptide (n-25, cystine content: 7.0 mol% as half cystine) obtained by enzymatically decomposing feathers was reacted. Put it in a container, 30
While stirring at °C, 80 g of phthalic anhydride was added over 3 hours, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 11.0. After adding phthalic anhydride, while maintaining the pH at 11.0,
After continuing to stir for 24 hours and then standing for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 1.
8 mmol, and 90% of the amino nitrogen had reacted. Next, the reaction solution was neutralized to pH 7, and the by-produced sodium salt of phthalic acid was removed by electrodialysis.
The mixture was concentrated under reduced pressure to obtain an aqueous solution of N-phthaloylkeratin peptide as N-dibasic carboxylic acid monoacylated keratin peptide with a concentration of 30%. Amino acid analysis of this N-phthaloyl keratin peptide revealed that the cystine content in the amino acids constituting the keratin peptide was 6.1 mol % as half cystine.
反応前のケラチンペプチドと反応後の生成物の平均分子
量を参考例１と同様の方法により測定したところ、反応
前のケラチンペプチドの平均分子量は３．６００で、反
応後の生成物の平均分子量は３．７５０であった。この
ようにして求めた反応前後の平均分子量変化とアミノ態
チッ素の減少量から、反応生成物がケラチンペプチドと
無水フタル酸との反応によるＮ−フタロイルケラチンペ
プチドであることが確認された。なお、このようにして
得られたＮ−フタロイルケラチンペプチドは、ＰＨ７と
なっているため部分的にナトリウム塩として存在してい
るものと考えられる。The average molecular weight of the keratin peptide before the reaction and the product after the reaction were measured using the same method as in Reference Example 1. The average molecular weight of the keratin peptide before the reaction was 3.600, and the average molecular weight of the product after the reaction was It was 3.750. From the change in average molecular weight before and after the reaction and the amount of decrease in amino nitrogen determined in this manner, it was confirmed that the reaction product was an N-phthaloylkeratin peptide resulting from the reaction of a keratin peptide and phthalic anhydride. Note that the N-phthaloylkeratin peptide thus obtained has a pH of 7, so it is considered that it partially exists as a sodium salt.
実施例１〜４および比較例１〜４ 第２表に示す組成の脱臭剤組成物を凋製した。Examples 1-4 and Comparative Examples 1-4 A deodorizing composition having the composition shown in Table 2 was prepared.
なお、第２表中の各成分の配合部数は重量部によるもの
である。Note that the number of parts of each component in Table 2 is based on parts by weight.
上記のようにして調製した実施例１〜４および比較例１
〜４の脱臭剤組成物ならびに市販の脱臭剤〔Ａ：活性炭
、Ｂ：酸性担体に鉄アスコルビン酸を含浸させたもの、
Ｃ：５〜ｌＯメツシユのシリカゲル、Ｄ：茶抽出物〕の
脱臭効果を次のようにして確認した。Examples 1 to 4 and Comparative Example 1 prepared as above
Deodorant compositions of ~4 and commercially available deodorizers [A: activated carbon, B: acidic carrier impregnated with iron ascorbic acid,
The deodorizing effect of C: 5-10 mesh silica gel, D: tea extract] was confirmed as follows.
内容積５１の広口瓶（ビン）の中に、あらかじめ実施例
１〜４および比較例１〜４の脱臭剤組成物をそれぞれ５
ｇ（したがって有効成分として１ｇ）ずつ入れ、ガラス
管を通したゴム栓で栓をした。また、同様に内容積５１
の広口瓶の中に市販の各脱臭剤をそれぞれｔｇずつ入れ
、ガラス管を通したゴム栓で栓をした。Into a wide mouth bottle (bottle) having an internal volume of 51 kg, 5 ml of each of the deodorizing compositions of Examples 1 to 4 and Comparative Examples 1 to 4 was placed in advance.
g (therefore, 1 g as the active ingredient) was added, and the tube was stopped with a rubber stopper passed through a glass tube. Similarly, the internal volume is 51
tg of each commercially available deodorizer was placed in a wide-mouthed bottle, and the bottle was stopped with a rubber stopper passed through a glass tube.
上記のようにして実施例１〜４および比較例１〜４の脱
臭剤組成物ならびに市販の脱臭剤を封入した広口瓶中に
、悪臭物質としてアンモニア、トリメチルアミン、硫化
水素、エチルメルカプタンをガスタイトのディスポーザ
ル型注射器で同量ずつ注入し、一定時間経過後にガスを
抜き、悪臭物質をガスクロマトグラフにより定量し、そ
の脱臭率を求めて、その結果をそれぞれ第３〜６表に示
した。なお、この脱臭効果確認試験にあたって、実施例
１〜４および比較例１〜４の脱臭基剤濃度を２０％と高
く調製したのは、固体系の市販脱臭剤との比較上、水に
よる影響をできるかぎり少なくするためである。As described above, ammonia, trimethylamine, hydrogen sulfide, and ethyl mercaptan were added as malodorous substances into wide-mouthed bottles filled with the deodorizing compositions of Examples 1 to 4 and Comparative Examples 1 to 4 and commercially available deodorizers using a gas-tight disposer. The same amount was injected using a double-shaped syringe, and after a certain period of time, the gas was removed, and the malodorous substances were determined using a gas chromatograph.The deodorization rate was determined, and the results are shown in Tables 3 to 6, respectively. In addition, in this deodorizing effect confirmation test, the concentration of the deodorizing base in Examples 1 to 4 and Comparative Examples 1 to 4 was prepared as high as 20%, in order to reduce the influence of water in comparison with solid commercially available deodorizers. This is to reduce the amount as much as possible.
ンモニ
（（１）市販品Ａ：活性炭
市販品Ｂ：酸性担体に鉄アスコルビン酸を含浸させたち
の市販品Ｃニジリカゲル
市販品Ｄ：茶抽出物
（注）市販品Ａ：活性炭
市販品Ｂ：酸性担体に鉄アスコルビン酸を含浸させたち
の市販品Ｃニジリカゲル
市販品Ｄ：茶抽出物
ル 々ン
（巾市販品Ａ：活性炭
市販品Ｂ：酸性担体に鉄アスコルビン酸を含浸させたち
の市販品Ｃニジリカゲル
市販品Ｄ：茶抽出物
エ ルメルカブ ン
（由市販品Ａ：活性炭
市販品Ｂ：酸性担体に鉄アスコルビン酸を含浸させたも
の市販品Ｃニジリカゲル
市販品Ｄ：茶抽出物
第３〜第６表に示すように、本発明の実施例１〜４の脱
臭剤組成物は、アンモニア、トリメチルアミンに対する
脱臭効率が高く、また、硫化水素、エチルメルカプタン
に対する脱臭効率も高く、アンモニアやトリメチルアミ
ンなどから発生するアミン臭に対しても、また硫化水素
やエチルメルカプタンから発生するメルカプト臭に対し
ても、脱臭効果が優れていた。(1) Commercial product A: Activated carbon Commercial product B: Commercial product made by impregnating an acidic carrier with iron ascorbic acid C Nijirikageru Commercial product D: Tea extract (Note) Commercial product A: Activated carbon Commercial product B: Acidic carrier Commercially available product C Nijirica gel made by impregnating iron ascorbic acid with iron ascorbic acid.Commercial product D: Tea extract. Product D: Tea extract Elmelkabun (Commercial product A: Activated carbon Commercial product B: Acidic carrier impregnated with iron ascorbic acid Commercial product C Nijiri Kagel Commercial product D: Tea extract shown in Tables 3 to 6 As shown, the deodorizing compositions of Examples 1 to 4 of the present invention have high deodorizing efficiency against ammonia and trimethylamine, and also high deodorizing efficiency against hydrogen sulfide and ethyl mercaptan, and are effective against amine odor generated from ammonia, trimethylamine, etc. It also had an excellent deodorizing effect against mercapto odor generated from hydrogen sulfide and ethyl mercaptan.
これに対し、ケラチンペプチドを脱臭基剤とする比較例
１〜３の脱臭剤組成物は、アンモニア、トリメチルアミ
ンなどのアミン臭に対する脱臭効果は比較的良好であっ
たが、硫化水素に対する脱臭効果は本発明の実施例１〜
４の脱臭剤組成物に比べて低く、エチルメルカプタンに
対する脱臭効果はさらに低かった。これら硫化水素、エ
チルメルカプタンなどのメルカプト臭に対する本発明の
実施例１〜４の脱臭剤組成物と比較例１〜３の脱臭剤組
成物の脱臭効果の差は、本発明の脱臭剤組成物では、ケ
ラチンペプチドのアシル化によって導入された炭化水素
骨格により、これらメルカプト臭を発生する物質に対す
る親和性が高まっていることによるものと考えられる。On the other hand, the deodorizing compositions of Comparative Examples 1 to 3 using keratin peptide as a deodorizing base had a relatively good deodorizing effect on amine odors such as ammonia and trimethylamine, but had a poor deodorizing effect on hydrogen sulfide. Example 1 of the invention
The deodorizing effect on ethyl mercaptan was lower than that of the deodorizing composition No. 4, and the deodorizing effect on ethyl mercaptan was even lower. The difference in the deodorizing effect between the deodorizing compositions of Examples 1 to 4 of the present invention and the deodorant compositions of Comparative Examples 1 to 3 against these mercapto odors such as hydrogen sulfide and ethyl mercaptan is that This is thought to be due to the hydrocarbon skeleton introduced by acylation of keratin peptides, which increases the affinity for these mercapto odor-producing substances.
また、コラーゲンペプチドを脱臭基剤として用いた比較
例４の脱臭剤組成物は、コラーゲンペプチドがシスチン
（このシスチンがメルカプト化合物と反応する）を含有
しないため、硫化水素、エチルメルカプタンなどのメル
カプト化合物に対する脱臭効果が非常に低かった。In addition, the deodorizing composition of Comparative Example 4 using collagen peptide as a deodorizing base has a high resistance to mercapto compounds such as hydrogen sulfide and ethyl mercaptan because the collagen peptide does not contain cystine (this cystine reacts with mercapto compounds). The deodorizing effect was very low.
市販品Ａ１つまり、活性炭は、トリメチルアミンやエチ
ルメルカプタンに対する脱臭効果は比較的良好であった
が、分子が小さいアンモニアや硫化水素に対する脱臭効
果が低かった。また、市販品Ｂ、つまり、酸性担体にア
スコルビン酸鉄を含浸させたものは、アンモニアやトリ
メチルアミンに対する脱臭効果は比較的良好であったが
、硫化水素やエチルメルカプタンに対する脱臭効果が低
く、市販品Ｃ１つまり、シリカゲルや、市販品Ｄ、つま
り、茶抽出物も、同様に硫化水素やエチルメルカプタン
に対する脱臭効果が非常に低かった。Commercial product A1, that is, activated carbon had a relatively good deodorizing effect on trimethylamine and ethyl mercaptan, but had a low deodorizing effect on ammonia and hydrogen sulfide, which have small molecules. In addition, commercial product B, which is an acidic carrier impregnated with iron ascorbate, had a relatively good deodorizing effect on ammonia and trimethylamine, but had a low deodorizing effect on hydrogen sulfide and ethyl mercaptan, and commercial product C1 In other words, silica gel and commercially available product D, that is, tea extract, similarly had very low deodorizing effects on hydrogen sulfide and ethyl mercaptan.
実施例５〜７および比較例５〜８
第７表に示す組成のパーマネントウェーブ用脱臭剤組成
物を調製した。なお、第７表中の各成分の配合部数は重
量部によるものである。Examples 5 to 7 and Comparative Examples 5 to 8 Deodorant compositions for permanent waves having the compositions shown in Table 7 were prepared. Note that the number of parts of each component in Table 7 is based on parts by weight.
上記実施例５〜７および比較例５〜８のパーマネントウ
ェーブ用脱臭剤組成物の脱臭効果を次のようにして検討
した。The deodorizing effects of the deodorant compositions for permanent waves of Examples 5 to 7 and Comparative Examples 5 to 8 were examined as follows.
（ｉ）パーマネントウェーブ用剤の調製：上記パーマネ
ントウェーブ用脱臭剤組成物の脱臭効果を確認するにあ
たって、毛髪にパーマネントウェーブ処理を施すために
、第８表に示す２種類のパーマネントウェーブ用第１剤
（第１７ＰＪＸおよび第１ｗＩＹ）および第９表に示す
パーマネントウェーブ用第２剤を調製した。なお、第８
表および第９表における各成分の配合量は重量部による
ものである。(i) Preparation of permanent waving agent: In order to confirm the deodorizing effect of the above deodorant composition for permanent waving, two types of first agent for permanent waving shown in Table 8 were used to perform permanent waving treatment on hair. (No. 17 PJX and No. 1 wIY) and a second agent for permanent waving shown in Table 9 were prepared. In addition, the 8th
The amounts of each component in Tables and Table 9 are based on parts by weight.
（１１）処理方法：
長さ１８ｃｍの毛髪を束ねた重さ１ｇの毛束を、それぞ
れ３５°Ｃに温度調整したパーマネントウェーブ用第１
剤（第１剤Ｘおよび第１剤Ｙ）に１５分間浸漬し、第１
剤中から取り出した後、水洗し、ついで３５°Ｃに温度
調整したパーマネントウェーブ用第２剤に１５分間浸漬
してパーマネントウェーブ処理を行った後、第２剤から
取り出し、水洗後、軽（しぼってから、それぞれ３５°
Ｃに温度調整した前記実施例５〜７および比較例５〜８
のパーマネントウェーブ用脱臭剤組成物ならびに水に１
０分間浸漬した。(11) Treatment method: Hair bundles of 18 cm long and weighing 1 g were each heated to 35°C using the first permanent wave treatment method.
(first agent X and first agent Y) for 15 minutes.
After taking it out from the agent, wash it with water, and then immerse it in the second agent for permanent wave whose temperature is adjusted to 35°C for 15 minutes to perform permanent wave treatment. and then 35° each
Examples 5 to 7 and Comparative Examples 5 to 8 whose temperature was adjusted to C
Permanent wave deodorizing composition and 1 part in water
It was immersed for 0 minutes.
浸漬後、毛束を液中から取り出して、乾燥し、２４時間
後、各毛束に残ったパーマネントウェーブ用第１剤に基
づく奥の残存程度をそれぞれ１０人の専門パネルによっ
て４段階評価した。After soaking, the hair bundles were taken out of the solution and dried, and 24 hours later, the degree of residual depth based on the first agent for permanent waving remaining on each hair bundle was evaluated in four grades by a panel of 10 experts.
−１段Ｕ厘
４：最も強い
（水で処理したものを基準とする）
３：強い
２：弱い
に最も弱い
（パーマネントウェーブ処理を行わなかった毛束を基準
とする）
１０人の専門パネルによる評価結果の平均値をパーマネ
ントウェーブ用第１剤の種別ごとに次の第１０表に示す
。-1 stage U Rin 4: Strongest (based on hair treated with water) 3: Strong 2: Weakest (based on hair strands that have not been permanently waved) Based on a panel of 10 experts The average values of the evaluation results are shown in Table 10 below for each type of first agent for permanent waving.
第
表
第１Ｏ表に示すように、本発明の実施例５〜７の脱臭剤
組成物は、比較例５〜８の脱臭剤組成物に比べて、パー
マネントウェーブ用第１剤に基づく奥の残存が少なく、
脱臭効果が優れていた。また、本発明の実施例５〜７の
脱臭剤組成物は、パーマネントウェーブ用第１剤の種類
が変わっても、脱臭効果を変わらなかった。As shown in Table 1O, the deodorant compositions of Examples 5 to 7 of the present invention have a higher residual residual amount based on the first agent for permanent waving than the deodorant compositions of Comparative Examples 5 to 8. There are few
It had an excellent deodorizing effect. Further, the deodorizing compositions of Examples 5 to 7 of the present invention did not change their deodorizing effects even if the type of the first agent for permanent waving was changed.
以上説明したように、本発明の脱臭剤組成物は、アミン
臭、メルカプト臭のいずれに対しても脱臭効果が優れて
おり、しかも水に容易に溶解し、かつ皮膚、粘膜に対し
て刺激性がなく、安全性が高く、パーマネントウェーブ
処理後の毛髪の脱臭にあたっても、容易にかつ安心して
使用することができ、しかも優れた脱臭効果を発揮する
ことができる。As explained above, the deodorizing composition of the present invention has an excellent deodorizing effect against both amine odor and mercapto odor, is easily dissolved in water, and is irritating to the skin and mucous membranes. It is highly safe, can be used easily and safely even when deodorizing hair after permanent wave treatment, and can exhibit excellent deodorizing effects.
ｖｋＪ、’・ζすvkJ,'・ζsu
Claims (3)
ケラチンペプチドを構成するアミノ酸の側鎖を示す。Ｍ
＿１およびＭ＿２は、ＨまたはＮａ、Ｋ、Ｌｉ、Ｍｇ／
２、Ｃａ／２などのアルカリ金属あるいはアルカリ土類
金属、またはアンモニア、トリメチルアミン、トリエチ
ルアミン、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−メチルプロ
パン、２−アミノ−２−メチル−１，３−プロパンジオ
ールなどの無機アミンあるいは有機アミン、またはアル
ギニン、リジンなどの塩基性アミノ酸のオニウムを示し
、Ｍ＿１およびＭ＿２は同一でもよく、また異なってい
てもよい。ｎは２〜３０である） で示されるＮ−二塩基カルボン酸モノアシル化ケラチン
ペプチドを脱臭基剤として含有することを特徴とする脱
臭剤組成物。(1) General formula (I) ▲Mathematical formulas, chemical formulas, tables, etc.▼ (In the formula, A represents a hydrocarbon skeleton having 2 to 6 carbon atoms, and R represents the side chain of the amino acid that constitutes the keratin peptide. M
_1 and M_2 are H or Na, K, Li, Mg/
2, alkali metals or alkaline earth metals such as Ca/2, or ammonia, trimethylamine, triethylamine, monoethanolamine, diethanolamine, triethanolamine, 2-amino-2-methylpropane, 2-amino-2-methyl-1 M_1 and M_2 may be the same or different. n is 2 to 30) A deodorizing composition comprising an N-dibasic carboxylic acid monoacylated keratin peptide as a deodorizing base.
モノアシル化ケラチンペプチドのケラチンペプチドを構
成するアミノ酸のうち、シスチンがハーフシスチンとし
て６．０モル％以上含まれていることを特徴とする請求
項１記載の脱臭剤組成物。(2) Among the amino acids constituting the keratin peptide of the N-dibasic carboxylic acid monoacylated keratin peptide represented by the general formula (I), cystine is contained in an amount of 6.0 mol% or more as half cystine. The deodorizing composition according to claim 1.
項１記載の脱臭剤組成物。(3) The deodorizing composition according to claim 1, which has a pH in the range of 1 to 6.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1027925A JP2788467B2 (en) | 1989-02-07 | 1989-02-07 | Deodorant composition |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1027925A JP2788467B2 (en) | 1989-02-07 | 1989-02-07 | Deodorant composition |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH02207017A true JPH02207017A (en) | 1990-08-16 |
| JP2788467B2 JP2788467B2 (en) | 1998-08-20 |
Family
ID=12234461
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1027925A Expired - Fee Related JP2788467B2 (en) | 1989-02-07 | 1989-02-07 | Deodorant composition |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2788467B2 (en) |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH1045543A (en) * | 1996-08-07 | 1998-02-17 | Taiyo Koryo Kk | Deodorizing composition and deodorizing shampoo |
| WO2001051011A3 (en) * | 2000-01-08 | 2002-04-11 | Cognis Deutschland Gmbh | Condensation products of proteins, whereby azelaic acid is used |
| JP2006320711A (en) * | 2005-04-21 | 2006-11-30 | Kao Corp | Deodorant |
| JP2006320712A (en) * | 2005-04-21 | 2006-11-30 | Kao Corp | Deodorant composition |
| JP2007160071A (en) * | 2005-11-18 | 2007-06-28 | Kao Corp | Deodorant compositions |
| JP2007175405A (en) * | 2005-12-28 | 2007-07-12 | Kao Corp | Deodorant composition |
| JP2007209464A (en) * | 2006-02-08 | 2007-08-23 | Kao Corp | Deodorant composition |
| JP2007229356A (en) * | 2006-03-03 | 2007-09-13 | Kao Corp | Deodorant composition |
| JP2007296063A (en) * | 2006-04-28 | 2007-11-15 | Kao Corp | Liquid deodorant composition |
| JP2007296062A (en) * | 2006-04-28 | 2007-11-15 | Kao Corp | Liquid deodorant composition |
| JP2007300963A (en) * | 2006-05-08 | 2007-11-22 | Kao Corp | Deodorant composition |
| JP2008188326A (en) * | 2007-02-07 | 2008-08-21 | Kao Corp | Deodorant composition |
-
1989
- 1989-02-07 JP JP1027925A patent/JP2788467B2/en not_active Expired - Fee Related
Cited By (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH1045543A (en) * | 1996-08-07 | 1998-02-17 | Taiyo Koryo Kk | Deodorizing composition and deodorizing shampoo |
| WO2001051011A3 (en) * | 2000-01-08 | 2002-04-11 | Cognis Deutschland Gmbh | Condensation products of proteins, whereby azelaic acid is used |
| JP4590369B2 (en) * | 2005-04-21 | 2010-12-01 | 花王株式会社 | Deodorants |
| JP2006320711A (en) * | 2005-04-21 | 2006-11-30 | Kao Corp | Deodorant |
| JP2006320712A (en) * | 2005-04-21 | 2006-11-30 | Kao Corp | Deodorant composition |
| JP2007160071A (en) * | 2005-11-18 | 2007-06-28 | Kao Corp | Deodorant compositions |
| JP2007175405A (en) * | 2005-12-28 | 2007-07-12 | Kao Corp | Deodorant composition |
| JP2007209464A (en) * | 2006-02-08 | 2007-08-23 | Kao Corp | Deodorant composition |
| JP2007229356A (en) * | 2006-03-03 | 2007-09-13 | Kao Corp | Deodorant composition |
| JP2007296063A (en) * | 2006-04-28 | 2007-11-15 | Kao Corp | Liquid deodorant composition |
| JP2007296062A (en) * | 2006-04-28 | 2007-11-15 | Kao Corp | Liquid deodorant composition |
| JP2007300963A (en) * | 2006-05-08 | 2007-11-22 | Kao Corp | Deodorant composition |
| JP2008188326A (en) * | 2007-02-07 | 2008-08-21 | Kao Corp | Deodorant composition |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2788467B2 (en) | 1998-08-20 |
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