CN109265536A - A kind of calcium chelating peptide and its preparation method and application - Google Patents
A kind of calcium chelating peptide and its preparation method and application Download PDFInfo
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- CN109265536A CN109265536A CN201811020236.6A CN201811020236A CN109265536A CN 109265536 A CN109265536 A CN 109265536A CN 201811020236 A CN201811020236 A CN 201811020236A CN 109265536 A CN109265536 A CN 109265536A
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- Prior art keywords
- calcium
- preparation
- chelating peptide
- calcium chelating
- tilapia
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Links
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 title claims abstract description 71
- 239000011575 calcium Substances 0.000 title claims abstract description 71
- 229910052791 calcium Inorganic materials 0.000 title claims abstract description 71
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 51
- 238000002360 preparation method Methods 0.000 title claims abstract description 22
- 210000000988 bone and bone Anatomy 0.000 claims abstract description 28
- 241000276707 Tilapia Species 0.000 claims abstract description 24
- 102000008186 Collagen Human genes 0.000 claims abstract description 18
- 108010035532 Collagen Proteins 0.000 claims abstract description 18
- 229920001436 collagen Polymers 0.000 claims abstract description 16
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 5
- 230000009919 sequestration Effects 0.000 claims abstract description 5
- 230000007071 enzymatic hydrolysis Effects 0.000 claims description 19
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 19
- 238000004140 cleaning Methods 0.000 claims description 13
- 238000000034 method Methods 0.000 claims description 13
- 241000276701 Oreochromis mossambicus Species 0.000 claims description 10
- 238000012545 processing Methods 0.000 claims description 10
- 239000002253 acid Substances 0.000 claims description 9
- 238000005238 degreasing Methods 0.000 claims description 9
- 235000013372 meat Nutrition 0.000 claims description 8
- 239000003513 alkali Substances 0.000 claims description 7
- 238000001514 detection method Methods 0.000 claims description 7
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 7
- 239000004365 Protease Substances 0.000 claims description 6
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 claims description 5
- 102000004190 Enzymes Human genes 0.000 claims description 5
- 108090000790 Enzymes Proteins 0.000 claims description 5
- 108090000526 Papain Proteins 0.000 claims description 5
- 229940088598 enzyme Drugs 0.000 claims description 5
- 235000019834 papain Nutrition 0.000 claims description 5
- 229940055729 papain Drugs 0.000 claims description 5
- 108090000145 Bacillolysin Proteins 0.000 claims description 4
- 102000035092 Neutral proteases Human genes 0.000 claims description 4
- 108091005507 Neutral proteases Proteins 0.000 claims description 4
- 238000010828 elution Methods 0.000 claims description 4
- 239000006228 supernatant Substances 0.000 claims description 4
- 230000009849 deactivation Effects 0.000 claims description 3
- 238000004108 freeze drying Methods 0.000 claims description 3
- 235000020510 functional beverage Nutrition 0.000 claims description 3
- 238000004007 reversed phase HPLC Methods 0.000 claims description 3
- 241000251468 Actinopterygii Species 0.000 claims description 2
- 238000002224 dissection Methods 0.000 claims description 2
- 238000003756 stirring Methods 0.000 claims description 2
- 238000000825 ultraviolet detection Methods 0.000 claims description 2
- 239000000243 solution Substances 0.000 claims 2
- 241000219112 Cucumis Species 0.000 claims 1
- 235000015510 Cucumis melo subsp melo Nutrition 0.000 claims 1
- 108091005804 Peptidases Proteins 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- FJJCIZWZNKZHII-UHFFFAOYSA-N [4,6-bis(cyanoamino)-1,3,5-triazin-2-yl]cyanamide Chemical compound N#CNC1=NC(NC#N)=NC(NC#N)=N1 FJJCIZWZNKZHII-UHFFFAOYSA-N 0.000 claims 1
- 239000012670 alkaline solution Substances 0.000 claims 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 claims 1
- 235000019419 proteases Nutrition 0.000 claims 1
- 239000002023 wood Substances 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 13
- 238000010521 absorption reaction Methods 0.000 abstract description 7
- 239000000047 product Substances 0.000 abstract description 7
- 229940069978 calcium supplement Drugs 0.000 abstract description 6
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 6
- 239000002994 raw material Substances 0.000 abstract description 5
- 238000009509 drug development Methods 0.000 abstract description 3
- 231100000252 nontoxic Toxicity 0.000 abstract description 3
- 230000003000 nontoxic effect Effects 0.000 abstract description 3
- 239000000126 substance Substances 0.000 abstract description 3
- 230000014759 maintenance of location Effects 0.000 description 8
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 4
- 229910001424 calcium ion Inorganic materials 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 3
- 229910000831 Steel Inorganic materials 0.000 description 3
- 235000005911 diet Nutrition 0.000 description 3
- 230000000378 dietary effect Effects 0.000 description 3
- 238000002953 preparative HPLC Methods 0.000 description 3
- 239000010959 steel Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- CPBJMKMKNCRKQB-UHFFFAOYSA-N 3,3-bis(4-hydroxy-3-methylphenyl)-2-benzofuran-1-one Chemical compound C1=C(O)C(C)=CC(C2(C3=CC=CC=C3C(=O)O2)C=2C=C(C)C(O)=CC=2)=C1 CPBJMKMKNCRKQB-UHFFFAOYSA-N 0.000 description 2
- 102000005701 Calcium-Binding Proteins Human genes 0.000 description 2
- 108010045403 Calcium-Binding Proteins Proteins 0.000 description 2
- 241000040710 Chela Species 0.000 description 2
- IMQLKJBTEOYOSI-GPIVLXJGSA-N Inositol-hexakisphosphate Chemical compound OP(O)(=O)O[C@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O IMQLKJBTEOYOSI-GPIVLXJGSA-N 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- IMQLKJBTEOYOSI-UHFFFAOYSA-N Phytic acid Natural products OP(O)(=O)OC1C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1OP(O)(O)=O IMQLKJBTEOYOSI-UHFFFAOYSA-N 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 239000003518 caustics Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 235000006408 oxalic acid Nutrition 0.000 description 2
- 235000002949 phytic acid Nutrition 0.000 description 2
- 239000000467 phytic acid Substances 0.000 description 2
- 229940068041 phytic acid Drugs 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
- 238000011160 research Methods 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- TUSDEZXZIZRFGC-UHFFFAOYSA-N 1-O-galloyl-3,6-(R)-HHDP-beta-D-glucose Natural products OC1C(O2)COC(=O)C3=CC(O)=C(O)C(O)=C3C3=C(O)C(O)=C(O)C=C3C(=O)OC1C(O)C2OC(=O)C1=CC(O)=C(O)C(O)=C1 TUSDEZXZIZRFGC-UHFFFAOYSA-N 0.000 description 1
- XXMFJKNOJSDQBM-UHFFFAOYSA-N 2,2,2-trifluoroacetic acid;hydrate Chemical compound [OH3+].[O-]C(=O)C(F)(F)F XXMFJKNOJSDQBM-UHFFFAOYSA-N 0.000 description 1
- 206010070817 Bone decalcification Diseases 0.000 description 1
- 230000010736 Chelating Activity Effects 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 239000001263 FEMA 3042 Substances 0.000 description 1
- CAVKXZMMDNOZJU-UHFFFAOYSA-N Gly-Pro-Ala-Gly-Pro Natural products C1CCC(C(O)=O)N1C(=O)CNC(=O)C(C)NC(=O)C1CCCN1C(=O)CN CAVKXZMMDNOZJU-UHFFFAOYSA-N 0.000 description 1
- ZZJVYSAQQMDIRD-UWVGGRQHSA-N Gly-Pro-His Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O ZZJVYSAQQMDIRD-UWVGGRQHSA-N 0.000 description 1
- BMWFDYIYBAFROD-WPRPVWTQSA-N Gly-Pro-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)CN BMWFDYIYBAFROD-WPRPVWTQSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- LRBQNJMCXXYXIU-PPKXGCFTSA-N Penta-digallate-beta-D-glucose Natural products OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-PPKXGCFTSA-N 0.000 description 1
- 108010001441 Phosphopeptides Proteins 0.000 description 1
- 244000300264 Spinacia oleracea Species 0.000 description 1
- 235000009337 Spinacia oleracea Nutrition 0.000 description 1
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 description 1
- 244000269722 Thea sinensis Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 230000003913 calcium metabolism Effects 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000009514 concussion Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 235000018823 dietary intake Nutrition 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 108010036413 histidylglycine Proteins 0.000 description 1
- 238000003859 hyphenated technique Methods 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 239000008274 jelly Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000005191 phase separation Methods 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000012797 qualification Methods 0.000 description 1
- 238000002390 rotary evaporation Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 239000012453 solvate Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 229920002258 tannic acid Polymers 0.000 description 1
- LRBQNJMCXXYXIU-NRMVVENXSA-N tannic acid Chemical compound OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-NRMVVENXSA-N 0.000 description 1
- 229940033123 tannic acid Drugs 0.000 description 1
- 235000015523 tannic acid Nutrition 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- 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
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/52—Adding ingredients
-
- 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
- A23L33/16—Inorganic salts, minerals or trace elements
- A23L33/165—Complexes or chelates
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- 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
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
- Mycology (AREA)
- Genetics & Genomics (AREA)
- Inorganic Chemistry (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
The present invention relates to a kind of calcium chelating peptides and its preparation method and application.The amino acid sequence of the calcium chelating peptide: GPAGPHGPVG.Calcium chelating peptide provided by the invention is safe and non-toxic, has preferably physical and chemical activity compared with traditional calcium supplement, and calcium sequestration capacity is up to 43.018 mg/g；Can while improving calcium absorption in human body and bioavailability, can also replenishing collagen peptide, can be used as the raw material of drug development and biological calcium supplement.Preparation method provided by the invention successfully obtains the calcium chelating peptide, can make full use of fishery -ies product resource, easy to operate, provides new way for the higher value application of Tilapia bone.
Description
Technical field
The invention belongs to functional health-care food preparation technical fields, and in particular to a kind of calcium chelating peptide and preparation method thereof
And application.
Background technique
Calcium constituent is the main component of bone mineral, and human body mainly obtains calcium by dietary intake, it has been investigated that, by
Calcium metabolism caused by calcium insufficiency of intake is unbalance, is the inducement for a variety of diseases that mankind each age group crowd is occurred.Currently, calcium is sought
Feeding deficiency has become global nutrition phenomenon, and adult daily recommendation calcium intake is generally 1000 mg/d, however due to
China's dietary structure problem, the intake of people's dietary calcium is more low, and the requirement of daily recommended intake is much not achieved.According to
Report, some dietary factors may will affect the absorption of calcium, in the phytic acid in parchment covering and seed, the oxalic acid and tea in spinach
Tannic acid can reduce the absorption of calcium.Oxalic acid is believed to the insoluble salt by forming calcium to interfere the absorption of calcium.Phytic acid is flesh
Six phosphate of alcohol make them be difficult to be absorbed and utilized in conjunction with calcium and iron.
Calcium chelating peptide can form soluble complexes, high stability with calcium ion, and calcium ion can be made with chela
Solvate form is absorbed and utilized by small intestine, improves its bioavailability, while being also beneficial to the release of calcium ion, is mended as biology
The good selection of calcium agent.More and more domestic and international researchers are separated from animal, plant, marine products protein resource at present has calcium
The peptide of ion chelating activity: soybean peptide, pale blue peptide, casein phosphopeptide etc..Research has shown that Hydrolyzed Collagen peptide is to bone
Arthritis and osteoporosis have potential therapeutic effect.China's marine resources are abundant, and Rofe fish culture and process scale occupy generation
Boundary is the first, and due to the industrial structure, generated leftover bits and pieces Tilapia mossambica skeleton is not utilized effectively in process,
It results in waste of resources.
Therefore, how there is the Tilapia bone collagen protein source calcium chelating peptide of high calcium sequestering activity, Yi Jishi using acquisition
It is the research direction for preparing calcium constituent replenishers and needing now to the higher value application of Tilapia bone.
Summary of the invention
It is an object of the invention to overcome the defect and deficiency that Tilapia mossambica skeleton is not utilized effectively in the prior art, mention
For a kind of calcium chelating peptide.Calcium chelating peptide provided by the invention has preferable calcium sequestering activity, and calcium sequestration capacity reaches
43.018mg/g。
Another object of the present invention is to provide the preparation methods of above-mentioned calcium chelating peptide.
Another object of the present invention is to provide above-mentioned calcium chelating peptides to prepare answering in calcium-supplementing preparation or functional beverage
With.
For achieving the above object, the present invention adopts the following technical scheme:
A kind of calcium chelating peptide, the amino acid sequence of the calcium chelating peptide: GPAGPHGPVG(Gly-Pro-Asp-Gly-Pro-His-
Gly-Pro-Val-Gly).
Calcium chelating peptide provided by the invention is safe and non-toxic, has preferably physical and chemical activity, calcium compared with traditional calcium supplement
Sequestering power is up to 43.018 mg/g；Collagen can also be supplemented while the absorption of raising calcium in human body and bioavailability
Protein peptides can be used as the raw material of drug development and biological calcium supplement.
Preferably, the molecular weight of the calcium chelating peptide is 844.4340 Da；The calcium sequestration capacity of the calcium chelating peptide is
43.018 mg/g。
The preparation method of above-mentioned calcium chelating peptide, includes the following steps:
S1: Tilapia mossambica skeleton is carried out to digest de- meat, alkali cleaning degreasing obtains Tilapia bone collagen egg after decalcification processing and acid processing
It is white；
S2: after the enzymatic hydrolysis of Tilapia bone collagen obtained by S1, enzyme deactivation, the freeze-drying of centrifuging and taking supernatant；
S3: it after being isolated and purified step by step using preparative reversed-phase high performance liquid chromatography progress multistage, is obtained using RT-HPLC purifying
The calcium chelating peptide.
The present invention be using calcium sequestering activity as evaluation index, it is efficient using preparative reversed-phase high performance liquid chromatography and analytic type
Liquid chromatogram isolates and purifies Tilapia bone collagen enzymatic hydrolysis product to arrive the calcium chela of Tilapia bone collagen protein source
Close peptide.
Preparation method provided by the invention successfully obtains the calcium chelating peptide, can make full use of fishery -ies product resource, easy to operate,
New way is provided for the higher value application of Tilapia bone.
Preferably, the process of the de- meat of enzymatic hydrolysis described in S1 are as follows: by Tilapia mossambica skeleton dissection, after neutral protease enzymolysis,
Remove the meat mincing on Tilapia mossambica skeleton.
Preferably, Tilapia mossambica skeleton is cut into the section shape of 4 ~ 7cm in S1；The time of the neutral protease enzymolysis be 1 ~
3h, temperature are 45 ~ 60 DEG C, and pH is 7 ~ 8.
It is further preferable that the time of the neutral protease enzymolysis is 2h, temperature is 55 DEG C, pH 7.5.
Preferably, the process of alkali cleaning degreasing described in S1 are as follows: utilize inorganic caustic solutions cleaning and degreasing, then clean into
Property.
It is further preferable that the inorganic caustic solutions are sodium hydroxide solution.
Preferably, the process of the processing of decalcification described in S1 are as follows: Tilapia bone after alkali cleaning degreasing is placed in EDTA-2Na solution
In, it freezes, stirring, cleaning to neutrality.
It is further preferable that the pH of the EDTA-2Na solution is 7.2, the quality of the Tilapia bone and EDTA-2Na solution
Volume ratio is 1:10.
Preferably, the process of the processing of acid described in S1 are as follows: the fish-bone after decalcification is washed to neutrality after being handled with acid solution,
Obtain Tilapia bone collagen.
It is further preferable that the hydrochloric acid solution that the acid solution is 4%；The time of the acid processing is 18h.
Preferably, papain is selected to be digested in S2；Mass fraction of the papain in enzymatic hydrolysis system
It is 0.3 ~ 1%；The time of the enzymatic hydrolysis is 3 ~ 6h；The temperature of the enzymatic hydrolysis is 40 ~ 60 DEG C；The pH of the enzymatic hydrolysis is 6 ~ 7.
It is further preferable that the papain is 1% in the mass fraction of enzymatic hydrolysis system；The time of the enzymatic hydrolysis is 5h；
The temperature of the enzymatic hydrolysis is 60 DEG C；The pH of the enzymatic hydrolysis is 7.0.
Preferably, the condition of RT-HPLC described in S3 are as follows: sample volume 20mL；Chromatographic column is C18 chromatographic column；Mobile phase
For the TFA containing 0.1wt%；Elution speed is 1.0 mL/min；Ultraviolet detection wavelength is double Detection wavelengths: 214 nm, 280
nm。
Above-mentioned calcium chelating peptide is to prepare the application in calcium-supplementing preparation or functional beverage also within the scope of the present invention.
Compared with prior art, the invention has the following beneficial effects:
Calcium chelating peptide provided by the invention is safe and non-toxic, has preferably physical and chemical activity, calcium chelating compared with traditional calcium supplement
Ability is up to 43.018 mg/g；Can be while the absorption of raising calcium in human body and bioavailability, it can also replenishing collagen
Peptide can be used as the raw material of drug development and biological calcium supplement.Preparation method provided by the invention successfully obtains the calcium chelating peptide,
Fishery -ies product resource can be made full use of, it is easy to operate, new way is provided for the higher value application of Tilapia bone.
Detailed description of the invention
Fig. 1 is the smashed Tilapia bone collagen of decalcification；
Fig. 2 be preparative high performance liquid chromatography for the first time isolate and purify (C1 crest segment be 11 ~ 12.5 min, C2 crest segment be 12.5 ~
16 min, C3 crest segment are 17 ~ 20 min, and C4 crest segment is 21 ~ 22 min, and C5 crest segment is 22 ~ 30 min, and C6 crest segment is 20 ~ 38
Min, C7 crest segment are 38 ~ 48 min, and C8 crest segment is 48 ~ 60 min)；
Fig. 3 is that preparative high performance liquid chromatography isolates and purifies for the second time；
Fig. 4 is the analytic type high performance liquid chromatography of calcium chelating peptide (calcium sequestering activity peptide monomer)；
Fig. 5 is the HPLC-MS qualification figure of calcium chelating peptide peptide (Gly-Pro-Asp-Gly-Pro-His-Gly-Pro-Val-Gly)
Spectrum.
Specific embodiment
Below with reference to embodiment, the present invention is further explained.These embodiments are merely to illustrate the present invention rather than limitation
The scope of the present invention.Test method without specific conditions in lower example embodiment usually according to this field normal condition or is pressed
The condition suggested according to manufacturer；Used raw material, reagent etc., unless otherwise specified, being can be from the business such as conventional market
The raw materials and reagents that approach obtains.The variation for any unsubstantiality that those skilled in the art is done on the basis of the present invention
And replacement belongs to scope of the present invention.
Embodiment 1
The present embodiment provides a kind of calcium chelating peptide, amino acid sequences are as follows: GPAGPHGPVG(Gly-Pro-Asp-Gly-Pro-
His-Gly-Pro-Val-Gly).
The calcium chelating peptide can be prepared by the following procedure method and be prepared:
(1) preparation of Tilapia bone collagen
A. it digests de- meat: fish-bone frame is cut into 5 cm or so, h(55 DEG C of enzymatic hydrolysis 2, pH are carried out to fish-bone frame with neutral proteinase
=7.5), to remove the meat mincing invested on bone.
B. it alkali cleaning degreasing: is washed away after enzymatic hydrolysis and carries out degreasing, cleaning to neutrality with NaOH solution after impurity.
C. Tilapia bone decalcification handle: fish-bone is put into EDTA-2Na(pH=7.2, w/v=1:10) in, be placed in 4 DEG C it is cold
In library, periodic agitation is during which carried out, handles 5 d, it is stand-by after then cleaning fish-bone to neutrality.
D. acid processing: the fish-bone after decalcification is arrived with neutrality is washed to after 18 h of HCl treatment of 4 % of mass fraction
Tilapia bone collagen (such as Fig. 1).
(2) Tilapia bone collagen digests
According to 6%(w/w) ratio is added 0.6 g Tilapia bone collagen into tertiary effluent, and it adjusts pH to be accurate to 7.0, is then added
Papain, enzyme dosage 1%(enzyme and fish-bone mass ratio: w/w), after digesting 5h under temperature 60 C, enzyme deactivation 10 in boiling water bath
Min is placed in and cools down at room temperature, and 4000 r/min of sample is then centrifuged 20 min, supernatant is taken to be lyophilized.
(3) calcium chelating peptide isolates and purifies
1) C18Prepare the separation of steel column chromatography:
1. using Shimadu PRC-ODS steel column (15 mm, 30 mm × 250 mm), by calcium sequestration capacity in enzymolysis product
After preferable component freeze-drying, adding level-one water to its concentration is 62 mg/mL, and what is be loaded to again after 0.45 um filter membrane excessively prepares steel column
On, applied sample amount is 4 mL, flow velocity are as follows: 10 mL/min, Detection wavelength are 214 nm and 280 nm.With deionized water (containing 0.1%
TFA) and acetonitrile (%TFA containing 0.1) gradient elution, elution program are as follows:
According to the difference of liquid chromatogram appearance time, by the component of collection be divided into six sections be named as (C1, C2, C3, C4, C5, C6,
C7, C8), component is pipetted to 4 mL centrifuge tubes, by -40 DEG C, 0.1 Kpa vacuumizes jelly after 50 DEG C of rotary evaporations are concentrated
It is dry, it then carries out the measurement of calcium sequestering activity and filters out active component C2.See Fig. 2.
2. further being isolated and purified in 1. system to said components C2, using identical flow velocity, eluent and detection wave
Long, elution program changes as follows:
The C2 component picked up when by first time preparative separation carries out second on preparative high performance liquid chromatography and separates, and obtains
C2-1, C2-2, C2-3, C2-4, C2-5, C2-6, C2-7 and 7 seven peaks, are shown in Fig. 3.
2) analytic type efficient liquid phase purified monomer
Using analytic type high performance liquid chromatography, using C18 column (5 m, 4.6 mm × 250 mm), by the component of above-mentioned acquisition
C2-7 carries out purifying confirmation (see figure 4), flow velocity are as follows: 10 mL/min, Detection wavelength are 214 nm and 280 nm.(contain 0.1% with water
TFA) and acetonitrile (TFA containing 0.1%) gradient elution, elution program it is as follows:
3) Tilapia bone Calcium-binding peptides activity rating is carried out using o-cresolphthalein colorimetric method.Take 5 mg of polypeptide sample in 10
In mL centrifuge tube, the CaCl of 1 mL, 5 mmol/L is added2 With the sodium phosphate buffer of 0.2 mol/L of pH=7.8.Take one
Centrifuge tube does not add sample sets as blank control group.It is subsequently placed in mixed liquor in shaking table and carries out 60 min of 37oC water-bath.
It is centrifuged in taking-up, removal precipitating.After supernatant is diluted 5 times, the o-cresolphthalein work developing solution of 5 times of volumes is added,
Concussion mixes 20 s.It is the absorbance value under 570nm wavelength with microplate reader Detection wavelength in 10 min, three, each sample
In parallel.Calcium content-light absorption value standard curve: y=1.2522x+0.5884 (r is made under the same conditions2=0.9824), Tilapia mossambica
It is as follows that Bone gillg calcium chelates peptide activity calculation formula:
Calcium sequestering activity (mg/g-peptide)=5x/1.667
Structure detection: component C2-7 is detected as simple spike, is measured using high performance liquid chromatography mass spectrometric hyphenated technique (HPLC-MS)
Obtaining amino acid sequence is Gly-Pro-Asp-Gly-Pro-His-Gly-Pro-Val-Gly.
Measurement result shows: can be seen that by table one, enzymolysis product is purified by liquid phase separation, and calcium ion sequestering activity improves
To 43.018 mg/g-peptide.
1 Tilapia bone Calcium-binding peptides activity of table
Finally it is pointed out that above embodiments are only representative examples of the invention.Obviously, technology of the invention
Scheme is not limited to above-described embodiment, can also there are many deformation.Those skilled in the art can be direct from the content of present invention
All deformations are exported or associated, scope of protection of the claims of the invention are considered as.
Sequence table
<110>Agricultural University Of South China
<120>a kind of calcium chelating peptide and its preparation method and application
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 10
<212> PRT
<213> 1(1)
<400> 1
Gly Pro Ala Gly Pro His Gly Pro Val Gly
1 5 10
Claims (10)
1. a kind of calcium chelating peptide, which is characterized in that the amino acid sequence of the calcium chelating peptide: GPAGPHGPVG.
2. calcium chelating peptide according to claim 1, which is characterized in that the molecular weight of the calcium chelating peptide is 844.4340 Da；
The calcium sequestration capacity of the calcium chelating peptide is 43.018 mg/g.
3. the preparation method of any calcium chelating peptide of claim 1 ~ 2, which comprises the steps of:
S1: Tilapia mossambica skeleton is carried out to digest de- meat, alkali cleaning degreasing obtains Tilapia bone collagen egg after decalcification processing and acid processing
It is white；
S2: after the enzymatic hydrolysis of Tilapia bone collagen obtained by S1, enzyme deactivation, the freeze-drying of centrifuging and taking supernatant；
S3: it after being isolated and purified step by step using preparative reversed-phase high performance liquid chromatography progress multistage, is obtained using RT-HPLC purifying
The calcium chelating peptide.
4. preparation method according to claim 3, which is characterized in that the process of the de- meat of enzymatic hydrolysis described in S1 are as follows: by Tilapia mossambica
Skeleton dissection removes the meat mincing on Tilapia mossambica skeleton after neutral protease enzymolysis.
5. preparation method according to claim 3, which is characterized in that the process of alkali cleaning degreasing described in S1 are as follows: utilize inorganic
Then alkaline solution cleaning and degreasing is cleaned to neutrality.
6. preparation method according to claim 3, which is characterized in that the process of the processing of decalcification described in S1 are as follows: take off alkali cleaning
Tilapia bone is placed in EDTA-2Na solution after rouge, is freezed, stirring, cleaning to neutrality.
7. preparation method according to claim 3, which is characterized in that the process of the processing of acid described in S1 are as follows: the fish after decalcification
Bone is washed to neutrality to get Tilapia bone collagen is arrived after being handled with acid solution.
8. preparation method according to claim 3, which is characterized in that select papain to be digested in S2；The wood
Melon protease is 0.3% ~ 1% in the mass fraction of enzymatic hydrolysis system；The time of the enzymatic hydrolysis is 3 ~ 6h；The temperature of the enzymatic hydrolysis is 40
~60℃；The pH of the enzymatic hydrolysis is 6.0 ~ 7.0.
9. preparation method according to claim 3, which is characterized in that the condition of RT-HPLC described in S3 are as follows: sample volume is
20mL；Chromatographic column is C18 chromatographic column；Mobile phase is the TFA containing 0.1%；Elution speed is 1.0 mL/min；Ultraviolet detection wave
A length of double Detection wavelengths: 214 nm, 280 nm.
10. any calcium chelating peptide of claim 1 ~ 2 is preparing the application in calcium-supplementing preparation or functional beverage.
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| CN109762864A (en) * | 2019-03-25 | 2019-05-17 | 泰安市海之润食品有限公司 | A kind of preparation method of tuna bone collagen polypeptide |
| CN110627896A (en) * | 2019-09-03 | 2019-12-31 | 华南农业大学 | Calcium chelating peptide and preparation method and application thereof |
| CN110669127A (en) * | 2019-09-03 | 2020-01-10 | 华南农业大学 | Novel calcium chelating peptide and preparation method and application thereof |
| CN111454347A (en) * | 2020-04-20 | 2020-07-28 | 广东海洋大学 | Peptide calcium chelate as well as preparation method and application thereof |
| CN112679581A (en) * | 2021-01-27 | 2021-04-20 | 华南农业大学 | Novel tilapia mossambica scale bone formation promoting peptide and application thereof |
| CN112956700A (en) * | 2021-01-27 | 2021-06-15 | 华南农业大学 | Application of bone formation promoting peptide in preparation of functional food, health product or medicine for promoting proliferation, differentiation or mineralization of osteoblast |
| CN116239666A (en) * | 2023-04-25 | 2023-06-09 | 华南农业大学 | Four goat milk chelated calcium peptides and preparation method thereof |
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| CN109762864A (en) * | 2019-03-25 | 2019-05-17 | 泰安市海之润食品有限公司 | A kind of preparation method of tuna bone collagen polypeptide |
| CN110627896A (en) * | 2019-09-03 | 2019-12-31 | 华南农业大学 | Calcium chelating peptide and preparation method and application thereof |
| CN110669127A (en) * | 2019-09-03 | 2020-01-10 | 华南农业大学 | Novel calcium chelating peptide and preparation method and application thereof |
| CN110627896B (en) * | 2019-09-03 | 2022-02-18 | 华南农业大学 | Calcium chelating peptide and preparation method and application thereof |
| CN111454347A (en) * | 2020-04-20 | 2020-07-28 | 广东海洋大学 | Peptide calcium chelate as well as preparation method and application thereof |
| CN112679581A (en) * | 2021-01-27 | 2021-04-20 | 华南农业大学 | Novel tilapia mossambica scale bone formation promoting peptide and application thereof |
| CN112956700A (en) * | 2021-01-27 | 2021-06-15 | 华南农业大学 | Application of bone formation promoting peptide in preparation of functional food, health product or medicine for promoting proliferation, differentiation or mineralization of osteoblast |
| CN116239666A (en) * | 2023-04-25 | 2023-06-09 | 华南农业大学 | Four goat milk chelated calcium peptides and preparation method thereof |
| CN116239666B (en) * | 2023-04-25 | 2023-09-19 | 华南农业大学 | Chelating calcium peptide mixture |
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