US2517572A - Process of utilizing detergents to solubilize keratin materials - Google Patents
Process of utilizing detergents to solubilize keratin materials Download PDFInfo
- Publication number
- US2517572A US2517572A US61694A US6169448A US2517572A US 2517572 A US2517572 A US 2517572A US 61694 A US61694 A US 61694A US 6169448 A US6169448 A US 6169448A US 2517572 A US2517572 A US 2517572A
- Authority
- US
- United States
- Prior art keywords
- sodium
- keratin
- solution
- parts
- alkyl
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 102000011782 Keratins Human genes 0.000 title claims description 38
- 108010076876 Keratins Proteins 0.000 title claims description 38
- 239000000463 material Substances 0.000 title claims description 14
- 238000000034 method Methods 0.000 title claims description 8
- 239000003599 detergent Substances 0.000 title description 13
- 239000000243 solution Substances 0.000 claims description 32
- 230000007935 neutral effect Effects 0.000 claims description 14
- 239000003795 chemical substances by application Substances 0.000 claims description 10
- 239000000271 synthetic detergent Substances 0.000 claims description 8
- 239000007864 aqueous solution Substances 0.000 claims description 5
- 238000010438 heat treatment Methods 0.000 claims description 4
- 230000002829 reductive effect Effects 0.000 claims description 4
- 229910052783 alkali metal Inorganic materials 0.000 claims description 3
- 150000001340 alkali metals Chemical class 0.000 claims description 2
- 150000003467 sulfuric acid derivatives Chemical class 0.000 claims description 2
- -1 alkyl sulphates Chemical class 0.000 description 22
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 18
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 17
- 239000006185 dispersion Substances 0.000 description 14
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 9
- GEHJBWKLJVFKPS-UHFFFAOYSA-N bromochloroacetic acid Chemical compound OC(=O)C(Cl)Br GEHJBWKLJVFKPS-UHFFFAOYSA-N 0.000 description 8
- 210000003746 feather Anatomy 0.000 description 8
- 229910052708 sodium Inorganic materials 0.000 description 8
- 239000011734 sodium Substances 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 7
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 241000287828 Gallus gallus Species 0.000 description 5
- JXLHNMVSKXFWAO-UHFFFAOYSA-N azane;7-fluoro-2,1,3-benzoxadiazole-4-sulfonic acid Chemical compound N.OS(=O)(=O)C1=CC=C(F)C2=NON=C12 JXLHNMVSKXFWAO-UHFFFAOYSA-N 0.000 description 5
- 229910021653 sulphate ion Inorganic materials 0.000 description 5
- DLFVBJFMPXGRIB-UHFFFAOYSA-N Acetamide Chemical compound CC(N)=O DLFVBJFMPXGRIB-UHFFFAOYSA-N 0.000 description 4
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 4
- 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 4
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 125000000217 alkyl group Chemical group 0.000 description 4
- 150000003863 ammonium salts Chemical class 0.000 description 4
- 238000009835 boiling Methods 0.000 description 4
- 239000004202 carbamide Substances 0.000 description 4
- 125000004432 carbon atom Chemical group C* 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 229910052700 potassium Inorganic materials 0.000 description 4
- 239000011591 potassium Substances 0.000 description 4
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 4
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 4
- 210000002268 wool Anatomy 0.000 description 4
- UHOVQNZJYSORNB-UHFFFAOYSA-N Benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 3
- 101710200191 Feather keratin Proteins 0.000 description 3
- 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 3
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 239000003513 alkali Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 210000004209 hair Anatomy 0.000 description 3
- 210000000003 hoof Anatomy 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000005185 salting out Methods 0.000 description 3
- 229910052717 sulfur Inorganic materials 0.000 description 3
- 239000011593 sulfur Substances 0.000 description 3
- 229920002994 synthetic fiber Polymers 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 2
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 2
- ABBQHOQBGMUPJH-UHFFFAOYSA-M Sodium salicylate Chemical compound [Na+].OC1=CC=CC=C1C([O-])=O ABBQHOQBGMUPJH-UHFFFAOYSA-M 0.000 description 2
- 239000012670 alkaline solution Substances 0.000 description 2
- NBZANZVJRKXVBH-GYDPHNCVSA-N alpha-Cryptoxanthin Natural products O[C@H]1CC(C)(C)C(/C=C/C(=C\C=C\C(=C/C=C/C=C(\C=C\C=C(/C=C/[C@H]2C(C)=CCCC2(C)C)\C)/C)\C)/C)=C(C)C1 NBZANZVJRKXVBH-GYDPHNCVSA-N 0.000 description 2
- SOIFLUNRINLCBN-UHFFFAOYSA-N ammonium thiocyanate Chemical compound [NH4+].[S-]C#N SOIFLUNRINLCBN-UHFFFAOYSA-N 0.000 description 2
- 229960003067 cystine Drugs 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 2
- 239000002270 dispersing agent Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 229960004198 guanidine Drugs 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- HSZCZNFXUDYRKD-UHFFFAOYSA-M lithium iodide Chemical compound [Li+].[I-] HSZCZNFXUDYRKD-UHFFFAOYSA-M 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 2
- 239000004289 sodium hydrogen sulphite Substances 0.000 description 2
- 229960004025 sodium salicylate Drugs 0.000 description 2
- HFQQZARZPUDIFP-UHFFFAOYSA-M sodium;2-dodecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O HFQQZARZPUDIFP-UHFFFAOYSA-M 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 150000004763 sulfides Chemical class 0.000 description 2
- UMGDCJDMYOKAJW-UHFFFAOYSA-N thiourea Chemical compound NC(N)=S UMGDCJDMYOKAJW-UHFFFAOYSA-N 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- RFKPMHFTLZKWIP-UHFFFAOYSA-N 1,2-bis(2-methylpropyl)benzene;sodium Chemical compound [Na].CC(C)CC1=CC=CC=C1CC(C)C RFKPMHFTLZKWIP-UHFFFAOYSA-N 0.000 description 1
- TWWNLDITIRCJDN-UHFFFAOYSA-N 1,2-bis(2-methylpropyl)naphthalene;sodium Chemical compound [Na].C1=CC=CC2=C(CC(C)C)C(CC(C)C)=CC=C21 TWWNLDITIRCJDN-UHFFFAOYSA-N 0.000 description 1
- MRTOHWYKOIAOSC-UHFFFAOYSA-N 1,2-di(propan-2-yl)naphthalene;sodium Chemical compound [Na].C1=CC=CC2=C(C(C)C)C(C(C)C)=CC=C21 MRTOHWYKOIAOSC-UHFFFAOYSA-N 0.000 description 1
- UKIMGCJPCFNHHF-UHFFFAOYSA-N 2-methylpropyl naphthalene-1-sulfonate;sodium Chemical compound [Na].C1=CC=C2C(S(=O)(=O)OCC(C)C)=CC=CC2=C1 UKIMGCJPCFNHHF-UHFFFAOYSA-N 0.000 description 1
- 241000272525 Anas platyrhynchos Species 0.000 description 1
- PFEJAYXTHRDPDH-UHFFFAOYSA-N C(C(C)C)C=1C(=C(C2=CC=CC=C2C1)CC(C)C)CC(C)C.[Na] Chemical compound C(C(C)C)C=1C(=C(C2=CC=CC=C2C1)CC(C)C)CC(C)C.[Na] PFEJAYXTHRDPDH-UHFFFAOYSA-N 0.000 description 1
- UQEAQAKWTXGXOS-UHFFFAOYSA-N C(C(C)C)C=1C(=C(C=CC1)CC(C)C)CC(C)C.[Na] Chemical compound C(C(C)C)C=1C(=C(C=CC1)CC(C)C)CC(C)C.[Na] UQEAQAKWTXGXOS-UHFFFAOYSA-N 0.000 description 1
- ZPRJMAVKGZIUOX-UHFFFAOYSA-N C(CC(C)C)OS(=O)(=O)C1=CC=CC2=CC=CC=C12.[Na] Chemical compound C(CC(C)C)OS(=O)(=O)C1=CC=CC2=CC=CC=C12.[Na] ZPRJMAVKGZIUOX-UHFFFAOYSA-N 0.000 description 1
- UUUXCBNPERIZJL-UHFFFAOYSA-N C(CCCCCCCCCCCCCCCC)OS(=O)(=O)C1=CC=CC=C1.[Na] Chemical compound C(CCCCCCCCCCCCCCCC)OS(=O)(=O)C1=CC=CC=C1.[Na] UUUXCBNPERIZJL-UHFFFAOYSA-N 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 241000270295 Serpentes Species 0.000 description 1
- 239000004141 Sodium laurylsulphate Substances 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241000270708 Testudinidae Species 0.000 description 1
- 241001122767 Theaceae Species 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- 238000003811 acetone extraction Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 125000002877 alkyl aryl group Chemical group 0.000 description 1
- 150000008055 alkyl aryl sulfonates Chemical class 0.000 description 1
- 150000004996 alkyl benzenes Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001555 benzenes Chemical class 0.000 description 1
- 229940077388 benzenesulfonate Drugs 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- PUBNPKMXGRPTQT-UHFFFAOYSA-N decyl benzenesulfonate Chemical compound CCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 PUBNPKMXGRPTQT-UHFFFAOYSA-N 0.000 description 1
- VQZHOOBGYXKMLU-UHFFFAOYSA-N decyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 VQZHOOBGYXKMLU-UHFFFAOYSA-N 0.000 description 1
- FEQWRQDZXXJRIL-UHFFFAOYSA-N decyl naphthalene-1-sulfonate;sodium Chemical compound [Na].C1=CC=C2C(S(=O)(=O)OCCCCCCCCCC)=CC=CC2=C1 FEQWRQDZXXJRIL-UHFFFAOYSA-N 0.000 description 1
- 230000002951 depilatory effect Effects 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical class CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000010408 film Substances 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- QKIAYRRGJHLRAQ-UHFFFAOYSA-N hexadecyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 QKIAYRRGJHLRAQ-UHFFFAOYSA-N 0.000 description 1
- 210000003284 horn Anatomy 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 125000002349 hydroxyamino group Chemical group [H]ON([H])[*] 0.000 description 1
- 239000003350 kerosene Substances 0.000 description 1
- 239000010985 leather Substances 0.000 description 1
- KIHUPOKUSVEICJ-UHFFFAOYSA-N nonyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 KIHUPOKUSVEICJ-UHFFFAOYSA-N 0.000 description 1
- MXXDSLLVYZMTFA-UHFFFAOYSA-N octadecyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCCCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 MXXDSLLVYZMTFA-UHFFFAOYSA-N 0.000 description 1
- YSVFUNHOUJFANW-UHFFFAOYSA-N octyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCOS(=O)(=O)C1=CC=CC=C1 YSVFUNHOUJFANW-UHFFFAOYSA-N 0.000 description 1
- CYGLRHJCEUFWFD-UHFFFAOYSA-N octyl naphthalene-1-sulfonate;sodium Chemical compound [Na].C1=CC=C2C(S(=O)(=O)OCCCCCCCC)=CC=CC2=C1 CYGLRHJCEUFWFD-UHFFFAOYSA-N 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 229940066779 peptones Drugs 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- FVEFRICMTUKAML-UHFFFAOYSA-M sodium tetradecyl sulfate Chemical compound [Na+].CCCCC(CC)CCC(CC(C)C)OS([O-])(=O)=O FVEFRICMTUKAML-UHFFFAOYSA-M 0.000 description 1
- ZKBBQUFQDGOTBZ-UHFFFAOYSA-N sodium;1,2,3-tri(propan-2-yl)naphthalene Chemical compound [Na].C1=CC=C2C(C(C)C)=C(C(C)C)C(C(C)C)=CC2=C1 ZKBBQUFQDGOTBZ-UHFFFAOYSA-N 0.000 description 1
- GWCMKOHVMSHWKI-UHFFFAOYSA-M sodium;4-tetradecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCCCC1=CC=C(S([O-])(=O)=O)C=C1 GWCMKOHVMSHWKI-UHFFFAOYSA-M 0.000 description 1
- DUXXGJTXFHUORE-UHFFFAOYSA-M sodium;4-tridecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCCC1=CC=C(S([O-])(=O)=O)C=C1 DUXXGJTXFHUORE-UHFFFAOYSA-M 0.000 description 1
- AZXQLMRILCCVDW-UHFFFAOYSA-M sodium;5-propan-2-ylnaphthalene-1-sulfonate Chemical compound [Na+].C1=CC=C2C(C(C)C)=CC=CC2=C1S([O-])(=O)=O AZXQLMRILCCVDW-UHFFFAOYSA-M 0.000 description 1
- MWZFQMUXPSUDJQ-KVVVOXFISA-M sodium;[(z)-octadec-9-enyl] sulfate Chemical compound [Na+].CCCCCCCC\C=C/CCCCCCCCOS([O-])(=O)=O MWZFQMUXPSUDJQ-KVVVOXFISA-M 0.000 description 1
- MZSDGDXXBZSFTG-UHFFFAOYSA-M sodium;benzenesulfonate Chemical class [Na+].[O-]S(=O)(=O)C1=CC=CC=C1 MZSDGDXXBZSFTG-UHFFFAOYSA-M 0.000 description 1
- XZTJQQLJJCXOLP-UHFFFAOYSA-M sodium;decyl sulfate Chemical compound [Na+].CCCCCCCCCCOS([O-])(=O)=O XZTJQQLJJCXOLP-UHFFFAOYSA-M 0.000 description 1
- HHURSJAUVYNJBT-UHFFFAOYSA-M sodium;heptadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCCCOS([O-])(=O)=O HHURSJAUVYNJBT-UHFFFAOYSA-M 0.000 description 1
- GGHPAKFFUZUEKL-UHFFFAOYSA-M sodium;hexadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCCOS([O-])(=O)=O GGHPAKFFUZUEKL-UHFFFAOYSA-M 0.000 description 1
- FTWCSAMTIKSPAT-UHFFFAOYSA-M sodium;nonyl sulfate Chemical compound [Na+].CCCCCCCCCOS([O-])(=O)=O FTWCSAMTIKSPAT-UHFFFAOYSA-M 0.000 description 1
- NWZBFJYXRGSRGD-UHFFFAOYSA-M sodium;octadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCCCCOS([O-])(=O)=O NWZBFJYXRGSRGD-UHFFFAOYSA-M 0.000 description 1
- WFRKJMRGXGWHBM-UHFFFAOYSA-M sodium;octyl sulfate Chemical compound [Na+].CCCCCCCCOS([O-])(=O)=O WFRKJMRGXGWHBM-UHFFFAOYSA-M 0.000 description 1
- SMECTXYFLVLAJE-UHFFFAOYSA-M sodium;pentadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCOS([O-])(=O)=O SMECTXYFLVLAJE-UHFFFAOYSA-M 0.000 description 1
- HQCFDOOSGDZRII-UHFFFAOYSA-M sodium;tridecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCOS([O-])(=O)=O HQCFDOOSGDZRII-UHFFFAOYSA-M 0.000 description 1
- NZRSEGYTVSNMCK-UHFFFAOYSA-N sodium;undecyl benzenesulfonate Chemical compound [Na].CCCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 NZRSEGYTVSNMCK-UHFFFAOYSA-N 0.000 description 1
- UOWRKHDWHDWJHK-UHFFFAOYSA-M sodium;undecyl sulfate Chemical compound [Na+].CCCCCCCCCCCOS([O-])(=O)=O UOWRKHDWHDWJHK-UHFFFAOYSA-M 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 210000000538 tail Anatomy 0.000 description 1
- 229940071127 thioglycolate Drugs 0.000 description 1
- CWERGRDVMFNCDR-UHFFFAOYSA-M thioglycolate(1-) Chemical compound [O-]C(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-M 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
- D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
- D01F4/00—Monocomponent artificial filaments or the like of proteins; Manufacture thereof
Definitions
- This invention relates to a method of dispersing keratin proteins obtained from a keratin ma.- terial, such as feathers, hoofs, horns, wool, and so forth, and has among its objects the use of such keratins, either in the dispersed or recovered forms, in the preparation of artificial fibers, films, plastics and the like.
- Keratins like themore soluble proteins, can be readily dispersed by hydrolysis in strong acids or alkalis, but the keratin thus dispersed cannot be recovered except as simple degradation products, such as amino acids or complex degradation products, such as peptides, peptones, and proteoses, the properties of which differ radically from those of the original keratin.
- Keratins can also be dispersed in alkaline solutions of metallic sulphides and such sulphides are commonly used in cosmetic depilatories and in the removal of hair from hides in the tanning industry.
- Keratins have also been dispersed at neutral reactions, but in these cases heat and high temperatures were employed to the point of charring, which produced drastic degradation oi the proteins.
- keratins may be dispersed in strong alkaline solutions by treatment with reducing agents, and the recovered protein is more similar to the original protein in regard to solubility, molecular size, and so forth, than are the peptides, proteoses, and so forth, referred to previously.
- the presence of the strong alkali is undesirable because it presents an opportunity for the hydrolysis of the keratin, destruction of the cystine constituent of the keratin (keratins being unique among proteins in that they contain exceptionally large amounts of cystine), and destruction of the hydroxy amino acid residues of the keratin.
- keratin materials are dispersed under mild conditions, that is, in neutral or practically neutral reaction, and at relatively low temperatures. These conditions produce less degradation of the original keratin than occurred in the prior art and the dispersed keratin may be recovered in a form substantially similar to that of the original keratin in regard to its composition, lsoelectric point, solubility, and other properties.
- the method involved in this invention is based partly on the reduction of the disulphide bonds within the keratin molecule by treating it with sulfur-containing, reductive disulphide-splitting agents, such as monoethylene thioglycol (thioglycol), thioglycolic acid (present as the thioglycolate in neutral solution) and sodium bisulphite.
- sulfur-containing, reductive disulphide-splitting agents such as monoethylene thioglycol (thioglycol), thioglycolic acid (present as the thioglycolate in neutral solution) and sodium bisulphite.
- alkali is obviated by the use of any of a number of protein-denaturing or protein-dispersing agents, such as urea, guanidine hydrochloride, ammonium thiocyanate, tormamide, acetamide, thiourea, sodium salicylate, urethane, phenol, lithium iodide, and surfaceactive agents, such as synthetic detergents composed of alkyl aryl sulfonates or alkyl sulphates and dispersion or the keratin is thus eflected at neutral or practically neutral reaction.
- protein-denaturing or protein-dispersing agents such as urea, guanidine hydrochloride, ammonium thiocyanate, tormamide, acetamide, thiourea, sodium salicylate, urethane, phenol, lithium iodide, and surfaceactive agents, such as synthetic detergents composed of alkyl aryl sulfonates or alkyl sulphates
- the keratin molecule undergoes minimal degradation, the only chemical attack on the covalent linkages of the keratin being the cleavage or the disulphide bonds of the cystine moiety.
- the hoof kera- 3 tin is dispersed in the solution.
- the dispersed keratin may be precipitated either by dilution with several volumes of water, by salting out with M3804, (NHa) 2804. etc., by acidification, or by dialysis.
- the guanidine may be removed from the dispersion by dialysis and may be recovered from thedialysate by precipitation as the nitrate or by other suitable means.
- EXAMPLE lI 1.1 parts of NaHSOa and 21 parts of urea are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution at about pH 7.1. 2.5 parts of wool are treated with this solution in a water bath at about 40 C. about for 18 hours, during which period the mixture isstirred at frequent intervals. 52% of the original weight of the wool is dispersed by this treatment.
- the dispersed wool may be precipitated and recovered from the solution either by dialysis, by salting out with M8504. (N114) 2804, etc., or by careful addition of a suitable amount of acid or alkali.
- EXAMPLE III 40 parts of a synthetic detergent (a sodium alkyl benzene sulphonate'wherein the alkyl group contains 12 to 18 carbon atoms) and 4 parts of Hal-ISO: are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 400 parts of solution at about pH 6.5
- This solution is heated to boiling and 64' parts of I chicken feathers are added. The solution is kept boiling gently for about minutes with frequent stirring. During this period considerable dispersion of the feathers occurs and the undispersed portion becomes very soft and loses its original shape. 200 parts of boiling water are now added and the solution is boiled and stirred for about another 30 minutes. The undispersed residue is removed by suitable filtration and is washed several times in hot water. The washings and filtrate may be combined and evaporated to dryness to obtain 70 parts of a water-soluble product that has been found useful for the preparation of artificial fibers. This material contains 8.5% to 8.6% nitrogen on a dry basis.
- EXAMPLE IV 50 parts of a synthetic detergent, composed of sodium dodecyl sulphate, and 10 parts of NaHSOa are dissolved in 940 parts of water. A saturated solution of sodium hydroxide is added until the pH of the solution is about 6.0. The solution is heated to boiling and 80 parts of chicken feathers are added. The solution is gently boiled for about one hour with frequent stirring. The undispersed residue is removed by suitable filtration and is washed several times in hot water. The combined washings and filtrate are evaporated to dryness. parts of dry product are obtained having a nitrogen content of 8.5% to 9.6%. This material has been found useful for the preparation of artificial fibers.
- EXAMPLE v 1 1.6 parts of thioglycolic acid and 21 parts of urea are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution at about pH 7.0 (20.2). 2.5 parts of duck feathers are added, and the mixture is heated at about 40 C. about for 18 hours. About 78% of the feather keratin is dispersed by this treatment.
- EXAMPLEVI 1.4 parts of monothioethylene glycol and 24 parts of ammonium thiocyanate are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution having a pH of about 6.9. 2.5 parts of chicken feathers are treated with this solution for about 18 hours at about 40 C. During this period about 82% of the feather keratin is dispersed.
- EXAMPLE VII 1.4 parts of monothioethylene glycol and 20.7 parts of acetamide are dissolved in water. Sodium hydroxide solution and water are added to give 35 parts of solution having a pH of about 7.2. 2.5 parts of chicken feathers are treated with this solution at about 40 C. about for 18 hours. During this period about 59% of the feather keratin is dispersed.
- the solution be near the point of neutrality (pH 7.0)
- pH 7.0 the dispersibility of human hair in a solution of thioglycol and sodium salicylate is increased as the pH of the solution is increased about from 6.9 to 11.4.
- the use of neutral solutions merely minimizes the possibility of hydrolytic degradation of the protein which may be detrimental in some cases. If the pH is increased above about pH 10, dispersion occurs if only a disulphide-splitting agent is present; however, the presence of a protein-dispersing or proteindenaturing agent, as used in our invention permits dispersion below pH 10.
- the temperature at which dispersion, according to our invention, is obtained may range up to about 100 C., and the higher the temperature within this range, the shorter the time required for dispersion, and in some cases, a higher degree of dispersion is obtained. Therefore, it is recommended that the invention be conducted at a temperature range of up to about 100 C.
- the detergents which may be used to disperse the protein may be any alkyl aryl sulphonate or alkyl sulphate which has detergent properties.
- the held of detergents has been developed thoroughly in the last years and almost innumerable series of alkyl aryl sulphonates and alkyl sulphates having detergent properties have been described and/or patented. It has been shown that it is advantageous that besides the sulphate or sulphonate group (the hydrophilic group) the compound must also contain a high-molecular weight hydrocarbon or other hydrophobic group. There must be a balance between these two opposed groups to give the compound the requisite detergent properties.
- alkyl radical must possess 8 to 18 carbon atoms.
- alkyl naphthalene sulphonates the suiting alkylated benzene.
- alkyl group may contain less carbon atomsdown to. three are efiective.
- These detergents are generally employed in the form of their alkali metal salts-i. e., their potassium, sodium, or ammonium salts.
- Some or the particular detergents which we may use are sodium octyl benzene sulphonate, sodium nonyl benzene sulphonate, sodium decyl benzene sulphonate, sodium undecyl benzene sulphonate, sodium dodecyl benzene sulphonate, sodium tridecyl benzene sulphonate, sodium tetradecyl benzene sul phonate, sodium hexadecyl benzene sulphonate, sodium heptadecyl benzene sulphonate, sodium octadecyl benzene sulphonate, sodium tri (isopropyl) benz
- alkyl aryl sulphonate and alkyl sulphate detergents available in commerce are well suited for use in preparing the dispersions.
- alkyl benzene sulfonate where the alkyl group contains 12 to 18 carbon atoms is suitable.
- This detergent is prepared by condensation of chlorinated kerosene with benzene and sulphonation or the re-
- Other commercially available detergents which are suitable are so-, dium decyl benzene sulphonate, sodium dodecyl benzene sulphonate, alkylated monosodium benzene sulphonate containing several alkyl groups totaling 10 carbon atoms, a mixture of sodium alkyl sulphates consisting mostly of sodium lauryl sulphate, etc.
- any alkyl aryl sulphonate or alkyl sulphate which has detergent properties.
- the process comprising heating a keratin material in an essentially neutral aqueous solution containing a sulfur-containing, reductive disulphide-splitting agent and. a synthetic detergent selected from the group consisting of alkali metal salts of alkyl aryl sulphonates and of alkyl sulphates at a temperature up to about C. to disperse said keratin material in said solution.
- the process comprising heating a. keratin material in an essentially neutral aqueous solution containing sodium bisulphite and. a synthetic detergent consisting of sodium alkyl aryl tea at a temperature up to about 100' C. to disperse said keratin'material in' said solution.
- the process comprising heating a keratin material in an essentially neutral aqueous solution containing sodium bisuiphite and a synthetic detergent consisting 01' sodium alkyi sulphates at a temperature up to about 100 C. to disperse sa keratin material in said solution.
- a composition of matter consisting essentially of a dispersion of a keratin material in an essentially neutral aqueous solution containing a sulfur-containing, reductive disulphide-splittin: asent and a synthetic detergent selected from thezroupcomistinzoi'slkalimetaleeltl oi alkyl aryl smphonatu and oi alkyl sulphates.
Description
Patented Aug. 8, 1950 PROCESS OF UTILIZING DETERGENTS TO SOLUBILIZE KERATIN MATERIALS Chase B. Jones, Waltham, Mass., and Dale K. Mecham, Richmond, CaliL, assignors to the United States of America as represented by the Secretary of Agriculture No Drawing. Application November 23, 1948, Serial No. 61,694
(Granted under the act of March 3, 1883, as amended April 30, 1928; 370 0. G. 757) 4 Claims.
This application is made under the act of March 3, 1883, as amended by the act of April 30, 1928, and the invention herein described, if patented in any country, may be manufactured and used by or for the Government of the United States of America for governmental purposes throughout the world without the payment to us of any royalty thereon.
This application is a continuation-in-part of our copending application for patent, serial No.-
74B,849, filed May 8, 1947, now abandoned.
This invention relates to a method of dispersing keratin proteins obtained from a keratin ma.- terial, such as feathers, hoofs, horns, wool, and so forth, and has among its objects the use of such keratins, either in the dispersed or recovered forms, in the preparation of artificial fibers, films, plastics and the like.
Keratins, like themore soluble proteins, can be readily dispersed by hydrolysis in strong acids or alkalis, but the keratin thus dispersed cannot be recovered except as simple degradation products, such as amino acids or complex degradation products, such as peptides, peptones, and proteoses, the properties of which differ radically from those of the original keratin.
Keratins can also be dispersed in alkaline solutions of metallic sulphides and such sulphides are commonly used in cosmetic depilatories and in the removal of hair from hides in the tanning industry.
Keratins have also been dispersed at neutral reactions, but in these cases heat and high temperatures were employed to the point of charring, which produced drastic degradation oi the proteins.
Also, keratins may be dispersed in strong alkaline solutions by treatment with reducing agents, and the recovered protein is more similar to the original protein in regard to solubility, molecular size, and so forth, than are the peptides, proteoses, and so forth, referred to previously. However, the presence of the strong alkali is undesirable because it presents an opportunity for the hydrolysis of the keratin, destruction of the cystine constituent of the keratin (keratins being unique among proteins in that they contain exceptionally large amounts of cystine), and destruction of the hydroxy amino acid residues of the keratin.
According to our invention, keratin materials are dispersed under mild conditions, that is, in neutral or practically neutral reaction, and at relatively low temperatures. These conditions produce less degradation of the original keratin than occurred in the prior art and the dispersed keratin may be recovered in a form substantially similar to that of the original keratin in regard to its composition, lsoelectric point, solubility, and other properties.
The method involved in this invention is based partly on the reduction of the disulphide bonds within the keratin molecule by treating it with sulfur-containing, reductive disulphide-splitting agents, such as monoethylene thioglycol (thioglycol), thioglycolic acid (present as the thioglycolate in neutral solution) and sodium bisulphite.
The presence of alkali is obviated by the use of any of a number of protein-denaturing or protein-dispersing agents, such as urea, guanidine hydrochloride, ammonium thiocyanate, tormamide, acetamide, thiourea, sodium salicylate, urethane, phenol, lithium iodide, and surfaceactive agents, such as synthetic detergents composed of alkyl aryl sulfonates or alkyl sulphates and dispersion or the keratin is thus eflected at neutral or practically neutral reaction.
Theretore, under the above conditions of employing disulphide-splitting and protein-dispersing or protein-denaturing agents to efiect the dispersion in neutral or practically neutral reaction and at relatively low temperatures, the keratin molecule undergoes minimal degradation, the only chemical attack on the covalent linkages of the keratin being the cleavage or the disulphide bonds of the cystine moiety.
The following examples are illustrative of our invention:
EXAMPIE I ings are treated with this neutralized solution in,
a water bath at about 40 C. about :for 18 hours. The mixture is stirred at convenient intervals.
During this period about 74% ot the hoof kera- 3 tin is dispersed in the solution. After removal oi the undispersed hoof by filtration, the dispersed keratin may be precipitated either by dilution with several volumes of water, by salting out with M3804, (NHa) 2804. etc., by acidification, or by dialysis. If desired, the guanidine may be removed from the dispersion by dialysis and may be recovered from thedialysate by precipitation as the nitrate or by other suitable means.
EXAMPLE lI 1.1 parts of NaHSOa and 21 parts of urea are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution at about pH 7.1. 2.5 parts of wool are treated with this solution in a water bath at about 40 C. about for 18 hours, during which period the mixture isstirred at frequent intervals. 52% of the original weight of the wool is dispersed by this treatment. The dispersed wool may be precipitated and recovered from the solution either by dialysis, by salting out with M8504. (N114) 2804, etc., or by careful addition of a suitable amount of acid or alkali.
EXAMPLE III 40 parts of a synthetic detergent (a sodium alkyl benzene sulphonate'wherein the alkyl group contains 12 to 18 carbon atoms) and 4 parts of Hal-ISO: are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 400 parts of solution at about pH 6.5
This solution is heated to boiling and 64' parts of I chicken feathers are added. The solution is kept boiling gently for about minutes with frequent stirring. During this period considerable dispersion of the feathers occurs and the undispersed portion becomes very soft and loses its original shape. 200 parts of boiling water are now added and the solution is boiled and stirred for about another 30 minutes. The undispersed residue is removed by suitable filtration and is washed several times in hot water. The washings and filtrate may be combined and evaporated to dryness to obtain 70 parts of a water-soluble product that has been found useful for the preparation of artificial fibers. This material contains 8.5% to 8.6% nitrogen on a dry basis.
EXAMPLE IV 50 parts of a synthetic detergent, composed of sodium dodecyl sulphate, and 10 parts of NaHSOa are dissolved in 940 parts of water. A saturated solution of sodium hydroxide is added until the pH of the solution is about 6.0. The solution is heated to boiling and 80 parts of chicken feathers are added. The solution is gently boiled for about one hour with frequent stirring. The undispersed residue is removed by suitable filtration and is washed several times in hot water. The combined washings and filtrate are evaporated to dryness. parts of dry product are obtained having a nitrogen content of 8.5% to 9.6%. This material has been found useful for the preparation of artificial fibers.
EXAMPLE v 1 1.6 parts of thioglycolic acid and 21 parts of urea are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution at about pH 7.0 (20.2). 2.5 parts of duck feathers are added, and the mixture is heated at about 40 C. about for 18 hours. About 78% of the feather keratin is dispersed by this treatment.
EXAMPLEVI 1.4 parts of monothioethylene glycol and 24 parts of ammonium thiocyanate are dissolved in water. Sodium hydroxide solution and water are added as required to obtain 35 parts of solution having a pH of about 6.9. 2.5 parts of chicken feathers are treated with this solution for about 18 hours at about 40 C. During this period about 82% of the feather keratin is dispersed.
EXAMPLE VII 1.4 parts of monothioethylene glycol and 20.7 parts of acetamide are dissolved in water. Sodium hydroxide solution and water are added to give 35 parts of solution having a pH of about 7.2. 2.5 parts of chicken feathers are treated with this solution at about 40 C. about for 18 hours. During this period about 59% of the feather keratin is dispersed.
EXAMPLE VIII other experiments were performed, the results of which are shown in the following tables:
TABLE I Dispersz'bz'lzties of keratins in difierent dispersing agents upon reduction by 0.5 M thioglycol [2.5 g. of keratin was treated for 18 hours at about 40 C. with 35 mi. 0! solution at pH 7.]
Guanidine S thetic l N H CNS Formamide Acetamlde Thlourea 3m Kent 5% 9.0 M) (10.0 M) (10.0 M) 1.2 M) 83 2? Per cent Per cent Per cent Per cent Per cent Per cent 2 Chicken feather 84 82 66 5 l 79, Due]: leather 83 80 41 36 6 51, 53 Tortoise scutes 84 52 10, 8 Snake skim" 55 44 26, 30v Cattle hooi 74 56 7 6 5 58, 64
l 61 36 4 6 4 44, 50 Cattle horn 36 27 3 5 4 14, 12' 0g hair 56 26 2 2 2 4, 3 Human a 50 ll 0 0 2 2, l v Ovokeratin 8 6 4 3 l5 2, 4
1 Composed of sodium dodecyl sulphate. 1 First values calculated from dry weights of residues after acetone extraction; second values calculated from nitrogen analyses.
TABLE II Dispersibilities of keratins in M urea upon reduction by difierent disulphide-splitting agents Many changes and variations in the conditions for dispersion shown in the foregoing examples and tables may be made. As a rule, the higher the concentration of protein-dispersing or protein-denaturing agent, the reater is the percentage of keratin dispersed, the solubility of the dispersing or denaturing agent being a limiting factor. A greater degree of dispersion may also be obtained in some cases by increasing the concentration of the disulphide-splitting agent, as for example, for monoethylene thioglycol and thloglycolic acid. An increase in the concentration of NaHSOs, however, often results in a decrease in the extent of dispersion of the keratin, presumably due to a salting-out efiect.
Also, it is not necessary in every case that the solution be near the point of neutrality (pH 7.0) For example, the dispersibility of human hair in a solution of thioglycol and sodium salicylate is increased as the pH of the solution is increased about from 6.9 to 11.4. The use of neutral solutions merely minimizes the possibility of hydrolytic degradation of the protein which may be detrimental in some cases. If the pH is increased above about pH 10, dispersion occurs if only a disulphide-splitting agent is present; however, the presence of a protein-dispersing or proteindenaturing agent, as used in our invention permits dispersion below pH 10.
The temperature at which dispersion, according to our invention, is obtained may range up to about 100 C., and the higher the temperature within this range, the shorter the time required for dispersion, and in some cases, a higher degree of dispersion is obtained. Therefore, it is recommended that the invention be conducted at a temperature range of up to about 100 C.
The detergents which may be used to disperse the protein may be any alkyl aryl sulphonate or alkyl sulphate which has detergent properties. The held of detergents has been developed thoroughly in the last years and almost innumerable series of alkyl aryl sulphonates and alkyl sulphates having detergent properties have been described and/or patented. It has been shown that it is esential that besides the sulphate or sulphonate group (the hydrophilic group) the compound must also contain a high-molecular weight hydrocarbon or other hydrophobic group. There must be a balance between these two opposed groups to give the compound the requisite detergent properties. Thus in the case of the alkyl sulphates and alkyl benzene sulphonates the alkyl radical must possess 8 to 18 carbon atoms. In the case of alkyl naphthalene sulphonates the suiting alkylated benzene.
alkyl group may contain less carbon atomsdown to. three are efiective. These detergents are generally employed in the form of their alkali metal salts-i. e., their potassium, sodium, or ammonium salts. Some or the particular detergents which we may use are sodium octyl benzene sulphonate, sodium nonyl benzene sulphonate, sodium decyl benzene sulphonate, sodium undecyl benzene sulphonate, sodium dodecyl benzene sulphonate, sodium tridecyl benzene sulphonate, sodium tetradecyl benzene sul phonate, sodium hexadecyl benzene sulphonate, sodium heptadecyl benzene sulphonate, sodium octadecyl benzene sulphonate, sodium tri (isopropyl) benzene sulphonate, sodium tetra (isopropyl) benzene sulphonate, sodium di (isobutyl) benzene sulphonate, sodium tri (isobutyl) benzene sulphonate, sodium tetra (isobutyl) benzene sulphonate, any of the above named compounds in the form of their potassium or ammonium salts, sodium isopropyl naphthalene sulphonate, sodium di (isopropyl) naphthalene sulphonate, sodium tri (isopropyl) naphthalene sulphonate, sodium isoamyl naphthalene sulphonate, sodium di (isoamyl) naphthalene sulphonate, sodium isobutyl naphthalene sulphonate, sodium di (isobutyl) naphthalene sulphonate, sodium tri (isobutyl) naphthalene sulphonate, sodium octyl naphthalene sulphonate, sodium decyl naphthalene sulphonate, or any of the above named alkyl naphthalene sulphonates in the form of their potassium or ammonium salts, sodium octyl sulphate, sodium nonyl sulphate, sodium decyl sulphate, sodium undecyl sulphate, sodium dodecyl sulphate, sodium tridecyl sulphate, sodium tetradecyl sulphate, sodium pentadecyl sulphate, sodium cetyl sulphate, sodium heptadecyl sulphate, sodium octadecyl sulphate, sodium Z-pentadecyl sulphate, sodium oleyl sulphate, and any of the above named alkyl sulphates in the form of their potassium or ammonium salts. It has been found that many of the alkyl aryl sulphonate and alkyl sulphate detergents available in commerce are well suited for use in preparing the dispersions. For instance the sodium alkyl benzene sulfonate where the alkyl group contains 12 to 18 carbon atoms is suitable. This detergent is prepared by condensation of chlorinated kerosene with benzene and sulphonation or the re- Other commercially available detergents which are suitable are so-, dium decyl benzene sulphonate, sodium dodecyl benzene sulphonate, alkylated monosodium benzene sulphonate containing several alkyl groups totaling 10 carbon atoms, a mixture of sodium alkyl sulphates consisting mostly of sodium lauryl sulphate, etc. Thus we can use any alkyl aryl sulphonate or alkyl sulphate which has detergent properties.
Having thus described our invention, we claim:
1. The process comprising heating a keratin material in an essentially neutral aqueous solution containing a sulfur-containing, reductive disulphide-splitting agent and. a synthetic detergent selected from the group consisting of alkali metal salts of alkyl aryl sulphonates and of alkyl sulphates at a temperature up to about C. to disperse said keratin material in said solution.
2. The process comprising heating a. keratin material in an essentially neutral aqueous solution containing sodium bisulphite and. a synthetic detergent consisting of sodium alkyl aryl tea at a temperature up to about 100' C. to disperse said keratin'material in' said solution.
3. The process comprising heating a keratin material in an essentially neutral aqueous solution containing sodium bisuiphite and a synthetic detergent consisting 01' sodium alkyi sulphates at a temperature up to about 100 C. to disperse sa keratin material in said solution.
4. A composition of matter consisting essentially of a dispersion of a keratin material in an essentially neutral aqueous solution containing a sulfur-containing, reductive disulphide-splittin: asent and a synthetic detergent selected from thezroupcomistinzoi'slkalimetaleeltl oi alkyl aryl smphonatu and oi alkyl sulphates.
I CHASE n. .roum.
DALE K. mncnsu.
REFERENCES cI'rEn The following references are of record in the file of this patent:
UNITED STATES PATENTS
Claims (1)
1. THE PROCESS COMPRISING HEATING A KERATIN MATERIAL IN AN ESSENTIALLY NEUTRAL AQUEOUS SOLUTION CONTAINING A SULFUR-CONTAINING, REDUCTIVE DISULPHIDE-SPLITTING AGENT AND A SYNTHETIC DETERGENT SELECTED FROM THE GROUP CONSISTING OF ALKALI METAL SALTS OF ARYL SULPHONATES AND OF ALKYL SULPHATES AT A TEMPERATURE UP TO ABOUT 100*C. TO DISPERSE SAID KERATIN MATERIAL IN SAID SOLUTION
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US2615782A (en) * | 1950-08-11 | 1952-10-28 | Procter & Gamble | Modification of keratin |
DE2809559A1 (en) * | 1977-03-07 | 1978-09-21 | Sekisui Chemical Co Ltd | KERATIN-LIKE SUBSTANCE WITH HIGH ADSORPTION, THEIR PRODUCTION AND USE |
US4369037A (en) * | 1980-11-19 | 1983-01-18 | Kao Soap Co., Ltd. | Hair treatment cosmetics containing cationic keratin derivatives |
US20010047082A1 (en) * | 1999-06-11 | 2001-11-29 | Van Dyke Mark E. | Soluble keratin peptide |
US20030228353A1 (en) * | 2002-01-28 | 2003-12-11 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
US20040076599A1 (en) * | 1999-09-13 | 2004-04-22 | Southwest Research Institute | Keratin-based powders and hydrogel for pharmaceutical applications |
US20040082717A1 (en) * | 2002-06-24 | 2004-04-29 | Southwest Research Institute | Keratin-silicone copolymers and interpenetrating networks (IPN's), methods of production and methods of use thereof |
US6783546B2 (en) | 1999-09-13 | 2004-08-31 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
US6849092B2 (en) | 1999-09-13 | 2005-02-01 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
US20070166348A1 (en) * | 2005-10-21 | 2007-07-19 | Van Dyke Mark E | Keratin bioceramic compositions |
US20080274165A1 (en) * | 2006-02-17 | 2008-11-06 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
US20090004242A1 (en) * | 2006-02-17 | 2009-01-01 | Van Dyke Mark E | Coatings and Biomedical Implants Formed From Keratin Biomaterials |
US20090047260A1 (en) * | 2007-08-17 | 2009-02-19 | Wake Forest University Health Sciences | Keratin biomaterials for cell culture and methods of use |
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DE2809559A1 (en) * | 1977-03-07 | 1978-09-21 | Sekisui Chemical Co Ltd | KERATIN-LIKE SUBSTANCE WITH HIGH ADSORPTION, THEIR PRODUCTION AND USE |
US4141888A (en) * | 1977-03-07 | 1979-02-27 | Sekisui Kagaku Kogyo Kabushiki Kaisha | Process for producing reduced keratinous substances using urea or thiourea |
US4369037A (en) * | 1980-11-19 | 1983-01-18 | Kao Soap Co., Ltd. | Hair treatment cosmetics containing cationic keratin derivatives |
US20010047082A1 (en) * | 1999-06-11 | 2001-11-29 | Van Dyke Mark E. | Soluble keratin peptide |
US20040076599A1 (en) * | 1999-09-13 | 2004-04-22 | Southwest Research Institute | Keratin-based powders and hydrogel for pharmaceutical applications |
US6783546B2 (en) | 1999-09-13 | 2004-08-31 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
US6849092B2 (en) | 1999-09-13 | 2005-02-01 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
US20050169963A1 (en) * | 1999-09-13 | 2005-08-04 | Southwest Ressearch Institute | Implantable prosthetic or tissue expanding device |
US20080089930A1 (en) * | 1999-09-13 | 2008-04-17 | Keraplast Technologies, Ltd. | Keratin-Based Powders and Hydrogel for Pharmaceutical Applications |
US7501485B2 (en) | 2002-01-28 | 2009-03-10 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
US20030228353A1 (en) * | 2002-01-28 | 2003-12-11 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
US8324346B2 (en) | 2002-01-28 | 2012-12-04 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
US20110070276A1 (en) * | 2002-01-28 | 2011-03-24 | Keraplast Technologies, Ltd. | Bioactive keratin peptides |
US20040082717A1 (en) * | 2002-06-24 | 2004-04-29 | Southwest Research Institute | Keratin-silicone copolymers and interpenetrating networks (IPN's), methods of production and methods of use thereof |
US8637231B2 (en) | 2004-08-17 | 2014-01-28 | Wake Forest University Health Sciences | Method for increasing the volume of a blood substitute with an expander comprising basic alpha keratose |
US11173233B2 (en) | 2005-10-21 | 2021-11-16 | Wake Forest University Health Sciences | Keratin bioceramic compositions |
US8920827B2 (en) | 2005-10-21 | 2014-12-30 | Wake Forest University Health Sciences | Keratin bioceramic compositions |
US20070166348A1 (en) * | 2005-10-21 | 2007-07-19 | Van Dyke Mark E | Keratin bioceramic compositions |
US9968706B2 (en) | 2006-02-10 | 2018-05-15 | Wake Forest University Health Sciences | Nerve regeneration employing keratin biomaterials |
US20110137329A1 (en) * | 2006-02-10 | 2011-06-09 | Dyke Mark E Van | Nerve regeneration employing keratin biomaterials |
US8968764B2 (en) | 2006-02-10 | 2015-03-03 | Wake Forest University Health Sciences | Nerve regeneration employing keratin biomaterials |
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US8273702B2 (en) | 2006-02-17 | 2012-09-25 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
US20080274165A1 (en) * | 2006-02-17 | 2008-11-06 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
US8258093B2 (en) | 2006-02-17 | 2012-09-04 | Wake Forest University Health Sciences | Wound healing compositions containing keratin biomaterials |
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US9149566B2 (en) | 2006-02-17 | 2015-10-06 | Wake Forest University Health Sciences | Coatings and biomedical implants formed from keratin biomaterials |
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US20090047260A1 (en) * | 2007-08-17 | 2009-02-19 | Wake Forest University Health Sciences | Keratin biomaterials for cell culture and methods of use |
US9068162B2 (en) | 2007-08-17 | 2015-06-30 | Wake Forest University Health Sciences | Keratin biomaterials for cell culture and methods of use |
US10434213B2 (en) | 2010-03-05 | 2019-10-08 | Wake Forest University Health Sciences | Controlled delivery system |
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US20110217285A1 (en) * | 2010-03-08 | 2011-09-08 | Van Dyke Mark E | Keratin biomaterials for treatment of ischemia |
US8545893B2 (en) | 2010-03-08 | 2013-10-01 | Wake Forest University Health Sciences | Keratin biomaterials for treatment of ischemia |
US9220754B2 (en) | 2010-11-17 | 2015-12-29 | Wake Forest University Health Sciences | Keratin compositions for treatment of bone deficiency or injury |
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