CN110218755A - A kind of preparation method of hypoglycemic tree peony active peptide - Google Patents
A kind of preparation method of hypoglycemic tree peony active peptide Download PDFInfo
- Publication number
- CN110218755A CN110218755A CN201910432490.5A CN201910432490A CN110218755A CN 110218755 A CN110218755 A CN 110218755A CN 201910432490 A CN201910432490 A CN 201910432490A CN 110218755 A CN110218755 A CN 110218755A
- Authority
- CN
- China
- Prior art keywords
- tree peony
- active peptide
- hypoglycemic
- preparation
- added
- 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
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 67
- 240000005001 Paeonia suffruticosa Species 0.000 title claims abstract description 56
- 235000003889 Paeonia suffruticosa Nutrition 0.000 title claims abstract description 56
- 238000002360 preparation method Methods 0.000 title claims abstract description 24
- 230000002218 hypoglycaemic effect Effects 0.000 title claims abstract description 16
- 241000736199 Paeonia Species 0.000 claims abstract description 34
- 235000006484 Paeonia officinalis Nutrition 0.000 claims abstract description 33
- 235000007164 Oryza sativa Nutrition 0.000 claims abstract description 15
- 230000000694 effects Effects 0.000 claims abstract description 15
- 235000009566 rice Nutrition 0.000 claims abstract description 15
- 102000004190 Enzymes Human genes 0.000 claims abstract description 14
- 108090000790 Enzymes Proteins 0.000 claims abstract description 14
- 102000004400 Aminopeptidases Human genes 0.000 claims abstract description 13
- 108090000915 Aminopeptidases Proteins 0.000 claims abstract description 13
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 13
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 13
- 230000007071 enzymatic hydrolysis Effects 0.000 claims abstract description 12
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims abstract description 12
- 239000002994 raw material Substances 0.000 claims abstract description 6
- 229920000858 Cyclodextrin Polymers 0.000 claims abstract description 3
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 claims abstract description 3
- 240000007594 Oryza sativa Species 0.000 claims abstract 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 33
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 25
- 108091005804 Peptidases Proteins 0.000 claims description 24
- 239000004365 Protease Substances 0.000 claims description 24
- 238000006243 chemical reaction Methods 0.000 claims description 23
- 150000001875 compounds Chemical class 0.000 claims description 18
- 238000000034 method Methods 0.000 claims description 17
- 239000007788 liquid Substances 0.000 claims description 16
- 229910001868 water Inorganic materials 0.000 claims description 15
- 238000001976 enzyme digestion Methods 0.000 claims description 11
- 230000002779 inactivation Effects 0.000 claims description 11
- 230000035484 reaction time Effects 0.000 claims description 11
- 238000013019 agitation Methods 0.000 claims description 9
- 238000005238 degreasing Methods 0.000 claims description 9
- 239000008367 deionised water Substances 0.000 claims description 9
- 229910021641 deionized water Inorganic materials 0.000 claims description 9
- 238000001914 filtration Methods 0.000 claims description 9
- 238000000746 purification Methods 0.000 claims description 9
- 238000007873 sieving Methods 0.000 claims description 9
- 239000006228 supernatant Substances 0.000 claims description 9
- 230000001376 precipitating effect Effects 0.000 claims description 8
- 229910052799 carbon Inorganic materials 0.000 claims description 2
- 239000000047 product Substances 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
- 238000004140 cleaning Methods 0.000 claims 1
- 239000003595 mist Substances 0.000 claims 1
- 230000007935 neutral effect Effects 0.000 claims 1
- 239000000843 powder Substances 0.000 claims 1
- 238000003756 stirring Methods 0.000 claims 1
- 239000002253 acid Substances 0.000 abstract description 5
- 150000001413 amino acids Chemical class 0.000 abstract description 5
- 239000003102 growth factor Substances 0.000 abstract description 5
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 5
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 abstract description 4
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 abstract description 4
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 abstract description 4
- 230000007062 hydrolysis Effects 0.000 abstract description 4
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 4
- 229920001184 polypeptide Polymers 0.000 abstract description 4
- 102000005593 Endopeptidases Human genes 0.000 abstract description 2
- 108010059378 Endopeptidases Proteins 0.000 abstract description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 abstract description 2
- 230000002209 hydrophobic effect Effects 0.000 abstract description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 abstract description 2
- 102000004142 Trypsin Human genes 0.000 abstract 1
- 108090000631 Trypsin Proteins 0.000 abstract 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
- 238000000605 extraction Methods 0.000 abstract 1
- 239000012460 protein solution Substances 0.000 abstract 1
- -1 trypsase Proteins 0.000 abstract 1
- 239000012588 trypsin Substances 0.000 abstract 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 24
- 102000035195 Peptidases Human genes 0.000 description 22
- 235000019419 proteases Nutrition 0.000 description 22
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 18
- 241000209094 Oryza Species 0.000 description 12
- 210000004369 blood Anatomy 0.000 description 10
- 239000008280 blood Substances 0.000 description 10
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 9
- 239000008103 glucose Substances 0.000 description 9
- 229910052757 nitrogen Inorganic materials 0.000 description 9
- 241000700159 Rattus Species 0.000 description 8
- 239000000523 sample Substances 0.000 description 8
- 230000000052 comparative effect Effects 0.000 description 6
- QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 5
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
- RAHZWNYVWXNFOC-UHFFFAOYSA-N Sulphur dioxide Chemical compound O=S=O RAHZWNYVWXNFOC-UHFFFAOYSA-N 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 238000011049 filling Methods 0.000 description 4
- 239000000975 dye Substances 0.000 description 3
- 238000004043 dyeing Methods 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 239000011521 glass Substances 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- MKYBYDHXWVHEJW-UHFFFAOYSA-N N-[1-oxo-1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propan-2-yl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(C(C)NC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 MKYBYDHXWVHEJW-UHFFFAOYSA-N 0.000 description 2
- 101710180313 Protease 3 Proteins 0.000 description 2
- HIMXGTXNXJYFGB-UHFFFAOYSA-N alloxan Chemical compound O=C1NC(=O)C(=O)C(=O)N1 HIMXGTXNXJYFGB-UHFFFAOYSA-N 0.000 description 2
- 235000020661 alpha-linolenic acid Nutrition 0.000 description 2
- DTOSIQBPPRVQHS-PDBXOOCHSA-N alpha-linolenic acid Chemical compound CC\C=C/C\C=C/C\C=C/CCCCCCCC(O)=O DTOSIQBPPRVQHS-PDBXOOCHSA-N 0.000 description 2
- 238000004176 ammonification Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 2
- 239000004327 boric acid Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000001569 carbon dioxide Substances 0.000 description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 description 2
- 239000003054 catalyst Substances 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- UGWKCNDTYUOTQZ-UHFFFAOYSA-N copper;sulfuric acid Chemical compound [Cu].OS(O)(=O)=O UGWKCNDTYUOTQZ-UHFFFAOYSA-N 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 239000003292 glue Substances 0.000 description 2
- 229960004488 linolenic acid Drugs 0.000 description 2
- KQQKGWQCNNTQJW-UHFFFAOYSA-N linolenic acid Natural products CC=CCCC=CCC=CCCCCCCCC(O)=O KQQKGWQCNNTQJW-UHFFFAOYSA-N 0.000 description 2
- VUZPPFZMUPKLLV-UHFFFAOYSA-N methane;hydrate Chemical compound C.O VUZPPFZMUPKLLV-UHFFFAOYSA-N 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 230000005012 migration Effects 0.000 description 2
- 235000019198 oils Nutrition 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000006318 protein oxidation Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 239000012488 sample solution Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 2
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 2
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 2
- 235000015112 vegetable and seed oil Nutrition 0.000 description 2
- KPYXMALABCDPGN-HYOZMBHHSA-N (4s)-5-[[(2s)-6-amino-1-[[(2s,3s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2r)-1-[[2-[[2-[[(1s)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]a Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN)CC1=CC=C(O)C=C1 KPYXMALABCDPGN-HYOZMBHHSA-N 0.000 description 1
- 241000209035 Ilex Species 0.000 description 1
- 235000003332 Ilex aquifolium Nutrition 0.000 description 1
- 235000002710 Ilex cornuta Nutrition 0.000 description 1
- 241001310146 Ilex cornuta Species 0.000 description 1
- 235000002296 Ilex sandwicensis Nutrition 0.000 description 1
- 235000002294 Ilex volkensiana Nutrition 0.000 description 1
- OYHQOLUKZRVURQ-HZJYTTRNSA-N Linoleic acid Chemical compound CCCCC\C=C/C\C=C/CCCCCCCC(O)=O OYHQOLUKZRVURQ-HZJYTTRNSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 235000010326 Osmanthus heterophyllus Nutrition 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 239000001045 blue dye Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 235000004626 essential fatty acids Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 201000001421 hyperglycemia Diseases 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 235000020778 linoleic acid Nutrition 0.000 description 1
- OYHQOLUKZRVURQ-IXWMQOLASA-N linoleic acid Natural products CCCCC\C=C/C\C=C\CCCCCCCC(O)=O OYHQOLUKZRVURQ-IXWMQOLASA-N 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000003360 nephrocyte Anatomy 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 235000021590 normal diet Nutrition 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000004988 splenocyte Anatomy 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
Classifications
-
- 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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/54—Improvements relating to the production of bulk chemicals using solvents, e.g. supercritical solvents or ionic liquids
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Plant Substances (AREA)
Abstract
The invention discloses a kind of preparation methods of hypoglycemic tree peony active peptide, it is specific as follows, using the peony seeds dregs of rice with kind skin as raw material, tree peony albumen is first obtained by extraction, complex enzyme is added into tree peony protein solution, the complex enzyme is neutral proteinase, trypsase, aminopeptidase, the tree peony active peptide obtained after enzymatic hydrolysis is embedded with cyclodextrin, remove acid, peptide bond in tree peony albumen, under neutral proteinase and the effect of trypsase these two types endopeptidase, protein is hydrolyzed to polypeptide inside peptide chain, trypsin hydrolysis carboxyl side is basic amino acid polypeptide, the tree peony active peptide of hydrolysis contains IGF-I growth factor, aminopeptidase can act on amino terminal, bitter peptide containing hydrophobic amino acid structure is thoroughly degraded to amino acid, the male of specified molecular weight 1000Da-1500Da is obtained after enzymatic hydrolysis Red active peptide, yield have the function of tree peony active peptide hypoglycemic, are confirmed by zoopery in 95% or more, IGF-I growth factor.
Description
Technical field
The invention belongs to food processing technology fields, are related to a kind of preparation method of hypoglycemic tree peony active peptide.
Background technique
Incomplete statistics data show that China is now with 94,000,000 diabetics, in other words, average every 10 adults
Just there is 1 diabetic in people, blood glucose refers to the glucose content in blood, and energy needed for internal each cellular activity is big
Majority comes from glucose, thus blood glucose it is necessary to keep must it is horizontal could each organ and movable demand in keeping body, just
The fasting plasma glucose concentration of ordinary person is 3.9~6.1 mM/ls, if surmounting 7.0 mM/ls is known as hyperglycemia, normal condition
Under, human body can ensure that the source of blood glucose and outlet keep balancing by hormone control and nerve modulation this two big regulating system,
Blood glucose is set to maintain certain level, but under the collective effect of inherent cause and environmental factor, two big regulatory functions occur disorderly
Disorderly, it just will appear the raising of blood glucose level.
Tree peony is the fallen leaves undershrub of Paeonia, is one of the Wild related germplasm of Chinese cultivated Varieties of Peony, peony can
With edible, unsaturated fatty acid rich in peony seed oil has very important health care and medicinal value, peony seeds
Unsaturated fatty acid content is up to 87.60% in oil, wherein linoleic content accounts for 22.19%, linolenic acid accounts for 35.70%, oil
Acid accounts for 27.14%, and linoleic acid plus linolenic acid is essential fatty acid, has reducing blood lipid, norcholesterol and promotion fatty generation
It thanks, enhancing is immune, and the physiological activity such as prevention coronary heart disease, in recent years, peony seed oil uses more and more, the discarded pair of generation
The product peony seeds dregs of rice also increase therewith, how the reasonable utilization peony seeds dregs of rice, be a more and more important research topic.
Summary of the invention
It is an object of the invention to overcome the above problem, the method that specified molecular weight tree peony active peptide can be obtained is developed,
This method preparation safety, simple process are not had to be classified using ultrafiltration, improve preparation efficiency, reduce production cost.
The purpose of the present invention is achieved by the following technical programs:
A kind of preparation method of hypoglycemic tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:20~30 with water,
NaOH is added and adjusts pH9~10,60~70min of magnetic agitation under the conditions of 50~60 DEG C, be centrifuged (3500~4000r/min, 13
~18min), supernatant is taken, HCl is added, adjusts pH3.0~4.0, is centrifuged (3500~4000r/min, 13~18min), is sunk
Shallow lake is freeze-dried after being cleaned with a small amount of deionized water to neutrality, obtains peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
1~3 part of protease, 3~5 parts of trypsase, 6~7 parts of aminopeptidase, 90~110u/mL of enzyme activity, enzyme digestion reaction pH be 6.0~
7.0,40~50 DEG C of reaction temperature, 3~4h of reaction time, after enzymatic hydrolysis, 10%~15% HCl is added in high-temperature inactivation, is adjusted
PH to 4.0~4.5 is stirred under the conditions of 50~70r/min, and the tree peony albumen not digested is precipitated in curdy, filtering point
From being spray-dried to obtain tree peony active peptide after purification, SDS-PAGE electrophoretic determination tree peony bioactive peptide molecule amount is 1000Da-
Between 1500Da, the yield of 1000Da-1500Da tree peony active peptide is calculated 95% or more with Kjeldahl's method.
Protein is hydrolyzed to polypeptide, trypsase inside peptide chain by neutral proteinase and trypsase these two types endopeptidase
Hydrolysis carboxyl side is basic amino acid polypeptide, and the tree peony active peptide of hydrolysis contains IGF-I growth factor, and aminopeptidase can act on
In amino terminal, the bitter peptide containing hydrophobic amino acid structure is thoroughly degraded to amino acid.
Preferably, the tree peony albumen seed dregs of rice are the raw material with kind skin, have part soluble component to be miscible in kind skin male
It is that tree peony peptide activity is higher in red peptide.
Preferably, step S1 peony seeds crushed 80~100 meshes.
Preferably, it is 150~160 DEG C that inlet temperature is spray-dried in the step S2, and outlet temperature is 50~60 DEG C.
Preferably, the enzyme digestion reaction pH value is 6.5, and reaction temperature is 45 DEG C, reaction time 2.5h.
Preferably, the enzymolysis liquid high-temperature inactivation temperature is 85~95 DEG C, 15-20min.
Preferably, the tree peony active peptide carries out embedding treatment with cyclodextrin, removes acid.
Another object of the present invention is to provide a kind of tree peony active peptides being prepared by the above method.
Another object of the present invention is to provide a kind of purposes of above-mentioned tree peony active peptide, IGF- in the tree peony active peptide
I growth factor is a kind of activated protein peptide material, is present in human hepatocyte, nephrocyte, in the various kinds of cell such as splenocyte,
There are this factors for human body itself, can be used for hypoglycemic.
The present invention has following technical effect that compared with prior art
The peony seeds dregs of rice with kind skin are used to prepare peony seeds albumen for raw material, complex enzyme is added into peony seeds protein liquid,
The complex enzyme is 1~3 part of neutral proteinase, 3~5 parts of trypsase, 6~7 parts of aminopeptidase, and after enzymatic hydrolysis, enzymolysis liquid high temperature goes out
It is living, using being spray-dried after the heavy method of acid, tree peony active peptide between 1000Da-1500Da is obtained, for yield 95% or more, gained is male
Red active peptide contains IGF-I growth factor, can act on human body, there is hypoglycemic effect.
Specific embodiment
Present invention will be further explained below with reference to specific examples.These embodiments are merely to illustrate the present invention and do not have to
In limiting the scope of the invention.Test method without specific conditions in lower example embodiment, usually according to this field conventional strip
Part or the condition suggested according to manufacturer.Those skilled in the art is done any insubstantial on the basis of the present invention
The variation and replacement of property belong to scope of the present invention.
Embodiment 1
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
1 part of protease, 3 parts of trypsase, 6 parts of aminopeptidase, enzyme activity 107u/mL, enzyme digestion reaction pH be 6.0,45 DEG C of reaction temperature,
Reaction time 3.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 96.3% between 1000Da-1500Da is spray-dried to obtain after purification.
Embodiment 2
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
2 parts of protease, 4 parts of trypsase, 6.5 parts of aminopeptidase, enzyme activity 101u/mL, enzyme digestion reaction pH are 6.5, reaction temperature 45
DEG C, reaction time 3.5h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min
It mixes, is separated by filtration, tree peony active peptide, yield 95.9% between 1000Da-1500Da are spray-dried to obtain after purification.
Embodiment 3
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
Protease 3 part, 5 parts of trypsase, 7 parts of aminopeptidase, enzyme activity 99u/mL, enzyme digestion reaction pH be 7.0,45 DEG C of reaction temperature,
Reaction time 4.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 95.4% between 1000Da-1500Da is spray-dried to obtain after purification.
Comparative example 1
A kind of preparation method of tree peony active peptide, the method step are
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
1 part of protease, 1 part of trypsase, 1 part of aminopeptidase, enzyme activity 39u/mL, enzyme digestion reaction pH be 6.0,45 DEG C of reaction temperature,
Reaction time 3.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 31.2% between 1000Da-1500Da is spray-dried to obtain after purification.
Comparative example 2
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
1 part of protease, 2 parts of trypsase, 3 parts of aminopeptidase, enzyme activity 43u/mL, enzyme digestion reaction pH be 7.0,45 DEG C of reaction temperature,
Reaction time 4.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 36.4% between 1000Da-1500Da is spray-dried to obtain after purification.
Comparative example 3
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
Protease 3 part, 3 parts of trypsase, 3 parts of aminopeptidase, enzyme activity 37u/mL, enzyme digestion reaction pH be 7.0,45 DEG C of reaction temperature,
Reaction time 4.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 41.7% between 1000Da-1500Da is spray-dried to obtain after purification.
Comparative example 4
A kind of preparation method of tree peony active peptide, the method step be,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:25 with water, is added
NaOH adjusts pH9.4, and magnetic agitation 67min under the conditions of 55 DEG C is centrifuged (3800r/min, 15min), takes supernatant, is added
HCl adjusts pH3.5, is centrifuged (3800r/min, 15min), and precipitating is freeze-dried after being cleaned with a small amount of deionized water to neutrality,
Obtain peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, and the compound protease includes neutrality
4 parts of protease, 2 parts of trypsase, 1 part of aminopeptidase, enzyme activity 48u/mL, enzyme digestion reaction pH be 5.0,45 DEG C of reaction temperature,
Reaction time 3.0h, after enzymatic hydrolysis, 13% HCl is added in high-temperature inactivation, is adjusted pH to 4.5, is stirred under the conditions of 60r/min,
It is separated by filtration, tree peony active peptide, yield 31.8% between 1000Da-1500Da is spray-dried to obtain after purification.
Embodiment 1-3, the reaction result of comparative example 1-4, as shown in table 1.
Table 1 takes 3 parts of tree peony albumen, the preparation yield of tree peony active peptide under the conditions of differential responses
Experimental example 1
SDS-PAGE electrophoretic determination protein relative molecular mass
(1) instrument, raw materials and reagents
Instrument: vertical version type electrophoresis tank;D.C. regulated power supply;50uL pipette tips, glass plate, water-bath, staining trough, beaker,
Pipette, dropper.
Raw material: 0.5mg/mL sample solution
Reagent: Tris-HCl pH of buffer 8.9, Tris-HCl pH of buffer 6.7,30% separation gel liquid storage, 10% concentration
Glue liquid storage, 10%SDS solution, dyeing liquor, destainer.
(2) experimental procedure
1, electrophoresis tank is installed
2, match glue
3, gel slab is prepared
4, sample treatment and sample-adding
0.5mg/mL sample solution and standard protein liquid boiling water bath are heated 3 minutes, be cooled to room temperature it is spare, by 15uL
Sample is carefully added to gel spill sample trench bottom, to all add sample in all spill sample cells, starts electrophoresis.
5, electrophoresis
Electrophoresis apparatus is opened, electric current is transferred to 10mA.When sample separation, electric current is adjusted to 25mA, when blue dyes migrates
To bottom, electric current is set to zero, and closes power supply, pulls out fixed plate, takes out glass plate, one block of glass is gently pried open shifting with blade
It goes, makes marks in offset plate one end, dye.
6, it dyes and decolourizes
Dyeing liquor is poured into culture dish, dyeing 1h or so for several times, then with destainer is decolourized with distilled water rinsing, until
Zone of protein is clear, measures each band at a distance from gel top with ruler.
7, it calculates
It is mapped with the logarithm of standard protein molecular weight to relative mobility, standard curve is obtained, according to sample to be tested phase
To mobility, its molecular weight can be found out from standard curve.
Relative mobility mR=sample migration distance (cm)/dye migration distance (cm)
Experimental example 2
Kjeldahl nitrogen determination activity peptide yield
(1) nitrogen content in protein is measured
By protein and concentrated sulfuric acid heat together, catalyst sulfuric acid copper is added thereto, sulfuric acid decomposition is sulfur dioxide, water and original
Sub- state oxygen, protein oxidation is carbon dioxide and water, and nitrogen therein changes ammonification, and further generates ammonium sulfate;It has reacted
NaOH is added after complete, NH4+ is changed into NH3, and NH3 is imported in excessive boric acid solution by distilling, is dripped by standard hydrochloric acid
Fixed, the standard hydrochloric acid molal quantity for titrating consumption is the molal quantity of NH3, i.e., the content M of nitrogen in protein.
(2) nitrogen content in active peptide is measured
By active peptide and concentrated sulfuric acid heat together, catalyst sulfuric acid copper is added thereto, sulfuric acid decomposition is sulfur dioxide, water and original
Sub- state oxygen, protein oxidation is carbon dioxide and water, and nitrogen therein changes ammonification, and further generates ammonium sulfate;It has reacted
NaOH is added after complete, NH4+ is changed into NH3, and NH3 is imported in excessive boric acid solution by distilling, is dripped by standard hydrochloric acid
Fixed, the standard hydrochloric acid molal quantity for titrating consumption is the molal quantity of NH3, the content m of nitrogen as in active peptide.
Nitrogen content M*100% in nitrogen content m/ protein in active peptide yield=active peptide
Experimental example 3
Animal experiment is carried out to rat using tree peony active peptide prepared by embodiment 1, by check experiment, it is living to investigate tree peony
Property peptide to test rat therapeutic effect.
Healthy adult rat is selected, normal diet group (Normal group, 10) and high lipid food group (100 are randomly divided into
Only), after persistently feeding 30 days, high lipid food group disposably injects alloxan 25mmol/L, rats in normal control group injection etc.
Chinese holly edge acid sodium-Chinese holly edge acid buffer of amount;Type II diabetes model is considered as with 16mmol/L≤blood glucose < 30mmol/L person after 3d
Rat modeling success, is randomly divided into eight groups (every group 10): model control group (water stomach-filling) for successful 80 rats of modeling,
(high dose group dosage is 100mg/kg, middle dose group to the high, medium and low dosage group of peony seeds active peptide prepared by embodiment 1
Tree peony active peptide for 50 mg/kg, low dose group 25mg/kg, stomach-filling), comparative example 1-4 preparation (all uses high dose group
100 mg/kg, stomach-filling).Stomach-filling 10 days, monitoring experiment rat indices surveyed fasting blood sugar.
Data processing is carried out using SPSS16.0 statistical software, experimental data is indicated with mean ± standard deviation (± s), is used
T is examined, inspection level a=0.05.As shown in table 2.
Influence of the 2 peony seeds active peptide of table to type II diabetes rat blood sugar
The word of such as "include", "comprise", " having " etc. is open vocabulary in the disclosure, refer to " including but it is unlimited
In ", and can be used interchangeably with it.Vocabulary "or" and "and" used herein above refer to vocabulary "and/or", and can exchange and make with it
With unless it is not such that context, which is explicitly indicated,.Vocabulary " such as " used herein above refer to phrase " such as, but not limited to ", and
It can be used interchangeably with it.
In addition, as used herein, the "or" instruction separation used in the enumerating of the item started with "at least one"
Enumerate, for example, " at least one of A, B or C " enumerate mean A or B or C or AB or AC or BC or ABC (i.e. A and B and
C).In addition, wording " exemplary " does not mean that the example of description is preferred or more preferable than other examples.
The above description of disclosed aspect is provided so that any person skilled in the art can make or use this
It is open.Various modifications in terms of these are readily apparent to those skilled in the art, and are defined herein
General Principle can be applied to other aspect without departing from the scope of the present disclosure.Therefore, the disclosure is not intended to be limited to
Aspect shown in this, but according to principle disclosed herein and the consistent widest range of novel feature.
Above description is had been presented for for purposes of illustration and description.In addition, this description is not intended to the reality of the disclosure
It applies example and is restricted to form disclosed herein.Although already discussed above multiple exemplary aspects and embodiment, this field skill
Its certain modifications, modification, change, addition and sub-portfolio will be recognized in art personnel.
Claims (9)
1. a kind of preparation method of hypoglycemic tree peony active peptide, which is characterized in that the method step is,
S1: the peony seeds dregs of rice are crushed, supercritical CO is used2Degreasing is extracted, sieving is mixed by solid-liquid ratio 1:20~30 with water, is added
NaOH adjusts pH9~10,60~70min of magnetic agitation under the conditions of 50~60 DEG C, be centrifuged (3500~4000r/min, 13~
18min), supernatant is taken, HCl is added, adjusts pH3.0~4.0, is centrifuged (3500~4000r/min, 13~18min), precipitating is used
A small amount of deionized water is freeze-dried after cleaning to neutrality, obtains peony seeds albumen;
S2: taking obtained by step S1 3 parts of albumen, and compound protease is added and is digested, the compound protease includes neutral protein
1~3 part of enzyme, 3~5 parts of trypsase, 6~7 parts of aminopeptidase, 90~110u/mL of enzyme activity, enzyme digestion reaction pH are 6.0~7.0,
40~50 DEG C of reaction temperature, 3~4h of reaction time, after enzymatic hydrolysis, 10%~15% HCl is added in high-temperature inactivation, adjust pH to
4.0~4.5, it stirs, is separated by filtration under the conditions of 50~70r/min, tree peony active peptide is spray-dried to obtain after purification.
2. the preparation method of hypoglycemic tree peony active peptide according to claim 1, which is characterized in that the tree peony albumen seed
The dregs of rice are the raw material with kind skin.
3. the preparation method of hypoglycemic tree peony active peptide according to claim 1, which is characterized in that step S1 peony seeds powder
Broken 80~100 mesh of mistake.
4. the preparation method of hypoglycemic tree peony active peptide according to claim 1, which is characterized in that sprayed in the step S2
The dry inlet temperature of mist is 150~160 DEG C, and outlet temperature is 50~60 DEG C.
5. the preparation method of hypoglycemic tree peony active peptide according to claim 1, which is characterized in that the enzyme digestion reaction pH
Value is 6.5, and reaction temperature is 45 DEG C, reaction time 2.5h.
6. the preparation method of hypoglycemic tree peony active peptide according to claim 1, which is characterized in that the enzymolysis liquid high temperature
Inactivation temperature is 85~95 DEG C, 15-20min.
7. the preparation method of tree peony hypoglycemic activity peptide according to claim 1, which is characterized in that the tree peony active peptide is used
Cyclodextrin carries out embedding treatment.
8. the tree peony active peptide that any one of claim 1-7 the method is prepared.
9. tree peony active peptide described in claim 8 is in preparation for the application in hypoglycemic product.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201910432490.5A CN110218755A (en) | 2019-05-23 | 2019-05-23 | A kind of preparation method of hypoglycemic tree peony active peptide |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201910432490.5A CN110218755A (en) | 2019-05-23 | 2019-05-23 | A kind of preparation method of hypoglycemic tree peony active peptide |
Publications (1)
Publication Number | Publication Date |
---|---|
CN110218755A true CN110218755A (en) | 2019-09-10 |
Family
ID=67818170
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201910432490.5A Pending CN110218755A (en) | 2019-05-23 | 2019-05-23 | A kind of preparation method of hypoglycemic tree peony active peptide |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN110218755A (en) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN112795613A (en) * | 2021-04-06 | 2021-05-14 | 西北大学 | Peony seed meal-derived blood sugar-reducing polypeptide and application thereof |
CN112891509A (en) * | 2021-01-28 | 2021-06-04 | 衍生健康医药(广东)有限公司 | Seven-star tea granules and preparation method thereof |
CN116478261A (en) * | 2023-04-27 | 2023-07-25 | 山东牡丹爱生物科技有限公司 | Anti-fatigue antioxidant peony peptide and preparation method thereof |
Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN104017850A (en) * | 2014-06-26 | 2014-09-03 | 河南科技大学 | Method for preparing peony small peptides from peony seed cakes and application of peony small peptides |
CN105624251A (en) * | 2016-03-09 | 2016-06-01 | 江苏科技大学 | Peony seed blood sugar decreasing peptide and purification method and application thereof |
US20170182107A1 (en) * | 2014-05-23 | 2017-06-29 | Korea Institute Of Oriental Medicine | Pharmaceutical composition for preventing or treating diabetic complications and angioedema, containing natural mixture extract as active ingredient |
CN108823273A (en) * | 2018-07-09 | 2018-11-16 | 齐鲁工业大学 | A kind of peony seeds dregs of rice polypeptide and its preparation method and application with antioxidant activity |
CN109111497A (en) * | 2018-09-06 | 2019-01-01 | 武汉轻工大学 | A kind of method for producing of peony seeds albumen |
-
2019
- 2019-05-23 CN CN201910432490.5A patent/CN110218755A/en active Pending
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US20170182107A1 (en) * | 2014-05-23 | 2017-06-29 | Korea Institute Of Oriental Medicine | Pharmaceutical composition for preventing or treating diabetic complications and angioedema, containing natural mixture extract as active ingredient |
CN104017850A (en) * | 2014-06-26 | 2014-09-03 | 河南科技大学 | Method for preparing peony small peptides from peony seed cakes and application of peony small peptides |
CN105624251A (en) * | 2016-03-09 | 2016-06-01 | 江苏科技大学 | Peony seed blood sugar decreasing peptide and purification method and application thereof |
CN108823273A (en) * | 2018-07-09 | 2018-11-16 | 齐鲁工业大学 | A kind of peony seeds dregs of rice polypeptide and its preparation method and application with antioxidant activity |
CN109111497A (en) * | 2018-09-06 | 2019-01-01 | 武汉轻工大学 | A kind of method for producing of peony seeds albumen |
Non-Patent Citations (2)
Title |
---|
郑建仙: "《现代功能性粮油制品开发》", 31 May 2003, 科学技术文献出版社 * |
颜辉等: "超声酶解制备牡丹籽降血糖肽的响应面优化研究", 《食品工业科技》 * |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN112891509A (en) * | 2021-01-28 | 2021-06-04 | 衍生健康医药(广东)有限公司 | Seven-star tea granules and preparation method thereof |
CN112795613A (en) * | 2021-04-06 | 2021-05-14 | 西北大学 | Peony seed meal-derived blood sugar-reducing polypeptide and application thereof |
CN116478261A (en) * | 2023-04-27 | 2023-07-25 | 山东牡丹爱生物科技有限公司 | Anti-fatigue antioxidant peony peptide and preparation method thereof |
CN116478261B (en) * | 2023-04-27 | 2023-10-27 | 德州蓝力生物技术有限公司 | Anti-fatigue antioxidant peony peptide and preparation method thereof |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
EP3228625B1 (en) | Preparation method for water-soluble conchiolin and acid-soluble conchiolin | |
CN110218755A (en) | A kind of preparation method of hypoglycemic tree peony active peptide | |
CN103667408B (en) | A kind of method utilizing wheat protein to prepare intestine nutritive peptide | |
CN105018555A (en) | Preparation method of giant salamander skin collagen peptide | |
CN1932027A (en) | Double enzyme hydrolysis process for preparing soybean peptide without bitter | |
CN110218240B (en) | Tyrosinase inhibitory peptide and application thereof | |
CN101974589A (en) | Method for preparing immunocompetent soybean peptide by enzymolysis and membrane separation | |
CN102018727A (en) | Preparation method of pearl hydrolysate | |
CN105420325B (en) | A kind of preparation method of placenta polypeptide | |
CN110477381A (en) | A kind of albumin amino acid Calcium oral liquid prescription and preparation method with immunological regulation healthcare function | |
CN100402548C (en) | Method for preparing physiological active polypeptide of deer placenta | |
CN107095312A (en) | A kind of krill polypeptide formulations with reducing blood lipid ability and preparation method thereof | |
CN106075384B (en) | Pea active peptide is inhibiting the application and preparation method thereof in growth of cancer cells | |
CN101649341A (en) | Method for extracting protein peptide from membranes of fowl eggshells | |
CN105111277A (en) | Preparation method of ginseng peptide | |
CN110257460A (en) | A kind of preparation method of the tree peony protein peptides of blood pressure lowering | |
CN102732591B (en) | Preparation method of soybean whey polypeptides with liver protection and antioxidation effects | |
CN111690704A (en) | Preparation method and application of pilose antler polypeptide | |
CN106868082A (en) | The preparation method of Cerebrolysin Vial in a kind of new ginseng Soviet Union capsule for tonifying kidney | |
CN105029449A (en) | Healthcare food | |
CN110205352A (en) | A kind of preparation method of tree peony protein peptides | |
CN110229860A (en) | A kind of Animal Skin small-molecular peptides preparation method promoting Marrow Stromal Cells in Proliferation | |
CN1240297C (en) | Peptide milk and its preparation technology | |
CN107789307A (en) | Double enzyme enzymatic hydrolysis and fermentation liquid of pea and preparation method and application | |
CN113208118A (en) | Preparation method of low-bitter-taste antioxidant peptide beverage |
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 |