EP2648538A1 - Hydrophobized protein hydrolysate - Google Patents
Hydrophobized protein hydrolysateInfo
- 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- Withdrawn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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Abstract
The invention relates to enzymatic hydrophobized protein hydrolysates, to the production thereof, to the use thereof, and to cosmetic preparations comprising same.
Description
E V O N I K G o l d s c h m i d t GmbH, Essen Hydrophobisiertes Proteinhydrolysat E V O N I K G o l d s c h m i d t GmbH, Essen Hydrophobized protein hydrolyzate
Gebiet der Erfindung Field of the invention
Gegenstand der Erfindung sind enzymatisch hydrophobisierte Proteinhydrolysate, deren Herstellung und Verwendung sowie kosmetische Zubereitungen enthaltend diese. The invention provides enzymatically hydrophobized protein hydrolysates, their preparation and use, and cosmetic preparations containing them.
Stand der Technik State of the art
Proteine und Proteinhydrolysate stellen eine interessante Rohstoffklasse dar, weil sie gut verfügbar, natürlichen Ursprungs und biologisch abbaubar sind. Aufgrund fehlender lipophiler Gruppen sind die grenzflächenaktiven Eigenschaften der Proteine aber nur schwach ausgeprägt. Daher ist es nötig, zusätzliche lipophile Gruppen einzubringen, um leistungsfähige, proteinbasierte, grenzflächenaktive Verbindungen zu erhalten. Nach dem Stand der Technik werden die gewünschten modifizierten Proteine seit längerer Zeit durch Kondensation von Proteinhydrolysaten und Säurechloriden (im folgenden PHFSK) hergestellt und aufgrund ihrer tensidischen Eigenschaften in verschiedenen Anwendungen eingesetzt (z.B. zur Herstellung von Emulsionen, Schäumen, Konditionierung von Haut und Haar, Dispergieren von Pigmenten in verschiedenen Lösungsmitteln etc.). 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.).
ci ci
Peptide/Protein (CH^ NH2 + \ ,C (CH^ie C H3 Peptides / protein (CH 2 N 2 H 2 +, C (CH) ie CH 3
O O
P ept ide/P rote i n (C H2)4 N H P ept ide / P red in (CH 2 ) 4 NH
\ (CH2)3_16 CH3 \ (CH2) 3 CH 3 _16
O O
Allerdings ist die Gewinnung der für die Synthese benötigten Säurechloride (z.B. mit Thionylchlorid aus Fettsäuregemischen) aus ökologischer Sicht nicht unbedenklich, außerdem fällt bei der Kondensationsreaktion eine nicht unerhebliche Salzfracht an, welche die Produkteigenschaften deutlich ändern kann und daher ggf. aufwändig
abgetrennt werden muss. Des weiteren sind die erhaltenen Modifizierungsgrade sehr klein, bzw. nur mit großen Säureüberschüssen zu erreichen (Roussel-Philippe et al., European Journal of Lipid Science and Technology 102[2], 97-101. 2000). Schließlich verändert die Derivatisierung das Repertoire zur Verfügung stehender basischer Gruppen, da bevorzugt die primären Aminogruppen der Lysinreste amidiert werden. Dies ist von Nachteil, da die Anwesenheit kationischer Gruppen in bestimmten Anwendung, wie z.B. der Haarkonditionierung, erwünscht ist, die Lysinreste nach Amidierung aber nicht mehr zur Verfügung stehen. Der Einsatz von Transglutaminasen (TG) zur Quervernetzung von Proteinen undHowever, the recovery of the required for the synthesis of acid chlorides (eg with thionyl chloride from fatty acid mixtures) from an environmental point of view is not safe, also falls in the condensation reaction to a considerable salt load, which can significantly change the product properties and therefore possibly consuming must be disconnected. Furthermore, the degrees of modification obtained are very small, or can only be achieved with large acid excesses (Roussel-Philippe et al., European Journal of Lipid Science and Technology 102 [2], 97-101, 2000). Finally, derivatization changes the repertoire of available basic groups, as it is preferred to amidate the primary amino groups of the lysine residues. This is disadvantageous because the presence of cationic groups in certain applications, such as hair conditioning, is desirable, but the lysine residues are no longer available after amidation. The use of transglutaminases (TG) for cross-linking of proteins and
Proteinhydrolysaten ist seit längerer Zeit bekannt. Bei der Reaktion handelt es sich um eine Transamidierungsreaktion zwischen Lysin und Glutaminresten von Proteinen bei der Ammoniak frei wird und eine Isopeptidbindung entsteht. 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.
Transglutaminase transglutaminase
+ NH, + NH,
Protein (CH2)2-Protein (CH 2 ) 2 -
N (CH2)4 Protein N (CH 2 ) 4 protein
H H
Transglutaminase katalysierte Quervernetzungsreaktion von Proteinen Transglutaminase catalyzed cross-linking reaction of proteins
Ebenso ist bekannt, dass auch primäre Alkylamine als Nukleophil anstelle des Lysins in der Transglutaminase katalysierten Transamidierungreaktion dienen können. Dies wurde in der Literatur für ein synthetisches Dipeptid als Modelsubstrat (Ohtsuka et al., (2000) J Agric. Food Chem 48:6230-6233) und für intakte Proteine (Nieuwenhuizen etal., (2004) Biotechnol Bioeng 85:248-258) gezeigt. It is also known that primary alkylamines can serve as nucleophiles instead of lysine in the transglutaminase-catalyzed transamidation reaction. This has been reported in the literature for a synthetic dipeptide as a model substrate (Ohtsuka et al., (2000) J Agric. Food Chem 48: 6230-6233) and for intact proteins (Nieuwenhuizen et al., (2004) Biotechnol Bioeng 85: 248-258 ).
Betrachtet man nur die Strukturen der Edukte und Produkte, so handelt es sich formal um eine Alkylierung des Peptides. Daher wird im Zusammenhang mit der vorliegenden Erfindung von„alkylierten Proteinhydrolysaten" oder„Alkylierung" gesprochen
Peptide/Protein (CH2)2 + H2N— R1 Considering only the structures of the educts and products, it is formally an alkylation of the peptide. Therefore, in the context of the present invention, "alkylated protein hydrolysates" or "alkylation" is used Peptides / protein (CH 2 ) 2 + H 2 N-R 1
NH2 NH 2
Transglutaminase transglutaminase
Transglutaminase katalysierte Alkylierung von Proteinen Transglutaminase catalyzed alkylation of proteins
Allerdings konnte im Falle der intakten Proteine im Vergleich zu den PHFSKs ein nur geringer Modifikationsgrad (g Alkylreste pro g Protein) erreicht werden (6-8 % für PHFSKs, 0,2-0,4 % für TG katalysierte Alkylierung, vgl. Ohtsuka et al., (2000) J Agric. Food Chem 48:6230-6233, Nieuwenhuizen etal., (2004) Biotechnol Bioeng 85:248-258 und Roussel-Philippe et al., European Journal of Lipid Science and Technology 102[2], 97-101. 2000). However, in the case of intact proteins, only a small degree of modification (g alkyl residues per g protein) was achieved in comparison to PHFSKs (6-8% for PHFSKs, 0.2-0.4% for TG-catalyzed alkylation, see Ohtsuka et al., (2000) J Agric. Food Chem 48: 6230-6233, Nieuwenhuizen et al., (2004) Biotechnol Bioeng 85: 248-258 and Roussel-Philippe et al., European Journal of Lipid Science and Technology 102 [2] , 97-101, 2000).
Somit ist der amphiphile Charakter dieser Reaktionsprodukte nur schwach ausgeprägt und diese mittels Transglutaminase-Katalyse hydrophobisierten Proteine können nicht als Ersatz für die klassischen PHFSKs dienen. Thus, the amphiphilic character of these reaction products is weak and these proteins hydrophobized by transglutaminase catalysis can not replace the classical PHFSKs.
Aufgabe der Erfindung war es, hydrophobisierte Peptide zur Verfügung zu stellen, die mindestens einen Nachteil des Standes der Technik überwinden.. The object of the invention was to provide hydrophobized peptides which overcome at least one disadvantage of the prior art.
Beschreibung der Erfindung Description of the invention
Überraschenderweise wurde gefunden, dass die im Folgenden beschriebenen, mit Hilfe von Transglutaminasen alkylierten Proteinhydrolysate die der Erfindung gestellte Aufgabe zu lösen Vermögen. Surprisingly, it has been found that the protein hydrolyzates, which are described below and have been alkylated by means of transglutaminases, are capable of solving the problem addressed by the invention.
Gegenstand der vorliegenden Erfindung sind daher enzymatisch hydrophobisierte Proteinhydrolysate, deren Herstellung und Verwendung. The present invention therefore enzymatically hydrophobized protein hydrolysates, their preparation and use.
Ein weiterer Gegenstand der Erfindung sind Formulierungen, insbesondere Another object of the invention are formulations, in particular
kosmetische Zubereitungen enthaltend erfindungsgemäße hydrophobisierte cosmetic preparations containing hydrophobicized according to the invention
Proteinhydrolysate.
Ein Vorteil der vorliegenden Erfindung ist, dass keine Säurechloride während der Synthese benötigt werden. Protein. An advantage of the present invention is that no acid chlorides are needed during the synthesis.
Ein weiterer Vorteil ist, dass die Produkte aufgrund des teilweise sehr hohen Another advantage is that the products due to the sometimes very high
Glutamingehalts der Proteinhydrolysate einen hohen Derivatisierungsgrad aufweisen können und gleichzeitig geringere Konzentrationen von Alkylaminen eingesetzt werden müssen da es, im Gegensatz zu den Säurechloriden, nicht zu Nebenreaktionen (Hydrolyse) kommt. 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).
Vorteilig kann dadurch ein hervorragendes Schäumungsverhalten beobachtet werden. Noch ein Vorteil ist es, dass als Nebenprodukt anstelle von Kochsalz (bei den Advantageously, an excellent foaming behavior can be observed. Another advantage is that as a by-product instead of common salt (in the
Säurechloriden) das leicht austreibbare Ammoniak entsteht. Zudem läuft die Reaktion im neutralen pH-Bereich ab, so dass auch kein Salzeintrag aufgrund von pH- Einstellungen erfolgt. Schließlich ist es ein bedeutender Vorteil, dass die Acid chlorides), the easily expelled ammonia. In addition, the reaction proceeds in the neutral pH range, so that no salt entry occurs due to pH settings. After all, it is a significant advantage that the
Aminogruppen des Proteinhydrolysates weitestgehend intakt bleiben, da in Gegenwart der Alkylamine mittels Transglutaminase-Katalyse hauptsächlich die Glutaminreste umgesetzt werden. Die primären Aminogruppen der Proteinhydrolysate (terminale und die ε-Aminogruppe des Lysins) tragen wesentlich zu den physikochemischen Amino groups of protein hydrolyzate remain largely intact, since in the presence of alkylamines by transglutaminase catalysis mainly the glutamine residues are reacted. The primary amino groups of the protein hydrolysates (terminal and the ε-amino group of lysine) contribute significantly to the physicochemical
Eigenschaften der Produkte bei (z.B. zur Wechselwirkung/Bindung mit/an negativ geladenen Oberflächen von Haut und Haar = Substantivität). Bei der Derivatisierung mit Säurechloriden werden bevorzugt diese nukleophilen Aminogruppen zu Amiden umgesetzt und können somit nicht mehr zur Substantivität beitragen. Properties of the products in (e.g., for interaction / binding with / on negatively charged surfaces of skin and hair = substantivity). When derivatizing with acid chlorides, these nucleophilic amino groups are preferably converted into amides and thus can no longer contribute to substantivity.
Gegenstand der vorliegenden Erfindung ist ein alkyliertes Peptidgemisch erhältlich durch ein Verfahren umfassend die Verfahrensschritte The subject matter of the present invention is an alkylated peptide mixture obtainable by a process comprising the process steps
A) Hydrolyse mindestens eines Proteins enthaltend mindestens einen Glutaminrest zu einem Proteinhydrolysat und gegebenenfalls Aufreinigung des A) hydrolysis of at least one protein containing at least one glutamine residue to a protein hydrolyzate and optionally purification of the
Proteinhydrolysates, protein hydrolyzate,
B) in Kontakt Bringen des Proteinhydrolysates mit einer Transglutaminase und B) contacting the protein hydrolyzate with a transglutaminase and
mindestens einem primären oder sekundären Amin der allgemeinen Formel (I), insbesondere einem primären Amin, at least one primary or secondary amine of the general formula (I), in particular a primary amine,
R2 R 2
/ /
R1 NH (|) R 1 NH (I)
wobei R1 und R2 unabhängig voneinander gleich oder verschieden ausgewählt ist aus gegebenenfalls ungesättigter, gegebenenfalls substituierter, gegebenenfalls
verzweigter organischer Rest mit 5 bis 40, bevorzugt 5 bis 22, insbesondere 6 bis 18 Kohlenstoffatomen. wherein 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.
Aufreinigen des alkylierten Peptidgemisches. Im Zusammenhang mit der vorliegenden Erfindung ist unter dem Begriff„alkyliertes Peptidgemisch" eine Mischung enthaltend mindestens zwei an jeweils mindestens einem Glutamin alkylierten Peptiden zu verstehen. Somit ist offenbar, dass für den Fall, dass in Verfahrensschritt A) nur das Protein eines Typs hydrolysiert wird, dieses Protein mindestens zwei Glutaminreste aufweisen muss. Purify the alkylated peptide mixture. In the context of the present invention, the term "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 Thus, it is apparent that in the case of step A) only the protein of one type is hydrolyzed , this protein must have at least two glutamine residues.
Alle angegebenen Prozent (%) sind wenn nicht anders angegeben Massenprozent. All percentages (%) are percentages by weight unless otherwise specified.
In der Praxis ist es vorteilhaft gut verfügbare Proteinquellen in Verfahrensschritt A) einzusetzen; diese sind insbesondere als Mischungen von Proteinen zugänglich. Somit ist das mindestens eine Protein bevorzugt ausgewählt aus der Liste umfassend, bevorzugt bestehend aus: In practice, it is advantageous to use readily available protein sources in process step A); these are particularly accessible as mixtures of proteins. Thus, the at least one protein is preferably selected from the list comprising, preferably consisting of:
Isolierte Pflanzenspeicherproteine wie z.B. Weizenprotein (Gluten), Sojaprotein, Erbsenprotein, Reisprotein, Maisprotein, Lupinenprotein, Isolated plant storage proteins such as e.g. Wheat protein (gluten), soy protein, pea protein, rice protein, corn protein, lupine protein,
tierische Proteine wie z.B. Kollagen, Keratin, Casein, Molkenproteine (Lactoglobuline), Seidenprotein (Fibroin) und animal proteins such as e.g. Collagen, keratin, casein, whey proteins (lactoglobulins), silk protein (fibroin) and
mikrobielle Proteine wie z.B. Hefeproteinextrakte, Algenproteine oder bakterielle Biomasse (SCP = Single cell protein). microbial proteins such as e.g. Yeast protein extracts, algae proteins or bacterial biomass (SCP = single cell protein).
Es ist erfindungsgemäß vorteilhaft, in Verfahrensschritt A) eine Mischung von It is inventively advantageous in process step A) a mixture of
Proteinen einzusetzen, die einen hohen Anteil an Glutaminresten aufweist, somit ist das Protein bevorzugt ausgewählt aus der Liste umfassend, bevorzugt bestehend aus, Weizengluten, isolierte Speicherproteine von Hülsenfrüchten, insbesondere Soja, Erbse, Lupine und Milcheiweiße, insbesondere Caseine und Lactoglobuline, wobei Weizengluten ganz besonders bevorzugt ist.. Thus, 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 ..
Die Hydrolyse in Verfahrensschritt A) wird bevorzugt durch Zugabe von Säure, besonders bevorzugt durch den Einsatz von Enzymen katalysiert. Geeignete Verfahren sind dem Fachmann bekannt; ebenso erfordert es keine Anstrengung, die jeweiligen Verfahrensparameter derart einzustellen, dass in Verfahrensschritt A) 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)
Proteinhydrolysate mit gewünschten mittleren Molekulargewichten entstehen. Protein hydrolysates with desired average molecular weights arise.
Derartige Anleitung für enzymatisch katalysierte Hydrolyse-Verfahren findet der Fachmann in Aaslyng et al., (1998) J Agric. Food Chem 46:481-489 und Adler-Nissen
J (1976) J Agric. Food Chem 24: 1090-1093, für durch Säure oder Alkali katalysierte Verfahren in Aaslyng et al., (1998) J Agric. Food Chem 46:481-489. Such guidance for enzymatically catalyzed hydrolysis procedures will be found in Aaslyng et al., (1998) J Agric. Food Chem 46: 481-489 and Eagle Nissen J (1976) J Agric. Food Chem 24: 1090-1093, for acid or alkali catalyzed processes in Aaslyng et al., (1998) J Agric. Food Chem 46: 481-489.
Erfindungemäß bevorzugt weist das Proteinhydrolysat aus Verfahrensschritt A) ein mittleres Molekulargewicht von 203 g/mol bis 100.000 g/mol, bevorzugt von 500 g/mol bis 20.000 g/mol, insbesondere von 1000 g/mol bis 15.000 g/mol auf. According to the invention, 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.
Nach Verfahrensschritt A) herstellbare und direkt in Verfahrensschritt B) einsetzbare Proteinhydrolysate sind auch kommerziell erhältlich; solche sind beispielsweise: 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 und Meripro 71 1 (Weizenproteinhydrolysate, enzymatisch und chemisch, Syral), Naturalys® W (Weizenproteinhydrolysat, Roquette) Cropeptide W, Meripro 810 and Meripro 71 1 (wheat protein hydrolysates, enzymatic and chemical, Syral), Naturalys® W (wheat protein hydrolyzate, Roquette) cropeptide W,
Hydrotriticum 2000, Tritisol, Tritisol XM (Weizenproteinhydrolysate mit Hydrotriticum 2000, Tritisol, Tritisol XM (wheat protein hydrolysates with
unterschiedlichen Molekulargewichtsverteilungen, Croda) , Hydrosoy 2000 different molecular weight distributions, Croda), Hydrosoy 2000
(Sojaproteinhydrolysat, Croda), Gluadin® W20 und Gluadin® WLM (Soy protein hydrolyzate, Croda), Gluadin® W20 and Gluadin® WLM
(Weizenproteinhydrolysate mit unterschiedlichen Molekulargewichtsverteilungen, Cognis), AMCO HCA41 1 bzw. HLA-198 (Casein- bzw. Molkeneiweißhydrolysat, American Casein Company). (Wheat protein hydrolysates with different molecular weight distributions, Cognis), AMCO HCA41 1 and HLA-198 (casein or whey protein hydrolyzate, American Casein Company).
In Verfahrensschritt B) können prinzipiell alle dem Fachmann bekannten In process step B), in principle all known to those skilled
Transglutaminasen, zugehörig der EC Klasse 2.3.2.13, eingesetzt werden, wie auch ein Fragment dieser Transglutaminasen, welches entsprechende Enzymaktivität aufweist. Solche Enzyme lassen sich beispielsweise aus Streptoverticillium, Bacillus, verschiedenen Actinomycetes und Myxomycetes, aber auch von Pflanzen, Fischen und Säuger-Quellen, wie beispielsweise Schweine-Leber, isolieren. Die EP2123756 und WO2009101762 beschreiben verglichen zu ihrem Wldtyp stabilisierte 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
Transglutaminasen, dessen Einsatz in Verfahrenschritt B) erfindungsgemäß bevorzugt ist. Transglutaminases whose use in process step B) according to the invention is preferred.
Es ist bevorzugt, dass die in Verfahrensschritt B) eingesetzten Transglutaminasen isolierbar sind ausgewählt aus der Liste bestehend aus Bacillus subtilis, Streptomyces mombaraensis (vormals Streptoverticillium mobaraense). In diesem Zusammenhang ist eine besonders bevorzugte Transglutaminase ausgewählt aus der unter dem Handelsnamen„Activa" erhältlichen Transglutaminasen der Firma Ajinomoto It is preferred that the transglutaminases used in process step B) are isolatable selected from the list consisting of Bacillus subtilis, Streptomyces mombaraensis (formerly Streptoverticillium mobaraense). In this connection, a particularly preferred transglutaminase is selected from the transglutaminases of the company Ajinomoto available under the trade name "Activa"
(Transglutaminasen aus Streptomyces mombaraensis), z.B. Activa®WM, Activa®EB, Activa®PB, Activa®WS, Activa®YG.
In Verfahrensschritt B) wird das Proteinhydrolysat bevorzugt in einer Konzentration zwischen 5 Gew.-% und 40 Gew.-%, bevorzugt zwischen 15 Gew.-% und 25 Gew.-%, bezogen auf den gesamten Reaktionsansatz eingesetzt, wobei das Lösungs- bzw. Dispergiermittel bevorzugt Wasser ist. Unter Umständen kann es vorteilhaft sein, vor Zugabe der Transglutaminase in Verfahrensschritt B) den Reaktionsansatz auf über 50 °C, bevorzugt auf über 70 °C, insbesondere auf über 80 °C zu erhitzen, um den Hydratisierungsprozess zu beschleunigen, wobei bevorzugt eine Durchmischung, etwa durch Rühren, des Reaktionsansatzes erfolgt. (Transglutaminases from Streptomyces mombaraensis), eg Activa®WM, Activa®EB, Activa®PB, Activa®WS, Activa®YG. In process step B), 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. Under certain circumstances, it 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.
Die Reste R1 und R2 des primären oder sekundären Amins der allgemeinen Formel (I) in Verfahrensschritt B), sind bevorzugt ausgewählt aus der Gruppe bestehend aus Alkyl- und Alkenylrest, bevorzugt linearer, unsubstituierter Alkyl- und Alkenylrest, insbesondere ein Oktyl-, Dekyl-, Dodekyl-, Tetradekyl-, Hexadekyl-, Octadekyl-, Octadecenyl-, Octadecadienyl- Eicosyl-, Docosylrest. 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.
Die Reste R1 und R2 können auch Mischungen von Alkylresten darstellen, The radicals R 1 and R 2 may also be mixtures of alkyl radicals,
insbesondere technische Gemische aus diesen Alkylresten. Die Alkylreste solcher technischen Gemische leiten sich bevorzugt von Fettsäuregemischen ab, die durch verschiedene Verfahren aus pflanzlichen Fettsäuregemischen gewonnen werden können und über verschiedene Verfahren fraktioniert werden können. Die in particular technical mixtures of these alkyl radicals. The 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. The
Fettsäurezusammensetzung solcher pflanzlicher Fettsäuregemische variiert in Fatty acid composition of such vegetable fatty acid mixtures varies in
Abhängigkeit der für die Gewinnung eingesetzten Ölsaat und ist dem Fachmann beispielsweise in Form von gegebenenfalls fraktionierten Rapsöl-, Sojaöl-, Dependence of the oilseed used for the production and is the expert, for example in the form of optionally fractionated rapeseed oil, soybean oil,
Sonnenblumenöl-, Talgöl-, Kokosölfettsäuren bekannt. Sunflower oil, tallow, coconut oil fatty acids known.
Somit sind die in Verfahrensschritt B) bevorzugt eingesetzten Alkylamine ausgewählt aus der Gruppe bestehend aus: Rapsfettamin, Sojafettamin, Sonnenblumenfettamin, Talgfettamin, Palmfettamin, Palmkernfettamin und Kokosfettamin. Thus, 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.
Das Amin der allgemeinen Formel (I) wird in Verfahrensschritt B) bevorzugt in einer Konzentration zwischen 0,25 Gew.-% und 10 Gew.-%, insbesondere zwischen 0,5 Gew.-% und 5 Gew.-%, bezogen auf den gesamten Reaktionsansatz eingesetzt. 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.
Die Enzymaktivität im Reaktionsansatz in Verfahrensschritt B) beträgt bevorzugt 10 - 25000 U/l, bevorzugt 200-1000 U/l besonders bevorzugt 300-600 U/l, wobei die Einheit U nach dem in Folk und Cole (1966), Biochim. Biophys. Acta 122:244-264, 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,
beschriebenen Hydroxamat-Assay bestimmt werden kann. described hydroxamate assay can be determined.
In Verfahrensschritt B) beträgt der pH-Wert bevorzugt zwischen 5 und 10, bevorzugt zwischen 6 und 8, besonders bevorzugt zwischen 6,5 und 7,5. In process step B), the pH is preferably between 5 and 10, preferably between 6 and 8, particularly preferably between 6.5 and 7.5.
Bevorzugt findet eine Durchmischung, etwa durch Rühren, des Reaktionsansatzes während der Transglutaminasereaktion in Verfahrensschritt B) statt.
Die Temperatur des Reaktionsansatzes während der Transglutaminasereaktion in Verfahrensschritt B) beträgt bevorzugt 20 °C bis 50°C, bevorzugt 30 °C bis 45 °C und besonders bevorzugt 35 °C bis 40 °C . Preferably, thorough mixing takes place, for example by stirring, of the reaction mixture during the transglutaminase reaction in process step B). 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.
Die Reaktionsdauer der Transglutaminasereaktion in Verfahrensschritt B) beträgt je nach eingesetzter Temperatur bis zu mehrere Stunden. The reaction time of the transglutaminase reaction in process step B) is up to several hours, depending on the temperature used.
Wenn in Verfahrensschritt A) die Hydrolyse durch den Einsatz mindestens eines Enzyms katalysiert wird, kann es aus Gründen der Zeitersparnis vorteilhaft sein, wenn Verfahrensschritt A) und Verfahrensschritt B) gleichzeitig durchgeführt werden. If, in 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.
Ein weiterer Gegenstand der vorliegenden Erfindung ist das oben beschriebene Verfahren, mit dem erfindungsgemäße Peptidgemische hergestellt werden können. Erfindungsgemäß bevorzugte Verfahren, sind solche, die zu den oben genannten bevorzugten, erfindungsgemäßen Peptidgemischen führen. 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.
Die erfindungsgemäßen, alkylierten Peptidgemische lassen sich vorteilhaft in The alkylated peptide mixtures according to the invention can be advantageously used in
Reinigungsmitteln, in kosmetischen oder pharmazeutischen Formulierungen sowie in Pflanzenschutz-Formulierungen einsetzen. Detergents, in cosmetic or pharmaceutical formulations and in crop protection formulations.
Somit sind ein weiterer Gegenstand der vorliegenden Erfindung kosmetische, dermatologische oder pharmazeutische Formulierungen, Pflanzenschutz- Formulierungen sowie Pflege- und Reinigungsmittel und Tensidkonzentrate enthaltend erfindungsgemäße, alkylierte Peptidgemische. Thus, 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.
Unter dem Begriff„Pflegemittel" wird hier eine Formulierung verstanden, die den Zweck erfüllt, einen Gegenstand in seiner ursprünglichen Form zu erhalten, die Auswirkungen äußerer Einflüsse (z.B. Zeit, Licht, Temperatur, Druck, Verschmutzung, chemische Reaktion mit anderen, mit dem Gegenstand in Kontakt tretenden reaktiven The term "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
Verbindungen) wie beispielsweise Altern, Verschmutzen, Materialermüdung, Compounds) such as aging, fouling, fatigue,
Ausbleichen, zu mindern oder zu vermeiden oder sogar gewünschte positive Fade, diminish or avoid or even desired positive ones
Eigenschaften des Gegenstandes zu verbessern. Für letzten Punkt sei etwa ein verbesserter Haarglanz oder eine größere Elastizität des betrachteten Gegenstandes genannt. Properties of the object to improve. For the last point is about an improved hair shine or greater elasticity of the object considered called.
Unter„Pflanzenschutz-Formulierungen" sind solche Formulierungen zu verstehen, die von der Art ihrer Herrichtung nach augenfällig zum Pflanzenschutz verwendet werden; dies ist insbesondere dann der Fall, wenn in der Formulierung mindestens eine Verbindung aus den Klassen der Herbizide, Fungizide, Insektizide, Akarizide,
Nematizide, Schutzstoffe gegen Vogelfraß, Pflanzennährstoffe und By "crop protection formulations" is 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 . Nematicides, bird repellants, plant nutrients and
Bodenstrukturverbesserungsmittel enthalten ist. Soil structure improver is included.
Erfindungemäß bevorzugte kosmetische Kompositionen sind ausgewählt aus der Gruppe bestehend aus: Cremes, Lotionen, Spülungen und Shampoos. According to the invention, preferred cosmetic compositions are selected from the group consisting of: creams, lotions, rinses and shampoos.
Erfindungemäße Peptidgemische weisen vorteilhafte emulgierende und Invention peptide mixtures have advantageous emulsifying and
schaumstabilisierende Eigenschaften auf. Somit ist noch ein Gegenstand der vorliegenden Erfindung eine Verwendung der erfindungsgemäßen Peptidgemische als Emulgator, wie beispielsweise O/W- oder W/O-Emulgator, als Konditionierungsmittel für Haut und Haar, als Dispergierhilfsmittel, insbesondere für kosmetische Pigmente, als Schaumbildner oder Schaumstabilisator. foam stabilizing properties. Thus, 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.
In den nachfolgend aufgeführten Beispielen wird die vorliegende Erfindung beispielhaft beschrieben, ohne dass die Erfindung, deren Anwendungsbreite sich aus der gesamten Beschreibung und den Ansprüchen ergibt, auf die in den Beispielen genannten Ausführungsformen beschränkt sein soll. In the examples given below, the present invention is described by way of example, without the invention, the scope of application of which is apparent from the entire description and the claims, to be limited to the embodiments mentioned in the examples.
Folgende Abbildungen sind Bestandteil der Beispiele: The following figures are part of the examples:
Abbildung 1 : Verbesserung der Schaumstabilität durch Transglutaminase katalysierte hydrophobisierung von modifiziertem Weizenproteinhydrolysat. („MP810" (Quadrate) = Meripro 810, Syral;„MP810 + OA + TG (inakt.)" (Dreiecke) = Meripro 810 + Octylamin (OA) + inaktivierte Transglutaminase (TG) = Negativkontrolle;„MP810 + OA + TG" (Rauten) = Meripro 810 + Octylamin (OA) + Transglutaminase (TG) Figure 1: Improvement in foam stability by transglutaminase-catalyzed hydrophobization of modified wheat protein hydrolyzate. ("MP810" (squares) = Meripro 810, Syral; "MP810 + OA + TG (inact.)" (Triangles) = Meripro 810 + octylamine (OA) + inactivated transglutaminase (TG) = negative control; "MP810 + OA + TG "(Diamonds) = Meripro 810 + octylamine (OA) + transglutaminase (TG)
Beispiele: Examples:
Beispiel 1. Transglutaminase katalysierte Hydrophobisierung eines Example 1. Transglutaminase catalyzed hydrophobization of a
Weizenproteinhydrolysats mit Octylamin oder Laurylamin und Vergleich mit dem Produkt aus nicht hydrolysiertem Weizenprotein und Vergleich mit nicht Wheat protein hydrolyzate with octylamine or laurylamine and comparison with the product of unhydrolyzed wheat protein and comparison with non
hydrophobisiertem Weizenproteinhydrolysats. hydrophobized wheat protein hydrolyzate.
Ein kommerzielles Weizenprotein (Amygluten 1 10, Syral, Molekulargewicht > 200 kD) und ein aus diesem hergestelltes Hydrolysat (Meripro 810, Molekulargewicht - 10 kD) wurden jeweils bei pH = 7,5 und einer Konzentration von 10 Gew.-% zusammen mit Octyl- oder Laurylamin (2,5 Gew.-%) in Wasser dispergiert. Es wurde 1 Gew.-% einer kommerziellen Transglutaminasepräparation (Activa WM, Ajinomoto) zugegeben und bei 45 °C über einen Zeitraum von 24 h gerührt. Anschließend wurde das Enzym bei einer Temperatur von 80 °C inaktiviert. Als Kontrollen wurden jeweils Ansätze mit
inaktiviertem Enzym und Ansätze ohne Alkylamin durchgeführt. Der Umsatz der Alkylamine wurde durch einen photometrischen Assay nach Derivatisierung mit 1-Chloro-2,4-Dinitro-Benzol (CDNB) im Vergleich zu den Kontrollreaktionen bestimmt (Ekladius und King, (1957) Biochem J 65: 128-131). A commercial wheat protein (Amygluten 110, syral, molecular weight> 200 kD) and a hydrolyzate (Meripro 810, molecular weight - 10 kD) prepared therefrom were each added at pH = 7.5 and a concentration of 10% by weight together with octyl - or laurylamine (2.5 wt .-%) dispersed in water. 1% by weight of 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 conversion of the alkylamines was determined by a photometric assay after derivatization with 1-chloro-2,4-dinitrobenzene (CDNB) compared to the control reactions (Ekladius and King, (1957) Biochem J 65: 128-131).
Während bei der Reaktion mit nicht hydrolysiertem Weizenprotein (Amygluten 110, Syral) kein Umsatz des Alkylamines detektiert werden konnte, wurde bei dem While no reaction of the alkylamine could be detected in the reaction with unhydrolyzed wheat protein (Amygluten 110, Syral), in the
Hydrolysat ein Alkylaminumsatz von über 50 % gemessen. Etwa 10 % der Hydrolyzate an alkylamine conversion of over 50% measured. About 10% of
Aminosäurereste und ~ 30 % der verfügbaren Glutaminreste wurden modifiziert. Amino acid residues and ~ 30% of the available glutamine residues were modified.
Beispiel 2: Oberflächenaktivität Example 2: Surface activity
Die Oberflächenspannnung gegen Luft bzw. die Grenzflächenspannung gegen Paraffin bzw. Diethylhexylcarbonat (DEC) wurde mittels des Pendant-Drop-Verfahrens bestimmt. Es wurden 1 %ige Lösungen des mit Octylamin modifizierten 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
Weizenproteinhydrolysats und der entsprechenden Kontrollreaktionen vermessen. Durch die Modifikation konnte die Grenzflächenaktivität deutlich verbessert werden, (Reduktion von Grenz- und Oberflächenspannung, Tabelle 1). Wheat protein hydrolyzate and the corresponding control reactions. As a result of the modification, the interfacial activity could be significantly improved (reduction of the boundary and surface tension, Table 1).
Tabelle 1 : Einfluss der Transglutaminase katalysierten Hydrophobisierung eines Weizenproteinhydrolysats (Meripro 810, Syral) auf die Grenzflächenaktivität. Table 1: Influence of transglutaminase catalyzed hydrophobization of a wheat protein hydrolyzate (Meripro 810, Syral) on interfacial activity.
Beispiel 3: Schaumbildung und Schaumstabilität Example 3: Foaming and foam stability
Der Effekt der Hydrophobisierung des Weizenproteinhydrolysates mit Octylamin auf die Schaumbildung und Schaumstabilität wurde in Schüttelversuchen von 1 % Lösungen mit den entsprechenden Kontrollen verglichen. Hierfür wurden 10 ml der The effect of hydrophobization of the wheat protein hydrolyzate with octylamine on foam formation and foam stability was compared with the corresponding controls in shake trials of 1% solutions. For this purpose, 10 ml of
entsprechenden Proben in ein 50 ml Polypropylen Zentrifugenröhrchen mit appropriate samples in a 50 ml polypropylene centrifuge tube with
Volumenskala gefüllt und unter gleichen Bedingungen für eine Minute geschüttelt. Das Schaumvolumen über der Flüssigkeit wurde im Verlauf der Zeit abgelesen, um
Anfangsschaumvolumen und Schaumstabilität zu beurteilen. Hierbei zeigte sich eine deutliche schaumstabilisierende Wirkung des hydrophobisierten 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
Weizenproteinhydrolysats (Abbildung 1). Beispiel 4: Emulsionsleistung Wheat protein hydrolyzate (Figure 1). Example 4: Emulsion Performance
Die Emulgiereigenschaften des mit Octylamin und des mit Laurylamin modifizierten Weizenproteinhydrolysates wurden im 1 ml Maßstab in Schüttelversuchen untersucht. Bei einem Triglycerid/Wasser/Emulgatorverhältniss von 20/79/1 wurden die The emulsifying properties of the octylamine-modified and laurylamine-modified wheat protein hydrolyzate were investigated on a 1 ml scale in shaking experiments. At a triglyceride / water / emulsifier ratio of 20/79/1, the
verschiedenen Proben und Kontrollen untersucht. Die Emulsion wurde durch intensives Schütteln hergestellt und die Kinetik der Phasentrennung wurde verfolgt. Dabei zeigte sich, dass die Phasentrennung bei den hydrophobisierten Proteinhydrolysaten deutlich langsamer als bei den entsprechenden Kontrollen erfolgte und nicht vollständig war. various samples and controls. The emulsion was prepared by vigorous shaking and the kinetics of the phase separation were followed. It was found that the phase separation in the hydrophobized protein hydrolysates was much slower than in the corresponding controls and was not complete.
Beispiel 5: Vergleich zu einem Säurechlorid-modifizierten Weizenproteinhydrolysat Es wurde ein, Laurylamin modifizierte Weizenproteinhyrolysat wie in Beispiel 1 beschrieben dargestellt; die Konzentration des eingesetzten Laurylamins betrug 0,625 % (w/w). 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).
Es wurde mit Hilfe von Säurechlorid ein mit Laurylchlorid modifiziertes It was with the aid of acid chloride modified with lauryl chloride
Weizenproteinhydrolysat (ein PHFSK) hergestellt, wobei die gleichen Wheat protein hydrolyzate (a PHFSK) produced using the same
Eduktkonzentrationen und das gleiche Weizenproteinhydrolysat eingesetzt wurde, wie bei der durch Transglutaminase katalysierten Herstellung. Für die Schotten-Baumann Kondensationsreaktion wurde in Anlehnung an literaturbeschriebene, optimale Eduktkonzentrationen and the same wheat protein hydrolyzate was used, as in the transglutaminase catalyzed preparation. For the Schotten-Baumann condensation reaction was based on literature described, optimal
Reaktionsbedingungen gearbeitet (Roussel-Philippe et al., European Journal of Lipid Science and Technology 102[2], 97-101. 2000): Vor Zugabe des Laurylchlorids zum Weizenproteinhydrolysat (10 Gew.% in Wasser) wurde durch Zugabe von NaOH ein pH Wert von 9 eingestellt. Dann wurde bei einer Temperatur von 4 °C schrittweise Laurylchlorid bis zu einer Konzentration von 0,625 Gew.-% zugegeben. Nach 4 Stunden wurde der pH-Wert durch die Zugabe von HCl auf 5 gestellt, um Reaction conditions (Roussel-Philippe et al., European Journal of Lipid Science and Technology 102 [2], 97-101, 2000): Before addition of the lauryl chloride to the wheat protein hydrolyzate (10% by weight in water), addition of NaOH produced a pH Value of 9 is set. Then, at a temperature of 4 ° C, lauryl chloride was gradually added to a concentration of 0.625% by weight. After 4 hours, the pH was adjusted to 5 by the addition of HCl to give
möglicherweise nicht umgesetztes Säurechlorid zur Fettsäure zu hydrolysieren. possibly unreacted acid chloride to hydrolyze the fatty acid.
Anschließend wurde der pH Wert durch NaOH-Zugabe auf 7,5 eingestellt. Das Subsequently, the pH was adjusted to 7.5 by adding NaOH. The
Schaumvolumen und die Schaumstabilität des Alkylamin- und des Säurechlorid- modifizierte Weizenproteinhydrolysates wurden wie in Beispiel 3 beschrieben gegeneinander verglichen. Die Proben wurden für den Versuch auf einen Proteingehalt von 1 Gew.% eingestellt. Bei dem Alkylamin modifizierten Weizenproteinhydrolysat wurde eine stärkere Schaumbildung beobachtet (15 ml anstelle von 10 ml beim Foam volume and foam stability of the alkylamine and acid chloride modified wheat protein hydrolyzate were compared as described in Example 3. The samples were adjusted for the experiment to a protein content of 1 wt.%. In the alkylamine modified wheat protein hydrolyzate, greater foaming was observed (15 ml instead of 10 ml at
Säurechlorid-modifizierten).
Acid chloride-modified).
Claims
1. Alkyliertes Peptidgemisch erhältlich durch ein Verfahren umfassend die An alkylated peptide mixture obtainable by a process comprising
Verfahrensschritte steps
A) Hydrolyse mindestens eines Proteins enthaltend mindestens einen A) hydrolysis of at least one protein containing at least one
Glutaminrest zu einem Proteinhydrolysat und gegebenenfalls Aufreinigung des Proteinhydrolysates, Glutamine residue to a protein hydrolyzate and optionally purification of the protein hydrolyzate,
B) in Kontakt Bringen des Proteinhydrolysates mit einer Transglutaminase und mindestens einem primären oder sekundären Amin der allgemeinen Formel (I) B) bringing the protein hydrolyzate into contact with a transglutaminase and at least one primary or secondary amine of the general formula (I)
wobei R1 und R2 unabhängig voneinander gleich oder verschieden ausgewählt ist aus gegebenenfalls ungesättigter, gegebenenfalls substituierter, gegebenenfalls verzweigter organischer Rest mit 5 bis 40 Kohlenstoffatomen und H, wherein R 1 and R 2 are independently or identically selected from optionally unsaturated, optionally substituted, optionally branched organic radical having 5 to 40 carbon atoms and H,
und gegebenenfalls and optionally
C) Aufreinigen des alkylierten Peptidgemisches. C) Purification of the alkylated peptide mixture.
2. Alkyliertes Peptidgemisch gemäß Anspruch 1 , dadurch gekennzeichnet, dass das mindestens eine Protein ausgewählt ist aus der Liste umfassend isolierte Pflanzenspeicherproteine, tierische Proteine und mikrobielle Proteine. 2. Alkylated peptide mixture according to claim 1, characterized in that the at least one protein is selected from the list comprising isolated plant storage proteins, animal proteins and microbial proteins.
3. Alkyliertes Peptidgemisch gemäß Anspruch 1 oder 2, dadurch gekennzeichnet, dass die Hydrolyse in Verfahrensschritt A) durch Zugabe mindestens einer Säure oder durch den Einsatz mindestens eines Enzyms katalysiert wird. 3. Alkylated peptide mixture according to claim 1 or 2, characterized in that the hydrolysis in process step A) is catalyzed by the addition of at least one acid or by the use of at least one enzyme.
4. Alkyliertes Peptidgemisch gemäß mindestens einem der vorherigen Ansprüche, dadurch gekennzeichnet, dass das Proteinhydrolysat aus Verfahrensschritt A) ein mittleres Molekulargewicht von 203 g/mol bis 100.000 g/mol aufweist. 4. Alkylated peptide mixture according to at least one of the preceding claims, characterized in that the protein hydrolyzate from process step A) has an average molecular weight of 203 g / mol to 100,000 g / mol.
5. Alkyliertes Peptidgemisch gemäß mindestens einem der vorherigen Ansprüche, dadurch gekennzeichnet, dass das Proteinhydrolysat aus Verfahrensschritt A) den kommerziell erhältlichen Produkten Meripro 810, Meripro 71 1 , Naturalys W, Cropeptide W, Hydrotriticum 2000, Tritisol, Tritisol XM, Hydrosoy 2000, Gluadin W20, Gluadin WLM, AMCO HCA411 oder HLA-198 entspricht. 5. Alkylated peptide mixture according to at least one of the preceding claims, characterized in that the protein hydrolyzate from process step A) the commercially available products Meripro 810, Meripro 71 1, Naturalys W, Cropeptide W, Hydrotriticum 2000, Tritisol, Tritisol XM, Hydrosoy 2000, Gluadin W20, Gluadin WLM, AMCO HCA411 or HLA-198.
6. Alkyliertes Peptidgemisch gemäß mindestens einem der vorherigen Ansprüche, dadurch gekennzeichnet, dass die in Verfahrensschritt B) eingesetzte 6. Alkylated peptide mixture according to at least one of the preceding claims, characterized in that the used in process step B)
Transglutaminase isolierbar ist ausgewählt aus der Liste bestehend aus Bacillus subtilis, Streptoverticillium mombaraensis. Transglutaminase isolatable is selected from the list consisting of Bacillus subtilis, Streptoverticillium mombaraensis.
7. Alkyliertes Peptidgemisch gemäß mindestens einem der vorherigen Ansprüche, dadurch gekennzeichnet, dass die Reste R1 und R2 des primären oder sekundären Amins der allgemeinen Formel (I) in Verfahrensschritt B), ausgewählt sind aus der Gruppe bestehend aus Alkyl- und Alkenylrest, bevorzugt linearer, unsubstituierter Alkyl- und Alkenylrest, insbesondere ein Oktyl-, Dekyl-, Dodekyl-, Tetradekyl-, Hexadekyl-, Octadekyl-, Octadecenyl-, Octadecadienyl- Eicosyl-, Docosylrest. 7. Alkylated peptide mixture according to at least one of the preceding claims, characterized in that the radicals R 1 and R 2 of the primary or secondary amine of the general formula (I) in process step B), are 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 radical.
8. Alkyliertes Peptidgemisch gemäß mindestens einem der vorherigen Ansprüche, dadurch gekennzeichnet, dass in Verfahrensschritt A) die Hydrolyse durch den Einsatz mindestens eines Enzyms katalysiert wird und Verfahrensschritt A) und Verfahrensschritt B) gleichzeitig durchgeführt werden. 8. Alkylated peptide mixture according to at least one of the preceding claims, characterized in that in process step A) the hydrolysis is catalyzed by the use of at least one enzyme and process step A) and process step B) are carried out simultaneously.
9. Verfahren zur Herstellung alkylierter Peptidgemische umfassend die 9. A process for preparing alkylated peptide mixtures comprising
Verfahrensschritte steps
A) Hydrolyse mindestens eines Proteins enthaltend mindestens einen A) hydrolysis of at least one protein containing at least one
Glutaminrest zu einem Proteinhydrolysat und gegebenenfalls Aufreinigung des Proteinhydrolysates, Glutamine residue to a protein hydrolyzate and optionally purification of the protein hydrolyzate,
B) in Kontakt Bringen des Proteinhydrolysates mit einer Transglutaminase und mindestens einem primären oder sekundären Amin der allgemeinen Formel (I) B) bringing the protein hydrolyzate into contact with a transglutaminase and at least one primary or secondary amine of the general formula (I)
R2 R 2
/ /
R1 NH (|) R 1 NH (I)
wobei R1 und R2 unabhängig voneinander gleich oder verschieden ausgewählt ist aus gegebenenfalls ungesättigter, gegebenenfalls substituierter, gegebenenfalls verzweigter organischer Rest mit 5 bis 40 Kohlenstoffatomen und H, wherein R1 and R2 independently of one another are identically or differently selected from optionally unsaturated, if appropriate substituted, optionally branched organic radical having 5 to 40 carbon atoms and H,
und gegebenenfalls and optionally
C) Aufreinigen des alkylierten Peptidgemisches C) Purification of the alkylated peptide mixture
10. Kosmetische, dermatologische oder pharmazeutische Formulierung, 10. Cosmetic, dermatological or pharmaceutical formulation,
Pflanzenschutz-Formulierung, Pflege- und Reinigungsmittel oder Crop protection formulation, care and cleaning agents or
Tensidkonzentrat enthaltend mindestens ein Peptidgemisch gemäß mindestens einem der Ansprüche 1 bis 8. A surfactant concentrate containing at least one peptide mixture according to at least one of claims 1 to 8.
1 1. Verwendung mindestens eines Peptidgemisches gemäß mindestens einem der Ansprüche 1 bis 8 als Emulgator, Dispergierhilfsmittel, Konditionierungsmittel für Haut und Haar, Schaumbildner oder Schaumstabilisator. 1 1. Use of at least one peptide mixture according to any one of claims 1 to 8 as an emulsifier, dispersing agents, conditioners for skin and hair, foaming agent or foam stabilizer.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE102010062600A DE102010062600A1 (en) | 2010-12-08 | 2010-12-08 | Hydrophobized protein hydrolyzate |
| PCT/EP2011/069811 WO2012076284A1 (en) | 2010-12-08 | 2011-11-10 | Hydrophobized protein hydrolysate |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| EP2648538A1 true EP2648538A1 (en) | 2013-10-16 |
Family
ID=45044545
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP11788092.2A Withdrawn EP2648538A1 (en) | 2010-12-08 | 2011-11-10 | Hydrophobized protein hydrolysate |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20130251658A1 (en) |
| EP (1) | EP2648538A1 (en) |
| JP (1) | JP5951629B2 (en) |
| CN (1) | CN103249313A (en) |
| BR (1) | BR112013012390A8 (en) |
| DE (1) | DE102010062600A1 (en) |
| WO (1) | WO2012076284A1 (en) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE102012205372A1 (en) * | 2012-04-02 | 2013-10-02 | Evonik Industries Ag | Glutamine-rich peptides as air-entraining agents in building material |
| CN106082752B (en) * | 2016-06-15 | 2017-11-24 | 中原工学院 | A kind of preparation method of enzyme crosslinking mixed hydrolysis albumen cement blowing agent |
| CN112998010A (en) * | 2021-03-03 | 2021-06-22 | 成都嘉佑美康新材料科技有限公司 | Special auxiliary agent for unmanned aerial vehicle plant protection and flying prevention and preparation method and application thereof |
| CN115233450B (en) * | 2022-08-04 | 2023-12-26 | 江南大学 | Method for preparing alcohol soluble protein hydrophobic finishing agent by biological method |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH636248A5 (en) * | 1979-03-09 | 1983-05-31 | Nestle Sa | PROCESS FOR THE PREPARATION OF A PURIFIED PROTEIN HYDROLYSATE. |
| JPS635009A (en) * | 1986-06-24 | 1988-01-11 | Kao Corp | Cosmetic |
| JP2736425B2 (en) * | 1988-11-24 | 1998-04-02 | 一丸ファルコス株式会社 | Cosmetics containing alkylated modified products of animal or plant-derived protein hydrolysates |
| JPH0732678B2 (en) * | 1989-06-07 | 1995-04-12 | ハウス食品株式会社 | Doria in a container |
| CA2155762C (en) * | 1994-08-23 | 2000-04-25 | Haruya Sato | Protein modification method |
| 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 (en) * | 1995-10-12 | 2004-09-22 | ライオン株式会社 | Hair treatment agent and hair treatment method |
| FR2740331B1 (en) * | 1995-10-25 | 1997-12-19 | Sederma Sa | NEW COSMETIC COMPOSITIONS FOR THE TREATMENT OF HAIR AND SCALP |
| JP2000300287A (en) * | 1999-03-15 | 2000-10-31 | Shinichiro Nishimura | Introduction of sugar chain by using transglutaminase |
| JPWO2005095331A1 (en) * | 2004-03-31 | 2008-02-21 | 塩野義製薬株式会社 | Sugar chain-peptide binder |
| JP2007022958A (en) * | 2005-07-15 | 2007-02-01 | Katakura Chikkarin Co Ltd | Atelocollagen and/or its derivative derived from squid or catfish, method for producing the same, and cosmetic compounded of the atelocollagen and/or its derivative |
| EP2123756B1 (en) | 2007-02-15 | 2014-06-04 | Ajinomoto Co., Inc. | Transglutaminase having disulfide bond introduced therein |
| DE102007031202A1 (en) * | 2007-07-04 | 2009-03-19 | Henkel Ag & Co. Kgaa | New protein hydrolysate obtained from wool of Vicugna useful as laundry detergent, wool detergent, manual dishwashing agent and cosmetic agent, which is useful for treating skin and hair |
| DK2251421T3 (en) | 2008-02-13 | 2017-02-06 | Amano Enzyme Inc | Stabilized transglutaminase and process for its preparation |
-
2010
- 2010-12-08 DE DE102010062600A patent/DE102010062600A1/en not_active Withdrawn
-
2011
- 2011-11-10 CN CN2011800593001A patent/CN103249313A/en active Pending
- 2011-11-10 US US13/992,097 patent/US20130251658A1/en not_active Abandoned
- 2011-11-10 JP JP2013542436A patent/JP5951629B2/en not_active Expired - Fee Related
- 2011-11-10 EP EP11788092.2A patent/EP2648538A1/en not_active Withdrawn
- 2011-11-10 BR BR112013012390A patent/BR112013012390A8/en not_active IP Right Cessation
- 2011-11-10 WO PCT/EP2011/069811 patent/WO2012076284A1/en active Application Filing
Non-Patent Citations (2)
| Title |
|---|
| None * |
| See also references of WO2012076284A1 * |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2014506239A (en) | 2014-03-13 |
| BR112013012390A8 (en) | 2017-08-15 |
| BR112013012390A2 (en) | 2016-07-19 |
| CN103249313A (en) | 2013-08-14 |
| WO2012076284A1 (en) | 2012-06-14 |
| US20130251658A1 (en) | 2013-09-26 |
| JP5951629B2 (en) | 2016-07-13 |
| DE102010062600A1 (en) | 2012-06-14 |
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