EP2648538A1 - Hydrophobisiertes proteinhydrolysat - Google Patents
Hydrophobisiertes proteinhydrolysatInfo
- Publication number
- EP2648538A1 EP2648538A1 EP11788092.2A EP11788092A EP2648538A1 EP 2648538 A1 EP2648538 A1 EP 2648538A1 EP 11788092 A EP11788092 A EP 11788092A EP 2648538 A1 EP2648538 A1 EP 2648538A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- peptide mixture
- process step
- protein
- protein hydrolyzate
- mixture according
- 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.)
- Withdrawn
Links
- 239000003531 protein hydrolysate Substances 0.000 title claims abstract description 50
- 108010009736 Protein Hydrolysates Proteins 0.000 title abstract description 15
- 239000002537 cosmetic Substances 0.000 claims abstract description 8
- 238000004519 manufacturing process Methods 0.000 claims abstract description 3
- 238000000034 method Methods 0.000 claims description 45
- 239000000203 mixture Substances 0.000 claims description 42
- 235000018102 proteins Nutrition 0.000 claims description 37
- 102000004169 proteins and genes Human genes 0.000 claims description 37
- 108090000623 proteins and genes Proteins 0.000 claims description 37
- 108060008539 Transglutaminase Proteins 0.000 claims description 34
- 102000003601 transglutaminase Human genes 0.000 claims description 34
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 27
- 239000006260 foam Substances 0.000 claims description 13
- 239000002253 acid Substances 0.000 claims description 11
- 102000004190 Enzymes Human genes 0.000 claims description 9
- 108090000790 Enzymes Proteins 0.000 claims description 9
- 230000007062 hydrolysis Effects 0.000 claims description 9
- 238000006460 hydrolysis reaction Methods 0.000 claims description 9
- 238000009472 formulation Methods 0.000 claims description 8
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 claims description 7
- 230000008569 process Effects 0.000 claims description 7
- 125000000217 alkyl group Chemical group 0.000 claims description 5
- 125000002924 primary amino group Chemical class [H]N([H])* 0.000 claims description 5
- 238000000746 purification Methods 0.000 claims description 5
- 241000187747 Streptomyces Species 0.000 claims description 4
- 239000003995 emulsifying agent Substances 0.000 claims description 4
- 125000004432 carbon atom Chemical group C* 0.000 claims description 3
- 230000031787 nutrient reservoir activity Effects 0.000 claims description 3
- -1 octadecadienyl Chemical group 0.000 claims description 3
- 239000008194 pharmaceutical composition Substances 0.000 claims description 3
- 239000004094 surface-active agent Substances 0.000 claims description 3
- 244000063299 Bacillus subtilis Species 0.000 claims description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 2
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 claims description 2
- 235000021120 animal protein Nutrition 0.000 claims description 2
- 125000001204 arachidyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 239000012459 cleaning agent Substances 0.000 claims description 2
- 239000012141 concentrate Substances 0.000 claims description 2
- 125000002704 decyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 claims description 2
- 239000002270 dispersing agent Substances 0.000 claims description 2
- 125000003438 dodecyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 claims description 2
- 239000004088 foaming agent Substances 0.000 claims description 2
- 230000000813 microbial effect Effects 0.000 claims description 2
- 125000001421 myristyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 125000005064 octadecenyl group Chemical group C(=CCCCCCCCCCCCCCCCC)* 0.000 claims description 2
- 125000002347 octyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 125000000913 palmityl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 239000003381 stabilizer Substances 0.000 claims description 2
- 125000004079 stearyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 125000000467 secondary amino group Chemical class [H]N([*:1])[*:2] 0.000 claims 3
- 238000002360 preparation method Methods 0.000 abstract description 8
- 230000002255 enzymatic effect Effects 0.000 abstract description 2
- 241000209140 Triticum Species 0.000 description 24
- 235000021307 Triticum Nutrition 0.000 description 24
- 238000006243 chemical reaction Methods 0.000 description 15
- 150000003973 alkyl amines Chemical class 0.000 description 10
- IOQPZZOEVPZRBK-UHFFFAOYSA-N octan-1-amine Chemical compound CCCCCCCCN IOQPZZOEVPZRBK-UHFFFAOYSA-N 0.000 description 10
- 150000001412 amines Chemical class 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 150000001805 chlorine compounds Chemical class 0.000 description 6
- 235000014113 dietary fatty acids Nutrition 0.000 description 6
- 239000000194 fatty acid Substances 0.000 description 6
- 229930195729 fatty acid Natural products 0.000 description 6
- 150000004665 fatty acids Chemical class 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000011541 reaction mixture Substances 0.000 description 6
- 235000013305 food Nutrition 0.000 description 5
- NGNBDVOYPDDBFK-UHFFFAOYSA-N 2-[2,4-di(pentan-2-yl)phenoxy]acetyl chloride Chemical compound CCCC(C)C1=CC=C(OCC(Cl)=O)C(C(C)CCC)=C1 NGNBDVOYPDDBFK-UHFFFAOYSA-N 0.000 description 4
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 4
- 102000011632 Caseins Human genes 0.000 description 4
- 108010076119 Caseins Proteins 0.000 description 4
- 230000029936 alkylation Effects 0.000 description 4
- 238000005804 alkylation reaction Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 4
- 235000021240 caseins Nutrition 0.000 description 4
- JRBPAEWTRLWTQC-UHFFFAOYSA-N dodecylamine Chemical compound CCCCCCCCCCCCN JRBPAEWTRLWTQC-UHFFFAOYSA-N 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- YAYNEUUHHLGGAH-UHFFFAOYSA-N 1-chlorododecane Chemical group CCCCCCCCCCCCCl YAYNEUUHHLGGAH-UHFFFAOYSA-N 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- 230000003750 conditioning effect Effects 0.000 description 3
- 238000001212 derivatisation Methods 0.000 description 3
- 239000000839 emulsion Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000005187 foaming Methods 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 150000003141 primary amines Chemical class 0.000 description 3
- 235000002639 sodium chloride Nutrition 0.000 description 3
- VYZAHLCBVHPDDF-UHFFFAOYSA-N Dinitrochlorobenzene Chemical compound [O-][N+](=O)C1=CC=C(Cl)C([N+]([O-])=O)=C1 VYZAHLCBVHPDDF-UHFFFAOYSA-N 0.000 description 2
- 108010068370 Glutens Proteins 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 102000008192 Lactoglobulins Human genes 0.000 description 2
- 108010060630 Lactoglobulins Proteins 0.000 description 2
- 241000219745 Lupinus Species 0.000 description 2
- 108010073771 Soybean Proteins Proteins 0.000 description 2
- 108010046377 Whey Proteins Proteins 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- PXTQQOLKZBLYDY-UHFFFAOYSA-N bis(2-ethylhexyl) carbonate Chemical compound CCCCC(CC)COC(=O)OCC(CC)CCCC PXTQQOLKZBLYDY-UHFFFAOYSA-N 0.000 description 2
- 238000006555 catalytic reaction Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000006482 condensation reaction Methods 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 230000001804 emulsifying effect Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 235000019197 fats Nutrition 0.000 description 2
- 235000021312 gluten Nutrition 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000005191 phase separation Methods 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 150000003335 secondary amines Chemical class 0.000 description 2
- 229940001941 soy protein Drugs 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 239000003760 tallow Substances 0.000 description 2
- FYSNRJHAOHDILO-UHFFFAOYSA-N thionyl chloride Chemical compound ClS(Cl)=O FYSNRJHAOHDILO-UHFFFAOYSA-N 0.000 description 2
- 238000007056 transamidation reaction Methods 0.000 description 2
- 235000013311 vegetables Nutrition 0.000 description 2
- 235000021119 whey protein Nutrition 0.000 description 2
- 241000186361 Actinobacteria <class> Species 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- 244000060011 Cocos nucifera Species 0.000 description 1
- 235000013162 Cocos nucifera Nutrition 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 241000195493 Cryptophyta Species 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 244000024675 Eruca sativa Species 0.000 description 1
- 235000014755 Eruca sativa Nutrition 0.000 description 1
- 108010022355 Fibroins Proteins 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 244000020551 Helianthus annuus Species 0.000 description 1
- 235000003222 Helianthus annuus Nutrition 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 241001467460 Myxogastria Species 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 108010084695 Pea Proteins Proteins 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 235000019484 Rapeseed oil Nutrition 0.000 description 1
- 238000003436 Schotten-Baumann reaction Methods 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 241001495137 Streptomyces mobaraensis Species 0.000 description 1
- 235000019486 Sunflower oil Nutrition 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 240000000359 Triticum dicoccon Species 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 230000000895 acaricidal effect Effects 0.000 description 1
- 239000000642 acaricide Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 108091005588 alkylated proteins Proteins 0.000 description 1
- 229940059260 amidate Drugs 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 125000002511 behenyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 229940021722 caseins Drugs 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- POULHZVOKOAJMA-UHFFFAOYSA-N dodecanoic acid Chemical class CCCCCCCCCCCC(O)=O POULHZVOKOAJMA-UHFFFAOYSA-N 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- NPUKDXXFDDZOKR-LLVKDONJSA-N etomidate Chemical compound CCOC(=O)C1=CN=CN1[C@H](C)C1=CC=CC=C1 NPUKDXXFDDZOKR-LLVKDONJSA-N 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 239000000417 fungicide Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000003760 hair shine Effects 0.000 description 1
- 239000004009 herbicide Substances 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000002917 insecticide Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 235000021374 legumes Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 239000005645 nematicide Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000012038 nucleophile Substances 0.000 description 1
- 230000000269 nucleophilic effect Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 235000019702 pea protein Nutrition 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 239000002453 shampoo Substances 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 108010027322 single cell proteins Proteins 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000002600 sunflower oil Substances 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/10—Foods or foodstuffs containing additives; Preparation or treatment thereof containing emulsifiers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/02—Preparations for cleaning the hair
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/12—Preparations containing hair conditioners
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Definitions
- the invention provides enzymatically hydrophobized protein hydrolysates, their preparation and use, and cosmetic preparations containing them.
- Proteins and protein hydrolysates represent an interesting class of raw materials because they are readily available, of natural origin and biodegradable. Due to the lack of lipophilic groups, the surface-active properties of the proteins are weak. Therefore, it is necessary to introduce additional lipophilic groups to obtain powerful, protein-based, surface-active compounds. According to the state of the art, the desired modified proteins have been produced for some time by condensation of protein hydrolysates and acid chlorides (hereinafter PHFSK) and used in various applications (for example for the preparation of emulsions, foams, conditioning of skin and hair, dispersing because of their surfactant properties of pigments in various solvents, etc.).
- PHFSK protein hydrolysates and acid chlorides
- Protein hydrolysates has been known for some time.
- the reaction is a transamidation reaction between lysine and glutamine residues of proteins that releases ammonia and forms an isopeptide bond.
- alkylated protein hydrolysates or “alkylation” is used Peptides / protein (CH 2 ) 2 + H 2 N-R 1
- the object of the invention was to provide hydrophobized peptides which overcome at least one disadvantage of the prior art.
- the present invention therefore enzymatically hydrophobized protein hydrolysates, their preparation and use.
- Another object of the invention are formulations, in particular
- An advantage of the present invention is that no acid chlorides are needed during the synthesis.
- Glutamineehalts of protein hydrolysates may have a high degree of derivatization and at the same time lower concentrations of alkylamines must be used because it, in contrast to the acid chlorides, does not lead to side reactions (hydrolysis).
- the subject matter of the present invention is an alkylated peptide mixture obtainable by a process comprising the process steps
- R 1 and R 2 are independently or identically selected from optionally unsaturated, optionally substituted, optionally branched organic radical having 5 to 40, preferably 5 to 22, in particular 6 to 18 carbon atoms.
- alkylated peptide mixture is to be understood as meaning a mixture comprising at least two peptides which are each alkylated on at least one glutamine
- this protein must have at least two glutamine residues.
- the at least one protein is preferably selected from the list comprising, preferably consisting of:
- Isolated plant storage proteins such as e.g. Wheat protein (gluten), soy protein, pea protein, rice protein, corn protein, lupine protein,
- animal proteins such as e.g. Collagen, keratin, casein, whey proteins (lactoglobulins), silk protein (fibroin) and
- the protein is preferably selected from the list comprising, preferably consisting of, wheat gluten, isolated storage proteins of legumes, in particular soy, pea, lupine and milk proteins, in particular caseins and lactoglobulins, Whole wheat Whole is particularly preferred ..
- the hydrolysis in process step A) is preferably catalyzed by the addition of acid, more preferably by the use of enzymes. Suitable methods are known to the person skilled in the art; Likewise, no effort is required to set the respective process parameters in such a way that in process step A)
- Protein hydrolysates with desired average molecular weights arise.
- the protein hydrolyzate from process step A) preferably has an average molecular weight of from 203 g / mol to 100,000 g / mol, preferably from 500 g / mol to 20,000 g / mol, in particular from 1000 g / mol to 15,000 g / mol.
- Protein hydrolysates which can be prepared by process step A) and can be used directly in process step B) are also commercially available; such are for example:
- Meripro 810 and Meripro 71 1 (wheat protein hydrolysates, enzymatic and chemical, Syral), Naturalys® W (wheat protein hydrolyzate, Roquette) cropeptide W,
- Transglutaminases belonging to the EC class 2.3.2.13 as well as a fragment of these transglutaminases, which has corresponding enzyme activity.
- Such enzymes can be isolated, for example, from Streptoverticillium, Bacillus, various Actinomycetes and Myxomycetes, but also from plants, fish and mammalian sources such as swine liver.
- EP2123756 and WO2009101762 describe stabilized compared to their Wld type
- Transglutaminases whose use in process step B) according to the invention is preferred.
- transglutaminases used in process step B) are isolatable selected from the list consisting of Bacillus subtilis, Streptomyces mombaraensis (formerly Streptoverticillium mobaraense).
- a particularly preferred transglutaminase is selected from the transglutaminases of the company Ajinomoto available under the trade name "Activa"
- the protein hydrolyzate is preferably used in a concentration between 5 wt .-% and 40 wt .-%, preferably between 15 wt .-% and 25 wt .-%, based on the total reaction mixture, wherein the solution or Dispersant is preferably water.
- reaction mixture may be advantageous to heat the reaction mixture to above 50 ° C., preferably to above 70 ° C., in particular to above 80 ° C., before the addition of the transglutaminase in process step B), in order to accelerate the hydration process, wherein preferably a thorough mixing, as by stirring, the reaction mixture takes place.
- the radicals R 1 and R 2 of the primary or secondary amine of the general formula (I) in process step B) are preferably selected from the group consisting of alkyl and alkenyl radical, preferably linear, unsubstituted alkyl and alkenyl radical, in particular an octyl, Decyl, dodecyl, tetradecyl, hexadecyl, octadecyl, octadecenyl, octadecadienyl, eicosyl, docosyl.
- alkyl and alkenyl radical preferably linear, unsubstituted alkyl and alkenyl radical, in particular an octyl, Decyl, dodecyl, tetradecyl, hexadecyl, octadecyl, octadecenyl, octadecadienyl, eicosyl,
- radicals R 1 and R 2 may also be mixtures of alkyl radicals
- alkyl radicals of such technical mixtures are preferably derived from fatty acid mixtures which can be obtained by various processes from vegetable fatty acid mixtures and can be fractionated by various processes.
- Fatty acid composition of such vegetable fatty acid mixtures varies in
- oilseed used for the production and is the expert for example in the form of optionally fractionated rapeseed oil, soybean oil,
- the alkylamines preferably used in process step B) are selected from the group consisting of: rapeseed fatty amine, soybean fatty amine, sunflower fatty amine, tallow fatty amine, palm fat amine, palm kernel fat amine and coconut fatty amine.
- the amine of the general formula (I) is preferably used in process step B) in a concentration of between 0.25% by weight and 10% by weight, in particular between 0.5% by weight and 5% by weight, based on used the entire reaction mixture.
- the enzyme activity in the reaction batch in process step B) is preferably 10 to 25,000 U / l, preferably 200 to 1000 U / l, more preferably 300 to 600 U / l, the U unit being prepared according to the method described in Folk and Cole (1966), Biochim. Biophys. Acta 122: 244-264,
- hydroxamate assay can be determined.
- the pH is preferably between 5 and 10, preferably between 6 and 8, particularly preferably between 6.5 and 7.5.
- the temperature of the reaction mixture during the transglutaminase reaction in process step B) is preferably 20 ° C to 50 ° C, preferably 30 ° C to 45 ° C and particularly preferably 35 ° C to 40 ° C.
- the reaction time of the transglutaminase reaction in process step B) is up to several hours, depending on the temperature used.
- process step A the hydrolysis is catalyzed by the use of at least one enzyme, it may be advantageous for reasons of time saving if process step A) and process step B) are carried out simultaneously.
- Another object of the present invention is the method described above, can be prepared with the peptide mixtures of the invention.
- Preferred methods according to the invention are those which lead to the abovementioned preferred peptide mixtures according to the invention.
- Another object of the present invention are cosmetic, dermatological or pharmaceutical formulations, crop protection formulations and care and cleaning agents and surfactant concentrates containing alkylated peptide mixtures according to the invention.
- care products is understood here to mean a formulation which fulfills the purpose of obtaining an object in its original form, the effects of external influences (eg time, light, temperature, pressure, pollution, chemical reaction with others, with the object in contact reactive
- crop protection formulations are meant those formulations which are manifestly used for crop protection by the manner in which they are prepared, in particular when at least one of the classes of herbicides, fungicides, insecticides, acaricides, is included in the formulation .
- herbicides fungicides, insecticides, acaricides
- Soil structure improver is included.
- preferred cosmetic compositions are selected from the group consisting of: creams, lotions, rinses and shampoos.
- Another object of the present invention is a use of the peptide mixtures according to the invention as an emulsifier, such as O / W or W / O emulsifier, as a conditioning agent for skin and hair, as a dispersing aid, in particular for cosmetic pigments, as a foaming agent or foam stabilizer.
- an emulsifier such as O / W or W / O emulsifier
- Figure 1 Improvement in foam stability by transglutaminase-catalyzed hydrophobization of modified wheat protein hydrolyzate.
- MP810 squares
- MP810 + OA + TG (inact.) Triangles
- Meripro 810 + octylamine (OA) + inactivated transglutaminase (TG) negative control
- (Diamonds) Meripro 810 + octylamine (OA) + transglutaminase (TG)
- a commercial transglutaminase preparation (Activa WM, Ajinomoto) was added and stirred at 45 ° C. for a period of 24 h. Subsequently, the enzyme was inactivated at a temperature of 80 ° C. As controls were each approaches with inactivated enzyme and approaches without alkylamine performed.
- the surface tension against air or the interfacial tension against paraffin or diethylhexyl carbonate (DEC) was determined by means of the pendant drop method. There were 1% solutions of octylamine modified
- Table 1 Influence of transglutaminase catalyzed hydrophobization of a wheat protein hydrolyzate (Meripro 810, Syral) on interfacial activity.
- volume scale filled and shaken under the same conditions for one minute.
- the volume of foam over the liquid was read over time to To assess initial foam volume and foam stability. This showed a significant foam-stabilizing effect of the hydrophobicized
- Example 5 Comparison to an Acid Chloride Modified Wheat Protein Hydrolyzate A laurylamine modified wheat protein hydrolyzate was prepared as described in Example 1; the concentration of laurylamine used was 0.625% (w / w).
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE102010062600A DE102010062600A1 (de) | 2010-12-08 | 2010-12-08 | Hydrophobisiertes Proteinhydrolysat |
| PCT/EP2011/069811 WO2012076284A1 (de) | 2010-12-08 | 2011-11-10 | Hydrophobisiertes proteinhydrolysat |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| EP2648538A1 true EP2648538A1 (de) | 2013-10-16 |
Family
ID=45044545
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP11788092.2A Withdrawn EP2648538A1 (de) | 2010-12-08 | 2011-11-10 | Hydrophobisiertes proteinhydrolysat |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20130251658A1 (ja) |
| EP (1) | EP2648538A1 (ja) |
| JP (1) | JP5951629B2 (ja) |
| CN (1) | CN103249313A (ja) |
| BR (1) | BR112013012390A8 (ja) |
| DE (1) | DE102010062600A1 (ja) |
| WO (1) | WO2012076284A1 (ja) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE102012205372A1 (de) * | 2012-04-02 | 2013-10-02 | Evonik Industries Ag | Glutaminreiche Peptide als Luftporenbildner in Baustoffmassen |
| CN106082752B (zh) * | 2016-06-15 | 2017-11-24 | 中原工学院 | 一种酶交联混合水解蛋白水泥发泡剂的制备方法 |
| CN112998010A (zh) * | 2021-03-03 | 2021-06-22 | 成都嘉佑美康新材料科技有限公司 | 一种无人机植保飞防专用助剂及其制备方法和应用 |
| CN115233450B (zh) * | 2022-08-04 | 2023-12-26 | 江南大学 | 一种生物法制备醇溶蛋白疏水整理剂的方法 |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH636248A5 (fr) * | 1979-03-09 | 1983-05-31 | Nestle Sa | Procede de preparation d'un hydrolysat de proteines purifie. |
| JPS635009A (ja) * | 1986-06-24 | 1988-01-11 | Kao Corp | 化粧料 |
| JP2736425B2 (ja) * | 1988-11-24 | 1998-04-02 | 一丸ファルコス株式会社 | 動物又は植物由来蛋白加水分解物のアルキル化修飾物を含有する化粧料 |
| JPH0732678B2 (ja) * | 1989-06-07 | 1995-04-12 | ハウス食品株式会社 | 容器入りドリア |
| EP0725145A4 (en) * | 1994-08-23 | 1997-06-11 | Drug Delivery System Inst Ltd | PROTEIN MODIFICATION PROCESS |
| US5490980A (en) * | 1994-09-28 | 1996-02-13 | Chesebrough-Pond's Usa Co., Division Of Conopco, Inc. | Covalent bonding of active agents to skin, hair or nails |
| JP3567951B2 (ja) * | 1995-10-12 | 2004-09-22 | ライオン株式会社 | 毛髪処理剤及び毛髪処理方法 |
| FR2740331B1 (fr) * | 1995-10-25 | 1997-12-19 | Sederma Sa | Nouvelles compositions cosmetiques pour le traitement des cheveux et du cuir chevelu |
| JP2000300287A (ja) * | 1999-03-15 | 2000-10-31 | Shinichiro Nishimura | トランスグルタミナーゼを用いた糖鎖導入方法 |
| WO2005095331A1 (ja) * | 2004-03-31 | 2005-10-13 | Shionogi & Co., Ltd. | 糖鎖－ペプチド結合剤 |
| JP2007022958A (ja) * | 2005-07-15 | 2007-02-01 | Katakura Chikkarin Co Ltd | イカ又はナマズ由来アテロコラーゲン及び／又はその誘導体及びその製造方法、並びに該アテロコラーゲン及び／又はその誘導体を配合する化粧料 |
| KR101162049B1 (ko) | 2007-02-15 | 2012-07-04 | 아지노모토 가부시키가이샤 | 디설파이드 결합 도입 트랜스글루타미나제 |
| DE102007031202A1 (de) * | 2007-07-04 | 2009-03-19 | Henkel Ag & Co. Kgaa | Hydrolysat aus Vikunja-Wolle und dessen Verwendung in kosmetischen Zubereitungen |
| EP2251421B1 (en) | 2008-02-13 | 2016-11-16 | Amano Enzyme Inc. | Stabilized transglutaminase and process for production thereof |
-
2010
- 2010-12-08 DE DE102010062600A patent/DE102010062600A1/de not_active Withdrawn
-
2011
- 2011-11-10 JP JP2013542436A patent/JP5951629B2/ja not_active Expired - Fee Related
- 2011-11-10 EP EP11788092.2A patent/EP2648538A1/de not_active Withdrawn
- 2011-11-10 WO PCT/EP2011/069811 patent/WO2012076284A1/de active Application Filing
- 2011-11-10 CN CN2011800593001A patent/CN103249313A/zh active Pending
- 2011-11-10 BR BR112013012390A patent/BR112013012390A8/pt not_active IP Right Cessation
- 2011-11-10 US US13/992,097 patent/US20130251658A1/en not_active Abandoned
Non-Patent Citations (2)
| Title |
|---|
| None * |
| See also references of WO2012076284A1 * |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2014506239A (ja) | 2014-03-13 |
| BR112013012390A8 (pt) | 2017-08-15 |
| BR112013012390A2 (pt) | 2016-07-19 |
| DE102010062600A1 (de) | 2012-06-14 |
| US20130251658A1 (en) | 2013-09-26 |
| CN103249313A (zh) | 2013-08-14 |
| WO2012076284A1 (de) | 2012-06-14 |
| JP5951629B2 (ja) | 2016-07-13 |
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