CN108976290B - Preparation method of rambutan antioxidant peptide - Google Patents
Preparation method of rambutan antioxidant peptide Download PDFInfo
- Publication number
- CN108976290B CN108976290B CN201810967565.5A CN201810967565A CN108976290B CN 108976290 B CN108976290 B CN 108976290B CN 201810967565 A CN201810967565 A CN 201810967565A CN 108976290 B CN108976290 B CN 108976290B
- Authority
- CN
- China
- Prior art keywords
- rambutan
- polypeptide
- enzymolysis
- peptide
- red hair
- 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
Images
Classifications
-
- 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
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/145—Extraction; Separation; Purification by extraction or solubilisation
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
Abstract
The invention provides a preparation method of a rambutan antioxidant peptide, which takes the rambutan as a raw material, and obtains the rambutan antioxidant peptide by preparing rambutan powder, extracting rambutan protein, preparing rambutan polypeptide, separating, purifying and freeze-drying, wherein the complete amino acid sequence of the antioxidant peptide is as follows: GTGPVDEWCIAGAR are provided. The method for extracting the anti-oxidation peptide of the red hair algae has the advantages of low salt content, high protein extraction rate and high purity, fills up the blank of research on the polypeptide of the red hair algae in the prior art, and provides convenient conditions for obtaining the purer anti-oxidation peptide of the red hair algae through next chromatographic separation.
Description
Technical Field
The invention relates to the technical field of refining and processing of active ingredients of marine algae, in particular to a preparation method of a rambutan antioxidant peptide.
Background
Bioactive peptides (bioactive peptides) are a class of bioactive substances derived from bacteria, fungi or animals and plants with important physiological functions. The bioactive peptide not only has a plurality of remarkable physiological functions, such as nerve regulation, hormone action, rabbit disease regulation, antithrombotic, antihypertensive, cholesterol reduction, bacteriostasis, antivirus, anticancer, antioxidation and the like; in addition, the bioactive substance has the characteristics of simple structure, strong stability, easy direct absorption by human body and safety, so the bioactive substance is a hot spot in the research field of bioactive substances in recent years.
At present, methods for preparing active peptides mainly include an enzymatic hydrolysis method, a microbial fermentation method, a chemical synthesis method and the like. The enzymatic hydrolysis method has become the most common method for releasing bioactive peptides from proteins due to the advantages of mild production conditions, high safety, availability of bioactive peptides with specific functions, and the like. The research of preparing the bioactive peptide by the enzyme method is mostly found in animal-derived polypeptides, and the research of plant-derived polypeptides is relatively less. In the research of plant antioxidant active peptides, a plurality of researchers hydrolyze a plurality of plant proteins such as wheat, corn, buckwheat, soybean, rice bran and the like by protease to obtain polypeptide with higher antioxidant activity and part of other activities. The wheat germ protein is subjected to enzymolysis by using the Guo hong ying under the optimal enzymolysis condition, so that the polypeptide substance with remarkable antioxidant activity is obtained. The eucrypti japonica and the like select pepsin to carry out enzymolysis on water-soluble and salt-soluble proteins of multicystis montana, and the obtained polypeptide has stronger activity of removing DPPH free radicals. The research on the antioxidation of plant polypeptides at home and abroad is mostly limited to terrestrial plants, and the research on aquatic plants such as algae polypeptides is very little. Algae live in the ocean and have more complex living conditions, and may form protein structures and biological activities different from those of terrestrial plants. Therefore, the algae polypeptide has more potential research values, and the research on the algae polypeptide is beneficial to deeply developing and utilizing algae and changing the production structure and the application value of the algae.
Rhodophyta (Bangia fusco-purpura Lyngb.) belongs to Rhodophyta, class Rhodophyceae, order Lasiophyceae, and is a special product of coastal region of southeast China. It is rich in nutrients and has protein content as high as 45%. So far, no report related to the research of the polypeptide of the red hair algae is found.
Disclosure of Invention
The invention aims to provide a preparation method of an antioxidant peptide of red hair algae, wherein the antioxidant peptide has good DPPH free radical scavenging capacity.
In order to achieve the purpose, the invention adopts the following technical scheme:
the anti-oxidation peptide of the red hair algae is composed of 14 amino acids, and the amino acid sequence of the polypeptide is as follows: GTGPVDEWCIAGAR are provided.
A preparation method of the red hair algae antioxidant peptide comprises the following steps: (1) preparing the ruditapes powder; (2) extracting the protein of the red hair algae; (3) preparing the red hair algae polypeptide; (4) separating and purifying the red hair algae polypeptide; (5) and (5) freeze-drying the red hair algae polypeptide liquid.
The specific preparation method of the Haematococcus powder in the step (1) comprises the following steps: selecting Haematococcus, removing impurities, drying at 60 deg.C for 4 hr, pulverizing with high-speed pulverizer, sieving with 60 mesh sieve, and packaging.
The specific method for extracting the trichophyta protein in the step (2) comprises the following steps: weighing the hirsutella powder, adding pure water according to the mass-to-volume ratio of 1:20, fully stirring and swelling, adjusting the pH value to 10, performing ultrasonic assisted extraction at the ultrasonic power of 480w for 20 minutes, performing constant temperature extraction at 50 ℃ for 50 minutes, centrifuging at 4000r/min for 10 minutes, taking the supernatant, adjusting the pH value to 4.5, standing at room temperature for 60 minutes, centrifuging at 4000r/min for 15 minutes, removing the supernatant, precipitating, and freeze-drying to obtain the hirsutella protein.
The specific method for preparing the trichophyta polypeptide in the step (3) comprises the following steps: taking DPPH free radical clearance as a discrimination index, and obtaining the optimal enzymolysis condition by adopting an orthogonal test; weighing the Haematococcus protein, adding 10 times of pure water to dissolve, adding papain, regulating the enzyme-substrate ratio [ E ]/[ S ] to be 650-1850U/g, adjusting the pH to 4.0-8.0, the enzymolysis temperature to be 30-70 ℃, the enzymolysis time to be 30-150min, heating to 100 ℃ after the enzymolysis is finished, inactivating the enzyme for 5min to obtain the Haematococcus polypeptidase hydrolysate, and refrigerating for later use.
The specific method for separating and purifying the red hair algae polypeptide in the step (4) comprises the following steps: preparing a rhodophyta polypeptide solution with the molecular weight of less than 2000Da by using an ultrafiltration membrane with the molecular weight cut-off of 2000 Da; vacuum concentrating the polypeptide solution at 60 deg.C, and freeze drying to obtain Haematococcus polypeptides with molecular weight less than 2000 Da; separating the piliferin polypeptide with molecular weight less than 2000Da by Sephadex G-15 gel chromatography to obtain the antioxidant peptide of the piliferin.
The invention has the advantages that:
the invention adopts the alkaline method to extract the red hair algae protein with the assistance of ultrasonic, the salt content is low, and the protein extraction rate is high. The protein is separated by an isoelectric point method, the obtained protein contains few micromolecular compounds, the purity is high, the papayotin is used for preparing the red hair algae antioxidant peptide, the clearance rate of DPPH free radicals is used as a judgment index of enzymolysis conditions, and the obtained enzymolysis conditions can be more accurately used for preparing the red hair algae antioxidant peptide. The rhodophyta polypeptide is prepared by adopting an ultrafiltration membrane with the molecular weight cutoff of 2000Da, and a convenient condition is provided for obtaining purer antioxidant peptide of the rhodophyta by the next chromatographic separation. Different chromatographic separation modes are adopted according to different molecular weights of the red hair algae polypeptide, and the obtained red hair algae polypeptide has higher purity.
Drawings
FIG. 1 shows the effect of the enzymolysis temperature on the enzymolysis effect.
FIG. 2 shows the effect of enzymolysis time on the enzymolysis effect.
FIG. 3 shows the effect of pH on the enzymatic effect.
FIG. 4 shows the effect of enzyme-substrate ratio on the enzymolysis effect.
FIG. 5 is a diagram of Sephadex G-15 gel chromatography separation and purification.
Detailed Description
The present invention will be described in detail below with reference to the accompanying drawings and preferred embodiments, and the objects and effects of the present invention will become more apparent, and the present invention will be further described in detail below with reference to the accompanying drawings and embodiments. It should be understood that the specific embodiments described herein are merely illustrative of the invention and are not intended to limit the invention.
Example 1
Selecting Haematococcus, removing impurities, drying at 60 deg.C for 4 hr, pulverizing with high-speed pulverizer, sieving with 60 mesh sieve, and packaging. Weighing 10.00g of Haematococcus powder, adding pure water according to the mass-to-volume ratio of 1:20, fully stirring and swelling, adjusting the pH value to 10, performing ultrasonic-assisted extraction at the ultrasonic power of 480w for 20 minutes, performing constant-temperature extraction at 50 ℃ for 50 minutes, centrifuging at 4000r/min for 10 minutes, taking the supernatant, adjusting the pH value to 4.5, standing at room temperature for 60 minutes, centrifuging at 4000r/min for 15 minutes, removing the supernatant precipitate, and performing freeze drying to obtain Haematococcus protein for later use.
The influence of various factors on the antioxidation effect of the zymohydrolysis polypeptide of the red hair algae protein is carried out by taking the clearance rate of the zymohydrolysis liquid on DPPH free radicals as an index. Weighing Haematococcus protein, dissolving with 10 times of pure water, adding papain, adjusting pH to 6.0, performing enzymolysis at 55 deg.C for 120min, heating to 100 deg.C, inactivating enzyme for 5min, and refrigerating.
1. Influence of temperature on the enzymolysis Effect
Adjusting the enzymolysis temperature to 30-70 deg.C, keeping other conditions unchanged, and studying the influence of enzymolysis temperature on enzymolysis effect. As can be seen from fig. 1, the clearance rate gradually increases with the increase in temperature at 30 ℃ to 50 ℃, and reaches the maximum at 50 ℃, so that the temperature range of the orthogonal test was determined to be 45 ℃ to 55 ℃.
2. Effect of time on the Effect of enzymolysis
Adjusting the enzymolysis time to 30-150min, keeping other conditions unchanged, and studying the influence of the enzymolysis time on the enzymolysis effect. As can be seen from FIG. 2, the enzymolysis time is from 30min to 90min, the DPPH free radical clearance rate of the enzymolysis liquid is obviously improved, and then is slowly reduced. The enzymolysis time is prolonged, and the time period of the orthogonal test is selected from 60min, 90min and 120 min.
3. Influence of pH on the Effect of enzymolysis
Adjusting the enzymolysis pH to 4.0-8.0, keeping other conditions unchanged, and studying the influence of pH on the enzymolysis effect. As can be seen from FIG. 3, the clearance rate increases linearly with the increase of pH between pH4.0 and pH6.0, and rapidly decreases between pH6.0 and pH7.0, and then the rate of decrease tends to be gentle. The activity of the enzyme is closely related to the pH of the system, and since the enzymatic hydrolysis does not proceed to completion, the nature of the enzymatic product is directly determined. Thus, pHs of 5.5, 6.0, and 6.5 were selected as the three levels of the orthogonal experiment.
4. Influence of enzyme substrate ratio [ E ]/[ S ] on enzymolysis Effect
Regulating the enzyme substrate ratio [ E ]/[ S ] to 650-1850U/g, keeping other conditions unchanged, and researching the influence of the enzyme substrate ratio on the enzymolysis effect. As can be seen from FIG. 4, when the enzyme substrate ratio is between 650U/g and 1250U/g, the clearance of the enzymatic hydrolysate to DPPH free radicals gradually increases with the increase of the enzyme substrate ratio, the clearance reaches the maximum clearance at 1250U/g and then starts to slowly decrease, but in the interval of the enzyme substrate ratio between 950U/g and 1550U/g, the influence degree of the change of the enzyme substrate ratio on the clearance is less than the influence degree of the temperature between 40 ℃ and 60 ℃ and the influence degree of the pH between 5.0 and 7.0 on the clearance, and the time is an important research factor, so the enzyme substrate ratio can be set as a fixed factor which is 1250U/g.
5. Optimization of zymohydrolysis conditions of red hair algae protein
Rhodophyta proteolysis condition optimized L9（34) Orthogonal experimental results are shown in table 1, and analysis results are shown in tables 2 and 3 according to the experimental results by analysis of variance.
TABLE 1L9（34) Orthogonal test table
TABLE 2 results and analysis of orthogonal experiments
TABLE 3 ANOVA TABLE
As shown in the range analysis in Table 2, the optimal condition combination for proteolysis of Haematococcus is A3B3C2The temperature is 55 ℃, the time is 120min, and the pH value is 6.0; the influence of each factor on the proteolysis is C in turn>A>B, the influence of pH (C) is greatest, temperature (A) times, and time (C) influence is least. The variance analysis of 3 finds that the experimental results among the blocks have no significant difference, so that the results obtained by parallel tests are credible; the influence of temperature, time and pH on the enzymolysis of the trichophyta protein by the papain is very obvious; in addition, model errors were not significant, indicating that the interaction between the 3 experimental factors was not significant.
Example 2
1. Verification of optimal enzymolysis conditions
Three 50mL centrifuge tubes were taken and 1.000g of Haematococcus protein, 10mL of distilled water and enzyme base ratio [ E ]]/[S]1250U/g papain, then using the optimal enzymatic conditions obtained in the orthogonal test: the enzymolysis is carried out at 55 deg.C and pH of 6.0 for 120 min. The enzymatic hydrolysates obtained in the three experiments were measured for DPPH radical scavenging rate and found to be (87.46. + -. 0.76)% (n = 3), as shown in Table 4. The clearance obtained by the verification experiment is larger than that of any experimental group in the table 2, so A3B3C2Is the optimal condition combination of papain enzymolysis of the red hair algae protein.
TABLE 4 validation of optimal enzymatic conditions
2. Concentrating by ultrafiltration
Preparing a rhodophyta polypeptide solution with the molecular weight of less than 2000Da by using an ultrafiltration membrane with the molecular weight cut-off of 2000 Da. The trichomonas campestris polypeptide solution is subjected to vacuum concentration at 60 ℃, and then is subjected to freeze drying, so as to obtain the trichomonas campestris polypeptide with the molecular weight of less than 2000 Da. The DPPH radical scavenging ability and superoxide anion radical scavenging ability of the obtained polypeptide were measured, and the experimental results are shown in Table 5.
TABLE 5 Ultrafiltration for the isolation of Haematococcus polypeptides with a molecular weight of less than 2000Da
3. Sephadex G-15 gel chromatography separation and purification
Separating the Haematococcus polypeptides with molecular weight less than 2000Da obtained by ultrafiltration with Sephadex G-15 gel chromatography, separating with glass chromatographic column 40cm × 2.6cm chromatographic filler Sephadex G-15, flowing phase pure water at flow rate of 1.5mL/min, and collecting 10mL per tube. A large molecular weight component a and a relatively small molecular weight component B are obtained, see fig. 5. Collecting the collection tube of the combined component A, carrying out concentrated liquid chromatography to determine the component purity, and the sequencing result shows that the amino acid sequence of the red hair algae polypeptide is GTGPVDEWCIAGAR.
The polypeptide structure was determined using liquid chromatography-quadrupole-time of flight mass spectrometry (LC-Q-TOF-Ms/Ms) technique from Thermo corporation, USA. Methanol and water are used as mobile phases of a system, a sample is dissolved in ultrapure water, the sample is filtered through a 0.22-micron microporous filter membrane and then is loaded to 10 mu L, linear elution is carried out for 40 min by using 0-40% methanol mobile phase, and the detection wavelength is 220 nm. The mass spectrum was scanned in positive ion mode. And collecting mass spectrograms of the samples, and comparing the mass spectrograms with a polypeptide mass spectrographic library through MaxQuant 1.5.2.8.
The DPPH radical scavenging ability and superoxide anion radical scavenging ability of the obtained polypeptide were measured, and the experimental results are shown in Table 6.
TABLE 6 Haematococcus polypeptide Activity assay
The above description is only a preferred embodiment of the present invention, and all equivalent changes and modifications made in accordance with the claims of the present invention should be covered by the present invention.
SEQUENCE LISTING
<110> quan State college of education
<120> preparation method of Rhodophyta antioxidant peptide
<130> 1
<160> 1
<170> PatentIn version 3.3
<210> 1
<211> 14
<212> PRT
<213> Artificial sequence
<400> 1
Gly Thr Gly Pro Val Asp Glu Trp Cys Ile Ala Gly Ala Arg
1 5 10
Claims (1)
1. A rambutan antioxidant peptide is characterized in that: the amino acid sequence of the peptide is: GTGPVDEWCIAGAR are provided.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201810967565.5A CN108976290B (en) | 2018-08-23 | 2018-08-23 | Preparation method of rambutan antioxidant peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201810967565.5A CN108976290B (en) | 2018-08-23 | 2018-08-23 | Preparation method of rambutan antioxidant peptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN108976290A CN108976290A (en) | 2018-12-11 |
| CN108976290B true CN108976290B (en) | 2021-06-25 |
Family
ID=64547069
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201810967565.5A Active CN108976290B (en) | 2018-08-23 | 2018-08-23 | Preparation method of rambutan antioxidant peptide |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN108976290B (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007037475A (en) * | 2005-08-04 | 2007-02-15 | Ogawa & Co Ltd | Method for producing seaweed extract |
| CN101039594A (en) * | 2004-08-10 | 2007-09-19 | 化成龙 | Natural bean-curd and its preparation method |
| CN102170889A (en) * | 2008-09-18 | 2011-08-31 | 化成龙 | Pharmaceutical composition for preventing liver injury or improving liver function, containing the activated water of ENA actimineral resource A as an active ingredient |
| CN102241754A (en) * | 2010-05-12 | 2011-11-16 | 曹敏杰 | Method for separating and purifying phycoerythrin from bangia fusco-purpurea |
| CN107488695A (en) * | 2017-08-25 | 2017-12-19 | 兰溪市哥特生物技术有限公司 | A kind of preparation method of the nostoc albumen of promotion plant growth |
-
2018
- 2018-08-23 CN CN201810967565.5A patent/CN108976290B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101039594A (en) * | 2004-08-10 | 2007-09-19 | 化成龙 | Natural bean-curd and its preparation method |
| JP2007037475A (en) * | 2005-08-04 | 2007-02-15 | Ogawa & Co Ltd | Method for producing seaweed extract |
| CN102170889A (en) * | 2008-09-18 | 2011-08-31 | 化成龙 | Pharmaceutical composition for preventing liver injury or improving liver function, containing the activated water of ENA actimineral resource A as an active ingredient |
| CN102241754A (en) * | 2010-05-12 | 2011-11-16 | 曹敏杰 | Method for separating and purifying phycoerythrin from bangia fusco-purpurea |
| CN107488695A (en) * | 2017-08-25 | 2017-12-19 | 兰溪市哥特生物技术有限公司 | A kind of preparation method of the nostoc albumen of promotion plant growth |
Non-Patent Citations (4)
| Title |
|---|
| Effects of physicochemical factors and in vitro gastrointestinal digestion on antioxidant activity of R-phycoerythrin from red algea Bangia fusco-purpurea;Wu 等;《international journal of food science and technology》;20150630;第50卷;第1445-1451页 * |
| Purification and characterization of two nocel angiotensin-converting enzyme inhibitory peptides derived from R-phycoerythrin of red algea (Bangia fusco-purpurea);Wu 等;《Eur Food Res Technol》;20160928;第243卷;第779-789页 * |
| R-藻红蛋白的抗氧化活性及其抗氧化肽;伍强 等;《2014年中国水产学会学术年会论文摘要集》;20141031;第5页 * |
| 红毛藻及坛紫菜藻红蛋白的分离纯化与相关性质的研究;付晓萍;《中国优秀硕士学位论文全文数据库 工程科技Ⅰ辑》;20071115(第5期);B024-101 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN108976290A (en) | 2018-12-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN108823273B (en) | Peony seed meal polypeptide with antioxidant activity and preparation method and application thereof | |
| CN103937864B (en) | A kind of active polypeptide be separated from anchovy | |
| CN110623860B (en) | Giant salamander active peptide and hyaluronic acid composition capable of effectively promoting fibroblast proliferation | |
| CN107602688B (en) | Milk alphas2Preparation and application of casein-derived bioactive peptides | |
| CN111041059B (en) | Preparation method of Antarctic krill peptide with antioxidant activity | |
| CN105111282A (en) | Walnut peptide having ACE inhibitory activity and preparation method thereof | |
| CN105925652A (en) | Method for producing small peptides through bionic enzymatic hydrolysis | |
| CN109320588A (en) | A kind of ACE inhibitory activity peptide in stichopus japonicus source | |
| CN109021072B (en) | Rhodophyta antioxidant peptide and preparation method thereof | |
| CN106072632B (en) | Ganoderma lucidum extract and preparation method and application thereof | |
| CN116731108B (en) | Straw mushroom antioxidant peptide and application thereof | |
| CN108976290B (en) | Preparation method of rambutan antioxidant peptide | |
| CN116715724B (en) | Antioxidant peptide derived from fruiting body of straw mushroom and application thereof | |
| CN111662946A (en) | Method for preparing oligopeptide by enzymolysis of ganoderma lucidum water-soluble protein | |
| CN116606369A (en) | Spirulina immunoregulatory peptide and preparation method and application thereof | |
| CN106173185A (en) | A kind of preparation method of the little peptide of Pupa bombycis | |
| CN109369781A (en) | A kind of anti-oxidant tetrapeptide of Eucheuma and its application | |
| CN111154826A (en) | Preparation method and screening method of locusta migratoria manilensis antioxidant peptide | |
| CN108048518B (en) | Chicken blood cell antioxidant peptide and enzymolysis preparation method thereof | |
| CN108441535A (en) | The production method of three enzymes, one ferment silkworm peptide | |
| CN114032267A (en) | Preparation method and application of active peptide | |
| CN114163494A (en) | Preparation method and application of octopus antioxidant peptide for resisting oxidative stress damage | |
| CN103126967B (en) | Yeast refined extract and preparation method thereof | |
| CN114350732B (en) | Egg white protein peptide with antioxidant and anti-inflammatory effects | |
| CN109762861A (en) | A kind of preparation method and applications of Perna viridis small peptide |
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 | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |