CN104628823A - Anti-oxidative seaweed polypeptide and preparation method thereof - Google Patents
Anti-oxidative seaweed polypeptide and preparation method thereof Download PDFInfo
- Publication number
- CN104628823A CN104628823A CN201510065376.5A CN201510065376A CN104628823A CN 104628823 A CN104628823 A CN 104628823A CN 201510065376 A CN201510065376 A CN 201510065376A CN 104628823 A CN104628823 A CN 104628823A
- Authority
- CN
- China
- Prior art keywords
- polypeptide
- component
- molecular weight
- antioxidation polypeptide
- oxidant activity
- 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
Landscapes
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Plant Substances (AREA)
Abstract
The invention provides anti-oxidative seaweed polypeptide and a preparation method thereof. According to the method, by enzymolysis of acid proteinase, seaweed protein is taken as a raw material to be separated and purified to obtain specific anti-oxidative polypeptide of which the complete sequence of amino acids is avvkeagdacf. The anti-oxidative seaweed polypeptide disclosed by the invention has the advantages of eliminating defects of natural antioxidants, also eliminating worries of publics on artificial synthesis of antioxidants, and laying the foundation for developing the anti-oxidative polypeptide based on a food source and exploring wide application of the anti-oxidative seaweed polypeptide in foods and medical science.
Description
Technical field
The invention provides main laver antioxidation polypeptide and preparation method thereof, belong to biological technical field.
Background technology
The oxidation of biomolecules is the process of a free radical mediated, and it can cause many adverse influences to food and biosystem.In aerobic organ, in many with arteriosclerosis, cancer etc., the free free radical of disease-related can inevitably produce along with the process of oxygen metabolism.In food, the oxidation of food nutrient composition can produce superoxide, and it not only can affect Nutritive value of food, causes Food Quality to decline, the serious health generation disease that even also can cause absorption person.Therefore, the antioxidant of safety is found to suppress superoxide generation to be the study hotspot of biochemistry nutrition always.Because the chemosynthesis antioxidants such as BHT, TBHQ have better effect and more cheap price than natural antioxidants, therefore it has been widely used in food service industry.But, studies have found that synthetized oxidation preventive agent has accumulative carcinogenesis to organs such as human liver, spleen, lungs at present, thus cause the worry of people to its security, and start to limit its use in food gradually.So people turn to natural antioxidants sight.Alpha-tocopherol is a kind of by the natural antioxidants the most generally used, and it effectively can keep the stability of grease in food, but is but unfavorable for Food preservation.Therefore, we are necessary the natural antioxidants of the safety finding other source a kind of.
Polypeptide is the compounds of molecular structure between amino acid and protein, makes protein have certain physiological function.In the vital movement of the mankind, peptide in vivo digest and assimilate the amino acid being better than dissociating, and be different from delivery system in amino acid whose body.Some small peptide, while providing growth in humans, growing necessary nutritive substance, can also be prevented and cured diseases, and regulate function of human body, these have bioactive polypeptide and are called as biologically active peptides.Research finds, the polypeptide of a lot of different sources all has resistance of oxidation, and the polypeptide obtained as caseinhydrolysate, soybean protein, bovine serum albumin, Protalbinic acid, oil seed protein, wheat gliadin and zein etc. all has certain oxidation-resistance.
China has abundant marine algae resource, but due to resource utilization low, the reason such as tankage waste that the course of processing produces causes the wasting of resources, or even environmental pollution.Containing a large amount of protein in laver, and its composition is balanced, utilizing modern biotechnology to carry out deep processing to protein resource, reasonably select enzyme etc., by making the research of biologically active peptides, there is more wide prospect by the product yield of process optimization biologically active peptides.
Summary of the invention
The invention provides main laver antioxidation polypeptide and preparation method thereof, anti-oxidant activity is realized efficiently.
A kind of antioxidation polypeptide of the present invention, aminoacid sequence is avvkeagdacf.
Present invention also offers a kind of preparation method of antioxidation polypeptide, is that raw material extracts albumen with laver, and then adopt aspartic protease to carry out enzymolysis to it, separation and purification, lyophilize obtain antioxidation polypeptide; Described enzymatic hydrolysis condition is: pH is 4.0, temperature 45 C, enzymolysis time are 7h, enzyme-substrate proportioning is 3000U/g; Described enzyme is aspartic protease.The means of described separation and purification comprise ultrafiltration, SP-Sephadex C-25 ion-exchange chromatography, Sephadex G-50 molecular sieve and RP-HPLC RPLC.
The concrete steps of described separation and purification are:
(1) first enzymolysis product utilizes molecular weight to retain the ultra-filtration membrane that scope is 8000Da and 3500Da to carry out ultra-filtration and separation to enzymolysis product, be divided into the component that 3 molecular weight ranges are different, be respectively molecular weight and be greater than the component of 8000Da, molecular weight be less than 3500Da component between the component of 3500Da and 8000Da, molecular weight; (2) component with best anti-oxidant activity is collected, be separated with SP-Sephadex C-25 cation-exchange chromatography again, non-absorbed component is washed away after loading, linear gradient elution is carried out again with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer solution containing 0 ~ 0.35mol/L NaCl, flow velocity is 0.5ml/min, measure under 225nm, measure the anti-oxidant activity of elution fraction corresponding to each absorption peak; (3) collect the peak with best anti-oxidant activity, then be separated with Sephadex G-50 gel chromatography, elutriant is deionized water, and flow velocity is 0.5ml/min, measures under 225nm, measures the anti-oxidant activity of elution fraction corresponding to each absorption peak; (4) peak with best anti-oxidant activity is collected, sharp RP-HPLC RPLC is further separated again, RP-HPLC RPLC is utilized further to be separated the best anti-oxidant activity component separated, chromatographic column used is Gemini 5 μ C18, applied sample amount is 100 μ L, flow velocity is 1ml/min, and determined wavelength is 225nm.The self-contained volume fraction of elutriant is that the mixed solution of 10% acetonitrile and 90% water (v/v) starts, the mixed solution being 90% acetonitrile and 10% water (v/v) to volume fraction terminates, carry out gradient elution, collected volume mark is the elution peak at 25% acetonitrile and 75 % water (v/v) places, obtains highly purified antioxidation polypeptide of the present invention.Utilize proteinaceous solid facies sequence analysis instrument to identify the aminoacid sequence of polypeptide, the aminoacid sequence obtaining antioxidation polypeptide of the present invention is: avvkeagdacf.
In order to realize such scheme, the concrete steps that the present invention takes are as follows:
(1) extraction of laver albumen
Laver albumen of the present invention is that difference fermentation obtains.
Purple laver protein extracting factor is: cleaned 3-5 time by laver, ultrasonic disruption, lixiviate.Lixiviate pH is 8.0, and solid-liquid ratio is 20:1(weight ratio).Extraction time 6h, centrifugal 10000g 20 minutes, collect supernatant liquor, after filtration, concentrates and obtain laver albumen after lyophilize.
(2) enzymolysis of laver albumen
Enzyme is purchased from Shanghai biological reagent company (Chinese Shanghai).
Adopt aspartic protease enzymolysis laver albumen, protein concentration is 30mg/ml, enzymatic hydrolysis condition gets that pH is 4.0, temperature 45 C, enzymolysis time are 7h, enzyme-to-substrate is than being 3000U/g, regulate pH to stablize with 2M HCl, after hydrolysis 5h, go out in boiling water bath enzyme 15min, then room temperature is cooled to rapidly, be placed in whizzer, with the centrifugal 15min of 4000r/min, get supernatant liquor for subsequent use.
(3) separation of enzymolysis product, purifying
Utilized by the enzymolysis product obtained molecular weight to retain the ultra-filtration membrane that scope is 8000Da and 3500Da and ultra-filtration and separation is carried out to enzymolysis product, be divided into the component that 3 molecular weight ranges are different, be respectively molecular weight and be greater than the component of 8000Da, molecular weight be less than 3500Da component between the component of 3500Da and 8000Da, molecular weight; Collect the component with best anti-oxidant activity, again through SP-Sephadex C-25 cation-exchange chromatography (long 20cm, diameter 1.6cm) be separated, carry out linear gradient elution with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer solution containing 0 ~ 0.35mol/L NaCl, flow velocity is 0.5ml/min; Collect and there is the peak of best anti-oxidant activity, then use the long 100cm of Sephadex G-50(, diameter 2.6cm) gel chromatography is separated, and elutriant is deionized water, and flow velocity is 0.5ml/min, and elution peak is measured under 225nm; Collect the peak with best anti-oxidant activity, utilize RP-HPLC RPLC to be further separated, chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and determined wavelength is 225nm.The mixed solution of self-contained 10% acetonitrile of elutriant and 90% water (v/v) starts, mixed solution to 90% acetonitrile and 10% water (v/v) terminates, carry out gradient elution, collect the elution peak at 25% acetonitrile and 75 % water (v/v) places, obtain highly purified antioxidation polypeptide of the present invention.
(4) determined amino acid sequence of antioxidation polypeptide
Proteinaceous solid facies sequence analysis instrument (Applied Biosystems Model 476A, Perkin Elmer Co. MA, U.S.A) is utilized to measure the overall amino acid sequence of antioxidation polypeptide of the present invention.
(5) test of anti-oxidant activity
A. the mensuration of DPPH radical scavenging activity:
Utilize DPPH(1,1-Diphenyl-2-picryl-hydrazyl) free radical scavenging activity assay method research antioxidation polypeptide.Compound concentration is 1 × 10
-5the DPPH ethanolic soln of mol/L, keeps in Dark Place.The DPPH ethanol solution of 2mL, 0.1mM is joined in the clean tube containing the different enzymolysis sample of 2mL, mixing.After ambient temperatare puts 30min, measure absorbancy in 517 nm places, light absorption value is less, shows that radical scavenging activity is stronger.
Clearance rate (%)=(1-(A
i-A
j)/A
0) × 100%
In formula, A
0be the sample solvent of the DPPH ethanol solution+2mL of 2 mL, 0.1mM, blank; A
ifor the sample of the DPPH ethanol solution+2mL of 2mL, 0.1mM; A
jfor the sample of dehydrated alcohol+2 mL of 2mL.
B. the mensuration of ABTS free radical scavenging activity:
With deionized water, ABTS is dissolved, make ABTS concentration reach 7mmol/L, add Potassium Persulphate, make the concentration of Potassium Persulphate be 2.45 mmol/L.Afterwards this solution is at room temperature placed in dark place to spend the night 12 ~ 16h.By ABTS free-atom aqueous solution phosphoric acid buffer (PBS, 0.2 mol/L, the pH 7.4) dilution generated, its light absorption value under 734nm is made to be 0.70.Get 0.1ml enzymolysis solution to mix with the free base fluid of 2.9ml ABTS, shake up 30s, 10 min are reacted in dark place, then the light absorption value of assaying reaction liquid under 734nm.Hydrolyzed solution is replaced to do with distilled water blank.
Clearance rate (%)=(A
0-A
j)/A
0× 100%
In formula, A
0it is the light absorption value of 2.9 mL ABTS reagent and 0.1 mL distilled water mixed solution; A
jit is the light absorption value of 2.9 mL ABTS reagent and 0.1 mL enzymolysis solution mixed solution.
C. the mensuration of anti-peroxidation activity
The egg yolk fresh with equal-volume and phosphoric acid buffer (pH7.4,0.1mol/L) mixing, dilution 25 times before using also stirs with magnetic stirrer.2.4ml yolk diluent, 2.4ml 25mmol/L FeSO is added respectively in test tube
4h
2o, 200 μ L hydrolyzed solution samples, after mixing at 37 DEG C water-bath 4h, add 0.8ml 50% trichoroacetic acid(TCA) and 2ml TBA, at 95 DEG C of constant temperature 30min after mixing.After being cooled to room temperature, the centrifugal 20min of 8000r/min, gets supernatant liquor and measure light absorption value under 532nm.Replace hydrolyzed solution as blank using distilled water.
Inhibiting rate (%)=((A
0-A
j)/A
0) × 100%
In formula, A
0for sky is from the absorbancy of control group; A
jfor the absorbancy of sample sets.
The present invention is based on the antioxidant finding a kind of efficiency natural, to come from laver albumen for starting point, controlled by the cutting condition of aspartic protease, be cut into the active polypeptide with specific peptide chain length and structural domain composition, and anti-oxidant activity is realized efficiently.
The present invention changes the extraction of existing antioxidant and the thinking and countermeasure of utilization, eliminates the side effect that synthetic antioxidant may cause, and is a kind of natural antioxidants, can replaces traditional synthetized oxidation preventive agent.And present invention also improves China to laver protein utilization rate situation on the low side, both the recycling problem of a large amount of aquatic resources can have been solved, human consumer can be removed again to the misgivings of antioxidant in food safety, will profound significance be had to the development of science and technology, economy and grocery trade.
Accompanying drawing explanation
Fig. 1 is the RP-HPLC collection of illustrative plates of antioxidation polypeptide.
Fig. 2 is " amount-effect " relation curve of the antioxidation polypeptide removing DPPH free radical of purifying.
Fig. 3 is " amount-effect " relation curve of the antioxidation polypeptide removing ABTS free radical of purifying.
Fig. 4 is that the antioxidation polypeptide of purifying suppresses Fe
2+" amount-effect " relation curve of induction lipovitellinin polyunsaturated fatty acid peroxidation.
Embodiment
Preparation method is as follows:
Be that raw material extracts albumen with laver, then use aspartic protease to carry out enzymolysis to it, protein concentration is 30mg/ml, pH is 4.0, temperature 45 C, enzymolysis time are 7h, enzyme-substrate proportioning is 3000U/g; Utilized by the enzymolysis product obtained molecular weight to retain the ultra-filtration membrane that scope is 8000Da and 3500Da and ultra-filtration and separation is carried out to enzymolysis product, be divided into the component that 3 molecular weight ranges are different, be respectively molecular weight and be greater than the component of 8000Da, molecular weight be less than 3500Da component between the component of 3500Da and 8000Da, molecular weight; Collect the component with best anti-oxidant activity, again through SP-Sephadex C-25 cation-exchange chromatography (long 20cm, diameter 1.6cm) be separated, linear gradient elution is carried out with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer solution containing 0 ~ 0.35mol/L NaCl, flow velocity is 0.5ml/min, measures under 225nm; Collect and there is the peak of best anti-oxidant activity, then use the long 100cm of Sephadex G-50(, diameter 2.6cm) gel chromatography is separated, and elutriant is deionized water, and flow velocity is 0.5ml/min, and elution peak is measured under 225nm; Collect the peak with best anti-oxidant activity, utilize RP-HPLC RPLC to be further separated, chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and determined wavelength is 225nm.The mixed solution of self-contained 10% acetonitrile of elutriant and 90% water (v/v) starts, and the mixed solution to 90% acetonitrile and 10% water (v/v) terminates, and carries out gradient elution, obtains highly purified specific anti-oxidative polypeptide of the present invention.
The instrument that the present invention adopts, detection means are as follows:
The multiple separation and purification means such as the present invention's application ultrafiltration, SP-Sephadex C-25 ion-exchange chromatography, Sephadex G-50 gel filtration chromatography, RP-HPLC RPLC, realize the high efficiency separation purifying with the antioxidation polypeptide of remarkable activity.
Protein solid-phase sequencer (Applied Biosystems Model 476A, Perkin Elmer Co. MA, U.S.A) is utilized to measure the aminoacid sequence of the antioxidation polypeptide after purifying.
In order to understand content of the present invention, Characteristic further, hereby exemplify following examples:
Embodiment 1
Take 7.5 grams of laver albumen deionized water dissolvings and be settled to 250ml, then using 2mol/L HCl by its pH regulator to 4.0.First this solution water-bath is heated to 45 DEG C, the ratio being then 3000U/g according to enzyme-substrate proportioning again adds the enzyme of respective amount, and enzymolysis time is 7 hours.Then go out enzyme 15 minutes in boiling water bath, centrifugal 15 minutes of 4000rpm again after cooling.Collection supernatant liquor is for subsequent use.
The scope that retained by supernatant liquor molecular weight is that the ultra-filtration membrane of 8000Da and 3500Da carries out ultra-filtration and separation, be divided into the component that 3 molecular weight ranges are different, be respectively molecular weight and be greater than the component of 8000Da, molecular weight be less than 3500Da component between the component of 3500Da and 8000Da, molecular weight, and measure its anti-oxidant activity.The component that molecular weight is less than 3500Da has best anti-oxidant activity.
Collect the component that molecular weight is less than 3500Da, with SP-Sephadex C-25 cation-exchange chromatography (long 20cm, diameter 1.6cm) be further separated, linear gradient elution is carried out with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer solution containing 0 ~ 0.35mol/L NaCl, flow velocity is 0.5ml/min, elution peak is measured under 225nm, collects each peak and measures anti-oxidant activity.
The anti-oxidant activity the most obvious component peaks Sepadex G-50 gel filtration chromatography (long 20cm, diameter 1.6cm) separated be separated, elutriant is deionized water, and flow velocity is 0.5ml/min, and elution peak is measured under 225nm again.Collect each peak and measure anti-oxidant activity.
Utilize RP-HPLC RPLC to be further separated the best anti-oxidant activity component separated, chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and determined wavelength is 215nm.The mixed solution of self-contained 10% acetonitrile of elutriant and 90% water (v/v) starts, mixed solution to 90% acetonitrile and 10% water (v/v) terminates, and carries out gradient elution, collects the elution peak at 25% acetonitrile and 75 % water (v/v) places, obtain highly purified specific anti-oxidative polypeptide of the present invention, as shown in Figure 1.C peak is the chromatographic peak of this antioxidation polypeptide.Obtain highly purified anti-oxidation peptide.
Antioxidation polypeptide after purifying has very strong resistance of oxidation, and as can be seen from Fig. 2, Fig. 3 and Fig. 4, it has the ability of stronger removing DPPH free radical, ABTS free radical and anti-lipid peroxidation reaction.
Protein solid-phase sequencer (Applied Biosystems Model 476A, Perkin Elmer Co. MA, U.S.A) is utilized to measure the aminoacid sequence of the antioxidation polypeptide after purifying.Obtaining its overall amino acid sequence is: avvkeagdacf.
The foregoing is only preferred embodiment of the present invention, all equalizations done according to the present patent application the scope of the claims change and modify, and all should belong to covering scope of the present invention.
SEQUENCE LISTING
<110> University of Fuzhou
<120> mono-main laver antioxidation polypeptide and preparation method thereof
<130> 1
<160> 1
<170> PatentIn version 3.3
<210> 1
<211> 11
<212> PRT
<213> antioxidation polypeptide
<400> 1
Ala Val Val Lys Glu Ala Gly Asp Ala Cys Phe
1 5 10
Claims (5)
1. a main laver antioxidation polypeptide, is characterized in that: the aminoacid sequence of described antioxidation polypeptide is:
avvkeagdacf。
2. a preparation method for antioxidation polypeptide, is characterized in that: be that raw material extracts albumen with laver, and then adopt aspartic protease to carry out enzymolysis to it, separation and purification, lyophilize obtain antioxidation polypeptide.
3. the preparation method of a kind of antioxidation polypeptide according to claim 2, is characterized in that: described enzymatic hydrolysis condition is: pH is 4.0, temperature 45 C, enzymolysis time are 7h, enzyme-substrate proportioning is 3000U/g; Described enzyme is aspartic protease.
4. the preparation method of antioxidation polypeptide according to claim 2, is characterized in that: the means of described separation and purification comprise ultrafiltration, SP-Sephadex C-25 ion-exchange chromatography, Sephadex G-50 molecular sieve and RP-HPLC RPLC.
5. the preparation method of described antioxidation polypeptide is required according to right 2, it is characterized in that: the concrete steps of described separation and purification are: first (1) enzymolysis product utilizes molecular weight to retain the ultra-filtration membrane that scope is 8000Da and 3500Da to carry out ultra-filtration and separation to enzymolysis product, be divided into the component that 3 molecular weight ranges are different, be respectively molecular weight and be greater than the component of 8000Da, molecular weight be less than 3500Da component between the component of 3500Da and 8000Da, molecular weight; (2) component with best anti-oxidant activity is collected, be separated with SP-Sephadex C-25 cation-exchange chromatography again, non-absorbed component is washed away after loading, linear gradient elution is carried out again with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer solution containing 0 ~ 0.35mol/L NaCl, flow velocity is 0.5ml/min, measure under 225nm, measure the anti-oxidant activity of elution fraction corresponding to each absorption peak; (3) collect the peak with best anti-oxidant activity, then be separated with Sephadex G-50 gel chromatography, elutriant is deionized water, and flow velocity is 0.5ml/min, measures under 225nm, measures the anti-oxidant activity of elution fraction corresponding to each absorption peak; (4) peak with best anti-oxidant activity is collected, sharp RP-HPLC RPLC is further separated again, chromatographic column used is Gemini 5 μ C18, applied sample amount is 100 μ L, flow velocity is 1ml/min, determined wavelength is 215nm, the self-contained volume fraction of elutriant is that the mixed solution of 10% acetonitrile and 90% water starts, the mixed solution being 90% acetonitrile and 10% water to volume fraction terminates, carry out gradient elution, collected volume mark is the elution peak at 25% acetonitrile and 75 % water places, obtains highly purified antioxidation polypeptide of the present invention; Proteinaceous solid facies sequence analysis instrument is utilized to identify the aminoacid sequence of polypeptide.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510065376.5A CN104628823B (en) | 2015-02-09 | 2015-02-09 | One main laver antioxidation polypeptide and preparation method thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510065376.5A CN104628823B (en) | 2015-02-09 | 2015-02-09 | One main laver antioxidation polypeptide and preparation method thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN104628823A true CN104628823A (en) | 2015-05-20 |
| CN104628823B CN104628823B (en) | 2017-10-20 |
Family
ID=53208106
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510065376.5A Active CN104628823B (en) | 2015-02-09 | 2015-02-09 | One main laver antioxidation polypeptide and preparation method thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN104628823B (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106589068A (en) * | 2017-02-08 | 2017-04-26 | 福州大学 | Snapper anti-oxidation polypeptide and preparation method thereof |
| CN108794571A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | Antioxidation polypeptide is isolated and purified using black sharkskin |
| CN108794575A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | A kind of preparation method of black sharkskin antioxidation polypeptide |
| CN115947780A (en) * | 2022-08-29 | 2023-04-11 | 成都大学 | Polypeptide and preparation method and application thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102276708A (en) * | 2011-08-04 | 2011-12-14 | 连云港金海地食品有限公司 | Method for continuously preparing protein, polysaccharide, amino acid, taurine and polypeptide from laver |
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
-
2015
- 2015-02-09 CN CN201510065376.5A patent/CN104628823B/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102276708A (en) * | 2011-08-04 | 2011-12-14 | 连云港金海地食品有限公司 | Method for continuously preparing protein, polysaccharide, amino acid, taurine and polypeptide from laver |
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
Non-Patent Citations (1)
| Title |
|---|
| 姚翔等: "低值紫菜蛋白酶解产物中抗氧化活性肽的纯化及分析鉴定", 《食品与生物技术学报》 * |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106589068A (en) * | 2017-02-08 | 2017-04-26 | 福州大学 | Snapper anti-oxidation polypeptide and preparation method thereof |
| CN106589068B (en) * | 2017-02-08 | 2020-09-01 | 福州大学 | Sea bream antioxidant polypeptide and preparation method thereof |
| CN108794571A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | Antioxidation polypeptide is isolated and purified using black sharkskin |
| CN108794575A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | A kind of preparation method of black sharkskin antioxidation polypeptide |
| CN115947780A (en) * | 2022-08-29 | 2023-04-11 | 成都大学 | Polypeptide and preparation method and application thereof |
| CN115947780B (en) * | 2022-08-29 | 2023-09-19 | 成都大学 | Polypeptide and preparation method and application thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| CN104628823B (en) | 2017-10-20 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN103819541B (en) | A kind of micro-algae antioxidation polypeptide | |
| CN104356200A (en) | Anti-oxidative peptide and preparation method thereof | |
| CN104356201A (en) | Holothurian antioxidative peptide | |
| CN103880933B (en) | A kind of antioxidation polypeptide | |
| CN103804476B (en) | A kind of antioxidation polypeptide and its preparation method | |
| CN104402972A (en) | Sea cucumber antioxidant polypeptide and preparation method thereof | |
| CN102219828B (en) | Antioxidation polypeptide prepared from sharkskin collagen | |
| CN102219829B (en) | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease | |
| CN102219830B (en) | Oxidation resisting polypeptide and preparation method thereof | |
| Yang et al. | Preparation and characterization of gelatin and antioxidant peptides from gelatin hydrolysate of skipjack tuna (Katsuwonus pelamis) bone stimulated by in vitro gastrointestinal digestion | |
| Girard et al. | Mixotrophic cultivation of green microalgae Scenedesmus obliquus on cheese whey permeate for biodiesel production | |
| CN104610430A (en) | Antioxidant peptide prepared by utilizing lucid ganoderma albumen and preparation method thereof | |
| CN104628823A (en) | Anti-oxidative seaweed polypeptide and preparation method thereof | |
| CN108794577A (en) | A kind of preparation method of antioxidation polypeptide | |
| CN111647072A (en) | Antioxidant peptide and preparation method and application thereof | |
| CN102180945A (en) | Small peptides extracted from internal organs of squids, method for preparing same, composition thereof and use thereof as protein source of marine aquatic feed | |
| CN106892965A (en) | Antioxidation polypeptide prepared by a kind of utilization compound protease | |
| PT2326708E (en) | Photosynthetic microorganisms enriched in selenium using selenohydroxy acid compounds, uses thereof in nutrition, cosmetics and pharmacy | |
| CN103233054A (en) | Method for continuously preparing silkworm chrysalis protein antioxidant peptides by using enzyme membrane reactor | |
| CN106511383A (en) | Quick preparation method for ultrasonic-assisted extraction of effective components of lamb abomasum | |
| CN106589068B (en) | Sea bream antioxidant polypeptide and preparation method thereof | |
| CN101928744A (en) | Process for extracting active collagen peptide from salmon trout waste | |
| CN111269290A (en) | Sturgeon anti-inflammatory peptide preparation method | |
| CN116284341B (en) | Preparation and application of deep sea fish skin collagen peptide with low immunogenicity, blood pressure reduction and oxidation resistance | |
| CN104650191A (en) | Antioxidant polypeptide prepared from laver protein and preparation method of antioxidant polypeptide |
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 | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20230925 Address after: No. 9, Dingshan Road, Biomedical Port, Haicang District, Xiamen, Fujian, 361000 Patentee after: XIAMEN BLUE BAY SCIENCE&TECHNOLOGY CO.,LTD. Address before: 350108 new campus of Fuzhou University, No. 2, Xue Yuan Road, University Town, Minhou street, Minhou, Fujian. Patentee before: FUZHOU University |
|
| TR01 | Transfer of patent right |