CN116200365A - Active oligopeptide RYIVPL and preparation method and application thereof - Google Patents
Active oligopeptide RYIVPL and preparation method and application thereof Download PDFInfo
- Publication number
- CN116200365A CN116200365A CN202211627366.2A CN202211627366A CN116200365A CN 116200365 A CN116200365 A CN 116200365A CN 202211627366 A CN202211627366 A CN 202211627366A CN 116200365 A CN116200365 A CN 116200365A
- Authority
- CN
- China
- Prior art keywords
- oligopeptide
- active oligopeptide
- active
- wheat protein
- wheat
- 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
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 65
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 65
- 238000002360 preparation method Methods 0.000 title claims abstract description 14
- 241000209140 Triticum Species 0.000 claims abstract description 61
- 235000021307 Triticum Nutrition 0.000 claims abstract description 61
- 101800001982 Cholecystokinin Proteins 0.000 claims abstract description 46
- 102100025841 Cholecystokinin Human genes 0.000 claims abstract description 46
- 229940107137 cholecystokinin Drugs 0.000 claims abstract description 46
- 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 claims abstract description 46
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 39
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 39
- 230000000694 effects Effects 0.000 claims abstract description 27
- 238000000034 method Methods 0.000 claims abstract description 27
- 230000001737 promoting effect Effects 0.000 claims abstract description 17
- 150000001413 amino acids Chemical group 0.000 claims abstract description 7
- 230000030136 gastric emptying Effects 0.000 claims abstract description 7
- 238000000926 separation method Methods 0.000 claims abstract description 7
- 238000000746 purification Methods 0.000 claims abstract description 4
- 230000028327 secretion Effects 0.000 claims description 34
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 30
- 239000000047 product Substances 0.000 claims description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 18
- 208000008589 Obesity Diseases 0.000 claims description 12
- 235000020824 obesity Nutrition 0.000 claims description 12
- 108090000284 Pepsin A Proteins 0.000 claims description 10
- 102000057297 Pepsin A Human genes 0.000 claims description 10
- 229940111202 pepsin Drugs 0.000 claims description 10
- 239000006228 supernatant Substances 0.000 claims description 10
- 102000004142 Trypsin Human genes 0.000 claims description 9
- 108090000631 Trypsin Proteins 0.000 claims description 9
- 239000012588 trypsin Substances 0.000 claims description 9
- 230000002255 enzymatic effect Effects 0.000 claims description 8
- 230000037406 food intake Effects 0.000 claims description 8
- 239000000413 hydrolysate Substances 0.000 claims description 8
- 235000019789 appetite Nutrition 0.000 claims description 7
- 230000036528 appetite Effects 0.000 claims description 7
- 238000003786 synthesis reaction Methods 0.000 claims description 7
- 239000008367 deionised water Substances 0.000 claims description 6
- 229910021641 deionized water Inorganic materials 0.000 claims description 6
- 239000012153 distilled water Substances 0.000 claims description 6
- 235000012631 food intake Nutrition 0.000 claims description 6
- 102000004190 Enzymes Human genes 0.000 claims description 5
- 108090000790 Enzymes Proteins 0.000 claims description 5
- 229940088598 enzyme Drugs 0.000 claims description 5
- 210000003158 enteroendocrine cell Anatomy 0.000 claims description 4
- 239000003480 eluent Substances 0.000 claims description 3
- 238000010353 genetic engineering Methods 0.000 claims description 3
- 230000002797 proteolythic effect Effects 0.000 claims description 3
- 238000005406 washing Methods 0.000 claims description 3
- 238000004587 chromatography analysis Methods 0.000 claims description 2
- 238000001816 cooling Methods 0.000 claims description 2
- 238000005238 degreasing Methods 0.000 claims description 2
- 238000001035 drying Methods 0.000 claims description 2
- 238000000227 grinding Methods 0.000 claims description 2
- 230000003301 hydrolyzing effect Effects 0.000 claims description 2
- 102000040430 polynucleotide Human genes 0.000 claims description 2
- 108091033319 polynucleotide Proteins 0.000 claims description 2
- 239000002157 polynucleotide Substances 0.000 claims description 2
- 235000013305 food Nutrition 0.000 abstract description 7
- 210000001035 gastrointestinal tract Anatomy 0.000 abstract description 5
- 230000002496 gastric effect Effects 0.000 abstract description 4
- 230000036186 satiety Effects 0.000 abstract description 4
- 235000019627 satiety Nutrition 0.000 abstract description 4
- 238000010521 absorption reaction Methods 0.000 abstract description 3
- 229940079593 drug Drugs 0.000 abstract description 3
- 239000003814 drug Substances 0.000 abstract description 3
- 238000010532 solid phase synthesis reaction Methods 0.000 abstract description 3
- 210000003890 endocrine cell Anatomy 0.000 abstract description 2
- 230000004936 stimulating effect Effects 0.000 abstract description 2
- 239000000126 substance Substances 0.000 abstract description 2
- 231100000331 toxic Toxicity 0.000 abstract description 2
- 230000002588 toxic effect Effects 0.000 abstract description 2
- 102000038379 digestive enzymes Human genes 0.000 abstract 1
- 108091007734 digestive enzymes Proteins 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 30
- 108090000765 processed proteins & peptides Proteins 0.000 description 26
- 210000004027 cell Anatomy 0.000 description 22
- 102100030511 Stanniocalcin-1 Human genes 0.000 description 18
- 101710142157 Stanniocalcin-1 Proteins 0.000 description 18
- 239000000243 solution Substances 0.000 description 13
- 108010009736 Protein Hydrolysates Proteins 0.000 description 11
- 239000003531 protein hydrolysate Substances 0.000 description 11
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 230000000975 bioactive effect Effects 0.000 description 5
- 230000000968 intestinal effect Effects 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 150000002500 ions Chemical class 0.000 description 4
- 238000004949 mass spectrometry Methods 0.000 description 4
- 238000001819 mass spectrum Methods 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 208000017667 Chronic Disease Diseases 0.000 description 3
- 102000012515 Protein kinase domains Human genes 0.000 description 3
- 108050002122 Protein kinase domains Proteins 0.000 description 3
- 102000006668 UniProt protein families Human genes 0.000 description 3
- 108020004729 UniProt protein families Proteins 0.000 description 3
- 235000005911 diet Nutrition 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 230000007071 enzymatic hydrolysis Effects 0.000 description 3
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 229940088597 hormone Drugs 0.000 description 3
- 239000005556 hormone Substances 0.000 description 3
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- VSIVTUIKYVGDCX-UHFFFAOYSA-M sodium;4-[2-(2-methoxy-4-nitrophenyl)-3-(4-nitrophenyl)tetrazol-2-ium-5-yl]benzene-1,3-disulfonate Chemical compound [Na+].COC1=CC([N+]([O-])=O)=CC=C1[N+]1=NC(C=2C(=CC(=CC=2)S([O-])(=O)=O)S([O-])(=O)=O)=NN1C1=CC=C([N+]([O-])=O)C=C1 VSIVTUIKYVGDCX-UHFFFAOYSA-M 0.000 description 3
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108010068370 Glutens Proteins 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 210000005252 bulbus oculi Anatomy 0.000 description 2
- 235000019577 caloric intake Nutrition 0.000 description 2
- 230000003833 cell viability Effects 0.000 description 2
- 150000001793 charged compounds Chemical class 0.000 description 2
- 230000000378 dietary effect Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 235000019253 formic acid Nutrition 0.000 description 2
- 235000021312 gluten Nutrition 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 108060006613 prolamin Proteins 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- MLBZLJCMHFCTQM-UHFFFAOYSA-N (2-methylphenyl)-diphenylphosphane Chemical compound CC1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1 MLBZLJCMHFCTQM-UHFFFAOYSA-N 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 108020005199 Dehydrogenases Proteins 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 206010033307 Overweight Diseases 0.000 description 1
- 108010019160 Pancreatin Proteins 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical group [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000021245 dietary protein Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 235000013376 functional food Nutrition 0.000 description 1
- 235000013402 health food Nutrition 0.000 description 1
- 210000003016 hypothalamus Anatomy 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000003470 mitochondria Anatomy 0.000 description 1
- VMGAPWLDMVPYIA-HIDZBRGKSA-N n'-amino-n-iminomethanimidamide Chemical compound N\N=C\N=N VMGAPWLDMVPYIA-HIDZBRGKSA-N 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- BOLDJAUMGUJJKM-LSDHHAIUSA-N renifolin D Natural products CC(=C)[C@@H]1Cc2c(O)c(O)ccc2[C@H]1CC(=O)c3ccc(O)cc3O BOLDJAUMGUJJKM-LSDHHAIUSA-N 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000004885 tandem mass spectrometry Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
- C12N9/1205—Phosphotransferases with an alcohol group as acceptor (2.7.1), e.g. protein kinases
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/04—Anorexiants; Antiobesity agents
-
- 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
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Obesity (AREA)
- Pharmacology & Pharmacy (AREA)
- Child & Adolescent Psychology (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to an active oligopeptide RYIVPL, a preparation method and application thereof. The active oligopeptide is RYIVPL, and the amino acid sequence is as follows: arg-Tyr-Ile-Val-Pro-Leu has the function of obviously stimulating endocrine cells of intestinal tract to secrete cholecystokinin (CCK). Compared with the prior art, the oligopeptide can be synthesized artificially by adopting a chemical solid phase synthesis method, and can be obtained after separation and purification after enzymolysis of wheat protein. The oligopeptide has the characteristics of safety, no toxic or side effect, difficult enzymolysis by gastrointestinal digestive enzymes, easy absorption and the like, is suitable for serving as a functional component to develop foods, functional/health-care foods and medicines with the functions of delaying gastric emptying, promoting satiety and losing weight, and has great application value in the fields of foods, medicines and the like and wide prospect.
Description
Technical Field
The invention belongs to the technical field of bioactive peptides, and particularly relates to an active oligopeptide RYIVPL, a preparation method and application thereof.
Background
Obesity has become a global public health problem. Many chronic diseases including atherosclerosis, cardiovascular diseases, type II diabetes, etc. are associated with obesity. The imbalance in energy intake and energy expenditure is a direct cause of overweight obesity in an individual. Therefore, in order to prevent obesity, limiting excessive energy intake, i.e., limiting the intake of food, is an optimal means. The central hypothalamus and digestive tract of the body are key sites for controlling the regulation of ingestion, and a plurality of ghrelins related to the regulation of ingestion are distributed in the body. Cholecystokinin (CCK) is a member of classical brain-intestinal peptides, and can regulate the generation of satiety signals by organisms and reduce the food intake of organisms, thereby achieving the effect of suppressing appetite. Prior studies have shown that CCK secretion is regulated by dietary factors. Thus, the secretion of CCK in the intestinal tract can be regulated by diet, thereby improving or relieving obesity and related chronic diseases.
The food-borne bioactive peptide is a common dietary factor, has the characteristics of easy digestion and absorption by human bodies, high edible safety and the like, and has a wide application range in the food field. In view of the important role of CCK and the advantages of bioactive peptide, finding a bioactive peptide or extract capable of promoting intestinal CCK secretion has important value and great economic and social significance in preventing obesity or related chronic diseases.
Disclosure of Invention
Based on the current situation that bioactive peptide capable of promoting intestinal CCK secretion is lacking in the prior art, the invention provides an active oligopeptide RYIVPL with a function of promoting CCK secretion, and a preparation method and application thereof.
The aim of the invention can be achieved by the following technical scheme:
in a first aspect of the present invention, there is provided an active oligopeptide having CCK secretion promoting activity, wherein the active oligopeptide is RYIVPL, and the amino acid sequence is: arg-Tyr-Ile-Val-Pro-Leu.
Wheat proteins are mainly gluten and prolamin. The RYIVPL active oligopeptide is found to exist in wheat protein and is derived from wheat Protein kinase domain-containing protein (Uniprot protein accession number: A0A3B6D6B 8), so that the RYIVPL active oligopeptide can be prepared from the wheat protein.
In a second aspect of the invention, polynucleotides encoding the active oligopeptides are provided.
In a third aspect of the present invention, there is provided a method for preparing the active oligopeptide, which comprises performing biological enzymolysis on wheat protein, and then separating and purifying the wheat protein, or directly obtaining the active oligopeptide, and artificially synthesizing the active oligopeptide by genetic engineering, or directly preparing the active oligopeptide by chemical synthesis.
The artificial synthesis of the active oligopeptides by genetic engineering methods is a technical solution that can be achieved by a person skilled in the art, and for example, the sequence synthesis of the oligopeptides can be controlled by a suitable DNA template based on DNA recombination technology.
The method for directly obtaining the wheat protein by a separation and purification method can be as follows: based on the amino acid sequence of the given active oligopeptide, the active oligopeptide is obtained from wheat by adopting conventional enzymolysis, separation and purification methods in biological technology.
The method for preparing the active oligopeptide by chemical synthesis adopts a traditional solid-phase synthesis method.
According to a fourth aspect of the present invention, there is provided a method for preparing an enzymatic hydrolysate containing the active oligopeptide, wherein wheat protein is subjected to enzymatic hydrolysis by a two-step enzymatic hydrolysis method, comprising the steps of: and sequentially carrying out enzymolysis on wheat protein by using pepsin and trypsin to obtain a wheat protein enzymolysis product, namely an enzymolysis product containing the active oligopeptide.
In one embodiment of the invention, the method for sequentially hydrolyzing wheat protein by pepsin and trypsin comprises the following steps:
1) Extracting wheat protein from wheat;
2) Carrying out enzymolysis on the wheat protein by using the pepsin to obtain a first enzymolysis product;
3) And (3) carrying out enzymolysis on the first enzymolysis product by using the trypsin to obtain a wheat protein enzymolysis product.
In one embodiment of the present invention, a method for extracting wheat protein from wheat comprises the steps of:
grinding wheat, degreasing, adding into distilled water, setting the temperature to 50-60 ℃, adjusting the pH to 4-6, and pre-treating with saccharifying enzyme for 0.5-2h; cooling to room temperature, adjusting pH to 10-12, extracting protein, centrifuging to obtain supernatant, adjusting pH to 4.4-4.6, standing, centrifuging, and washing with water; and finally drying to obtain the wheat protein.
In one embodiment of the invention, the mass ratio of pepsin or trypsin to the wheat protein is 1:10-100.
In one embodiment of the invention, the enzymolysis condition of pepsin or trypsin is 37 ℃ for 1-4h.
In one embodiment of the present invention, after the wheat proteolytic product is obtained in step 3), the method further comprises the following steps:
separating the wheat protein enzymolysis product by using YMC ODS C18 chromatographic column, eluting with 5% methanol deionized water solution, 30% methanol deionized water solution, 80% methanol deionized water solution and 100% methanol solution as eluent at a certain flow rate, purifying by chromatography, and collecting different components; and then detecting the influence of different components on CCK secretion of the enteroendocrine cells, and selecting the component with the highest activity for stimulating CCK secretion as a target component, namely a product containing the active oligopeptide.
In a fifth aspect of the present invention, there is provided an enzymatic hydrolysate of an active oligopeptide prepared based on the above preparation method.
In a sixth aspect, the invention provides the use of said active oligopeptide, an enzymatic hydrolysate containing said oligopeptide, for the preparation of a product having at least one of the following functions 1) -4):
1) Promoting CCK secretion;
2) Slowing gastric emptying;
3) Suppressing appetite and reducing food intake;
4) Preventing or assisting in treating obesity.
The active oligopeptide and an enzymolysis product containing the active oligopeptide have the function of promoting CCK secretion, and can slow down gastric emptying, inhibit appetite, reduce food intake and prevent or assist in treating obesity.
In a seventh aspect, the present invention provides a product comprising said active oligopeptide, or an enzymatic hydrolysate comprising said active oligopeptide, said product having at least one of the following functions 1) to 4):
1) Promoting CCK secretion;
2) Slowing gastric emptying;
3) Suppressing appetite and reducing food intake;
4) Preventing or assisting in treating obesity.
The products include foods, functional foods/health foods and medicines.
Compared with the prior art, the invention has the advantages and beneficial effects that:
the invention screens out the active oligopeptide for promoting the secretion of intestinal CCK, and the active peptide has a novel peptide sequence structure, so far, other related reports are not yet seen; the active peptide can be prepared from food protein wheat protein, and has the advantages of safety and no toxic or side effect; the active oligopeptide is not easily degraded by pepsin and pancreatin in the gastrointestinal tract, has good stability, and can exert CCK secretion promoting activity to the maximum extent; the active oligopeptide disclosed by the invention has the advantages of small molecular weight which is smaller than 1000Da, and has the effect of promoting the secretion activity of intestinal CCK, and is easy to be absorbed by organisms, so that the active oligopeptide has a good nutrition function. The preparation method of the active oligopeptide or the enzymolysis product containing the oligopeptide is simple, easy to operate, convenient for industrialized mass production and wide in application prospect.
Drawings
FIG. 1 is a graph showing the effect of RYIVPL active oligopeptides on STC-1 cell viability;
FIG. 2 is a graph showing the effect of RYIVPL active oligopeptide on CCK secretion by STC-1 cells;
FIG. 3 shows the effect of wheat proteinase (W) on CCK secretion by STC-1 cells, C being the control group (no wheat proteinase added);
FIG. 4 is a graph showing the effect of wheat protein hydrolysate on CCK secretion by mouse enteroendocrine cells;
FIG. 5 is a diagram showing the separation of wheat protein hydrolysate by YMC ODS C18 column chromatography;
FIG. 6 is a graph showing the effect of isolated fractions on CCK secretion by STC-1 cells;
FIG. 7 is a MS/MS pattern and sequence analysis of the RYIVPL active oligopeptide in isolated fraction F7.
Detailed Description
The invention will now be described in detail with reference to the drawings and specific examples.
EXAMPLE 1 evaluation of RYIVPL Activity oligopeptide Synthesis and CCK secretion-promoting Activity
1. Synthesis of RYIVPL active oligopeptides
The active oligopeptide Arg-Tyr-Ile-Val-Pro-Leu (RYIVPL) is synthesized by adopting a peptide solid-phase synthesis method from Zhejiang Hongtao technology Co., ltd, and the purity of the synthesized peptide is verified to be more than 95% by a high performance liquid phase method and a mass spectrum technology.
2. Effect of RYIVPL on STC-1 cell Activity and CCK secretion
(1) Cultivation of STC-1 cells
STC-1 cells were cultured in DMEM medium containing 10% Fetal Bovine Serum (FBS), 1% non-essential amino acids (NEAA), 100U/mL penicillin and 0.1mg/mL streptomycin. The cells were incubated at 37℃with 5% CO 2 Is incubated in the cell incubator of (a) and subcultured by trypsinization when a density of 80-90% is reached.
(2) Cell Activity assay
The effect of RYIVPL active peptides on STC-1 cell viability was tested and assessed by cell proliferation and cytotoxicity of WST-8 (2- (2-methoxy-4-nitrophenyl) -3- (4-nitrophenyl) -5- (2, 4-disulfophenyl) -2H-tetrazolium monosodium salt). WST-8 is added into STC-1 cells treated by a 96-well plate, in the presence of an electron coupling reagent, the WST-8 can be reduced by some dehydrogenases in mitochondria to generate orange-yellow Formazan, and an enzyme-labeled instrument is used for measuring absorbance at the detection wavelength of 450nm, so that the absorbance is expressed as a percentage of a control group. The results are shown in FIG. 1, and the activity of the active oligopeptide is not changed compared with that of the control STC-1 at different test concentrations, so that the RYIVPL active peptide is nontoxic to cells.
(3) Determination of the content of secreted hormone of STC-1 cells
The RYIVPL active oligopeptide is prepared into peptide solutions with molar concentrations of 0.2,2 and 5mM respectively by Hank's buffer solution. STC-1 cells were grown in 24 well plates at 1.25X10 5 Density inoculation of individual cells. When the cells reached 80% -90% confluence, the cells were washed twice with Hank's buffer to remove the medium. The peptide solution was added to STC-1 cells and the cells were incubated in an incubator at 37℃for 2h. After the incubation, 1000g was centrifuged for 20min, and the supernatant was taken. CCK content was determined using a commercial CCK kit from Wohan cloud cloning technologies Co.
The total protein content of the supernatant measured using the Biyun biotechnology company BCA kit was used as a reference to reduce errors caused by handling between different batches. The calculation formula is as follows: c (C) CCK /(C BCA ×100)(×10 -7 ) Wherein C CCK Represents the CCK concentration (pg/mL), C in the supernatant BCA Represents the measured total protein concentration minus the measured peptide concentration (mg/mL) in the supernatant.
The effect of the RYIVPL active peptide on CCK secretion by STC-1 cells is shown in FIG. 2, and it can be seen that the RYIVPL active oligopeptide dose-dependent increases CCK secretion. Numerous studies have demonstrated that CCK is an important member of the brain-intestinal peptide group, which slows gastric emptying, regulates the production of satiety signals in the body, and reduces the intake of food in the body, thereby achieving the effect of suppressing appetite. Increasing secretion of CCK in the intestinal tract is of great importance for the prevention and alleviation of obesity. The RYIVPL active peptide can obviously promote the secretion of CCK by an intestinal endocrine cell STC-1, so that the peptide has important significance and application value for promoting satiety and losing weight.
Example 2 preparation of wheat protein hydrolysate and Activity evaluation
(1) Preparation of wheat protein zymolyte
Wheat flour was milled through an 80 mesh screen and then defatted with hexane. Soaking defatted wheat flour in distilled water at a mass ratio of 12:1 in beaker, adjusting pH to 5.0 with 1mol/L HCl, and treating with saccharifying enzyme at 50deg.C for 1 hr. The pH was then adjusted to 11.0 with 1mol/L NaOH and the supernatant was centrifuged after 2h action with a magnetic stirrer. Regulating pH of supernatant to isoelectric point (pH 4.5) with 1mol/L HCl, standing for 1 hr, centrifuging, washing with water, precipitating to neutrality, redissolving with small amount of distilled water, lyophilizing to obtain wheat protein, and storing at 4deg.C for use.
1g of the lyophilized protein powder was dissolved in 20mL of a freshly prepared aqueous pepsin solution containing 25mg, the pH of the solution was adjusted to 2.0 with HCl (1 mol/L) and incubated at 37℃for 2h. After the incubation was completed, the pH of the solution was adjusted to 6.8 with NaOH (1 mol/L), and then 50mg of trypsin was added to continue the enzymatic hydrolysis for 2 hours. And inactivating enzyme in boiling water bath for 8min, centrifuging, collecting supernatant, and lyophilizing to obtain wheat protein hydrolysate.
(2) Activity evaluation
The effect of wheat protein hydrolysate on the secretion of CCK by STC-1 cells was determined by using the above method by preparing a solution with a mass concentration of 5mg/mL with Hank's buffer, and the results are shown in FIG. 3. From the results, it can be seen that wheat protein hydrolysate can significantly stimulate the secretion of CCK by STC-1 cells.
Further, the effect of wheat proteolytic enzyme on hormone secretion by the mouse enteroendocrine cells was evaluated at the animal level. ICR mice were randomly divided into 2 groups (28 per group) after a 1 week adaptation period. Control group: lavage physiological saline; wheat protein hydrolysate group: gastric lavage wheat protein hydrolysate (1.0 g/kg body weight). After the stomach is irrigated, eyeballs are respectively subjected to blood collection at 0, 15min,30min,60min,90min,120min and 150min, the eyeballs are placed into a centrifuge tube containing EDTA (final concentration is 1 mg/mL) and aprotinin (final concentration is 0.6 TIU/mL), supernatant is centrifugally collected, and the CCK hormone content in serum is obtained through an ELISA method. CCK in the serum of the gastric lavage saline group was maintained at a level of about 40pg/mL during this period. The results of the gastric lavage wheat proteolytic enzyme group are shown in FIG. 4, and the wheat proteolytic enzyme can be found to greatly increase the CCK level in the mouse, and the CCK concentration in the blood of the mouse reaches about 90pg/mL in 60 min.
Example 3 preparation of active oligopeptides for promoting CCK secretion by wheat proteins
Taking YMC ODS C18 filler, conventional swelling and column loading (methanol is used as a filling buffer solution), wherein the height of the column is 25cm, the inner diameter of the column is 1.6cm, a water layer is required to be reserved at the top of the column at any moment, the column can be used after balancing about 3-4 column volumes, and the sample wheat proteolytic substance starts to be added when the liquid level is 2-3 mm. About 160mg of wheat protein hydrolysate powder is weighed and dissolved in 2mL of distilled water, a 0.45 mu m microporous filter membrane is added into a chromatographic column after filtration, the eluent is methanol solutions (5%, 30%, 80% and 100%) with different volume concentrations, the elution speed is 2mL/min, and the elution peak is collected. The wheat protein hydrolysate separation spectrum is shown in fig. 5, and it can be seen that the C18 chromatographic column separates the protein hydrolysate into 7 peptide components.
The first component has extremely high water absorption, can absorb moisture in air after freeze-drying, and the fourth component has extremely low proportion and is extremely difficult to obtain. The activity of 5 peptide fractions was evaluated by the method described above, and the results are shown in FIG. 6. It was found that the F7 component had the best ability to stimulate CCK secretion by STC-1 cells among the 5 peptide components. Thus, the F7 component is a highly active CCK secretion-promoting oligopeptide.
Example 4 identification of wheat proteins containing RYIVPL active peptides
The peptide sequences in the F7 fraction were identified using mass spectrometry techniques. The sample was dissolved in distilled water to prepare a 1mg/mL sample. A reverse phase chromatography column (150 μm i.d. x 150mm,packed with Acclaim PepMap RPLC C18,1.9 μm,
) Separating, wherein the mobile phase A is 0.1% formic acid aqueous solution, the mobile phase B is 0.1% formic acid/80% acetonitrile solution, and the gradient elution and separation gradient are carried out at the flow rate of 600 nL/min: 0-2min,4-8% B;2-45min,8-40% B;45-55min,40-60% B;55-56min,60-95% B;56-66min,95% B. The mass spectrum ion source type is electrospray ionization source (ESI), and positive ion scanning modeSpraying voltage 2200V, capillary temperature 270 ℃. Primary mass spectrum parameter setting: scan range 100-2000m/z, maximum resolution 70000, auto gain parameter 3000000. Secondary mass spectrometry parameter setting: the scanning range is 50-2000m/z, the maximum resolution is 17500, and the automatic gain parameter is 100000.
The ion peak mainly occurring in the F7 component was m/z=380.74, z=2, as detected by mass spectrometry. The molecular ion peak is further subjected to secondary mass spectrometry, and the secondary mass spectrum of the molecular ion peak is shown in fig. 7. Through database matching, the peptide corresponding to the ion peak is Arg-Tyr-Ile-Val-Pro-Leu (RYIVPL).
Wheat proteins are mainly gluten and prolamin. It was found that the RYIVPL active oligopeptide is derived from wheat Protein kinase domain-containing protein (Uniprot protein accession number: A0A3B6D6B 8), and that the RYIVPL active oligopeptide can be prepared from wheat protein.
The amino acid sequence of wheat Protein kinase domain-containing protein (Uniprot protein accession number: A0A3B6D6B 8) is shown in SEQ ID NO. 1. The RYIVPL active oligopeptide is positioned at the 602 th to 607 th positions of the amino acid sequence shown in SEQ ID NO. 1.
The amino acid sequence shown in SEQ ID NO.1 is specifically as follows:
MHERAVWIFL CDLGGQNMPF EGSIPVEIGN LVNLFSLGME SNFLYGSIPS SIGKLRNLYI 60
LNLSKNKLSG QIPPSIGDVT QLALLYLDGN NLGGNIPGSL AQCMGLFELN LSQNNLDGSI 120
PVRLFADLLF AWSLDFSHNN LTGELPPVLG TYGIGSGLVS LHMEGNRFHG QIPERWHLLV 180
STRQINLSHN DLSGVVPKFF EQLDKLEQLD LSYNNLEGAV PASGIFTHSA AVVLDGNKGL 240
CSNSPRLALP ICPGISGSAT KVKHHLSLLV TSLLIVLPPL TIGSLVLIWF MLTIWKKGSF 300
PFSRWDLVSK MFPNRREVHT APCHDEKKLK RVSYEDIVKA TNWFSLVHTI SSTCTGSVYV 360
GRFKSDKSLV AIKVFKLNEP GGYDSYLIEC EVLRSTRHRN IMRPVTLCST LDSQNHEFKA 420
LIFEFMVNGS LEAWLHSEQH NGIPDKVLGF GQRICIAADV ASALDYAHNE LTPPLIHCDL 480
KPNNVLLDDD MTARLSDFGS AKFLSPGLVI PKSLDDVGGT IGYVAPEYGM GCEISVAGDL 540
YSFGVLLLEL LTGKRPTDDM FVDGLSLCKF SESMFPDRVA EILDPHMAHE EHQGCTEAWM 600
ERYIVPLVAL GLSCTMESTK DRPGMKDVCA KLSDIRASFL ELS 643
the previous description of the embodiments is provided to facilitate a person of ordinary skill in the art in order to make and use the present invention. It will be apparent to those skilled in the art that various modifications can be readily made to these embodiments and the generic principles described herein may be applied to other embodiments without the use of the inventive faculty. Therefore, the present invention is not limited to the above-described embodiments, and those skilled in the art, based on the present disclosure, should make improvements and modifications without departing from the scope of the present invention.
Claims (10)
1. An active oligopeptide capable of promoting cholecystokinin secretion, which is characterized in that the oligopeptide is RYIVPL and has the amino acid sequence of: arg-Tyr-Ile-Val-Pro-Leu.
2. A polynucleotide encoding the active oligopeptide of claim 1.
3. The method for preparing the active oligopeptide according to claim 1, wherein the active oligopeptide is prepared directly by a chemical synthesis method, or is synthesized artificially by a genetic engineering method, or is obtained from wheat protein by a biological enzymolysis method and a separation and purification method.
4. A process for the preparation of an enzymatic hydrolysate comprising the active oligopeptide of claim 1, comprising the steps of: sequentially hydrolyzing wheat protein with pepsin and trypsin to obtain a wheat protein enzymolysis product, namely an enzymolysis product containing the active oligopeptide according to claim 1.
5. The method of claim 4, wherein the method of extracting wheat protein from wheat comprises the steps of:
grinding wheat, degreasing, adding into distilled water, setting the temperature to 50-60 ℃, adjusting the pH to 4-6, and pre-treating with saccharifying enzyme for 0.5-2h; cooling to room temperature, adjusting pH to 10-12, extracting protein, centrifuging to obtain supernatant, adjusting pH to 4.4-4.6, standing, centrifuging, and washing with water; and finally drying to obtain the wheat protein.
6. The method according to claim 4, wherein the mass ratio of pepsin or trypsin to the wheat protein is 1:10-100;
the enzymolysis condition of pepsin or trypsin is 37 ℃ for enzymolysis for 1-4 hours.
7. The method according to claim 4, further comprising the steps of, after obtaining the wheat proteolytic product:
separating the wheat protein enzymolysis product by using YMC ODS C18 chromatographic column, eluting with 5% methanol deionized water solution, 30% methanol deionized water solution, 80% methanol deionized water solution and 100% methanol solution as eluent at a certain flow rate, purifying by chromatography, and collecting different components; then detecting the influence of different components on CCK secretion of the enteroendocrine cell, and selecting the component which stimulates CCK secretion to have the highest activity as a target component, namely the active oligopeptide of claim 1.
8. An enzymatic hydrolysate comprising the active oligopeptide of claim 1 having the effect of promoting cholecystokinin secretion prepared on the basis of the preparation method of any one of claims 4 to 7.
9. Use of an active oligopeptide according to claim 1, an enzymatic hydrolysate comprising an active oligopeptide according to claim 1 for the preparation of a product having at least one of the following functions 1) -4):
1) Promoting CCK secretion;
2) Slowing gastric emptying;
3) Suppressing appetite and reducing food intake;
4) Preventing or assisting in treating obesity.
10. A product comprising the active oligopeptide of claim 1 or an enzymatic hydrolysate comprising the active oligopeptide of claim 1, said product having at least one of the following functions 1) to 4):
1) Promoting CCK secretion;
2) Slowing gastric emptying;
3) Suppressing appetite and reducing food intake;
4) Preventing or assisting in treating obesity.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202211627366.2A CN116200365A (en) | 2022-12-16 | 2022-12-16 | Active oligopeptide RYIVPL and preparation method and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202211627366.2A CN116200365A (en) | 2022-12-16 | 2022-12-16 | Active oligopeptide RYIVPL and preparation method and application thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN116200365A true CN116200365A (en) | 2023-06-02 |
Family
ID=86513787
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202211627366.2A Pending CN116200365A (en) | 2022-12-16 | 2022-12-16 | Active oligopeptide RYIVPL and preparation method and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN116200365A (en) |
-
2022
- 2022-12-16 CN CN202211627366.2A patent/CN116200365A/en active Pending
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN110724178B (en) | Tuna white meat ACE inhibitory peptide and preparation method thereof | |
| CN105203671B (en) | The high performance liquid chromatography and gel permeation chromatography isolation and purification method of marine organisms source polypeptide | |
| CN115353553B (en) | CCK secretion-promoting peptide targeting calcium sensitive receptor and preparation method and application thereof | |
| CN110964087B (en) | Fugu active peptide and preparation method thereof | |
| CN111072756B (en) | Tetrodotoxin ACE inhibitory peptide and preparation method thereof | |
| CN111004309B (en) | ACE inhibitory peptide prepared from Takifugu flavidus fish skin and preparation method thereof | |
| CN109293740A (en) | The ACE in one seed oyster source inhibits and anti-tumor activity peptide | |
| CN102453741B (en) | Method for preparing high-activity corn antihypertensive peptide | |
| CN116143869A (en) | Highland barley source active oligopeptide and preparation method and application thereof | |
| CN111100186A (en) | Puffer fish polypeptide with ACE inhibitory activity and preparation method thereof | |
| CN110819674A (en) | Method for preparing antihypertensive peptide by enzymolysis of walnut meal with compound protease | |
| Jiang et al. | Identification and analysis of antioxidant peptides from sorghum (Sorghum bicolor L. Moench) on the basis of in vitro simulated gastrointestinal digestion | |
| CN110759965A (en) | Tuna red meat ACE inhibitory peptide and preparation method thereof | |
| CN112679578B (en) | Polypeptide mixture with antioxidant activity and DPP-IV (dipeptidyl peptidase-IV) inhibitory activity and preparation method thereof | |
| CN116200365A (en) | Active oligopeptide RYIVPL and preparation method and application thereof | |
| CN103130869A (en) | Antihypertensive peptides prepared by ultrasonic-assisted flour weevil larva proteolysis and preparation method thereof | |
| CN116082451A (en) | Buckwheat-source cholecystokinin secretion peptide and preparation method and application thereof | |
| CN116606369A (en) | Spirulina immunoregulatory peptide and preparation method and application thereof | |
| CN113201047B (en) | Walnut meal anti-inflammatory peptide WPL and application thereof | |
| CN115353551B (en) | Oat-derived GLP-1 secretion-promoting oligopeptide and preparation method and application thereof | |
| CN108441535A (en) | The production method of three enzymes, one ferment silkworm peptide | |
| CN109438556B (en) | Active peptide, recombinant vector, recombinant cell, anti-inflammatory composition, and preparation method and application thereof | |
| CN115124606A (en) | Oligopeptide containing amino acid structure PQQP and preparation method and application thereof | |
| CN117700484B (en) | High F value corn peptide and corn oligopeptide composition, and preparation method and application thereof | |
| CN115353549A (en) | Small peptide for promoting intestinal hormone secretion and preparation method and application thereof |
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 |