CN103819541B - A kind of micro-algae antioxidation polypeptide - Google Patents
A kind of micro-algae antioxidation polypeptide Download PDFInfo
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- CN103819541B CN103819541B CN201410078641.9A CN201410078641A CN103819541B CN 103819541 B CN103819541 B CN 103819541B CN 201410078641 A CN201410078641 A CN 201410078641A CN 103819541 B CN103819541 B CN 103819541B
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Abstract
The invention provides a kind of micro-algae antioxidation polypeptide, with chlorella albumen for raw material, by the enzymolysis to aspartic protease, separation and purification obtains specific anti-oxidative polypeptide, and its overall amino acid sequence is: hpnkeeplp.This invention removes defect that natural antioxidants has and eliminate the worry of the public to synthetic antioxidant, for exploitation is based on the antioxidation polypeptide of food source and explore its widespread use in food, medicine and lay the foundation.
Description
Technical field
The invention provides a kind of micro-algae antioxidation polypeptide, 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 micro-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 micro-algae, 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 a kind of micro-algae antioxidation polypeptide, anti-oxidant activity is realized efficiently.
For achieving the above object, the present invention adopts following technical scheme:
A kind of micro-algae antioxidation polypeptide, the aminoacid sequence of described peptide is hpnkeeplp.
A preparation method for micro-algae antioxidation polypeptide is that raw material extracts albumen with chlorella, 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 3.0, temperature 50 C, enzymolysis time are 5h, enzyme-substrate proportioning is 3000U/g; Described enzyme is aspartic protease.The means of described separation and purification comprise ultrafiltration, SP-SephadexC-25 ion-exchange chromatography, SephadexG-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-SephadexC-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/LNaCl, 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 SephadexG-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 Gemini5 μ C18, applied sample amount is 100 μ L, flow velocity is 1ml/min, determined wavelength is 225nm, the self-contained volume ratio 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 ratio terminates, carry out gradient elution, collected volume is than the elution peak being 25% acetonitrile and 75% water place, obtain antioxidation polypeptide.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: hpnkeeplp.
The present invention is based on the antioxidant finding a kind of efficiency natural, to come from chlorella 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 micro-algae 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, and wherein A is the absorption peak containing 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
(1) extraction of chlorella albumen
Chlorella albumen of the present invention is that difference fermentation obtains.
Chlorella protein extracting factor is: cleaned 3-5 time by chlorella, and ultrasonic wave (adding tween, concentration 0.1%) is broken, lixiviate.Lixiviate pH is 8.0, and solid-liquid ratio is 20:1(weight ratio).Extraction time 6h, centrifugal 10000g20 minute, collect supernatant liquor, after filtration, concentrates and obtain chlorella albumen after 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 5h, enzyme-to-substrate is than being (3000U/g), regulate pH to stablize with 2MHCl, 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-SephadexC-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/LNaCl, flow velocity is 0.5ml/min; Collect and there is the peak of best anti-oxidant activity, then with the long 100cm of SephadexG-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 Gemini5 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) place, obtain highly purified antioxidation polypeptide of the present invention.
(4) determined amino acid sequence of antioxidation polypeptide
The overall amino acid sequence utilizing proteinaceous solid facies sequence analysis instrument (AppliedBiosystemsModel476A, PerkinElmerCo.MA, U.S.A) to measure antioxidation polypeptide of the present invention is hpnkeeplp.
(5) test of anti-oxidant activity
1) 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 517nm place, 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
0for the sample solvent of the DPPH ethanol solution+2mL of 2mL, 0.1mM, blank; A
ifor the sample of the DPPH ethanol solution+2mL of 2mL, 0.1mM; A
jfor the sample of the dehydrated alcohol+2mL of 2mL.
2) 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 2.45mmol/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, 0.2mol/L, the pH7.4) 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 2.9mlABTS, shake up 30s, dark place reaction 10min, the then 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
0for the light absorption value of 2.9mLABTS reagent and 0.1mL distilled water mixed solution; A
jfor the light absorption value of 2.9mLABTS reagent and 0.1mL enzymolysis solution mixed solution.
3) 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, 2.4ml25mmol/LFeSO is added respectively in test tube
4h
2o, 200 μ L hydrolyzed solution samples, after mixing at 37 DEG C water-bath 4h, add 0.8ml50% trichoroacetic acid(TCA) and 2mlTBA, 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.
In order to understand content of the present invention, Characteristic further, hereby exemplify following examples:
Preparation method is as follows:
Be that raw material extracts albumen with chlorella, then use aspartic protease to carry out enzymolysis to it, protein concentration is 30mg/ml, and enzymatic hydrolysis condition is: pH is 3.0, temperature is 50 DEG C, enzymolysis time is 5 hours, 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-SephadexC-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/LNaCl, flow velocity is 0.5ml/min, measures under 225nm; Collect and there is the peak of best anti-oxidant activity, then with the long 100cm of SephadexG-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 Gemini5 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-SephadexC-25 ion-exchange chromatography, SephadexG-50 gel filtration chromatography, RP-HPLC RPLC, realize the high efficiency separation purifying with the antioxidation polypeptide of remarkable activity.
Protein solid-phase sequencer (AppliedBiosystemsModel476A, PerkinElmerCo.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 chlorella albumen deionized water dissolvings and be settled to 250ml, then with 2mol/LHCl by its pH regulator to 3.0.First this solution water-bath is heated to 50 DEG C, the ratio being then 3000U/g according to enzyme-substrate proportioning again adds the enzyme of respective amount, and enzymolysis time is 5 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-SephadexC-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/LNaCl, 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 SepadexG-50 gel filtration chromatography separated (long 20cm, diameter 1.6cm) 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 Gemini5 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) place, obtain highly purified specific anti-oxidative polypeptide of the present invention, as shown in Figure 1.A 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 (AppliedBiosystemsModel476A, PerkinElmerCo.MA, U.S.A) is utilized to measure the aminoacid sequence of the antioxidation polypeptide after purifying.Obtaining its overall amino acid sequence is: hpnkeeplp.
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.
SEQUENCELISTING
<110> University of Fuzhou
The micro-algae antioxidation polypeptide of <120> mono-kind
<130>1
<160>1
<170>PatentInversion3.3
<210>1
<211>9
<212>PRT
<213> metal chelating peptide
<400>1
HisProAsnLysGluGluProLeuPro
15
Claims (1)
1. a micro-algae antioxidation polypeptide, is characterized in that: the aminoacid sequence of described antioxidation polypeptide is:
hpnkeeplp。
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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 |
| CN104650191B (en) * | 2015-02-05 | 2018-03-27 | 福建申石蓝食品有限公司 | A kind of antioxidation polypeptide prepared using seaweed albumen |
| CN104628823B (en) * | 2015-02-09 | 2017-10-20 | 福州大学 | One main laver antioxidation polypeptide and preparation method thereof |
| CN106854241A (en) * | 2016-11-24 | 2017-06-16 | 云南民族大学 | Smelly frog skin antioxidation polypeptide AOP OA1 in Yunnan and preparation method and application |
| 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 |
| CN108185267A (en) * | 2017-12-28 | 2018-06-22 | 广州市科能化妆品科研有限公司 | A kind of anti-oxidation peptide composition and its preparation method and application |
| CN108770882A (en) * | 2018-06-06 | 2018-11-09 | 广西宾德利生物科技有限公司 | Earthworm microalgae small-molecular peptides and the preparation method and application thereof |
| CN108794577A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | A kind of preparation method of antioxidation polypeptide |
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| CN102337318A (en) * | 2011-07-26 | 2012-02-01 | 南京林业大学 | Gingko antioxidant active peptide and preparation method thereof |
| CN103039987A (en) * | 2013-01-06 | 2013-04-17 | 吉林大学 | Soybean antioxidant peptide microcapsule and preparation method thereof |
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Effective date of registration: 20220815 Address after: Room 9#, Innovation and Entrepreneurship Center, No. 7 Xinqiang Road, High-tech Zone, Hongshan Town, Shishi City, Quanzhou City, Fujian Province, 362700 Patentee after: FUJIAN ZHONGYI PHARMACEUTICAL 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 |