CN116987142A - Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect - Google Patents
Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect Download PDFInfo
- Publication number
- CN116987142A CN116987142A CN202310890118.5A CN202310890118A CN116987142A CN 116987142 A CN116987142 A CN 116987142A CN 202310890118 A CN202310890118 A CN 202310890118A CN 116987142 A CN116987142 A CN 116987142A
- Authority
- CN
- China
- Prior art keywords
- active peptide
- alkaline
- aminobutyric acid
- gamma
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 title claims abstract description 207
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 142
- 239000006041 probiotic Substances 0.000 title claims abstract description 140
- 235000018291 probiotics Nutrition 0.000 title claims abstract description 140
- 229960003692 gamma aminobutyric acid Drugs 0.000 title claims abstract description 105
- OGNSCSPNOLGXSM-UHFFFAOYSA-N (+/-)-DABA Natural products NCCC(N)C(O)=O OGNSCSPNOLGXSM-UHFFFAOYSA-N 0.000 title claims abstract description 102
- 239000000203 mixture Substances 0.000 title claims abstract description 83
- 238000002360 preparation method Methods 0.000 title claims abstract description 14
- 230000003712 anti-aging effect Effects 0.000 title claims abstract description 12
- 230000000694 effects Effects 0.000 claims abstract description 81
- 150000001413 amino acids Chemical class 0.000 claims abstract description 78
- 210000004027 cell Anatomy 0.000 claims abstract description 26
- 102000008186 Collagen Human genes 0.000 claims abstract description 20
- 108010035532 Collagen Proteins 0.000 claims abstract description 20
- 229920001436 collagen Polymers 0.000 claims abstract description 20
- 230000014509 gene expression Effects 0.000 claims abstract description 18
- 230000006378 damage Effects 0.000 claims abstract description 17
- 210000001626 skin fibroblast Anatomy 0.000 claims abstract description 17
- 230000028327 secretion Effects 0.000 claims abstract description 15
- 230000001737 promoting effect Effects 0.000 claims abstract description 11
- 208000027418 Wounds and injury Diseases 0.000 claims abstract description 10
- 208000014674 injury Diseases 0.000 claims abstract description 10
- 210000004927 skin cell Anatomy 0.000 claims abstract description 10
- 230000000529 probiotic effect Effects 0.000 claims description 96
- 230000003078 antioxidant effect Effects 0.000 claims description 20
- 239000003963 antioxidant agent Substances 0.000 claims description 19
- 239000004475 Arginine Substances 0.000 claims description 14
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 14
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 14
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 14
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 14
- 239000004472 Lysine Substances 0.000 claims description 14
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 14
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 14
- 230000003833 cell viability Effects 0.000 claims description 6
- 230000032683 aging Effects 0.000 abstract description 11
- 230000006870 function Effects 0.000 abstract description 10
- 238000007254 oxidation reaction Methods 0.000 abstract description 10
- 230000003647 oxidation Effects 0.000 abstract description 8
- 238000011160 research Methods 0.000 abstract description 8
- 239000003814 drug Substances 0.000 abstract description 3
- 229940079593 drug Drugs 0.000 abstract description 2
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 2
- 241000244206 Nematoda Species 0.000 description 48
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 23
- 101000686031 Homo sapiens Proto-oncogene tyrosine-protein kinase ROS Proteins 0.000 description 22
- 238000004458 analytical method Methods 0.000 description 18
- 101100366137 Mesembryanthemum crystallinum SODCC.1 gene Proteins 0.000 description 16
- 101100096142 Panax ginseng SODCC gene Proteins 0.000 description 16
- FIKAKWIAUPDISJ-UHFFFAOYSA-L paraquat dichloride Chemical compound [Cl-].[Cl-].C1=C[N+](C)=CC=C1C1=CC=[N+](C)C=C1 FIKAKWIAUPDISJ-UHFFFAOYSA-L 0.000 description 16
- 101150017120 sod gene Proteins 0.000 description 16
- 230000002829 reductive effect Effects 0.000 description 14
- 102000004190 Enzymes Human genes 0.000 description 13
- 108090000790 Enzymes Proteins 0.000 description 13
- AJLNZWYOJAWBCR-OOPVGHQCSA-N (4s)-4-acetamido-5-[[(2s)-1-[[(2s)-1-[[(2s)-5-amino-1-[[(2s)-1-[[(2s)-1-amino-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-car Chemical compound OC(=O)CC[C@H](NC(C)=O)C(=C)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCCN=C(N)N)C(N)=O AJLNZWYOJAWBCR-OOPVGHQCSA-N 0.000 description 12
- 108010024636 Glutathione Proteins 0.000 description 11
- QNVSXXGDAPORNA-UHFFFAOYSA-N Resveratrol Natural products OC1=CC=CC(C=CC=2C=C(O)C(O)=CC=2)=C1 QNVSXXGDAPORNA-UHFFFAOYSA-N 0.000 description 11
- LUKBXSAWLPMMSZ-OWOJBTEDSA-N Trans-resveratrol Chemical compound C1=CC(O)=CC=C1\C=C\C1=CC(O)=CC(O)=C1 LUKBXSAWLPMMSZ-OWOJBTEDSA-N 0.000 description 11
- 238000002474 experimental method Methods 0.000 description 11
- 229960003180 glutathione Drugs 0.000 description 11
- 238000000034 method Methods 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 229940016667 resveratrol Drugs 0.000 description 11
- 235000021283 resveratrol Nutrition 0.000 description 11
- 210000003491 skin Anatomy 0.000 description 11
- 108010016160 Matrix Metalloproteinase 3 Proteins 0.000 description 10
- 102000001776 Matrix metalloproteinase-9 Human genes 0.000 description 10
- 108010015302 Matrix metalloproteinase-9 Proteins 0.000 description 10
- 102100030416 Stromelysin-1 Human genes 0.000 description 10
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 9
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 9
- 150000002500 ions Chemical class 0.000 description 9
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 9
- 230000001965 increasing effect Effects 0.000 description 8
- 230000002195 synergetic effect Effects 0.000 description 8
- 230000001976 improved effect Effects 0.000 description 7
- 230000002401 inhibitory effect Effects 0.000 description 7
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 239000001963 growth medium Substances 0.000 description 6
- 230000009759 skin aging Effects 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 102000012422 Collagen Type I Human genes 0.000 description 5
- 108010022452 Collagen Type I Proteins 0.000 description 5
- 102000001187 Collagen Type III Human genes 0.000 description 5
- 108010069502 Collagen Type III Proteins 0.000 description 5
- 239000013543 active substance Substances 0.000 description 5
- 235000006708 antioxidants Nutrition 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 230000003834 intracellular effect Effects 0.000 description 5
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 4
- 238000012258 culturing Methods 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 230000036542 oxidative stress Effects 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 3
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000000975 bioactive effect Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000000354 decomposition reaction Methods 0.000 description 3
- 230000002708 enhancing effect Effects 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 210000002744 extracellular matrix Anatomy 0.000 description 3
- 230000004792 oxidative damage Effects 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- 239000001888 Peptone Substances 0.000 description 2
- 108010080698 Peptones Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 241001052560 Thallis Species 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000003064 anti-oxidating effect Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 2
- 235000019341 magnesium sulphate Nutrition 0.000 description 2
- 238000001819 mass spectrum Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 235000019319 peptone Nutrition 0.000 description 2
- 239000008055 phosphate buffer solution Substances 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 150000003254 radicals Chemical class 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000002040 relaxant effect Effects 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 230000037303 wrinkles Effects 0.000 description 2
- 206010001497 Agitation Diseases 0.000 description 1
- 102100036213 Collagen alpha-2(I) chain Human genes 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000875067 Homo sapiens Collagen alpha-2(I) chain Proteins 0.000 description 1
- 208000002720 Malnutrition Diseases 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 206010051246 Photodermatosis Diseases 0.000 description 1
- 208000028990 Skin injury Diseases 0.000 description 1
- 102000046299 Transforming Growth Factor beta1 Human genes 0.000 description 1
- 102000009618 Transforming Growth Factors Human genes 0.000 description 1
- 108010009583 Transforming Growth Factors Proteins 0.000 description 1
- 101800002279 Transforming growth factor beta-1 Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- PMZXXNPJQYDFJX-UHFFFAOYSA-N acetonitrile;2,2,2-trifluoroacetic acid Chemical compound CC#N.OC(=O)C(F)(F)F PMZXXNPJQYDFJX-UHFFFAOYSA-N 0.000 description 1
- 238000003915 air pollution Methods 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000002249 anxiolytic agent Substances 0.000 description 1
- 230000000949 anxiolytic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- -1 e.g. Proteins 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 235000013376 functional food Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000001071 malnutrition Effects 0.000 description 1
- 235000000824 malnutrition Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 230000003020 moisturizing effect Effects 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 239000002858 neurotransmitter agent Substances 0.000 description 1
- 208000015380 nutritional deficiency disease Diseases 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229940127557 pharmaceutical product Drugs 0.000 description 1
- 230000008845 photoaging Effects 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 206010036067 polydipsia Diseases 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000003334 potential effect Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 239000008213 purified water Substances 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 239000000932 sedative agent Substances 0.000 description 1
- 230000001624 sedative effect Effects 0.000 description 1
- 230000009758 senescence Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- IZTQOLKUZKXIRV-YRVFCXMDSA-N sincalide Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](N)CC(O)=O)C1=CC=C(OS(O)(=O)=O)C=C1 IZTQOLKUZKXIRV-YRVFCXMDSA-N 0.000 description 1
- 230000008591 skin barrier function Effects 0.000 description 1
- 230000037394 skin elasticity Effects 0.000 description 1
- 244000005714 skin microbiome Species 0.000 description 1
- 230000000391 smoking effect Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 229940099456 transforming growth factor beta 1 Drugs 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000037373 wrinkle formation Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/175—Amino acids
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/195—Carboxylic acids, e.g. valproic acid having an amino group
- A61K31/197—Carboxylic acids, e.g. valproic acid having an amino group the amino and the carboxyl groups being attached to the same acyclic carbon chain, e.g. gamma-aminobutyric acid [GABA], beta-alanine, epsilon-aminocaproic acid or pantothenic acid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/195—Carboxylic acids, e.g. valproic acid having an amino group
- A61K31/197—Carboxylic acids, e.g. valproic acid having an amino group the amino and the carboxyl groups being attached to the same acyclic carbon chain, e.g. gamma-aminobutyric acid [GABA], beta-alanine, epsilon-aminocaproic acid or pantothenic acid
- A61K31/198—Alpha-amino acids, e.g. alanine or edetic acid [EDTA]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/41—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having five-membered rings with two or more ring hetero atoms, at least one of which being nitrogen, e.g. tetrazole
- A61K31/4164—1,3-Diazoles
- A61K31/4172—Imidazole-alkanecarboxylic acids, e.g. histidine
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
-
- 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
- A61K8/40—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
- A61K8/44—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof
-
- 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
- A61K8/49—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing heterocyclic compounds
- A61K8/494—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing heterocyclic compounds with more than one nitrogen as the only hetero atom
- A61K8/4946—Imidazoles or their condensed derivatives, e.g. benzimidazoles
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/16—Emollients or protectives, e.g. against radiation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/18—Antioxidants, e.g. antiradicals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q17/00—Barrier preparations; Preparations brought into direct contact with the skin for affording protection against external influences, e.g. sunlight, X-rays or other harmful rays, corrosive materials, bacteria or insect stings
- A61Q17/04—Topical preparations for affording protection against sunlight or other radiation; Topical sun tanning preparations
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
- A61K2800/59—Mixtures
- A61K2800/591—Mixtures of compounds not provided for by any of the codes A61K2800/592 - A61K2800/596
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Medicinal Chemistry (AREA)
- Epidemiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Dermatology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Birds (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Polymers & Plastics (AREA)
- Mycology (AREA)
- Immunology (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to the technical field of biological medicines, and particularly discloses a composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application thereof in preparation of products with anti-aging effect. The alkaline probiotics active peptide has an amino acid sequence shown in SEQ ID NO. 1; wherein, the amino acid sequence of SEQ ID NO. 1 is: ser-Glu-Phe-Gly-Met. The composition containing gamma-aminobutyric acid and alkaline probiotics active peptide comprises gamma-aminobutyric acid, alkaline amino acid and alkaline probiotics active peptide. The research shows that the alkaline probiotics active peptide and the composition containing gamma-aminobutyric acid and the alkaline probiotics active peptide have the functions of resisting oxidation and aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like.
Description
Technical Field
The invention relates to the technical field of biological medicine, in particular to a composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application thereof in preparation of products with anti-aging effect.
Background
The skin aging causes mainly comprise collagen and elastin reduction caused by natural aging, skin injury caused by ultraviolet radiation, damage to skin caused by air pollution, bad living habits such as smoking, excessive drinking, lack of exercise, malnutrition and the like, and the interaction of these factors can accelerate the aging of the skin.
A great deal of research on the aspects of antioxidation and antisenescence of amino acid shows that the amino acid can resist cell oxidative damage through various mechanisms, such as increasing the activity of intracellular antioxidant enzyme, reducing the generation of free radicals, enhancing the free radical removal of cells, inhibiting inflammatory reaction and the like, and has a certain potential effect on improving the anti-aging capability of organisms. While active peptides are a class of bioactive molecules consisting of amino acids, short chains consisting of amino acids, typically containing 2 to 50 amino acid residues. A large number of researches show that the active peptide in the aspect of aging resistance can play roles in resisting oxidization,
The anti-aging activity is exerted in the modes of promoting tissue repair, resisting inflammation, promoting collagen generation, regulating metabolism and the like.
Gamma-aminobutyric acid (gamma-aminobutyric acid, GABA for short) is a substance which plays a role in inhibiting neurotransmitters by inhibiting nerve cell excitability, and is widely used in foods, health products, medicines and the like. The research shows that GABA has anxiolytic, sedative and relaxing effects. In skin care products, GABA is used as an active ingredient having effects of soothing skin, relaxing muscles, moisturizing, etc., thereby reducing expression wrinkles and fine lines.
However, the use of gamma-aminobutyric acid alone has to be further improved in terms of antioxidant and anti-aging effects; therefore, the gamma-aminobutyric acid is taken as one of the raw materials, and the development of the composition with good anti-aging and/or oxidation resistance has important application value.
Disclosure of Invention
In order to overcome at least one technical problem existing in the prior art, the invention provides an alkaline probiotic active peptide and a composition containing gamma-aminobutyric acid and the alkaline probiotic active peptide.
The technical scheme of the invention is as follows:
the invention firstly provides an alkaline probiotics active peptide which has an amino acid sequence shown as SEQ ID NO. 1;
wherein, the amino acid sequence of SEQ ID NO. 1 is: ser-Glu-Phe-Gly-Met.
The invention also provides a composition containing gamma-aminobutyric acid and alkaline probiotic active peptide, which comprises gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide;
the alkaline probiotic active peptide is the alkaline probiotic active peptide of claim 1.
Preferably, the basic amino acid is selected from one or more of lysine, histidine or arginine.
Preferably, the composition comprises gamma-aminobutyric acid and lysine, arginine, histidine and an alkaline probiotic active peptide.
It is further preferred that the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1 (1-100): 1-100.
Still more preferably, the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1 (1-50): 1-50.
Most preferably, the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1:2.5:2.0:3.5:10.0.
The invention also provides application of the alkaline probiotics active peptide or the composition containing the gamma-aminobutyric acid and the alkaline probiotics active peptide in preparation of products with antioxidant and/or anti-aging effects.
The invention also provides application of the alkaline probiotics active peptide or the composition containing the gamma-aminobutyric acid and the alkaline probiotics active peptide in preparation of products with the effect of improving the activity of skin cells.
The invention also provides application of the alkaline probiotics active peptide or the composition containing the gamma-aminobutyric acid and the alkaline probiotics active peptide in preparation of products with the effect of improving ultraviolet injury resistance of cells.
The invention also provides application of the alkaline probiotics active peptide or the composition containing the gamma-aminobutyric acid and the alkaline probiotics active peptide in preparation of products with the effect of promoting expression and/or secretion of skin fibroblast collagen.
Preferably, the product is a food, a functional food, a skin care product or a pharmaceutical product.
The beneficial effects are that:
(1) The invention provides a brand new alkaline probiotics active peptide with an amino acid sequence shown as SEQ ID NO. 1; the research shows that the alkaline probiotics active peptide has the functions of resisting oxidation and aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like.
(2) Further researches show that the alkaline probiotics active peptide has the functions of resisting oxidation and aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like, which are obviously higher than that of the known acetyl hexapeptide-3 and glutathione; significant effects are achieved.
(3) The invention also provides a brand new composition containing gamma-aminobutyric acid and alkaline probiotics active peptide; research shows that the composition containing the gamma-aminobutyric acid and the alkaline probiotic active peptide, which is formed by combining the gamma-aminobutyric acid, the alkaline amino acid and the alkaline probiotic active peptide, has the functions of resisting oxidation and aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like, and is further and obviously improved; the effects of resisting oxidation, resisting aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like are obviously higher than those of the alkaline probiotics active peptide disclosed by the invention, and are also obviously higher than those of gamma-aminobutyric acid and alkaline amino acid; this may be the result of a synergistic effect of combining gamma-aminobutyric acid, a basic amino acid and a basic probiotic active peptide.
(4) As the alkaline probiotics active peptide and the composition containing gamma-aminobutyric acid and the alkaline probiotics active peptide have the functions of resisting oxidation and aging, improving the activity of skin cells, improving the ultraviolet injury resistance of cells, promoting the expression and secretion of collagen of skin fibroblasts and the like; therefore, the active ingredient of the compound has important application value in preparing products with corresponding functions.
Drawings
FIG. 1 is a HPLC detection spectrum of the alkaline probiotic active peptide of the present invention.
FIG. 2 is a mass spectrum of the basic probiotic active peptide of the present invention.
FIG. 3 is a graph showing the results of experiments on the influence of the alkaline probiotic active peptide and the composition containing gamma-aminobutyric acid and the alkaline probiotic active peptide on the oxidative index of insects.
FIG. 4 is a graph showing the experimental results of the influence of the alkaline probiotic active peptide and the composition containing gamma-aminobutyric acid and the alkaline probiotic active peptide on the oxidation index of skin fibroblasts and collagen.
Detailed Description
The technical scheme of the present invention will be clearly and completely described in the following examples. It will be apparent that the described embodiments are only some, but not all, embodiments of the invention. All other embodiments, which can be made by those skilled in the art based on the embodiments of the invention without making any inventive effort, are intended to be within the scope of the invention.
EXAMPLE 1 preparation method of alkaline probiotic active peptide of the present invention
(1) Collecting skin flora from healthy children, adding into culture medium, and standing at 37deg.C for 12 hr (the culture medium comprises peptone 9.0g/L, yeast powder 9.0g/L, glucose 9.0g/L, sodium acetate 3.0g/L, dipotassium hydrogen phosphate 1.0g/L, and magnesium sulfate 0.2 g/L).
(2) Culturing the bacterial colony culture solution obtained in the step (1) on a solid culture medium in a streaking wayAfter culturing, different strains are taken and respectively subjected to expansion culture (the composition of culture medium comprises 9.0g/L of peptone, 9.0g/L of yeast powder, 9.0g/L of glucose, 3.0g/L of sodium acetate, 1.0g/L of dipotassium hydrogen phosphate and 0.2g/L of magnesium sulfate.) by transferring the strains to an 8L fermentation tank, adding 8L liquid culture medium with pH value of 6.2, culturing at 37 ℃ for 24h, and stirring and culturing until the bacterial body reaches OD 600 At=2.5, the culture was terminated and the culture broth was collected, centrifuged and the cells were collected, and lyophilized).
(3) Preparation of cell lysate: mixing the freeze-dried powder of the thalli collected in the step (2) with purified water according to the mass ratio of 1:30, performing ultrasonic crushing for 30min, and adopting a dialysis membrane (the aperture of the dialysis membrane is less than 1 kDa); and freeze-drying the dialyzate, and then removing fat and sugar to obtain the bacterial lysate.
(4) The cell lysate was dissolved in a small amount of water, and the mixture was separated by Sephadex G15 column chromatography using 0.20,0.40,0.80,1.60mM (NH) 4 ) 2 SO 4 Gradient elution with buffers (each gradient buffer was used in an amount of 2 times the column volume of sephadex G15) and 0.80mM (NH) 4 ) 2 SO 4 Concentrating and drying the eluent eluted by the buffer solution to obtain a thallus active site;
(5) preparing the active site of the thalli by HPLC to obtain the alkaline probiotic active peptide;
wherein, the preparation conditions of HPLC are as follows:
taking 0.1% trifluoroacetic acid-acetonitrile solution as a mobile phase A, taking 0.1% trifluoroacetic acid aqueous solution as a mobile phase B, measuring the wavelength to be 220nm, and the flow rate to be 10mL/min; the chromatographic column is as follows: XBridge BEH C18 OBD Prep Column,5 μm,19mm x 150mm;
collecting eluent corresponding to a chromatographic peak for 12.03min, concentrating and drying to obtain the alkaline probiotic active peptide;
HPLC elution times were set as shown in the following table:
furthermore, the amino acid sequence of the alkaline probiotics active peptide is determined by identifying the amino acid sequence by a mass spectrum method and a Marfey method; the results were as follows:
m/z 570.2222 is inferred as [ M+H ]] + Ions; m/z 421.1719 is inferred as y4 ions; m/z 364.1502 is inferred as y3 ions; m/z 354.1480 is inferred to be [ b3+2H] + Ions; m/z 259.1084 is inferred as [ y3-y1-H ] 2 O+H] + Ions; m/z 217.0818 is inferred as y2 ion; m/z 150.0583 is inferred to be [ b1+2H] + Ions; m/z 120.0807 is inferred to be [ Phe-COOH+H ]] + Ions; m/z 104.0529 inferred as [ Met-COOH+H ]] + Ions. And finally, combining with a Marfey method, identifying the alkaline probiotics active peptide as the oligopeptide with the amino acid sequence of Ser-Glu-Phe-Gly-Met.
EXAMPLE 2 preparation of compositions containing gamma-aminobutyric acid and alkaline probiotic active peptides
Mixing gamma-aminobutyric acid, lysine, arginine, histidine and alkaline probiotics active peptide according to the mass ratio of 1:2.5:2.0:3.5:10.0, and obtaining the gamma-aminobutyric acid, alkaline amino acid and alkaline probiotics active peptide composition, namely the composition containing the gamma-aminobutyric acid and the alkaline probiotics active peptide.
Effect example 1 evaluation of antioxidant and anti-aging Activity
The implementation method comprises the following steps: n2 wild-type nematodes were grown at 18℃and randomly divided into 9 groups (not less than 60 per group) of 3 parallel control groups. The normal control group was replaced with phosphate buffer solution, the experimental group was pre-incubated at a dose of 40. Mu.g/mL of active substance for 3 days, and the remaining nematodes were transferred to a dish containing paraquat (30 nM) for further 3 days, except for the normal control group. The nematode living bodies are collected, and ROS, MDA, lipofuscin content and SOD and CAT activities in the same number (30) of living nematodes are measured.
As shown in fig. 3 and a, b, c, d, e, compared with the blank control group, paraquat exposure significantly increases the ROS, MDA and lipofuscin contents in the nematodes, and the antioxidant enzymes SOD and CAT activity significantly decreases, and the experimental results show that paraquat exposure severely oxidizes and damages the nematodes, induces nematode oxidative stress and accelerates senescence. Compared with a blank control group, the paraquat exposure increases the ROS content in the nematodes by 220.5 percent (p < 0.01), but the analysis experiment results show that the ROS content in the nematodes pretreated by the alkaline probiotic active peptide, especially gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition is obviously lower than that in the paraquat exposure group. Wherein, compared with the paraquat exposure group, the content of ROS in the nematode of the group of the gamma-aminobutyric acid, the basic amino acid and the basic probiotic active peptide composition is reduced by 58.8 percent (p < 0.01). Compared with gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid composition and basic probiotic active peptide with the same concentration, the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can better improve the function of removing ROS in a nematode body.
Further analysis and experiment results show that the paraquat exposure obviously increases the MDA and lipofuscin content in the nematode body; compared with the blank control group, the MDA and lipofuscin content in the paraquat exposure group nematodes are respectively increased by 125.4 percent (p < 0.01) and 201.6 percent (p < 0.01), which proves that paraquat exposure accelerates nematode aging while causing serious oxidative damage and inducing nematode oxidative stress. However, the analysis experiment results show that MDA and lipofuscin content in the nematode body pretreated by the alkaline probiotics active peptide, especially gamma-aminobutyric acid, alkaline amino acid and alkaline probiotics active peptide composition is obviously lower than that of the paraquat exposure group. Wherein, compared with paraquat exposure group, the MDA and lipofuscin contents in the nematodes of the group of active peptide composition of gamma-aminobutyric acid, basic amino acid and basic probiotics are respectively reduced by 46.2% (p < 0.01) and 55.7% (p < 0.01). Similar to the function of the active substances for enhancing the activity of the active substances in the nematode to clear away ROS in vivo, compared with the function of gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid composition or basic probiotic active peptide with the same concentration, the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can better improve the function of the nematode to clear away MDA in vivo or inhibit the generation of lipofuscin vivo.
And the analysis and experiment results show that paraquat exposure obviously reduces the activity of antioxidant enzyme SOD and CAT in the nematode body; compared with the blank control group, the activities of antioxidant enzymes SOD and CAT in the nematodes in the paraquat exposure group are respectively reduced by 48.4 percent (p < 0.01) and 39.6 percent (p < 0.01), which shows that the activities of antioxidant enzymes in the nematodes are sharply reduced when paraquat is exposed to induce the generation of active oxides in the nematodes. The analysis experiment results show that the antioxidant enzyme SOD and CAT activity in the nematode body pretreated by the alkaline probiotics active peptide, especially the gamma-aminobutyric acid, the alkaline amino acid and the alkaline probiotics active peptide composition are obviously higher than those of the paraquat exposure group. Compared with paraquat exposure groups, the antioxidant enzyme SOD and CAT activity in nematodes in the group of gamma-aminobutyric acid, alkaline amino acid and alkaline probiotics active peptide composition groups are respectively improved by 70.7% (p < 0.01) and 53.2% (p < 0.01). Similar to the effect of the active substances on enhancing the activity of the nematode for removing active oxygen and the like in vivo, compared with the gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid composition or basic probiotic active peptide with the same concentration, the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can better improve the activity of antioxidant enzymes SOD and CAT in the nematode. According to the experimental results, we speculate that the gamma-aminobutyric acid, the basic amino acid and the basic probiotic active peptide can play the roles of improving the ROS and MDA removal of nematodes, inhibiting lipofuscin generation activity and improving the SOD and CAT activities of nematode antioxidase through synergistic effect.
The experimental groupings are shown in the following table:
the basic probiotic active peptide tested in the embodiment of the effect is the basic probiotic active peptide with the amino acid sequence shown in SEQ ID NO. 1; the composition containing the gamma-aminobutyric acid and the alkaline probiotic active peptide is prepared by the method in the embodiment 2; the basic amino acid is a mixture obtained by combining lysine and arginine and histidine in a mass ratio of 2.5:2.0:3.5.
Effect example 2 evaluation of anti-oxidative, anti-UV-exposure-induced photo-aging Activity
The implementation method comprises the following steps: n2 wild-type nematodes were grown at 18℃and randomly divided into 9 groups (not less than 60 per group) of 3 parallel control groups. The normal control group was replaced with phosphate buffer solution, the experimental group was pre-incubated for 3 days at a dose of 40. Mu.g/mL of active, the remaining nematodes of each group, except the normal control group, were transferred to a freshly prepared NGM/OP50 plate and used with a 254nm UV bulb (20W) at 1000J/m 2 After 4 hours of irradiation with the intensity of (c). The nematode living bodies are collected, and ROS, MDA, lipofuscin content and SOD and CAT activities in the same number (30) of living nematodes are measured.
As shown in fig. 3 and f, g, h, i, j, after ultraviolet irradiation treatment, the ROS, MDA and lipofuscin contents in the nematodes in the ultraviolet irradiation group are significantly increased, and the activities of antioxidant enzymes SOD and CAT in the nematodes are significantly reduced, which means that ultraviolet irradiation induces oxidative stress of the nematodes, so that the nematodes are severely damaged by oxidation and the aging of the nematodes is accelerated. Analytical data shows that the ROS, MDA and lipofuscin content in the nematode of ultraviolet irradiation group are increased by 245.4% (p < 0.01), 151.3% (p < 0.01) and 311.3% (p < 0.01) respectively compared with the blank control group; the activity of the antioxidant enzyme SOD and CAT in the nematode body is respectively reduced by 35.2 percent (p < 0.01) and 28.7 percent (p < 0.01). Unlike UV irradiation group, SOD and CAT activity in nematode pretreated with gamma-aminobutyric acid, alkaline probiotic active peptide and gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition are effectively improved, and ROS, MDA and lipofuscin in nematode pretreated with gamma-aminobutyric acid, probiotic active peptide and gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition are lower than those in UV irradiation group. Compared with ultraviolet irradiation group, the content of ROS, MDA and lipofuscin in nematode in group of gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition is reduced by 55.4% (p < 0.01), 40.9% (p < 0.01) and 60.1% (p < 0.01), respectively.
Further analysis and experiment results show that the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can effectively improve the activities of antioxidant enzyme SOD and CAT in nematodes; compared with ultraviolet irradiation group, the antioxidant enzyme SOD and CAT activity in the nematode of the active peptide composition group of gamma-aminobutyric acid, alkaline amino acid and alkaline probiotics are respectively improved by 39.1 percent (p < 0.01) and 30.9 percent (p < 0.01).
The experimental results in the part show that the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can improve the activity of the nematode in eliminating ROS and MDA in vivo and inhibiting lipofuscin generation in vivo, and is stronger than gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid or basic probiotic active peptide under the condition of the same concentration. We speculate that gamma-aminobutyric acid, basic amino acid, and basic probiotic bioactive peptide can exert the activities of improving antioxidant enzyme SOD and CAT in the nematode body and improving the activities of scavenging ROS and MDA and inhibiting lipofuscin in the nematode body through synergistic effect.
The experimental groupings are shown in the following table:
the basic probiotic active peptide tested in the embodiment of the effect is the basic probiotic active peptide with the amino acid sequence shown in SEQ ID NO. 1; the composition containing the gamma-aminobutyric acid and the alkaline probiotic active peptide is prepared by the method in the embodiment 2; the basic amino acid is a mixture obtained by combining lysine and arginine and histidine in a mass ratio of 2.5:2.0:3.5.
Effect example 3 evaluation of skin cell Activity and UVB injury resistance Activity
The implementation method comprises the following steps: human skin fibroblasts were cultured normally, after cells were grown to 90% confluence, digested with 0.25% trypsin and inoculated into 24-well and 6-well plates, respectively, after 50% confluence of cells, actives (final concentration 50 μg/mL) were added and the culture was continued for 48 hours, and then ultraviolet irradiation experiments were performed. In the experiment, 6 UVA 360nm lamp tubes of Beijing optical instrument are used as UVA ultraviolet lamp, the ultraviolet lamp tube is sterilized and then placed in an ultra-clean bench, the constant-temperature water bath box is strictly sterilized and then added with pure water, and the ultra-clean bench is sterilized for 30min. Before irradiation, a long-wave ultraviolet lamp is placed on a constant-temperature water bath box, the distance between a measuring lamp tube and an irradiation plane of a 24-pore plate is 12cm, and the UVA irradiation power of the plane is measured by a photoelectric instrument of Beijing university. The long-wave ultraviolet lamp is preheated for 30min before measurement, the measured power is 18.8mI/s after the irradiation power is stable, the culture medium is replaced by PBS during irradiation, the cover is opened, and the cells are exposed to a UVA irradiation device in a constant-temperature water bath, wherein the irradiation distance is 12cm. Adding PBS (phosphate buffered saline) solution 2h before irradiation, placing a culture plate into a 37C constant-temperature water bath, placing DMEM containing 10% calf serum after irradiation into the culture box for continuous culture, collecting cells and culture supernatant after 24h, and detecting cell viability by using a CCK 8 kit; the content of the protein is detected according to the operation instructions of an ELISA kit of ROS, SOD, MMP-3, MMP-9, type I collagen, type III collagen and transforming growth factor beta 1 (TGF-beta 1).
The experimental groupings were as follows:
the basic probiotic active peptide tested in the embodiment of the effect is the basic probiotic active peptide with the amino acid sequence shown in SEQ ID NO. 1; the composition containing the gamma-aminobutyric acid and the alkaline probiotic active peptide is prepared by the method in the embodiment 2; the basic amino acid is a mixture obtained by combining lysine and arginine and histidine in a mass ratio of 2.5:2.0:3.5.
Analysis of the results the experimental results of the present examples (fig. 4 a) show that the uv irradiation reduced cell viability by 29.6% (p < 0.01) compared to the blank, but the experimental results of the analysis found that the activity of the cells pretreated with the active substance, especially gamma-aminobutyric acid, basic amino acid, basic probiotic active peptide composition, was significantly higher than in the uv irradiated group. Wherein, compared with the ultraviolet irradiation group, the cell viability of the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition group is improved by 34.6 percent (p < 0.01). Compared with gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid composition and basic probiotic active peptide with the same concentration, the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can better improve the cell activity of cells under the ultraviolet irradiation condition, which indicates that the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition can better improve the activity of cells against ultraviolet irradiation damage.
Further analysis of experimental results of the embodiment of the effect shows that compared with gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid and basic probiotic active peptide groups, the cell viability of the gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide composition groups is improved more obviously. The activity of the gamma-aminobutyric acid, basic amino acid and basic probiotics active peptide composition for improving the cell activity is stronger than that of gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid and basic probiotics active peptide. We speculate that gamma-aminobutyric acid, basic amino acid, basic probiotic active peptide may better improve cell viability and improve cell activity against ultraviolet injury through synergistic effect.
Excessive production of ROS induces oxidative stress and oxidative damage to cells. Therefore, the removal of excessive ROS in cells and organisms plays an important role in the antioxidant and anti-aging processes of skin. Further analysis of the experimental results of this effect example (fig. 4 b) shows that the uv irradiation increased intracellular ROS content by 198.2% (p < 0.01) compared to the blank, but analysis of the experimental results of this effect example revealed that the intracellular ROS content pretreated with the alkaline probiotic active peptide, especially gamma-aminobutyric acid, basic amino acid, alkaline probiotic active peptide composition, was significantly lower than in the uv irradiation group. Wherein the intracellular ROS content of the group of alkaline probiotic bioactive peptide compositions is reduced by 54.7% (p < 0.01) compared with the ultraviolet irradiation group. Further analysis and experiment results show that compared with gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, alkaline amino acid composition and alkaline probiotic active peptide with the same concentration, the gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition can better improve the activity of eliminating intracellular ROS of cells under the ultraviolet irradiation condition, and the gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition has better activity of improving ultraviolet irradiation damage resistance of the cells.
Matrix metalloproteinases play a key role in the degradation of extracellular matrix, etc., and can degrade extracellular matrix with or without collagen components. Studies have shown that matrix metalloproteinases [ e.g., matrix metalloproteinase 3 (MMP-3), matrix metalloproteinase 9 (MMP-9) ] are significantly enhanced in the expression of senescent skin fibroblasts, indicating that they play an important role in the skin aging and wrinkle formation process.
Analysis of the effects the experimental results of the examples found that the activity of matrix metalloproteinases (MMP-3 and MMP-9) was increased in the UV-irradiated group compared to the placebo group (FIGS. 4c, 4 d), indicating that UV irradiation was able to damage skin fibroblasts, activate MMP-3 and MMP-9 or promote their expression or secretion. Compared with a blank control group, the activity of MMP-3 and MMP-9 in an ultraviolet irradiation group is increased by 210.4 percent (p < 0.01) and 189.4 percent (p < 0.01), but the experimental result of the experimental example of the effect is analyzed, and the activity of MMP-3 and MMP-9 in an alkaline probiotic active peptide, especially gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition group is obviously lower than that in the ultraviolet irradiation group. Wherein, compared with the ultraviolet irradiation group, the activities of gamma-aminobutyric acid, basic amino acid and basic probiotic active peptide groups MMP-3 and MMP-9 are respectively reduced by 50.1 percent (p < 0.01) and 56.1 percent (p < 0.01). Further analysis of experimental results of the embodiment of the effect shows that under the condition of the same concentration, the activities of gamma-aminobutyric acid, basic amino acid and basic probiotics active peptide composition groups MMP-3 and MMP-9 are lower than those of gamma-aminobutyric acid, resveratrol, acetyl hexapeptide-3, glutathione, basic amino acid composition and basic probiotics active peptide groups. We speculate that gamma-aminobutyric acid, basic amino acids, basic probiotic active peptides may inhibit the activity or the expression or secretion of human skin fibroblasts MMP-3 and MMP-9 by synergistic action.
Skin is one of the important organs of the human body, and is not only an important protective barrier of the human body, but also involved in the synthesis of biomolecules such as proteins, e.g., collagen. Numerous studies have shown that collagen synthesis by skin cells is reduced during skin aging. The reduction of proteins in the skin further leads to a decrease in skin elasticity, an impaired skin barrier function and further accelerates skin aging.
Analysis of the results the experimental results of this example show that the cell collagen content of the uv-irradiated group is significantly lower than that of the blank group (fig. 4e, 4 f), indicating that uv-irradiation damages skin fibroblasts, inhibiting collagen expression, secretion or promoting their decomposition. Compared with a blank control group, the content of the type I collagen and the type III collagen in the ultraviolet irradiation group is reduced by 40.2 percent (p < 0.01) and 35.6 percent (p < 0.01), but the experimental result of the experimental example of the effect is analyzed, and the content of the type I collagen and the type III collagen in the alkaline probiotic active peptide composition, especially the gamma-aminobutyric acid, the alkaline amino acid and the alkaline probiotic active peptide composition, is obviously higher than that in the ultraviolet irradiation group. Compared with the ultraviolet irradiation group, the gamma-aminobutyric acid, the basic amino acid and the basic probiotic active peptide group type I collagen and type III collagen respectively increase by 44.8 percent (p < 0.01) and 42.2 percent (p < 0.01). Further analysis of experimental results of the embodiment of the effect shows that under the condition of the same concentration, the gamma-aminobutyric acid, the basic amino acid and the basic probiotic active peptide composition are higher than the gamma-aminobutyric acid, the resveratrol, the acetyl hexapeptide-3, the glutathione, the basic amino acid composition and the basic probiotic active peptide composition in the group I collagen and the group III collagen. We speculate that gamma-aminobutyric acid, basic amino acid, basic probiotic active peptide may promote expression or secretion of human skin fibroblast type I collagen, type III collagen content or inhibit decomposition or metabolism thereof by synergistic effect. The gamma-aminobutyric acid, the basic amino acid and the basic probiotic active peptide can better promote the expression and secretion of human skin fibroblast collagen through synergistic effect, exert better antioxidant and skin aging relieving activities caused by ultraviolet irradiation, and better delay the loss of skin collagen so as to reduce the appearance of skin wrinkles.
Transforming growth factors (TGF-beta) are a broad class of multifunctional cell growth regulating active proteins that induce extracellular matrix synthesis. As found by the research, TGF-beta can increase the expression of type I procollagen in photoaged skin and exert the activity of delaying skin aging. The experimental results of this example show (FIG. 4 g) that the activity of TGF-beta 1 in the ultraviolet irradiation group is significantly reduced compared with that in the blank control group, which means that the ultraviolet irradiation damages skin fibroblasts, inhibits the expression, secretion or promotes the decomposition or inhibits the activity of TGF-beta 1. Compared with a blank control group, the activity of TGF-beta 1 in an ultraviolet irradiation group is reduced by 31.3 percent (p is less than 0.01), but the experimental result of the experimental example of the effect is analyzed to find that the activity of TGF-beta 1 in an alkaline probiotic active peptide, especially gamma-aminobutyric acid, alkaline amino acid and alkaline probiotic active peptide composition group is obviously higher than that in the ultraviolet irradiation group. Wherein, compared with the ultraviolet irradiation group, the activity of the gamma-aminobutyric acid, basic amino acid and basic probiotics active peptide group TGF-beta 1 is increased by 32.9 percent (p < 0.01). Further analysis of experimental results of the embodiment of the effect shows that under the condition of the same concentration, the activity of the TGF-beta 1 of the gamma-aminobutyric acid, the alkaline amino acid and the alkaline probiotics active peptide composition group is higher than that of the gamma-aminobutyric acid, the resveratrol, the acetyl hexapeptide-3, the glutathione, the alkaline amino acid composition and the alkaline probiotics active peptide group. We speculate that gamma-aminobutyric acid, basic amino acids, basic probiotic active peptides might increase the expression or secretion of TGF- β1 or inhibit its breakdown or increase its activity by synergistic effects.
The above examples merely represent a few embodiments of the present invention, which facilitate a specific and detailed understanding of the technical solutions of the present invention, but are not to be construed as limiting the scope of the invention. It should be noted that it will be apparent to those skilled in the art that several variations and modifications can be made without departing from the spirit of the invention, which are all within the scope of the invention. It should be understood that, based on the technical solutions provided by the present invention, those skilled in the art may obtain technical solutions through logical analysis, reasoning or limited experiments, which are all within the scope of protection of the appended claims. The scope of the patent of the invention should therefore be determined with reference to the appended claims, which are to be construed as in accordance with the doctrines of claim interpretation.
Claims (10)
1. An alkaline probiotic active peptide is characterized by having an amino acid sequence shown in SEQ ID NO. 1;
wherein, the amino acid sequence of SEQ ID NO. 1 is: ser-Glu-Phe-Gly-Met.
2. A composition comprising gamma-aminobutyric acid and a basic probiotic active peptide, characterized by comprising gamma-aminobutyric acid, and a basic amino acid and a basic probiotic active peptide;
the alkaline probiotic active peptide is the alkaline probiotic active peptide of claim 1.
3. The composition of claim 2, wherein the basic amino acid is selected from one or more of lysine, histidine or arginine.
4. The composition of claim 2, wherein the composition comprises gamma-aminobutyric acid with lysine, arginine, histidine and a basic probiotic active peptide.
5. The composition containing gamma-aminobutyric acid and alkaline probiotic active peptide according to claim 4, wherein the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1 (1-100): 1-100.
6. The composition containing gamma-aminobutyric acid and alkaline probiotic active peptide according to claim 5, wherein the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1 (1-50): 1-50;
most preferably, the mass ratio of gamma-aminobutyric acid to lysine, arginine, histidine and alkaline probiotic active peptide is 1:2.5:2.0:3.5:10.0.
7. Use of the alkaline probiotic active peptide of claim 1 or the composition containing gamma-aminobutyric acid and alkaline probiotic active peptide of any one of claims 2 to 6 for preparing a product having antioxidant and/or anti-aging effects.
8. Use of the alkaline probiotic active peptide of claim 1 or the composition containing gamma-aminobutyric acid according to any one of claims 2 to 6 for the preparation of a product having an effect of improving skin cell viability.
9. Use of the alkaline probiotic active peptide of claim 1 or the composition containing gamma-aminobutyric acid according to any one of claims 2 to 6 for preparing a product having an effect of improving cell resistance to ultraviolet injury.
10. Use of the basic probiotic active peptide of claim 1 or the composition containing gamma-aminobutyric acid and the basic probiotic active peptide of any one of claims 2 to 6 for the preparation of a product having an effect of promoting the expression and/or secretion of collagen of skin fibroblasts.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202310890118.5A CN116987142A (en) | 2023-07-19 | 2023-07-19 | Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202310890118.5A CN116987142A (en) | 2023-07-19 | 2023-07-19 | Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect |
Publications (1)
Publication Number | Publication Date |
---|---|
CN116987142A true CN116987142A (en) | 2023-11-03 |
Family
ID=88531335
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN202310890118.5A Pending CN116987142A (en) | 2023-07-19 | 2023-07-19 | Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN116987142A (en) |
-
2023
- 2023-07-19 CN CN202310890118.5A patent/CN116987142A/en active Pending
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US9089576B2 (en) | Medicament comprising a peptide extract of avocado, which is intended for the treatment and prevention of illnesses that are linked to an immune system deficiency or oxidative stress or skin ageing or dry skin | |
KR102281774B1 (en) | Composition for enhancing skin condition having skin regeneration and anti-inflammation effect | |
KR102263479B1 (en) | Cosmetic composition for anti-aging comprising heat-killed Lactobacillus plantarum or culture of the Lactobacillus plantarum | |
KR20060087817A (en) | Anti-aging cosmetic composition | |
ES2537346T3 (en) | Proteasome activating peptide hydrolysates and compositions containing them | |
KR20090017490A (en) | Cosmetic active ingredient composed of arginine ferrulate and a microalgae extract and its uses | |
WO2009128279A1 (en) | Composition for oral ingestion | |
WO2009145419A2 (en) | Composition comprising vegetable peptone for promoting stem cell proliferation | |
KR102304419B1 (en) | Multifunctional cosmetic composition that contains amino acids and peptides derived from Moringa seeds, effective for skin moisturizing, skin whitening, maintaining and improving skin elasticity, and preventing skin wrinkles | |
KR101793703B1 (en) | Composition for skin-whitening and improving skin conditions containing fermented extracts of schizandra chinensis as active ingredient | |
JP5997275B2 (en) | Method for producing 4-aminobutyric acid from algae | |
Jang et al. | Antiaging activity of peptide identified from fermented Trapa Japonica fruit extract in human dermal fibroblasts | |
KR20180136797A (en) | Skin repairing, anti-wrinkle or anti-oxidant composition comprising functional peptide, growth factor and citrus peel fermentation product | |
JP2023171950A (en) | Anti-aging agent, antioxidant, anti-inflammatory agent, and whitening agent, as well as cosmetic | |
KR20110092856A (en) | Cosmetic composition for for improving skin-wrinkle | |
CN111732634A (en) | Application of earthworm active peptide for inhibiting melanocyte proliferation in preparation of medicines or cosmetics | |
CN115044519B (en) | Lactobacillus amyloliquefaciens and application thereof | |
CN116987142A (en) | Composition containing gamma-aminobutyric acid and alkaline probiotics active peptide and application of composition in preparation of product with anti-aging effect | |
KR101552472B1 (en) | Method for producing Crassostrea gigas extract with increased antioxidant and whitening activity | |
CN115058373A (en) | Lactobacillus sake and application thereof | |
Kim et al. | Preventive effect of fermented Gelidium amansii and Cirsium japonicum extract mixture against UVB-induced skin photoaging in hairless mice | |
KR101957435B1 (en) | Method for preparing extract of fermented silkworm cocoon for improving antiwrinkle and a cosmetic composition containing the fermented extract of silkworm cocoon as an active ingredients | |
KR20190139165A (en) | Manufacturing method of fermented product of fucoidan for functional cosmetics having good whitening function and anti-wrinkling function | |
Zhao et al. | Attenuating UVA-induced oxidative stress of human skin fibroblasts by enhancing bioactive components of Armillaria luteo-virens by Lactobacillus delbrueckii subsp. Bulgaricus fermentation | |
CN114903839B (en) | Facial essence containing bifidobacterium lactis fermentation product |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PB01 | Publication | ||
PB01 | Publication | ||
SE01 | Entry into force of request for substantive examination | ||
SE01 | Entry into force of request for substantive examination |