CN103804476A - Anti-oxidation polypeptide and preparation method thereof - Google Patents
Anti-oxidation polypeptide and preparation method thereof Download PDFInfo
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- CN103804476A CN103804476A CN201410079701.9A CN201410079701A CN103804476A CN 103804476 A CN103804476 A CN 103804476A CN 201410079701 A CN201410079701 A CN 201410079701A CN 103804476 A CN103804476 A CN 103804476A
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Abstract
The invention provides an anti-oxidation polypeptide and a preparation method thereof. The preparation method comprises the steps: with a chlorella protein as a raw material, through enzymolysis of an acid proteinase, separating and purifying to obtain the anti-oxidation polypeptide, wherein a complete sequence of an amino acid is aviknyya. According to the anti-oxidation polypeptide, the defect of a natural antioxidant is eliminated, the worry of manually synthesizing the antioxidant by the public is eliminated, and the foundation is laid for developing the anti-oxidation polypeptide based on a food source and exploring the wide application to the food and the medicine.
Description
Technical field
The invention provides a kind of 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, can inevitably produce along with the process of oxygen metabolism with the free free radical of many middle disease-relateds such as arteriosclerosis, cancer.In food, the oxidation of food nutrient composition can produce superoxide, and it not only can affect Nutritive value of food, causes that Food Quality declines, the serious health generation disease that even also can cause absorption person.Therefore, find safe antioxidant is the study hotspot that biochemistry nutrition is learned to suppress superoxide generation always.Because the chemosynthesis such as BHT, TBHQ antioxidant has better effect and more cheap price than natural antioxidants, therefore it has been widely used in food service industry.But, studies have found that at present synthetized oxidation preventive agent has the property of accumulating carcinogenesis to organs such as human liver, spleen, lungs, thereby caused the worry of people to its security, and start to limit gradually its use in food.So people turn to natural antioxidants sight.Alpha-tocopherol is a kind of by the natural antioxidants the most generally using, and it can effectively keep the stability of grease in food, but is but unfavorable for Food preservation.Therefore, we are necessary the natural antioxidants of the safety of finding a kind of other source.
Polypeptide is the compounds of molecular structure between amino acid and protein, makes protein have certain physiological function.In the mankind's vital movement, peptide digesting and assimilating is in vivo better than free amino acid, and is different from delivery system in amino acid whose body.Some small peptide, in people's bulk-growth being provided, growing necessary nutritive substance, can also be prevented and cured diseases, and regulates function of human body, and these have bioactive polypeptide and are called as biologically active peptides.Research is found, the polypeptide of a lot of different sourcess all has resistance of oxidation, and the polypeptide obtaining 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 micro-algae resource, but because resource utilization is low, the reasons such as the tankage waste that the course of processing produces cause the wasting of resources, or even environmental pollution.In micro-algae, contain a large amount of protein, and it forms balanced, utilize modern biotechnology to carry out deep processing to protein resource, reasonably select enzyme etc., by the product yield of process optimization biologically active peptides, the research that makes biologically active peptides is had to more wide prospect.
Summary of the invention
The invention provides a kind of antioxidation polypeptide and preparation method thereof, anti-oxidant activity is realized efficiently.
The present invention adopts following technical scheme:
A kind of antioxidation polypeptide, the aminoacid sequence of described antioxidation polypeptide is: aviknyya.
A preparation method for antioxidation polypeptide, extracts albumen take chlorella as raw material, then adopt aspartic protease to carry out enzymolysis to it, and separation and purification, lyophilize obtain antioxidation polypeptide.
Described enzymatic hydrolysis condition is: pH is 3.0, temperature 50 C, enzymolysis time are that 5h, enzyme-substrate proportioning are 3000U/g; Described enzyme is aspartic protease.
The method of described separation and purification comprises 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 hold back the ultra-filtration membrane that scope is 8000Da and 3500Da enzymolysis product is carried out to ultra-filtration and separation, be divided into 3 components that molecular weight ranges is different, be respectively component, molecular weight that molecular weight is greater than 8000Da between the component of 3500Da and 8000Da, the component that molecular weight is less than 3500Da;
(2) collect the component with best anti-oxidant activity, separate with SP-Sephadex C-25 cation-exchange chromatography again, after loading, wash away not absorbed component, carry out linear gradient elution with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer containing 0～0.35mol/L NaCl again, flow velocity is 0.5ml/min, under 225nm, measure, measure the anti-oxidant activity of the elution fraction that each absorption peak is corresponding;
(3) collect and have the peak of best anti-oxidant activity, then separate with Sephadex G-50 gel chromatography, elutriant is deionized water, and flow velocity is 0.5ml/min, under 225nm, measures, and measures the anti-oxidant activity of the elution fraction that each absorption peak is corresponding;
(4) collect the peak with best anti-oxidant activity, recycling RP-HPLC RPLC further separates, and chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and detection wavelength is 215nm; The self-contained volume ratio of elutriant is that the mixed solution of 10% acetonitrile and 90% water starts, and the mixed solution that is 90% acetonitrile and 10% water to volume ratio finishes, and carries out gradient elution, and collected volume, than the elution peak that is 61% acetonitrile and 39 % water places, obtains required antioxidation polypeptide; Utilize proteinaceous solid facies sequence analysis instrument to identify the aminoacid sequence of polypeptide.
The present invention is based on finding a kind of antioxidant of efficiency natural, to come from chlorella albumen as starting point, by the cutting condition control 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 has changed the extraction of existing antioxidant and the thinking of utilization and method, has eliminated the side effect that synthetic antioxidant may cause, is a kind of natural antioxidants, can replace traditional synthetized oxidation preventive agent.And the present invention has also improved China to micro-algae protein utilization rate situation on the low side, what both can solve a large amount of micro-algae resources efficiently utilizes problem, can remove again human consumer to antioxidant in the misgivings aspect food safety, will there is profound significance 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 that the antioxidation polypeptide of purifying is removed DPPH free radical.
Fig. 3 is " amount-effect " relation curve that the antioxidation polypeptide of purifying is removed ABTS free radical.
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:
(1) extraction of chlorella albumen
Chlorella albumen of the present invention is that difference fermentation obtains.
Chlorella proteins extraction processing condition are: chlorella cleaned 3-5 time, ultrasonic wave (add tween, concentration 0.1%) fragmentation, lixiviate.Lixiviate pH is 8.0, and solid-liquid ratio is 20:1(weight ratio).Extraction time 6h, centrifugal 10000g 20 minutes, collects supernatant liquor, after filtration, obtain chlorella albumen after concentrated and lyophilize.
(2) enzymolysis of chlorella albumen
Enzyme is purchased from Shanghai biological reagent company (Chinese Shanghai).
Adopt aspartic protease Chlorella albumen, protein concentration is 30mg/ml, enzymatic hydrolysis condition gets that pH is 3.0, temperature 50 C, enzymolysis time are that 5h, enzyme-to-substrate are than being (3000U/g), with 2M HCl adjusting, pH is stable, and after hydrolysis 5h, enzyme 15min goes out in boiling water bath, then be cooled to rapidly room temperature, be placed in whizzer, with the centrifugal 15min of 4000r/min, get supernatant liquor for subsequent use.
(3) separation of enzymolysis product, purifying
Utilize molecular weight to hold back the ultra-filtration membrane that scope is 8000Da and 3500Da the enzymolysis product obtaining enzymolysis product is carried out to ultra-filtration and separation, be divided into 3 components that molecular weight ranges is different, be respectively component, molecular weight that molecular weight is greater than 8000Da between the component of 3500Da and 8000Da, the component that molecular weight is less than 3500Da; Collection has the component of best anti-oxidant activity, pass through again SP-Sephadex C-25 cation-exchange chromatography (long 20cm, diameter 1.6cm) separate, carry out linear gradient elution with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer containing 0～0.35mol/L NaCl, flow velocity is 0.5ml/min, under 225nm, measures; Collection has the peak of best anti-oxidant activity, then with the long 100cm of Sephadex G-50(, diameter 2.6cm) gel chromatography separates, and elutriant is deionized water, and flow velocity is 0.5ml/min, and elution peak is measured under 225nm; Collection has the peak of best anti-oxidant activity, utilizes RP-HPLC RPLC further to separate, and chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and detection wavelength is 225nm.The mixed solution of self-contained 10% acetonitrile of elutriant and 90% water (v/v) starts, and finishes to the mixed solution of 90% acetonitrile and 10% water (v/v), carries out gradient elution, obtains highly purified specificity antioxidation polypeptide of the present invention.
(4) 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) to measure the amino acid complete sequence of antioxidation polypeptide of the present invention.
(5) test of anti-oxidant activity
A) 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.By 2mL, the DPPH ethanol solution of 0.1mM joins in the clean tube that contains the different enzymolysis samples of 2mL, mixes.Under room temperature, place after 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 2 mL, the sample solvent of DPPH ethanol solution+2mL of 0.1mM, blank; A
ifor 2mL, the sample of DPPH ethanol solution+2mL of 0.1mM; A
jfor the sample of dehydrated alcohol+2 mL of 2mL.
B) mensuration of ABTS free radical scavenging activity
With deionized water, ABTS is dissolved, make ABTS concentration reach 7mmol/L, add Potassium Persulphate, the concentration that makes Potassium Persulphate is 2.45 mmol/L.Afterwards this solution is at room temperature placed in to the dark place 12～16h that spends the night.By the ABTS generating phosphoric acid buffer (PBS, 0.2 mol/L, pH 7.4) dilution for free-atom aqueous solution, making its light absorption value under 734nm is 0.70.Get 0.1ml enzymolysis solution and 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.Replace hydrolyzed solution 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) mensuration of anti-peroxidation activity
Mix 25 times of dilutions stirring with magnetic stirrer before using with the fresh egg yolk of equal-volume and phosphoric acid buffer (pH7.4,0.1mol/L).In test tube, add respectively 2.4ml yolk diluent, 2.4ml 25mmol/L FeSO
4h
2o, 200 μ L hydrolyzed solution samples, after mixing at 37 ℃ water-bath 4h, add 0.8ml 50% trichoroacetic acid(TCA) and 2ml TBA, after mixing at 95 ℃ of constant temperature 30min.Be cooled to after 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.
In order further to understand content of the present invention, Characteristic, hereby exemplify following examples:
Embodiment 1
Take 7.5 grams of chlorella albumen deionized water dissolvings and be settled to 250ml, then using 2mol/L HCl by its pH regulator to 3.0.First this solution water-bath is heated to 50 ℃, the ratio that is then 3000U/g according to enzyme-substrate proportioning again adds the enzyme of respective amount, and enzymolysis time is 5 hours.Then go out in boiling water bath enzyme 15 minutes, cooling after centrifugal 15 minutes of 4000rpm again.Collection supernatant liquor is for subsequent use.
It is that the ultra-filtration membrane of 8000Da and 3500Da carries out ultra-filtration and separation that supernatant liquor is held back to scope with molecular weight, be divided into 3 components that molecular weight ranges is different, be respectively component, molecular weight that molecular weight is greater than 8000Da between the component of 3500Da and 8000Da, the component that molecular weight is less than 3500Da, and measure its anti-oxidant activity.The component that molecular weight is less than 3500Da has best anti-oxidant activity.
Collection molecular weight is less than the component of 3500Da, with SP-Sephadex C-25 cation-exchange chromatography (long 20cm, diameter 1.6cm) further separate, carry out linear gradient elution with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer 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 most obvious the anti-oxidant activity of separating component peaks is separated by Sepadex G-50 gel filtration chromatography (long 20cm, diameter 1.6cm) again, and elutriant is deionized water, and flow velocity is 0.5ml/min, and elution peak is measured under 225nm.Collect each peak and measure anti-oxidant activity.
Utilize RP-HPLC RPLC further to separate the best anti-oxidant activity component of separating, chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and detection 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) finishes, carry out gradient elution, collect the elution peak that 61% acetonitrile and 39 % water (v/v) are located, obtain highly purified specificity antioxidation polypeptide of the present invention, as shown in Figure 1, the chromatographic peak that T peak is this antioxidation polypeptide.Obtain highly purified anti-oxidation peptide.
Antioxidation polypeptide after purifying has very strong resistance of oxidation, can be found out by Fig. 2, Fig. 3 and Fig. 4, and it has stronger removing DPPH free radical, ABTS free radical and suppresses the ability of peroxidatic reaction of lipid.
Utilize protein solid phase sequenator (Applied Biosystems Model 476A, Perkin Elmer Co. MA, U.S.A) to measure the aminoacid sequence of the antioxidation polypeptide after purifying.Obtaining its amino acid total order classifies as: aviknyya.
The foregoing is only preferred embodiment of the present invention, all equalizations of doing 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> antioxidation polypeptide and preparation method thereof
<130> 1
<160> 1
<170> PatentIn version 3.3
<210> 1
<211> 8
<212> PRT
<213> metal chelating peptide
<400> 1
Ala Val Ile Lys Asn Tyr Tyr Ala
1 5
Claims (5)
1. an antioxidation polypeptide, is characterized in that: the aminoacid sequence of described antioxidation polypeptide is: aviknyya.
2. a preparation method for a kind of antioxidation polypeptide as claimed in claim 1, is characterized in that: extract albumen take chlorella as raw material, 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 3.0, temperature 50 C, enzymolysis time are that 5h, enzyme-substrate proportioning are 3000U/g; Described enzyme is aspartic protease.
4. the preparation method of a kind of antioxidation polypeptide according to claim 2, is characterized in that: the method for described separation and purification comprises ultrafiltration, SP-Sephadex C-25 ion-exchange chromatography, Sephadex G-50 molecular sieve and RP-HPLC RPLC.
5. the preparation method of a kind of antioxidation polypeptide according to claim 2, is characterized in that: the concrete steps of described separation and purification are:
(1) first enzymolysis product utilizes molecular weight to hold back the ultra-filtration membrane that scope is 8000Da and 3500Da enzymolysis product is carried out to ultra-filtration and separation, be divided into 3 components that molecular weight ranges is different, be respectively component, molecular weight that molecular weight is greater than 8000Da between the component of 3500Da and 8000Da, the component that molecular weight is less than 3500Da;
(2) collect the component with best anti-oxidant activity, separate with SP-Sephadex C-25 cation-exchange chromatography again, after loading, wash away not absorbed component, carry out linear gradient elution with 0.02mol/L, pH4.0 acetic acid-sodium acetate buffer containing 0～0.35mol/L NaCl again, flow velocity is 0.5ml/min, under 225nm, measure, measure the anti-oxidant activity of the elution fraction that each absorption peak is corresponding;
(3) collect and have the peak of best anti-oxidant activity, then separate with Sephadex G-50 gel chromatography, elutriant is deionized water, and flow velocity is 0.5ml/min, under 225nm, measures, and measures the anti-oxidant activity of the elution fraction that each absorption peak is corresponding;
(4) collect the peak with best anti-oxidant activity, recycling RP-HPLC RPLC further separates, and chromatographic column used is Gemini 5 μ C18, and applied sample amount is 100 μ L, and flow velocity is 1ml/min, and detection wavelength is 215nm; The self-contained volume ratio of elutriant is that the mixed solution of 10% acetonitrile and 90% water starts, and the mixed solution that is 90% acetonitrile and 10% water to volume ratio finishes, and carries out gradient elution, and collected volume, than the elution peak that is 61% acetonitrile and 39 % water places, obtains required antioxidation polypeptide; Utilize proteinaceous solid facies sequence analysis instrument to identify the aminoacid sequence of polypeptide.
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Cited By (9)
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| CN104356200A (en) * | 2014-11-05 | 2015-02-18 | 福州大学 | Anti-oxidative peptide and preparation method thereof |
| CN104402972A (en) * | 2014-11-05 | 2015-03-11 | 福州大学 | Sea cucumber antioxidant polypeptide and preparation method thereof |
| CN106478770A (en) * | 2016-10-13 | 2017-03-08 | 福州大学 | A kind of Fructus Perillae oxidation resistance dipeptide and preparation method and application |
| CN106589068A (en) * | 2017-02-08 | 2017-04-26 | 福州大学 | Snapper anti-oxidation polypeptide and preparation method thereof |
| CN106892965A (en) * | 2017-02-08 | 2017-06-27 | 福州大学 | Antioxidation polypeptide prepared by a kind of utilization compound protease |
| CN108191959A (en) * | 2018-04-02 | 2018-06-22 | 广州赛莱拉干细胞科技股份有限公司 | Anti-oxidation peptide and preparation method thereof and the cosmetics comprising the anti-oxidation peptide |
| CN108794571A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | Antioxidation polypeptide is isolated and purified using black sharkskin |
| CN108822208A (en) * | 2018-06-26 | 2018-11-16 | 福州大学 | The method of antioxidation polypeptide is prepared from black sharkskin |
| CN108822207A (en) * | 2018-06-26 | 2018-11-16 | 福州大学 | The method for preparing antioxidation polypeptide using alkali protease |
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| CN104356200B (en) * | 2014-11-05 | 2018-03-16 | 福州大学 | A kind of anti-oxidation peptide and preparation method thereof |
| CN104402972A (en) * | 2014-11-05 | 2015-03-11 | 福州大学 | Sea cucumber antioxidant polypeptide and preparation method thereof |
| CN104356200A (en) * | 2014-11-05 | 2015-02-18 | 福州大学 | Anti-oxidative peptide and preparation method thereof |
| CN104402972B (en) * | 2014-11-05 | 2018-03-16 | 福州大学 | A kind of sea cucumber anti-oxidation peptide and preparation method thereof |
| CN106478770A (en) * | 2016-10-13 | 2017-03-08 | 福州大学 | A kind of Fructus Perillae oxidation resistance dipeptide and preparation method and application |
| CN106478770B (en) * | 2016-10-13 | 2019-12-17 | 福州大学 | Perilla seed antioxidant dipeptide and preparation method and application thereof |
| CN106589068A (en) * | 2017-02-08 | 2017-04-26 | 福州大学 | Snapper anti-oxidation polypeptide and preparation method thereof |
| CN106892965A (en) * | 2017-02-08 | 2017-06-27 | 福州大学 | Antioxidation polypeptide prepared by a kind of utilization compound protease |
| CN106892965B (en) * | 2017-02-08 | 2020-09-01 | 福州大学 | Antioxidant polypeptide prepared by utilizing compound protease |
| CN106589068B (en) * | 2017-02-08 | 2020-09-01 | 福州大学 | Sea bream antioxidant polypeptide and preparation method thereof |
| CN108191959A (en) * | 2018-04-02 | 2018-06-22 | 广州赛莱拉干细胞科技股份有限公司 | Anti-oxidation peptide and preparation method thereof and the cosmetics comprising the anti-oxidation peptide |
| CN108794571A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | Antioxidation polypeptide is isolated and purified using black sharkskin |
| CN108822208A (en) * | 2018-06-26 | 2018-11-16 | 福州大学 | The method of antioxidation polypeptide is prepared from black sharkskin |
| CN108822207A (en) * | 2018-06-26 | 2018-11-16 | 福州大学 | The method for preparing antioxidation polypeptide using alkali protease |
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