CN106636274A - Separation and preparation method of rice bran antioxidant peptide - Google Patents
Separation and preparation method of rice bran antioxidant peptide Download PDFInfo
- Publication number
- CN106636274A CN106636274A CN201611071570.5A CN201611071570A CN106636274A CN 106636274 A CN106636274 A CN 106636274A CN 201611071570 A CN201611071570 A CN 201611071570A CN 106636274 A CN106636274 A CN 106636274A
- Authority
- CN
- China
- Prior art keywords
- rice bran
- glutelin
- value
- peptide
- active peptide
- 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.)
- Granted
Links
Classifications
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Botany (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention provides a bioactive peptide derived from rice bran glutelin, wherein the sequence of the bioactive peptide is shown as KHNRGDEF. The active peptide provided by the invention, which has an antioxidant activity, can be used for preparing foods and health care products capable of enhancing antioxidant efficacy. A polypeptide, which has an antioxidant activity in vitro, is separated from an enzymatic hydrolysate of the rice bran glutelin; an antioxidant active peptide product is prepared by extracting crude glutelin by virtue of a method of alkaline extraction and acid deposition, then conducting sequential extraction, separating and purifying the rice bran glutelin by virtue of ion-exchange chromatography and gel chromatography technologies, hydrolyzing obtained rice bran glutelin by virtue of alkaline protease, and conducting centrifuging, vacuum concentration and freeze-drying, wherein the rice bran glutelin is enzymatically hydrolyzed under the following conditions: an [E]/[S] ratio is 1.5% 1.8%, a pH value is 10.0, a temperature is at 50 DEG C and a duration is 4.2h; and a required antioxidant active peptide pure product is prepared by conducting ion-exchange chromatography and gel chromatography, preparing RP HPLC and analytical RP HPLC, and conducting separating and purifying. A separation and preparation method provided by the invention is low in production cost, simple and convenient in process and is green and environmentally friendly; the prepared rice bran active peptide has the characteristics of being reasonable in amino acid composition, low in allergy, safe and reliable, and the like; and the rice bran active peptide is relatively good in free radical scavenging capacity and excellent in antioxidant efficacy.
Description
Technical field
The present invention relates to a kind of method for separating and preparing of rice bran antioxidation active peptides.
Background technology
Rice bran is that more accessory substance is produced in rice production factory, protein in its gal4 amino acid composition and rice
Amino acid composition is similar, and amino acid composition is reasonable, is high-quality protein.The annual industrial production of China can all produce substantial amounts of rice
Chaff, and wherein most is not utilized effectively, it is therefore desirable to deep processing is carried out to rice bran protein to improve its added value, is realized
Resource makes full use of.Protein solubility in rice and rice bran is poor, has a strong impact on its application.And the molecular weight in rice bran
Peptide fragment then there is preferable dissolubility, and different peptide fragments has different effects, such as non-oxidizability, hypotensive, immune work
Property etc..Rice antioxidation active peptides have good radical scavenging activity, in the cardiovascular and cerebrovascular disease of prevention free radical induction
Aspect has very big potentiality to be exploited.Rice active peptide has good scavenging action to the free radical that oxidative damage is induced, and can improve
Human body cell oxidation resistance.
Through investigation, have no that Chinese scholar extracts the correlation of antioxidation active peptides in rice bran glutelin using neutral proteinase
The research field such as antioxidation active peptides is still in blank stage in document report, therefore neutral proteinase extraction rice bran glutelin.
The study find that the rice active peptide extracted using neutral proteinase in rice bran protein is had and being removed free radical, being suppressed cellular oxidation
Effect, effectively improve the surcharge of rice bran, realize the higher value application of rice bran.
The content of the invention
It is an object of the invention to provide a kind of method for separating and preparing of rice bran antioxidation active peptides, is with rice bran as original
Material, prepares the peptide product with antioxidation activity, to realize the higher value application of rice bran using neutral proteinase.
In order to achieve the above object, the technical scheme of present invention offer is：
The method for separating and preparing of the rice bran antioxidation active peptides is de- by alkali extraction and acid precipitation and Osborne grading extractions
Fat rice bran carries out separating pure obtaining rice bran glutelin, then from ion exchange and gel chromatography technology to rice bran glutelin
Change, then rice bran glutelin hydrolysis by novo, centrifugation, the concentrated in vacuo, freeze-drying after isolating and purifying, utilize afterwards
Ion-exchange chromatography, gel chromatography, preparation RP-HPLC and analytic type RP-HPLC are isolated and purified and are obtained antioxidation active peptides, described
The sequence of antioxidation active peptides is as shown in SEQ ID NO.1.
Preferably, the condition of the hydrolysis by novo is that [E]/[S] 1.5% -1.8%, pH value is 10.0, temperature
It is 4.2h for 50 DEG C, reaction time.
Preferably, methods described specifically includes following steps：
(1) extraction of glutelin：Defatted rice bran → add water and adjust pH value to be 9.0, solid-liquid ratio is 1:10, the solid-liquid ratio
Unit is mL/g, and 40 DEG C of water-bath 4h → be centrifuged → take supernatant → pH value sink → are centrifuged → take precipitation → water for acid under the conditions of 4.0
Wash, tune pH value is 7.0 → freeze-drying → alkali carries rice bran glutelin → Osborne grading extractions, obtains rice bran glutelin；
(2) it is 10.0 from pH value, concentration is the Na of 0.1mol/L2CO3-NaHCO3As buffer solution to big oryzenin
Carry out preliminary separation；With pH value 12.0, concentration is 0.05mol/L Na2HPO4- NaOH buffer solution alkali carries rice bran paddy eggs
In vain, alkali carries rice bran glutelin is further isolated and purified using DEAE-52 anion-exchange chromatographies medium；
(3) rice bran protein suspension is prepared, is added in ratio of the alkali protease/glutelin mass ratio for 1.5%-1.8%
Plus alkali protease → tune pH value be dissolve in thermostatic water-circulator bath enzyme reactor at 10.0 → 50 DEG C 30min → enzymolysis 4.2h →
Go out enzyme → be centrifuged → take supernatant → concentrated in vacuo → freeze-drying, obtains big oryzenin peptide；
(4) antioxidation active peptides are obtained after isolating and purifying to big oryzenin peptide.
Below the invention will be further described：
The preparation method of rice active peptide of the present invention is comprised the following steps：
(1) extraction of glutelin：Glutelin is extracted by alkali extraction and acid precipitation, from ion exchange and gel chromatography technology pair
Big oryzenin is isolated and purified；
(2) hydrolysis of rice bran glutelin：Under 5% (w/v, g/mL) rice bran glutelin suspension → tune pH value → uniform temperature
30min → digested by certain concentration of substrate, enzyme concentration, pH value, temperature is dissolved in thermostatic water-circulator bath enzyme reactor (permanent
PH titrators stablize system pH) → 85 DEG C, 10min go out enzyme → 3500r/min centrifugation 15min → supernatant → concentrated in vacuo →
Freeze-drying → rice bran glutelin peptide；
(3) rice bran glutelin peptide is isolated and purified
1. by the use of SP-Sephadex G-25 as ion-exchange chromatography media, pH4.0,0.02mol/L HAc-Na Ac
For start buffer, flow velocity 2mL/min, with level pad, the level pad containing 0.5mol/L NaCl and containing 1mol/L
The level pad gradient elution of NaCl, chooses radical scavenging activity in the multiple peptide compositions of rice bran gluten hydrolysate most strong
Component.
2. 1. into several components, radicals scavenging will be chosen by selected Component seperation using Sephadex G-15 gel chromatographies
The most strong component of ability.
3. component selected by last step is further separated using preparation RP-HPLC, chooses several key components, by surveying
The radical scavenging activity of fixed each key component filters out the stronger component of antioxidation activity, then Jing RP-HPLC analyse whether for
With respect to simple spike.
(4) relative molecular weight of the rice active peptide for extracting is measured using MALDI-TOF/TOF MS mass spectrometries.
Show that its amino acid composition puts in order with it with reference to TOF-MS/MS tandem mass spectrums.
Compared with prior art, the rice bran active peptide that prepared by the inventive method more effectively make use of rice bran, improve big
The utilization of accessory substance, also saves production cost, to realizing the comprehensive utilization of rice bran protein and improving its added value in rice production
Have great importance.
Description of the drawings
Fig. 1 is TOF-MS/MS tandem mass spectrum measurement result figures；
Fig. 2 is the ABTS of isolated component PA-PG of ion-exchange chromatography+Radical scavenging activity；* represents clear
Except there is significant difference between rate highest component and other components；
Fig. 3 is isolated component PF of gel chromatography1-PF4ABTS+Radical scavenging activity；* represents clearance rate
There is significant difference between highest component and other components；
Fig. 4 is isolated components PF of RP-HPLC3- α arrives F3The ABTS of-γ+Radical scavenging activity；* represents clear
Except there is significant difference between rate highest component and other components.
Specific embodiment
Embodiment 1
The method for separating and preparing of the rice bran antioxidation active peptides comprises the steps：
(1) alkali extraction and acid precipitation extract rice bran glutelin technological process be：Defatted rice bran (crossing 60 mesh sieves) → add water and adjust
PH9.0 (solid-liquid ratios 1:10, the unit of the solid-liquid ratio is mL/g, water-bath：40 DEG C, 4h) → centrifugation (8000r/min, 15min)
→ take supernatant → acid heavy (pH 4.0) → centrifugation (8000r/min, 15min) → take precipitation → washing three times, tune ph7.0 → cold
Dry (48h) → alkali carries rice bran glutelin (4 DEG C of hermetically storing+silica gel) → Osborne grading extractions are freezed, purer paddy egg is obtained
In vain；
(2) Na is selected2CO3-NaHCO3(pH10.0,0.1mol/L) carries out preliminary as buffer solution to big oryzenin
Separate.With 0.05mol/L Na2HPO4- NaOH (pH12.0) buffer solution alkali carries rice bran glutelin, using DEAE-52 it is cloudy from
Sub- displacement chromatography medium is further isolated and purified to alkali carries rice bran glutelin, successively with 0.15mol/L, 0.25mol/L,
The big oryzenin of saliferous buffer stage wash-out alkali carries of 0.35mol/L, 0.45mol/L, 0.55mol/L, isolated five
Eluting peak R1、R2、R3、R4、R5, using HPLC to R3Component carries out purity analysis, and its purity is 71.55%.Collect R3Using
Sephadex G-75 gel permeation chromatographies are further purified, and obtain R3-α、R3-β、R3Three eluting peaks of-γ, Jing HPLC detections,
Wherein R3The molecular weight of-γ eluting peaks is 37530.34, and purity is up to 93.45%；
(3) 5% (w/v, g/mL) rice bran glutelin suspension, are 1.5%-1.8% according to alkali protease/glutelin
(g/g) ratio addition alkali protease → tune pH value is dissolving in thermostatic water-circulator bath enzyme reactor at 10.0 → 50 DEG C
30min → enzymolysis 4.2h (stablizing system pH with pH titrators) → 85 DEG C, 10min goes out enzyme → 3,500r/min centrifugation 15min
→ supernatant → concentrated in vacuo → freeze-drying → big oryzenin peptide；
(4) big oryzenin peptide is isolated and purified
1. by the use of SP-Sephadex C-25 as ion-exchange chromatography media, pH4.0,0.02mol/L HAc-NaAc is
Start buffer, flow velocity 2m L/min, with level pad, the level pad containing 0.5mol/L NaCl and containing 1mol/L
The level pad gradient elution of NaCl, glutelin neutral proteinase hydrolysis product mixing peptide composition is separated seven components
(PA-PG), the ABTS of component PF+Radical scavenging activity is most strong (71.09%, Fig. 2).
2. using Sephadex G-15 gel chromatographies with ultra-pure water as buffer solution, sample introduction concentration is 15mg/mL again by component
PF divide into 4 components PF1、PF2、PF3And PF4.Detection discovery, component PF3ABTS+Radical scavenging activity is most strong, reaches
To 69.24% (Fig. 3).
3. utilize and prepare RP-HPLC by PF35 key components are further separated into, by the free radical for determining each component
Scavenging activity filters out the most strong component of antioxidation activity for PF3- γ (Fig. 4), its ABTS+Radical scavenging activity reaches
78.59%, Jing RP-HPLC analyses are relative simple spike.
(5) antioxidation active peptides PF is measured using MALDI-TOF MS mass spectrometries3The relative molecular weight of-γ is
1002.06 (Fig. 1).
Draw with reference to TOF-MS/MS tandem mass spectrums；PF3-γIt is made up of 8 amino acid, it puts in order as Lys-His-
Asn-Arg-Gly-Asp-Glu-Phe(KHNRGDEF).Jing looks into new discovery, and the active peptide that the present invention is obtained is with anti-oxidant work
The new bioactive peptides sequence of property.
The detection of antioxidation activity in the oryzenin active peptide body of embodiment 2
The cell of exponential phase is selected, with without cell suspension is made after the digestion of EDTA pancreatin, with tally suspension is determined
In cell concentration, be inoculated in 96 orifice plates according to 5000, every hole cell, per hole be inoculated with 100 μ L, 6 multiple holes are set per group, 37
DEG C 5%CO2It is divided into normal group, H after cultivating 6 hours in incubator2O2Treatment group, H2O2+ oryzenin active peptide protection group, by original
There is culture medium to suction out, all groups of culture mediums for being initially charged 80 μ L, normal group, H2O2Treatment group adds the serum free medium of 10 μ L,
H2O2+ oryzenin active peptide protection group is separately added into respective concentration equal-volume oryzenin active peptide, distinguishes medicine final concentration
For 100,150,200 μm of ol/L, in 37 DEG C of 5%CO2Incubator is protected in advance after 4h, H2O2Treatment group and H2O2+ oryzenin activity
Peptide protection group adds 10 μ L H per hole2O2, its final concentration of 100 μm of l/L, Normal group 10 μ L serum free mediums of addition, in
37 DEG C of 5%CO2After incubator incubation 24h, MTS methods detection cell viability (being shown in Table 1).Compare with normal group, H2O2Damage group it is thin
Born of the same parents' survival rate is remarkably decreased；And and H2O2Treatment group compares, and the high dose group (200 μm of ol/L) of oryzenin active peptide is to H2O2
The cell viability of induction has clear improvement.
The oryzenin active peptide of table 1 is to H2O2The impact of the cell viability of the endothelial progenitor cells of damage
Claims (3)
1. a kind of method for separating and preparing of rice bran antioxidation active peptides, it is characterised in that methods described is by alkali extraction and acid precipitation
Rice bran glutelin is obtained with Osborne grading extractions defatted rice bran, then from ion exchange and gel chromatography technology to rice
Chaff glutelin is isolated and purified, then the rice bran glutelin hydrolysis by novo after isolating and purifying, centrifugation, vacuum are dense
Contracting, freeze-drying, are isolated and purified afterwards using ion-exchange chromatography, gel chromatography, preparation RP-HPLC and analytic type RP-HPLC
Antioxidation active peptides are obtained, the sequence of the antioxidation active peptides is as shown in SEQ ID NO.1.
2. the method for claim 1, it is characterised in that the condition of the hydrolysis by novo is [E]/[S]
1.5% -1.8%, pH value be 10.0, temperature be 50 DEG C, the reaction time be 4.2h.
3. the method for claim 1, it is characterised in that methods described specifically includes following steps：
（1）The extraction of glutelin：Defatted rice bran → add water and adjust pH value to be 9.0, solid-liquid ratio is 1:10, the unit of the solid-liquid ratio
For mL/g, 40 DEG C of water-bath 4h → be centrifuged → take supernatant → pH value sink → are centrifuged → take precipitation → washing for acid under the conditions of 4.0, tune
PH value is 7.0 → freeze-drying → alkali carries rice bran glutelin → Osborne grading extractions, obtains rice bran glutelin；
（2）It is 10.0 from pH value, concentration is the Na of 0.1 mol/L2CO3-NaHCO3Big oryzenin is entered as buffer solution
The preliminary separation of row；With pH value 12.0, concentration is 0.05 mol/L Na2HPO4- NaOH buffer solution alkali carries rice bran glutelin,
Alkali carries rice bran glutelin is further isolated and purified using DEAE-52 anion-exchange chromatographies medium；
（3）Rice bran protein suspension is prepared, it is alkaline for the ratio addition of 1.5%-1.8% in alkali protease/glutelin mass ratio
Protease → tune pH values are to dissolve 30min → enzymolysis 4.2h → go out at 10.0 → 50 DEG C in thermostatic water-circulator bath enzyme reactor
Enzyme → be centrifuged → take supernatant → concentrated in vacuo → freeze-drying, obtains big oryzenin peptide；
（4）Antioxidation active peptides are obtained after isolating and purifying to big oryzenin peptide.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201611071570.5A CN106636274B (en) | 2016-11-29 | 2016-11-29 | Separation and preparation method of rice bran antioxidant active peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201611071570.5A CN106636274B (en) | 2016-11-29 | 2016-11-29 | Separation and preparation method of rice bran antioxidant active peptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN106636274A true CN106636274A (en) | 2017-05-10 |
| CN106636274B CN106636274B (en) | 2021-06-11 |
Family
ID=58813115
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201611071570.5A Active CN106636274B (en) | 2016-11-29 | 2016-11-29 | Separation and preparation method of rice bran antioxidant active peptide |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN106636274B (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112522354A (en) * | 2020-12-01 | 2021-03-19 | 中南林业科技大学 | Preparation method of rice antioxidant active peptide |
| CN113616773A (en) * | 2021-08-25 | 2021-11-09 | 中南林业科技大学 | Application of rice bran active peptide in intervention of caenorhabditis elegans aging or muscle injury |
| CN114150033A (en) * | 2021-12-06 | 2022-03-08 | 哈尔滨商业大学 | Preparation method of rice bran antioxidant peptide compound treated by peak alpha amylase |
| CN114478702A (en) * | 2022-04-06 | 2022-05-13 | 中南林业科技大学 | Rice bran-derived short peptide and application thereof in treatment of skin injury |
| CN114558106A (en) * | 2022-03-23 | 2022-05-31 | 长沙飞创生物技术有限责任公司 | Application of rice bran active peptide in preventing or treating lipid toxicity related diseases |
-
2016
- 2016-11-29 CN CN201611071570.5A patent/CN106636274B/en active Active
Non-Patent Citations (2)
| Title |
|---|
| 佟立涛等: "大米蛋白体外消化产物抗氧化活性的研究", 《现代食品科技》 * |
| 张君慧: "大米蛋白抗氧化肽的制备、分离纯化和结构鉴定", 《中国博士学位论文全文数据库（电子期刊）工程科技I辑》 * |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112522354A (en) * | 2020-12-01 | 2021-03-19 | 中南林业科技大学 | Preparation method of rice antioxidant active peptide |
| CN112522354B (en) * | 2020-12-01 | 2023-01-24 | 中南林业科技大学 | Preparation method of rice antioxidant active peptide |
| CN113616773A (en) * | 2021-08-25 | 2021-11-09 | 中南林业科技大学 | Application of rice bran active peptide in intervention of caenorhabditis elegans aging or muscle injury |
| CN113616773B (en) * | 2021-08-25 | 2023-11-14 | 中南林业科技大学 | Application of rice bran active peptide in intervention of caenorhabditis elegans aging or muscle injury |
| CN114150033A (en) * | 2021-12-06 | 2022-03-08 | 哈尔滨商业大学 | Preparation method of rice bran antioxidant peptide compound treated by peak alpha amylase |
| CN114150033B (en) * | 2021-12-06 | 2023-05-19 | 哈尔滨商业大学 | Preparation method of rice bran antioxidant peptide compound treated by peak alpha amylase |
| CN116218939A (en) * | 2021-12-06 | 2023-06-06 | 哈尔滨商业大学 | Rice bran antioxidant peptide compound treated by peak alpha amylase and pepsin and application thereof |
| CN116218939B (en) * | 2021-12-06 | 2023-09-15 | 哈尔滨商业大学 | Rice bran antioxidant peptide compound treated by peak alpha amylase and pepsin and application thereof |
| CN114558106A (en) * | 2022-03-23 | 2022-05-31 | 长沙飞创生物技术有限责任公司 | Application of rice bran active peptide in preventing or treating lipid toxicity related diseases |
| CN114558106B (en) * | 2022-03-23 | 2024-02-23 | 长沙飞创生物技术有限责任公司 | Application of rice bran active peptide in preventing or treating lipotoxicity related diseases |
| CN114478702A (en) * | 2022-04-06 | 2022-05-13 | 中南林业科技大学 | Rice bran-derived short peptide and application thereof in treatment of skin injury |
| CN114478702B (en) * | 2022-04-06 | 2023-12-12 | 中南林业科技大学 | Rice bran-derived short peptide and application thereof in treating skin injury |
Also Published As
| Publication number | Publication date |
|---|---|
| CN106636274B (en) | 2021-06-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN106636274A (en) | Separation and preparation method of rice bran antioxidant peptide | |
| CN104250285B (en) | Pseudosciaena crocea flesh antioxidative peptide and preparation method and use thereof | |
| CN110272932B (en) | Preparation method of ganoderma lucidum spore powder polysaccharide peptide | |
| JP7250362B2 (en) | Chinese giant salamander cartilage preparation | |
| CN105254774A (en) | Nostoc commune polysaccharide extraction method | |
| WO2012013112A1 (en) | Method for extracting effective ingredients from sea cucumber by salting out | |
| CN107541533A (en) | A kind of preparation method of medicine food hypha polysaccharide polypeptide immunopotentiator | |
| CN103130904A (en) | High-valued utilization method for patinopecten yessoensis offal | |
| CN104558115A (en) | Antioxidant polypeptide with Raja porosa meat protein as well as preparation method and application of antioxidant polypeptide | |
| CN111533823A (en) | Process for extracting polysaccharide from ganoderma lucidum mycelia | |
| Wang et al. | Isolation of a novel N-acetylglucosamine-specific lectin from fresh sclerotia of the edible mushroom Pleurotus tuber-regium | |
| CN104846031A (en) | Method for extracting oat beta-glucan through fermentation method | |
| CN104928339B (en) | A kind of preparation method with the oat protein peptide for inhibiting intestinal inflammatory activity | |
| CN106520877A (en) | Method for preparing pig cerebral protein antioxidative peptide | |
| US20200317822A1 (en) | Method for Preparing Arabinogalacturonan from Tangerine Peel | |
| CN107177650B (en) | Preparation method of antioxidant enzymolysis oligopeptide from peripherical glands of northern pacific squid | |
| CN117186264A (en) | Green and efficient highland barley beta-glucan extraction method | |
| CN116731108B (en) | Straw mushroom antioxidant peptide and application thereof | |
| KR20100138664A (en) | A functional deer antlers product produced by two-step process and method for preparing thereof | |
| CN113845565B (en) | Lumbricus bioactive small peptide, and preparation method and application thereof | |
| CN103694367B (en) | A kind of extraction and application method with anti-oxidant activity clam polysaccharide | |
| CN107190040B (en) | Antioxidant peptide of penaeus japonicus and preparation method thereof | |
| CN112457377B (en) | Periplaneta americana polypeptide and application thereof | |
| CN106191184B (en) | Preparation and application of novel arca inflata reeve antioxidant active peptide | |
| US4195076A (en) | Process for the preparation of hemagglutinin from viral sources and methods of utilizing same |
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 | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20230423 Address after: Room 609-B, 6th Floor, Building 007, Phase II Plant, No. 8 Lutian Road, Lugu Base, Changsha High tech Development Zone, Changsha City, Hunan Province, 410221 Patentee after: Changsha feichuang Biotechnology Co.,Ltd. Address before: 410004 No. 498 South Shaoshan Road, Hunan, Changsha Patentee before: CENTRAL SOUTH University OF FORESTRY AND TECHNOLOGY |
|
| TR01 | Transfer of patent right |