CN1552444A - Amino acid containing human milk and superoxide dismutase composition and its preparation - Google Patents
Amino acid containing human milk and superoxide dismutase composition and its preparation Download PDFInfo
- Publication number
- CN1552444A CN1552444A CNA031289479A CN03128947A CN1552444A CN 1552444 A CN1552444 A CN 1552444A CN A031289479 A CNA031289479 A CN A031289479A CN 03128947 A CN03128947 A CN 03128947A CN 1552444 A CN1552444 A CN 1552444A
- Authority
- CN
- China
- Prior art keywords
- sod
- aminoacids complex
- breast milk
- conjugate
- preparation
- 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
- 150000001413 amino acids Chemical class 0.000 title claims abstract description 56
- 235000020256 human milk Nutrition 0.000 title claims abstract description 24
- 210000004251 human milk Anatomy 0.000 title claims abstract description 24
- 102000019197 Superoxide Dismutase Human genes 0.000 title claims description 74
- 108010012715 Superoxide dismutase Proteins 0.000 title claims description 74
- 239000000203 mixture Substances 0.000 title claims description 14
- 238000002360 preparation method Methods 0.000 title claims description 9
- 239000002131 composite material Substances 0.000 claims abstract description 6
- 235000001014 amino acid Nutrition 0.000 claims description 51
- 229940024606 amino acid Drugs 0.000 claims description 51
- 239000008187 granular material Substances 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 4
- 239000000470 constituent Substances 0.000 claims description 4
- 239000000284 extract Substances 0.000 claims description 4
- 230000001954 sterilising effect Effects 0.000 claims description 4
- 101100020212 Mus musculus Klhdc3 gene Proteins 0.000 claims description 3
- 229920002472 Starch Polymers 0.000 claims description 3
- 235000019698 starch Nutrition 0.000 claims description 3
- 239000008107 starch Substances 0.000 claims description 3
- 238000004659 sterilization and disinfection Methods 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 3
- 239000004475 Arginine Substances 0.000 claims description 2
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 claims description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 2
- 239000004471 Glycine Substances 0.000 claims description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 2
- 239000004472 Lysine Substances 0.000 claims description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 2
- 239000004473 Threonine Substances 0.000 claims description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 2
- 239000002253 acid Substances 0.000 claims description 2
- 235000004279 alanine Nutrition 0.000 claims description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 2
- 235000003704 aspartic acid Nutrition 0.000 claims description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 2
- 229960003067 cystine Drugs 0.000 claims description 2
- 235000013922 glutamic acid Nutrition 0.000 claims description 2
- 239000004220 glutamic acid Substances 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 2
- 229960000310 isoleucine Drugs 0.000 claims description 2
- 229930182817 methionine Natural products 0.000 claims description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 2
- 239000004474 valine Substances 0.000 claims description 2
- 238000001035 drying Methods 0.000 claims 2
- 239000002245 particle Substances 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 19
- 238000000034 method Methods 0.000 abstract description 8
- 230000008569 process Effects 0.000 abstract description 7
- 150000001875 compounds Chemical class 0.000 abstract description 3
- 239000001301 oxygen Substances 0.000 description 24
- 229910052760 oxygen Inorganic materials 0.000 description 24
- 150000003254 radicals Chemical class 0.000 description 18
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 17
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 230000002779 inactivation Effects 0.000 description 8
- 239000002516 radical scavenger Substances 0.000 description 8
- 210000004027 cell Anatomy 0.000 description 7
- 229940123457 Free radical scavenger Drugs 0.000 description 6
- 230000006378 damage Effects 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 description 4
- 230000032683 aging Effects 0.000 description 4
- 230000003859 lipid peroxidation Effects 0.000 description 4
- 208000002177 Cataract Diseases 0.000 description 3
- 206010014561 Emphysema Diseases 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 208000014674 injury Diseases 0.000 description 3
- 230000035987 intoxication Effects 0.000 description 3
- 231100000566 intoxication Toxicity 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 238000004321 preservation Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 3
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 3
- DWNBOPVKNPVNQG-LURJTMIESA-N (2s)-4-hydroxy-2-(propylamino)butanoic acid Chemical compound CCCN[C@H](C(O)=O)CCO DWNBOPVKNPVNQG-LURJTMIESA-N 0.000 description 2
- GVJHHUAWPYXKBD-UHFFFAOYSA-N (±)-α-Tocopherol Chemical compound OC1=C(C)C(C)=C2OC(CCCC(C)CCCC(C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-UHFFFAOYSA-N 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 102000016938 Catalase Human genes 0.000 description 2
- 108010053835 Catalase Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 108010019160 Pancreatin Proteins 0.000 description 2
- 239000002537 cosmetic Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- -1 oxygen free radical Chemical class 0.000 description 2
- 229940055695 pancreatin Drugs 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 230000009897 systematic effect Effects 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- ZZZCUOFIHGPKAK-UHFFFAOYSA-N D-erythro-ascorbic acid Natural products OCC1OC(=O)C(O)=C1O ZZZCUOFIHGPKAK-UHFFFAOYSA-N 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- WSMYVTOQOOLQHP-UHFFFAOYSA-N Malondialdehyde Chemical compound O=CCC=O WSMYVTOQOOLQHP-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 206010037423 Pulmonary oedema Diseases 0.000 description 1
- 229930003268 Vitamin C Natural products 0.000 description 1
- 229930003427 Vitamin E Natural products 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 208000038016 acute inflammation Diseases 0.000 description 1
- 230000006022 acute inflammation Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000003712 anti-aging effect Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000012459 cleaning agent Substances 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000002198 cosolvency Effects 0.000 description 1
- 210000000695 crystalline len Anatomy 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001066 destructive effect Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000005611 electricity Effects 0.000 description 1
- 230000008519 endogenous mechanism Effects 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 230000007760 free radical scavenging Effects 0.000 description 1
- WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 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 1
- 235000003969 glutathione Nutrition 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 238000005469 granulation Methods 0.000 description 1
- 230000003179 granulation Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 210000003463 organelle Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 231100000915 pathological change Toxicity 0.000 description 1
- 230000036285 pathological change Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000005502 peroxidation Methods 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 231100000572 poisoning Toxicity 0.000 description 1
- 230000000607 poisoning effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 208000005333 pulmonary edema Diseases 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000010926 purge Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 201000008525 senile cataract Diseases 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000009747 swallowing Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 235000019154 vitamin C Nutrition 0.000 description 1
- 239000011718 vitamin C Substances 0.000 description 1
- 235000019165 vitamin E Nutrition 0.000 description 1
- 229940046009 vitamin E Drugs 0.000 description 1
- 239000011709 vitamin E Substances 0.000 description 1
Images
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
A compound containing breast milk type amino acid and SOD is disclosed. Its preparing process features use of composite amino acid as carrier to increase the stability and activity of SOD.
Description
Technical field
The present invention relates to the scavenger of superoxide radical and active oxygen, refer to that more specifically a kind of application aminoacids complex makes carrier, make superoxide dismutase (SOD) be difficult for inactivation, play SOD and remove superoxide radical and the effect of active oxygen and its production technology.
Background technology
Superoxide dismutase (SOD) is can remove ultra-oxygen anion free radical and the important antioxidase of a protection cytosis.Owing to physiological and pathologic reason, constantly produce free radical in the human body, in vivo in the free radical, oxygen-derived free radicals has accounted for significant proportion, it comprises ultra-oxygen anion free radical, hydroxy radical, hydrogen peroxide, single linear oxygen, and they are very active, destructive very big material.Free radical scavenger can be divided into two big classes: a class is micromolecular free radical scavenger, comprising antioxidant such as vitamin E, vitamin C; Another kind of is macromolecular free radical scavenger, and it is the interior natural free radical of body and the scavenger of active oxygen that several enzymes are arranged.Intravital formation of normal health and removing are in a kind of dynamic equilibrium, in case this dynamic equilibrium is destroyed, promptly free radical accumulates too much or very few in body, and then body will be ill or old and feeble.SOD is just listed in the object of emphasis systematic study as the generally acknowledged important free radical scavenger of international academic community by developed country as far back as the seventies.The preparation technologies of the effect of SOD and effect, SOD etc. are used for the product of medicine, food, cosmetics greatly gradually as additive about the nineties.The use that China also begins to enter product in middle nineteen nineties in last century, for example: " big precious SOD cosmetics ", " SOD medicated beer ", " SOD cleaning agent for mouth cavity " etc.Simultaneously, as removing the ultra-oxygen anion free radical scavenger, SOD has obtained to use widely clinically.
The caused disease of ultra-oxygen anion free radical, be mainly following these:
A, hyperbaric oxygen and oxygen intoxication.Three types of oxygen intoxication: i.e. pulmonary oxygen toxicity shows as pulmonary edema; The nerve oxygen intoxication shows as the brain electricity and changes; Ophthalmoretinal type of oxygen poisoning, it is impaired to show as retina.
B, phagocytosis and acute inflammation and edema.Reactive oxygen free radical plays main effect in the body inflammation, and superfluous free radical destroys normal cell as can not then being goed deep into cell by the timely decomposition of SOD.
C, autoimmune disease.The characteristics though the pathogenesis of various dissimilar autoimmune diseasees is had nothing in common with each other, oxygen-derived free radicals, prostate are derivative products and have hydrolase that the macrophage monocyte produces all to play an important role causing on the pathological changes usually.
D, emphysema.Contain elastoser and inhibitor thereof in the lung tissue, their imbalance is that emphysema become sick main cause.The vigor of inhibitor can be subjected to the attack of superoxide radical and inactivation, thereby causes elastoser to increase, and the emphysema probability is increased.
E, senile cataract.Crystalline lens is subjected to the oxidation of oxygen-derived free radicals alive and damages, and is the main cause of all types of cataract morbidities, and what reactive oxygen free radical accumulated within the eye when the people was old and feeble increases, and easily causes ophthalmic enzyme and memebrane protein and lenticular lipid peroxidation.The lipid peroxidation product malonaldehyde easily and crystalline protein be cross-linked to form cataract.
Radical pair injury of human effect when F, aging.To enrich manyly at human body unsaturated fatty acids acid ratio satisfied fatty acid.They mainly are distributed on the biomembrane.The characteristics of unsaturated fatty acid are that peroxidation takes place when radical initiator and oxygen exist.During body aging, because the imbalance of free radical causes the peroxidating of unsaturated fatty acid on the biomembrane in the body, membrane structure is changed, it is aging that body becomes, and causes that simultaneously lipofuscin produces.
The carcinogenesis of G, oxygen-derived free radicals.Produce from cancer, normal cell becomes cancerous cell must promptly be brought out and promotion through two stages.But bringing out stage active oxygen coup injury DNA, also can pass through lipid peroxidation enzyme indirect injury DNA.
As removing ultra-oxygen anion free radical scavenger SOD, not only very extensive in the clinical practice of above-mentioned disease.Simultaneously also has the excellent prevention effect as a kind of effective antiaging agent.
But SOD is a kind of organized enzyme, the half-life extremely weak point only be 6 minutes, and easy inactivation when running into high temperature and sour environment enters human body and is easily decomposed by gastric enzyme, pancreatin again after swallowing, this just is difficult to reach the ideal effect of absorption of human body.And the feature of simultaneously easy inactivation also makes it be difficult in medium-term and long-term its activity that keeps of ultimate product.Therefore, how to make SOD long period non-inactivation at normal temperatures? how does processing SOD guarantee by folk prescription to synthesizing and non-inactivation in many ways during product? how about its product guarantees when entering human body is not repelled, decomposes by pancreatin, keep being absorbed by the body? be Three Difficult Issues in SOD developmental research and the implementation process.Because the inconvenience of preserving and using, make developed country at the beginning of 21 century when the function preparation of systematic study SOD and using, setting about studying the SOD modified derivative of long half time.
Summary of the invention
The objective of the invention is to utilize the aminoacid that contains the breast milk type to make carrier, make SOD be combined into the conjugate that contains breast milk type aminoacid and SOD with it, this conjugate overcomes the unstability of SOD, make it producing, keeping its effective active when using, reach the purpose of removing superoxide radical and active oxygen effect in vivo.Be combined into simultaneously the activity of its SOD of assurance in the process of producing product of conjugate to several amino acids and SOD, the effect of SOD in human body really brought into play at folk prescription aminoacid.
Another object of the present invention provides the method that preparation contains breast milk type aminoacid and superoxide dismutase conjugated substance.
The present invention implements like this: design has the coexisting body of the aminoacids complex of breast milk structure component as SOD.
It is as follows to contain breast milk type aminoacid constituent structure: (* is the necessary aminoacid of human body)
| Title | Contain breast milk type aminoacid composition weight percent content % | Aminoacid composition weight percent content % of the present invention |
| Isoleucine * | ????5.12 | ????4.5 |
| Leucine * | ????11.02 | ????11-12 |
| Lysine * | ????6.89 | ????4-7 |
| Methionine * | ????1.67 | ????1.5-6.5 |
| Phenylalanine * | ????3.54 | ????1.5-4 |
| Valine * | ????5.61 | ????4-5 |
| Threonine * | ????4.43 | ????4-5 |
| Tryptophan * | ????1.67 | ????1.5-2 |
| Arginine | ????3.74 | ????3-4 |
| Cystine | ????2.07 | ????1.5-2.5 |
| Histidine | ????2.85 | ????2.5-3.5 |
| Alanine | ????3.84 | ????3.5-5 |
| Aspartic acid | ????8.76 | ????8-9.5 |
| Glutamic acid | ????18.60 | ????17-19 |
| Glycine | ????2.26 | ????2.5-4.5 |
| Proline | ????9.55 | ????8-10 |
| Serine | ????4.53 | ????4-5 |
| Tyrosine | ????3.84 | ????3.5-4 |
Aminoacids complex warp of the present invention is done a large amount of test contrasts with the SOD compatibility that general unisexuality amino acid structure is made carrier, finds the compossibility between the two, and promptly the level of activity of SOD has more obvious and bigger difference.The aminoacids complex of breast milk structure shape and cosolvency, the compossibility of SOD are much better than the structure carrier that adopts multiple unisexuality aminoacid compatibility.Adopt its active preservation of different types of unisexuality aminoacid composite structure and SOD compatibility all to fail to satisfy the product that is made generally in shelf life of products (18 months~24 months) requirement of guaranteeing the quality.The present invention is from continuous structure prescription contrast test, and the human milk structure carrier of the present invention's design is optimized the most.
The preparation method that the present invention contains breast milk type aminoacid and superoxide dismutase conjugated substance is as follows:
1, from the peas protein hydrolyzed solution, extracts aminoacids complex, measure more than 10 kind of free amino acid and become;
2, composite corresponding unisexuality aminoacid in the free amino acid by breast milk type amino acid structure composition (seeing constituent structure proportioning table);
3, mix the back composite back amino-acid powder constituent structure mensuration in addition;
4, will buy next extraction active SOD solution water-soluble (30 ℃) from animals and plants;
5, SOD adds that appropriate amount of starch mixes after doubly loosing;
6, under 0 ℃ of low temperature, make SOD form the unisexuality granule;
7, mix at compound propylhomoserin, dry and carry out in the granulation process temperature adjusting in 25 ℃ ± 5 ℃ adding SOD granule.
8, through sterilization tabletting (temperature is controlled at 50 ℃~60 ℃), make the aminoacids complex sheet that can keep the SOD activated state.
9, making product (18~24 months) in the shelf-life by above-mentioned flow process can make the SOD inactivation rate be controlled at below 5%.
Breast milk type aminoacid of the present invention enters intravital effect of people and influence to SOD.We have done the experiment of this project with white mice.Every group of 10 white mice raised 30 days, and the result is as showing:
| The matched group enzyme is lived | The experimental group enzyme is lived | Rate of increase | |
| First group | ??466.0+72.4 | ??670.7+52.2 | ????18.3 |
| Second group | ??460.0+55.1 | ??560.9+55.1 | ????21.3 |
| The 3rd group | ??452.8+80.9 | ??671.0+84.6 | ????20.7 |
Aerobe object internal memory the endogenous mechanism of free-radical generating, and a large amount of free-radical generating is all arranged every day.Also exist the purge mechanism of free radical simultaneously in the organism; removing task by free radical in the free radical scavenging system burden body of superoxide dismutase (SOD) catalase (CAT) and glutathion peroxidase (GSHPX) etc.; it is very low-level that interior free yl is remained on; wherein SOD plays an important role to the removing of O2 in the body; because free radical is very active, thereby body there is strong destruction.
A, free radical cause that connective tissue is macromolecular crosslinked, thereby hinder the diffusion and the damaged tissue vigor of nutrient substance.
B, radical pair DNA destroy, and can cause causing cell mutation, cause the expression of main enzyme in the body to produce defective, thereby cause body aging, death.
The film lipid peroxidation that C, free radical cause causes the integrity forfeiture of subcellular organelle and the accumulation of cell endoperoxides lipoprotein chip, and the latter understands the function of damaging cells.
Therefore the body inner enzyme vigor improves and can represent fully that the action and efficacy that enters into active SOD in the human body brings into normal play, and effect obviously.The SOD vigor that also can find out experimental group from above-mentioned table is obviously than matched group height.
The realization of the technology of the present invention: technology is with breast milk shape aminoacids complex and SOD compatibility, realizes the active long preservation of SOD.The compatibility generation that proves these two simultaneously significantly adds and potentiation.
The invention effect: breast milk shape aminoacids complex as SOD carrier situation under, the survival period of SOD and active conservation rate have all obtained sufficient assurance.
Description of drawings
Fig. 1 is a process chart of the present invention.
The specific embodiment
The present invention adopts and extract compound propylhomoserin from the peas protein hydrolyzed solution, extracting aminoacid in this hydrolyzed solution can buy from aminoacids complex manufacturing enterprise (the biochemical food factory in Huarong County, Hunan), measure its aminoacid composition and content amino acid analysis (conventional method mensuration), stand-by according to the amino-acid powder of the percentage by weight that contains the composite corresponding aminoacid composition of breast milk type aminoacid composition aminoacid composition of the present invention then.To from the animals and plants that SOD manufacturing enterprise (Bao'an, Shanghai biological product company limited) purchase comes, extract active SOD solution water-soluble (or in distilled water) temperature again and be controlled at room temperature, add the appropriate amount of starch mixing that stirs after the limit is stirred SOD doubly loose, it is stand-by to make SOD form monogenetic granule under 0 ℃ of low temperature.
Above-mentioned stand-by aminoacids complex dried carry out pelletize, this process temperature is controlled in 25 ℃ ± 5 ℃ usually, adds the SOD granule that makes then, and it is mixed to stir, again with mixture at 50 ℃ ± 60 ℃ sterilization tablettings, make the aminoacids complex sheet that can keep the SOD activated state.
The aminoacids complex sheet that can keep the SOD activated state of gained of the present invention is done the activity coexistence time test (seeing the following form) of SOD:
| The active coexistence time | Activity underspeeds | |||
| Project name | Multiple unisexuality aminoacid and SOD compatibility | 8~10 months | 3 months | ↓30% |
| 6 months | ↓70% | |||
| 10 months | ↓90% | |||
| 16 months | ↓97% | |||
| Project name | Breast milk structure aminoacid and SOD compatibility | More than 20 months | 3 months | ↓1.5% |
| 6 months | ↓2.8% | |||
| 10 months | ↓4.4% | |||
| 16 months | ↓5.7% | |||
Summary of the present invention: the present invention proposes with a kind of aminoacids complex of breast milk type structure as carrier solving short, the easy weakness of inactivation of SOD half-life, thereby reaches SOD active purpose of long preservation under the room temperature normality.Because above-mentioned structure and the SOD of design has very strong compossibility, mutual capacitive and also having adds and potentiation, so the activity maintenance phase of SOD reached more than 20 months.
Claims (5)
1, a kind of by monamino acid and Superoxide Dismutase (SOD) conjugate, it is characterized in that being combined into and containing breast milk type aminoacids complex superoxide dismutase conjugated substance by containing breast milk type aminoacids complex and superoxide dismutase thing.
2, conjugate according to claim 1, the prescription that it is characterized in that containing breast milk type aminoacids complex is as follows:
Title Aminoacid composition weight percent content % of the present invention
Isoleucine * ??4.5
Leucine * ??11-12
Lysine * ??4-7
Methionine * ??1.5-6.5
Phenylalanine * ??1.5-4
Valine * ??4-5
Threonine * ??4-5
Tryptophan * ??1.5-2
Arginine ??3-4
Cystine ??1.5-2.5
Histidine ??2.5-3.5
Alanine ??3.5-5
Aspartic acid ??8-9.5
Glutamic acid ??17-19
Glycine ??2.5-4.5
Proline ??8-10
Serine ??4-5
Tyrosine ??3.5-4
3, the preparation method of conjugate according to claim 1 is characterized in that comprising:
(1) extracts free amino acid from natural peas protein hydrolyzed solution;
(2) become it to satisfy the proportional quantity of aminoacids complex by containing the composite corresponding unisexuality aminoacid of breast milk type aminoacids complex constituent structure;
(3) add that appropriate amount of starch is mixed after soluble in water times of SOD is loose and, under proper temperature, make SOD form the unisexuality granule;
(4) will mix aminoacids complex, drying to select adds the SOD granule under the uniform temperature, stir mixed;
(5) above-mentioned mixture sterilization tabletting is made and is contained breast milk type aminoacids complex, SOD conjugate.
4,, it is characterized in that the aminoacids complex pelletize of drying is added the SOD particle temperature and regulates and control 20 ℃~30 ℃ according to the preparation method of the described conjugate of claim 3.
5, according to the preparation method of the described conjugate of claim 3, the tabletting humidity that it is characterized in that sterilizing is controlled at 50 ℃~60 ℃.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNA031289479A CN1552444A (en) | 2003-05-30 | 2003-05-30 | Amino acid containing human milk and superoxide dismutase composition and its preparation |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNA031289479A CN1552444A (en) | 2003-05-30 | 2003-05-30 | Amino acid containing human milk and superoxide dismutase composition and its preparation |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN1552444A true CN1552444A (en) | 2004-12-08 |
Family
ID=34322312
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNA031289479A Pending CN1552444A (en) | 2003-05-30 | 2003-05-30 | Amino acid containing human milk and superoxide dismutase composition and its preparation |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1552444A (en) |
-
2003
- 2003-05-30 CN CNA031289479A patent/CN1552444A/en active Pending
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2571924C2 (en) | Method and substance for site-activated complex-formation of biological molecules | |
| CA1052307A (en) | Method for the extraction and processing of glycoproteins, mucopolysaccharides and accompanying substances | |
| EP0261016B1 (en) | Lipase and lipasic extracts, process of preparation and therapeutic use | |
| FR2489145A1 (en) | PHARMACEUTICAL COMPOSITIONS ACCELERATING THE HEALING OF INJURIES | |
| TWI550063B (en) | Antioxidant composition | |
| RU2233320C2 (en) | Method for preparing biologically active preparation, biologically active nutrient supplement with prebiotic effect resulting to correction (leveling) of metabolic syndrome and medicinal preparation for regulation of digestive tract microbiocenosis | |
| CN113005040B (en) | Bifidobacterium lactis freeze-drying protective agent and application method thereof | |
| Yaghoubzadeh et al. | Extraction of bioactive peptides from Chlorella vulgaris using enzymatic hydrolysis: A green natural antioxidant | |
| CN100512808C (en) | Externally applied compound amino acid prepn for promoting wound healing and its preparation process and application thereof | |
| CN109662322A (en) | A kind of composition and preparation method thereof of protecting liver and heart blood vessel | |
| CN1302783C (en) | Oral taking preparation for aesthetic health care and preparation method | |
| JPH06502154A (en) | antimicrobial composition | |
| CN103262939A (en) | Preparation method of antioxidant activity mixed peptide originated from chick embryo | |
| CN1552444A (en) | Amino acid containing human milk and superoxide dismutase composition and its preparation | |
| JP2011116761A (en) | Antioxidative peptide derived from royal jelly | |
| US20150202311A1 (en) | Collagen-peptide complex | |
| CN117898964A (en) | Natural antiseptic cosmetic and preparation method thereof | |
| FR2720067A1 (en) | Hydrolyzate of marine animal proteins, process for obtaining it and applications. | |
| RU2552444C1 (en) | Product composition with biologically active properties | |
| RU2802015C1 (en) | Method of obtaining a tissue preparation with hepatoprotective properties and an agent based on it | |
| EP4347537B1 (en) | Method for producing an aqueous solution containing amino acids from fish soluble matter, aqueous solution and associated fertilising products | |
| JPH02279700A (en) | Highly tryptophan-containing peptide | |
| Prabhavathi et al. | Microbial degradation of chicken feathers to convert waste into value added biopolymer | |
| JP2006056904A (en) | Biological collagen synthesis promoter | |
| FR2690343A1 (en) | Compsn. with anti-radical and anti-lipo-peroxidising effect contg. polar lipid - for use in cosmetics, dietetics, food industry and pharmacology |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C02 | Deemed withdrawal of patent application after publication (patent law 2001) | ||
| WD01 | Invention patent application deemed withdrawn after publication |