CN104356200B - A kind of anti-oxidation peptide and preparation method thereof - Google Patents
A kind of anti-oxidation peptide and preparation method thereof Download PDFInfo
- Publication number
- CN104356200B CN104356200B CN201410614557.4A CN201410614557A CN104356200B CN 104356200 B CN104356200 B CN 104356200B CN 201410614557 A CN201410614557 A CN 201410614557A CN 104356200 B CN104356200 B CN 104356200B
- Authority
- CN
- China
- Prior art keywords
- polypeptide
- sea cucumber
- antioxidation
- oxidation peptide
- food
- 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.)
- Active
Links
Abstract
The invention provides a kind of anti-oxidation peptide and preparation method thereof, this method by the enzymolysis to acid protease, isolates and purifies to obtain specific anti-oxidative peptide, its overall amino acid sequence is using sea cucumber meat or sea cucumber visceral protein as raw material：GAVLGTY.Anti-oxidation peptide produced by the present invention makes up defect possessed by natural, and eliminates worry of the public to artificial synthesized antioxidant, is laid a good foundation to develop anti-oxidation peptide based on food source and exploring its extensive use in food, medicine.
Description
Technical field
The invention belongs to biological technical field, and in particular to a kind of antioxidation polypeptide and preparation method thereof.
Background technology
The oxidation of biomolecule is the process of a free radical mediated, and it is many unfavorable that it can be caused to food and biosystem
Influence.In aerobic organ, the free free radical related to a variety of diseases such as artery sclerosis, cancer can inevitably with
The process of oxygen metabolism and produce.In food, the oxidation of nutritional ingredient can produce peroxide, and it can not only influence the battalion of food
Value is supported, causes food quality to decline, disease occurs for the serious body for even also resulting in intake person.Therefore, safety is found
Antioxidant with suppress peroxide produce be always biochemical nutrition study hotspot.Due to chemical syntheses such as BHT, TBHQ
Antioxidant has more preferable effect and less expensive price than natural, therefore it has been widely used in food
In industry.But at present studies have found that synthetized oxidation preventive agent has accumulative carcinogenesis to organs such as human liver, spleen, lungs,
So as to cause worry of the people to its security, and start gradually to limit its use in food.Then people are mesh
Light turns to natural.Alpha-tocopherol is a kind of natural being commonly used, and it effectively can be kept in food
The stability of grease, but it is unfavorable for food preservation.Therefore, we are necessary to find a kind of the safe natural of other sources
Antioxidant.
Polypeptide is a kind of compound of the molecular structure between amino acid and protein, protein is had certain life
Manage function.In the vital movement of the mankind, peptide digesting and assimilating better than free amino acid in vivo, and it is different from amino
Delivery system inside acid.Some small peptides are while nutriment necessary to providing growth in humans, development, additionally it is possible to diseases prevention
Cure the disease, adjust function of human body, there is the polypeptide of bioactivity to be referred to as biologically active peptide for these.Research is found, many different next
The polypeptide in source all has oxidation resistance, such as caseinhydrolysate, soybean protein, bovine serum albumin(BSA), ovalbumin, oilseed
The polypeptide that albumen, wheat gliadin and zein etc. obtain all has certain inoxidizability.
Domestic Holothurian machining rests on the primary process segment mostly at present, and because resource utilization is low, process produces
Leftover bits and pieces waste etc. reason cause the wasting of resources, even environmental pollution.Contain a large amount of albumen in sea cucumber meat or sea cucumber internal organ
Matter, and its composition is balanced, deep processing is carried out to protein resource therein using modern biotechnology, reasonably from enzyme
Deng the research of antioxidation active peptides is had into broader prospect by process optimization.
The content of the invention
May it is an object of the invention to the deficiency for natural and the security of artificial synthesized antioxidant
A kind of sorrow, there is provided antioxidation polypeptide and preparation method thereof.Antioxidation polypeptide antioxidation activity produced by the present invention is high, compensate for day
The defects of right antioxidant, eliminate worry of the people to artificial synthesized antioxidant security.
In order to realize goal of the invention, the present invention adopts the following technical scheme that：
A kind of antioxidation polypeptide, its amino acid sequence are：GAVLGTY.
A kind of method for preparing antioxidation polypeptide as described above：Albumen is extracted as raw material using sea cucumber meat or sea cucumber internal organ,
Then it is digested；The concentrated sea cucumber polypeptide solution that cleans to obtain of enzymolysis product, sea cucumber polypeptide solution is through isolating and purifying, freezing
It is dried to obtain antioxidation polypeptide.
The enzymatic hydrolysis condition is：PH is 3.5, temperature 50 C, enzymolysis time are 6 h, enzyme-substrate proportioning is 3000U/g；Institute
It is acid protease to state enzyme.
The method isolated and purified includes ultrafiltration, SP-Sephadex C-25 ion-exchange chromatographies, Sephadex G-50
Molecular sieve and RP-HPLC RPLCs.
It is described isolate and purify concretely comprise the following steps：
（1）Ultra-filtration and separation is carried out to sea cucumber polypeptide solution first with membrane filtration system, obtains the polypeptide of different molecular weight
Component；
（2）The component with optimal antioxidation activity is collected, is carried out with SP-Sephadex C-25 cation-exchange chromatographies
Separate, unadsorbed component is washed away after loading, then linear gradient elution, flow velocity 0.5ml/ are carried out with acetic acid-sodium acetate buffer solution
Min, measured under 215nm, determine the antioxidation activity of elution fraction corresponding to each absworption peak；
（3）The component with optimal antioxidation activity is collected, is separated with Sephadex G-50 gel chromatographies, is eluted
Liquid is deionized water, flow velocity 0.5ml/min, is measured under 215nm, determines the anti-of elution fraction corresponding to each absworption peak
Oxidation activity；
（4）The component with optimal antioxidation activity is collected, is carried out using RP-HPLC RPLCs further
Separation, gradient elution is then carried out using the mixed liquor of acetonitrile and water, collected volume is than for washing at 24% acetonitrile and 76% water
De- peak, obtains antioxidation polypeptide；
（5）Utilize the amino acid sequence of proteinaceous solid facies sequence analysis instrument identification polypeptide.
Step（1）Described in polypeptide fractions include molecular weight >=3000 Da, 1500-3000 Da ,≤1500 Da group
Point.
Step（2）Described in acetic acid-sodium acetate buffer solution concentration be 0.02mol/L, pH4.5, containing 0~0.35mol/L
NaCl。
Step（4）Chromatographic column used is the μ C18 of Gemini 5 during middle separation, and applied sample amount is 100 μ L, flow velocity 1ml/min,
Detection wavelength is 215nm.
Step（4）Middle gradient elution is：The self-contained volume ratio of eluent starts for the mixed liquor of 10% acetonitrile and 90% water, to body
Product for the mixed liquor of 90% acetonitrile and 10% water than terminating.
The present invention, using sea cucumber albumen as starting point, passes through acid egg based on a kind of antioxidant of efficiency natural is found
The cutting condition control of white enzyme, the active peptides with specific peptide chain length and domain composition are cut into, and made anti-oxidant
Activity is efficiently realized.
The beneficial effects of the present invention are：
The present invention changes the extraction of existing antioxidant and the idea and method used, and eliminates artificial synthesized anti-oxidant
Side effect caused by agent institute is possible, separated obtained antioxidation polypeptide can substitute traditional synthetized oxidation preventive agent；And this
Invention further improves China's situation relatively low to sea cucumber protein utilization rate, and efficient utilize that can have both solved a large amount of Holothurian Resources is asked
Topic, and can release consumer to antioxidant in the misgivings of food security aspect, and the development to science and technology, economy and food industry has
There is far reaching significance.
Brief description of the drawings
Fig. 1 is the RP-HPLC collection of illustrative plates of antioxidation polypeptide, and A peaks are the chromatographic peak of antioxidation polypeptide；
Fig. 2 is that the antioxidation polypeptide of purifying removes " amount-effect " relation curve of DPPH free radicals；
Fig. 3 is that the antioxidation polypeptide of purifying removes " amount-effect " relation curve of ABTS free radicals；
Fig. 4 is that the antioxidation polypeptide of purifying suppresses Fe2+Induce lipovitellinin polyunsaturated fatty acid peroxidization
" amount-effect " relation curve.
Embodiment
The preparation method of antioxidation polypeptide is as follows：
(1) extraction of sea cucumber albumen
Sea cucumber Protein Extraction process conditions are：
Sea cucumber or sea cucumber internal organ are cleaned 3-5 times, extraction pH is 7.0, and Extracting temperature is 40-80 DEG C, solid-liquid ratio 1:
4-1:8 （Weight ratio）, extraction time is 2-6 h, centrifugation 10000g 20 minutes, collects supernatant, filtered, concentration and freezing
Sea cucumber albumen is obtained after drying.
(2) enzymolysis of sea cucumber albumen
Enzyme is purchased from Shanghai biological reagent company（Chinese Shanghai）.
Sea cucumber albumen, protein concentration 30mg/ml are digested using acid protease, enzymatic hydrolysis condition takes pH as 3.5, temperature 50
DEG C, enzymolysis time 6h, enzyme-to-substrate ratio be（3000U/g）, it is stable with 2M HCl regulations pH, after hydrolyzing 6h, gone out in boiling water bath
Enzyme 15min, is then rapidly cooled to room temperature, is placed in a centrifuge, and centrifuges 15min with 4000r/min, takes supernatant standby.
（3）The concentration and removal of enzymolysis product
After being concentrated using nanofiltration system to protein enzymatic hydrolyzate, 4 times of volume ethanol sedimentation macro-molecular proteins are added,
It is sea cucumber polypeptide solution that 12000r/min centrifugations 20min, which obtains supernatant,.
（4）The separation of enzymolysis product
Ultra-filtration and separation is carried out to sea cucumber polypeptide solution using membrane filtration system, the different ultrafiltration of scope is retained using molecular weight
Film separates to enzymolysis product, obtains the polypeptide of different molecular weight, including >=3000 Da, 1500-3000 Da, and≤1500
The components such as Da.
（5）The purifying of enzymolysis product
Obtained enzymolysis product is divided into 3 different components of molecular weight ranges, respectively molecular weight is more than 3000Da's
Component, molecular weight are between component of the 1500Da and 3000Da component, molecular weight less than 1500Da；Collect with optimal anti-oxidant
The component of activity, then by SP-Sephadex C-25 cation-exchange chromatographies（Long 20cm, diameter 1.6cm）Separated, with
The 0.02mol/L of the NaCl containing 0~0.35mol/L, pH4.5 acetic acid-sodium acetate buffer solutions carry out linear gradient elution, and flow velocity is
0.5ml/min；The component with optimal antioxidation activity is collected, then with Sephadex G-50（Long 100cm, diameter 2.6cm）It is solidifying
Glue chromatogram is separated, and eluent is deionized water, flow velocity 0.5ml/min, and eluting peak measures under 215nm；Collect
Component with optimal antioxidation activity, further separated using RP-HPLC RPLCs, color used
Spectrum post is the μ C18 of Gemini 5, and applied sample amount is 100 μ L, flow velocity 1ml/min, Detection wavelength 215nm.Eluent self-contained 10%
Acetonitrile and 90% water（v/v）Mixed liquor start, to 90% acetonitrile and 10% water（v/v）Mixed liquor terminate, carry out gradient elution,
Collect 24 % acetonitriles and 76 % water（v/v）The eluting peak at place, obtain the antioxidation polypeptide of the high-purity of the present invention.
（6）The determined amino acid sequence of antioxidation polypeptide
Utilize proteinaceous solid facies sequence analysis instrument (Applied Biosystems Model 476A, Perkin Elmer
Co. MA, U.S.A) overall amino acid sequence of antioxidation polypeptide of the measure present invention is GAVLGTY.
（7）The test of antioxidation activity
The measure of I DPPH radical scavenging activities
Utilize DPPH（1,1-Diphenyl-2-picryl-hydrazyl）Free radical scavenging activity determination method research is anti-oxidant
Polypeptide.Compound concentration is 1 × 10-5Mol/L DPPH ethanol solutions, are kept in dark place.By 2mL, 0.1mM DPPH absolute ethyl alcohols
Solution is added in the clean tube containing 2mL difference enzymolysis samples, is mixed.After placing 30min at room temperature, surveyed at 517 nm
Determine absorbance, light absorption value is smaller, shows that radical scavenging activity is stronger.
In formula, A0For 2 mL, 0.1mM DPPH ethanol solutions+2mL sample solvent, blank control；AiFor 2mL,
0.1mM DPPH ethanol solutions+2mL sample；AjFor the 2mL mL of absolute ethyl alcohol+2 sample.
The measure of II ABTS free radical scavenging activities
ABTS is dissolved with deionized water, ABTS concentration is reached 7mmol/L, potassium peroxydisulfate is added, makes potassium peroxydisulfate
Concentration is 2.45 mmol/L.The solution is placed in dark place 12~16h overnight at room temperature afterwards.By the ABTS free radicals of generation
Solution phosphate buffer（PBS, 0.2 mol/L, pH 7.4）Dilution, it is 0.70 to make its light absorption value under 734nm.Take
0.1ml enzymolysis liquids mix with the free base fluids of 2.9ml ABTS, shake up 30s, and dark place is reacted 10 min, then determined under 734nm
The light absorption value of reaction solution.Blank is made instead of hydrolyzate with distilled water.
In formula, A0The light absorption value of water mixed liquid is distilled for 2.9 mL ABTS reagents and 0.1 mL；AjTried for 2.9 mL ABTS
Agent and the light absorption value of 0.1 mL enzymolysis liquid mixed liquors.
The measure of III anti-peroxidation activity
With isometric fresh egg yolk and phosphate buffer（PH7.4,0.1mol/L）Mixing, use preceding 25 times of dilution
And stirred with magnetic stirrer.2.4ml yolk diluents, 2.4ml 25mmol/L FeSO are separately added into test tube4·
H2O, 200 μ L hydrolyzate samples, water-bath 4h, the addition trichloroacetic acids of 0.8ml 50% and 2ml TBA, mixing at 37 DEG C after mixing
Afterwards in 95 DEG C of constant temperature 30min.After being cooled to room temperature, 8000r/min centrifugation 20min, supernatant is taken to determine extinction under 532nm
Value.Blank is used as instead of hydrolyzate using distilled water.
In formula, A0Absorbance for sky from control group；AjFor the absorbance of sample sets.
In order to further appreciate that present invention, feature and effect, hereby enumerate following examples, but the invention is not restricted to
Lower embodiment.
Embodiment 1
Weigh 5.0 grams of sea cucumber albumen deionized water dissolvings and be settled to 250ml, then adjusted its pH with 2mol/L HCl
Save to 3.0.The solution water-bath is first heated to 50 DEG C, then added according still further to enzyme-substrate proportioning for 3000U/g ratio corresponding
The enzyme of amount, enzymolysis time are 6 hours.Then enzyme deactivation 15 minutes in boiling water bath, 4000rpm is centrifuged 15 minutes again after cooling.Receive
It is standby to collect supernatant.
Supernatant is subjected to ultra-filtration and separation to sea cucumber polypeptide solution using membrane filtration system, scope is retained not using molecular weight
With milipore filter enzymolysis product is separated, obtain the polypeptide of different molecular weight, >=3000 Da, 1500-3000 Da ,≤
1500 Da component, and determine its antioxidation activity.Component of the molecular weight less than 1500Da has best antioxidation activity.
The component that molecular weight is less than 1500Da is collected, with SP-Sephadex C-25 cation-exchange chromatographies（Long 20cm, directly
Footpath 1.6cm）Further separated, with 0.02mol/L, pH4.5 acetic acid-acetate buffer of the NaCl containing 0.1mol/L
Liquid carries out linear gradient elution, flow velocity 0.5ml/min, and eluting peak measures under 215nm, collects each peak and determine antioxygen
Change activity.
By the most obvious component peaks Sepadex G-50 gel filtration chromatographies of the antioxidation activity separated（It is long
20cm, diameter 1.6cm）Separated again, eluent is deionized water, flow velocity 0.5ml/min, and eluting peak enters under 215nm
Row measurement.Collect each peak and determine antioxidation activity.
The best antioxidation activity component separated is entered one again using RP-HPLC RPLCs
The separation of step, chromatographic column used are the μ C18 of Gemini 5, and applied sample amount is 100 μ L, flow velocity 1ml/min, and Detection wavelength is
215nm.Self-contained 10% acetonitrile of eluent and 90% water（v/v）Mixed liquor start, to 90% acetonitrile and 10% water（v/v）Mixed liquor
Terminate, carry out gradient elution, collect 24 % acetonitriles and 76 % water（v/v）The eluting peak at place, obtain the spy of the high-purity of the present invention
Different in nature antioxidation polypeptide, as shown in Figure 1.B peaks are the chromatographic peak of the antioxidation polypeptide, obtain the antioxidation polypeptide of high-purity.
Antioxidation polypeptide after purification has very strong oxidation resistance, and it has it can be seen from Fig. 2, Fig. 3 and Fig. 4
Stronger removing DPPH free radicals, ABTS free radicals and the ability of anti-lipid peroxidation reaction.
Utilize protein solid-phase sequencer (Applied Biosystems Model 476A, Perkin Elmer Co.
MA, U.S.A) measure antioxidation polypeptide after purification amino acid sequence.Obtaining its overall amino acid sequence is：GAVLGTY.
The foregoing is only presently preferred embodiments of the present invention, all equivalent changes done according to scope of the present invention patent with
Modification, it should all belong to the covering scope of the present invention.
SEQUENCE LISTING
<110>University of Fuzhou
<120>A kind of antioxidation polypeptide and preparation method thereof
<130> 1
<160> 1
<170> PatentIn version 3.3
<210> 1
<211> 7
<212> PRT
<213>Amino acid sequence
<400> 1
Gly Ala Val Leu Gly Thr Tyr
1 5
Claims (1)
- A kind of 1. anti-oxidation peptide, it is characterised in that：The amino acid sequence of the antioxidation polypeptide is：GAVLGTY.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201410614557.4A CN104356200B (en) | 2014-11-05 | 2014-11-05 | A kind of anti-oxidation peptide and preparation method thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201410614557.4A CN104356200B (en) | 2014-11-05 | 2014-11-05 | A kind of anti-oxidation peptide and preparation method thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN104356200A CN104356200A (en) | 2015-02-18 |
| CN104356200B true CN104356200B (en) | 2018-03-16 |
Family
ID=52523530
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201410614557.4A Active CN104356200B (en) | 2014-11-05 | 2014-11-05 | A kind of anti-oxidation peptide and preparation method thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN104356200B (en) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104974223A (en) * | 2015-05-12 | 2015-10-14 | 舟山拓智科技服务有限公司 | Actinopyga mauritiana polypeptides and application thereof |
| CN106916202A (en) * | 2015-12-25 | 2017-07-04 | 无限极（中国）有限公司 | Sea cucumber bio active peptide prepare it is anti-oxidant, prolong decline health food and cosmetics in application |
| CN106478770B (en) * | 2016-10-13 | 2019-12-17 | 福州大学 | Perilla seed antioxidant dipeptide and preparation method and application thereof |
| CN106589068B (en) * | 2017-02-08 | 2020-09-01 | 福州大学 | Sea bream antioxidant polypeptide and preparation method thereof |
| CN108129552B (en) * | 2017-12-22 | 2023-07-07 | 大连深蓝肽科技研发有限公司 | Sea cucumber-derived antioxidant active peptide and extraction method |
| CN108250291B (en) * | 2018-01-23 | 2020-12-11 | 北京化工大学 | Antioxidant ossein polypeptide and preparation method thereof |
| CN108822208A (en) * | 2018-06-26 | 2018-11-16 | 福州大学 | The method of antioxidation polypeptide is prepared from black sharkskin |
| CN108794571A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | Antioxidation polypeptide is isolated and purified using black sharkskin |
| CN110195090A (en) * | 2019-05-15 | 2019-09-03 | 池州市月亮湾生物科技有限公司 | The preparation method and gained sea cucumber intestine ovum polypeptide powder of sea cucumber intestine ovum polypeptide powder |
| CN111171138B (en) * | 2020-01-14 | 2022-11-15 | 大连深蓝肽科技研发有限公司 | Peptide fragment, monoclonal antibody, colloidal gold test strip and detection method for detecting stichopus japonicus oligopeptide |
| CN112574279B (en) * | 2020-12-23 | 2024-01-16 | 江苏海洋大学 | Antioxidant leuce Lai Tai and preparation method and application thereof |
| CN113416231B (en) * | 2021-05-11 | 2022-11-18 | 四川大学 | Sea squirt antioxidant polypeptide and preparation method thereof |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102219828A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidation polypeptide prepared from sharkskin collagen |
| CN102219829A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease |
| CN103804476A (en) * | 2014-03-06 | 2014-05-21 | 福州大学 | Anti-oxidation polypeptide and preparation method thereof |
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
| CN103880933A (en) * | 2014-03-06 | 2014-06-25 | 福州大学 | Antioxidative peptide |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102219830B (en) * | 2011-05-18 | 2012-11-21 | 福州大学 | Oxidation resisting polypeptide and preparation method thereof |
-
2014
- 2014-11-05 CN CN201410614557.4A patent/CN104356200B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102219828A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidation polypeptide prepared from sharkskin collagen |
| CN102219829A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease |
| CN103804476A (en) * | 2014-03-06 | 2014-05-21 | 福州大学 | Anti-oxidation polypeptide and preparation method thereof |
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
| CN103880933A (en) * | 2014-03-06 | 2014-06-25 | 福州大学 | Antioxidative peptide |
Also Published As
| Publication number | Publication date |
|---|---|
| CN104356200A (en) | 2015-02-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN104356200B (en) | A kind of anti-oxidation peptide and preparation method thereof | |
| CN104356201B (en) | A kind of sea cucumber antioxidation polypeptide | |
| CN104402972B (en) | A kind of sea cucumber anti-oxidation peptide and preparation method thereof | |
| CN102219828B (en) | Antioxidation polypeptide prepared from sharkskin collagen | |
| CN104610430B (en) | Antioxidation polypeptide prepared using ganoderma lucidum albumen and preparation method thereof | |
| CN103819541B (en) | A kind of micro-algae antioxidation polypeptide | |
| CN102219830B (en) | Oxidation resisting polypeptide and preparation method thereof | |
| CN102219829B (en) | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease | |
| CN103804476A (en) | Anti-oxidation polypeptide and preparation method thereof | |
| CN103880933B (en) | A kind of antioxidation polypeptide | |
| CN104710525A (en) | Tuna fishbone collagen sourced zinc chelated collagen peptide, preparation method and application thereof | |
| CN103882083B (en) | A kind of preparation method of antioxidant collagen peptide | |
| CN104628823B (en) | One main laver antioxidation polypeptide and preparation method thereof | |
| CN106892965A (en) | Antioxidation polypeptide prepared by a kind of utilization compound protease | |
| CN111269290B (en) | Preparation method of sturgeon anti-inflammatory peptide | |
| CN105820229A (en) | Duck gizzard duck's gizzard antioxidative peptide and application thereof | |
| CN104693272B (en) | Yak milk lactalbumin has the tripeptides of antioxidant activity and application thereof and compositions | |
| CN106589068B (en) | Sea bream antioxidant polypeptide and preparation method thereof | |
| CN106560518B (en) | Preparation method of anti-prostate cancer oligopeptide from actinia viridis | |
| CN104152518A (en) | Preparation method of hepatopathy complementary-food cod skin collagen peptide | |
| CN104650191B (en) | A kind of antioxidation polypeptide prepared using seaweed albumen | |
| CN115057916A (en) | Pinctada martensii meat antioxidant polypeptide and preparation method and application thereof | |
| CN107173815B (en) | Application of antioxidant enzymolysis oligopeptide from peripherical glands of northern pacific squid | |
| CN110655553B (en) | ACE inhibitory peptide derived from sesame, preparation method and application thereof in preparation of antihypertensive drugs | |
| CN106632633B (en) | Abelmoschus moschatus antitumor oligopeptide and application thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |