CN108484722A - A kind of preparation of antioxidation polypeptide and isolation and purification method - Google Patents
A kind of preparation of antioxidation polypeptide and isolation and purification method Download PDFInfo
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- CN108484722A CN108484722A CN201810670244.9A CN201810670244A CN108484722A CN 108484722 A CN108484722 A CN 108484722A CN 201810670244 A CN201810670244 A CN 201810670244A CN 108484722 A CN108484722 A CN 108484722A
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- antioxidation polypeptide
- antioxidant activity
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- polypeptide
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
- C07K5/1008—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
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- 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
Abstract
The present invention provides a kind of preparation of antioxidation polypeptide and isolation and purification method, this method is using black sharkskin as raw material, by the enzymolysis of alkali protease, isolates and purifies to obtain specific anti-oxidative polypeptide, molecular weight is in 452 Da, overall amino acid sequence：Ala‑Thr‑Val‑Tyr.This invention removes defect possessed by natural and worry of the public to artificial synthesized antioxidant is eliminated, to develop the antioxidation polypeptide based on food source and exploring its extensive use based theoretical in food, medicine.
Description
Technical field
The present invention provides a kind of preparation of antioxidation polypeptide and isolation and purification methods, have related more specifically to a kind of black shark
Fish-skin antioxidation polypeptide, belongs to biotechnology.
Background technology
Oxidation is ubiquitous in human life operating.During metabolism of human cell, generate free radicals and its
Its reactive oxygen species, when there is excessive free radical to generate, free radical is to cytoprotection enzyme, such as superoxide dismutase, peroxide
Change hydrogen enzyme and peroxidase damages, or even cause Apoptosis, such as oxidizing cellular proteins matter, membrane lipid.
In food, the oxidation of food nutrient composition will produce peroxide, can not only influence nutritive value of food,
Food quality is caused to decline, disease occurs for body that is serious or even also resulting in intake person.Therefore, it finds safe anti-oxidant
Agent is to inhibit peroxide to generate the research hotspot of always biochemical nutrition.Due to the chemical syntheses antioxidant such as BHT, TBHQ
There is better effect and less expensive price than natural, therefore it has been widely used in food service industry.
But at present studies have found that synthetized oxidation preventive agent has accumulative carcinogenic work to organs such as human liver, spleen, lungs
With so as to cause people to the worry of its safety, and beginning gradually limits its use in food.Then people's handle
Sight turns to natural.Alpha-tocopherol is a kind of natural most generally used, it can effectively keep eating
The stability of grease in product, but it is unfavorable for food preservation.Therefore, we it is necessary to find a kind of safety in other sources
Natural.
Since the communicable diseases such as aftosa, rabid ox disease took place frequently in recent years, the safe getting worse of terrestrial animal, therefore,
The safety of terrestrial animal albumen and its protein product is destroyed；Further, since having more believer of religion, land all over the world
Raw animal protein is not received by it.Therefore, there are broader market prospects by anti-oxidation peptide product made from marine fishes.
Black sharkskin is due to its shape and in uneven thickness, it is difficult to as high value added product（Such as leather and fur products）Processing and utilization.Research
It shows, protein content is high in fish-skin, and type is abundant, and especially collagen content is high（60~80%）, be fish-skin albumen mainly at
Point.In shark process of manufacture, a large amount of leftover bits and pieces is generated, these leftover bits and pieces are used for feed processing, big portion except small part
Divide and abandoned with form of waste, this not only results in environmental pollution, also causes the wasting of resources.Therefore, how to be obtained from fish-skin
High-efficiency antioxidant polypeptide with specific amino acid sequence just becomes urgent research direction.
Invention content
To solve the above-mentioned problems, the present invention provides a kind of antioxidation polypeptide prepared by black shark collagen, make
Antioxidant activity is efficiently realized.
To achieve the above object, using following technical scheme：
A kind of antioxidation polypeptide of the present invention, amino acid sequence Ala-Thr-Val-Tyr（ATVY）.
The present invention provides a kind of preparation methods of antioxidation polypeptide, using black sharkskin as raw material, using alkali protease
It is digested, isolated and purified, be freeze-dried and obtain antioxidation polypeptide；The enzymatic hydrolysis condition is：PH is 7.0 ~ 9.0, temperature
40 ~ 50 DEG C, enzymolysis time be 4.0 ~ 6.0h, concentration of substrate is 2.0 ~ 4.0%, enzyme additive amount be 9.0 ~ 10.0 wt.%.Preferably,
Enzymatic hydrolysis condition be pH be 8.0, temperature 45 C, enzymolysis time 4.9h, concentration of substrate 3%, enzyme additive amount be 9.6wt%.It is described
The means RP-HPLC reversed-phase high performance liquid chromatography isolated and purified.
It is described isolate and purify the specific steps are：
Enzymolysis product is detached using RP-HPLC reversed-phase high performance liquid chromatography, and monitors the antioxidant activity of separation component, collects tool
There is the component of best antioxidant activity；The separation of reversed-phase HPLC is with the concentration gradient of 0.05% trifluoroacetic acid containing volume fraction for 0%
~40% acetonitrile solution carries out linear elution as eluent, and chromatographic column used is 5 μ C18 of Gemini, and applied sample amount is 100 μ
L, flow velocity 1mL/min, Detection wavelength 214nm measure the antioxidant activity of the corresponding eluent of each absorption peak, and collection obtains
The highest component of antioxidant activity.The amino acid sequence that component is identified using Q-TOF LC-MS obtains the antioxidation polypeptide
Amino acid sequence be：Ala-Thr-Val-Tyr.
It takes and is as follows：
(1) enzymolysis of black shark hide collagen
Enzyme is purchased from Novozymes Company（Chinese Tianjin）.
Black shark hide collagen is digested using alkali protease, pH 8.0, temperature 45 C, enzymolysis time 4.9h, substrate are dense
Degree is 3%, and enzyme additive amount is 9.6wt%, and adjusting pH with 1M NaOH stablizes, and after hydrolyzing 5h, enzyme deactivation 15min in boiling water bath is then fast
Speed is cooled to room temperature, and is placed in a centrifuge, and is centrifuged 15min with 4000r/min, is taken supernatant spare.
(2) separation, purifying of enzymolysis product
Enzymolysis product is detached using RP-HPLC reversed-phase high performance liquid chromatography, and monitors the antioxidant activity of separation component, collects tool
There is the component of best antioxidant activity；The separation of reversed-phase HPLC is with the concentration gradient of 0.05% trifluoroacetic acid containing volume fraction for 0%
~40% acetonitrile solution carries out linear elution as eluent, and chromatographic column used is 5 μ C18 of Gemini, and applied sample amount is 100 μ
L, flow velocity 1mL/min, Detection wavelength 214nm measure the antioxidant activity of the corresponding eluent of each absorption peak, and collection obtains
The highest component of antioxidant activity.
(3) test of antioxidant activity
1, ABTS free radical scavenging abilities
The ABTS storage mother liquors of 7mM and the potassium persulfate solution of 2.45mM are prepared, is mixed before use with the ratio of 1 ︰ 1, room temperature is put
After setting 16h, phosphate buffer is used（5mM、pH7.4）It is 0.70 ± 0.02, i.e. ABTS free radicals to be diluted to light absorption value at 734nm
Solution.ABTS free-atom aqueous solutions mix in equal volume with the sample of various concentration, after reacting at room temperature 10min, measure and inhale under 734nm
Light value, phosphate buffer（5mM、pH7.4）Zeroing.Blank group replaces sample with distilled water.The ABTS radicals scavengings of sample
Vigor is calculated as the following formula：
In formula：Acontrol- blank group light absorption value
Asample- sample sets light absorption value
2, DPPH free radical scavenging abilities
Take various concentration sample 1mL and DPPH solution（0.1mM, 95% ethyl alcohol are prepared）1mL is mixed well, and room temperature is protected from light standing
30min, 517nm measure light absorption value；It is sample reference group to replace DPPH solution with 95% ethanol solutions of 1mL；Blank group is 1mL
DPPH solution and 95% ethanol solutions of 1mL.The DPPH radicals scavenging vigor of sample is calculated according to the following formula：
In formula：Ai- sample sets light absorption value
Aj- sample reference group light absorption value
A0- blank group light absorption value
3, lipid peroxidation inhibitory activity
It takes various concentration sample 1mL in color-comparison tube, 95% ethyl alcohol of 2mL, 26 μ L linoleic acid and 2mL phosphate-buffereds is added
Liquid（50mM、pH7.0）, closed to be placed on dark place and keep 40 DEG C of constant temperature after mixing well.Blank group replaces sample with 1mL distilled water
Product.Per system extent of peroxidation of measurement for 24 hours.
Level of lipid uses ferric rhodanate（FTC）Method is measured.Take 100 μ L of mixed liquor and 75% second of 4.7mL
0.1mL FeCl are added in alcoholic solution, 30% ammonium thiocyanate mixings of 0.1mL2Solution（20mM, 3.5% hydrochloric acid solution are prepared）, fully
After mixing light absorption value is measured under accurate timing 3min, 452nm wavelength.
4, hydroxyl radical free radical scavenging capacity
1mL samples and 0.3mL FeSO4（8mM）, 1mL salicylic acids（3mM）And 0.25mL H2O2（20mM）Mixing, 37 DEG C of heat preservations
30min, after flowing water cooling, 0.45mL distilled water, which is added, makes reaction solution total volume reach 3mL, and 3000g centrifuges 10min, in 510nm waves
Long lower measurement supernatant light absorption value, distilled water replace sample as blank control.
5, oxygen radical absorbability（ORAC）
Using 96 orifice plate fluorimetries, 7.4 phosphate buffering liquid concentrations of pH are 75mM, FL（Fluorescein）Solution concentration is
200nM, AAPH solution concentration are 80mM.It is 485nm, launch wavelength 538nm that excitation wavelength, which is arranged, in microplate reader, is read every 1min
Fluorescent value, METHOD FOR CONTINUOUS DETERMINATION is taken to carry out 90min altogether.Phosphate buffer replaces sample as blank control, and experimental implementation is as follows：
20 μ L samples, 80 μ L phosphate buffers and 50 μ L FL solution are mixed in 37 DEG C and are protected from light heat preservation 15min, are added after reaction
50 μ L AAPH solution measure fluorescent value in microplate reader rapidly.
ORAC values are with Trolox equivalents（μm ol Trolox equivalent per g peptide) it indicates, it uses
0.9375,1.875,3.75,7.5,15,30 and 60 μM of concentration draws fluorescent quenching curve, and calculates its integral area：
f 0：Fluorescence light absorption value when 0min；
f i：Fluorescence light absorption value when 1min；
ORAC values the ratio between sample curves slope and the Trolox slopes of curve, ORAC value units：μmol Trolox
equivalent /g peptide。
(4) determined amino acid sequence
Identify that the overall amino acid sequence of the antioxidation polypeptide of the present invention is Ala-Thr-Val-Tyr, molecule using Q-TOF LC-MS
Amount is 452 Da.
The present invention, to the worry of artificial synthesized antioxidant, is based oneself upon through the defect of current natural and the public
It is conceived to using the collagen for coming from black sharkskin as starting point in a kind of antioxidant of efficiency natural of searching and passes through alkali
Property protease cutting condition control, be cut into the active peptides with specific peptide chain length and structural domain composition, and make to resist
Oxidation activity is efficiently realized.
The present invention changes the extraction of existing antioxidant and the idea and method used, and eliminates artificial synthesized anti-oxidant
Side effect caused by agent institute is possible, is a kind of natural, can replace traditional synthetic antioxidants.And this
Invention further improves China's situation relatively low to protein utilization rate in aquatic livestock skin, can both solve the sharp again of a large amount of aquatic resources
With problem, and consumer can be released to antioxidant in the misgivings of food security aspect, the development to science and technology, economy and grocery trade
It will have far-reaching significance.
Description of the drawings
Fig. 1 is the ABTS free radical scavenging activity correlation curves of black sharkskin protein zymolyte.
Fig. 2 is the DPPH free radical scavenging activity correlation curves of black sharkskin protein zymolyte.
Fig. 3 is the lipid peroxidation inhibitory activity of black sharkskin protein zymolyte.
Fig. 4 is the hydroxyl radical free radical clearance rate correlation curve of black sharkskin protein zymolyte.
Fig. 5 is the RP-HPLC elution profiles of black sharkskin protein zymolyte.
Fig. 6 is the DPPH free radical scavenging activities of black sharkskin protein zymolyte RP-HPLC elution fractions.
Fig. 7 is F19 total ion current figures.
Fig. 8 is the first mass spectrometric figure of anti-oxidation peptide.
Fig. 9 is the second order ms figure of anti-oxidation peptide.
Specific implementation mode
The amino acid sequence of the antioxidation polypeptide of the present invention is Ala-Thr-Val-Tyr.
Preparation method is as follows：
Using black sharkskin as raw material, it is digested using alkali protease, isolate and purify, be freeze-dried obtain it is anti-oxidant more
Peptide；The enzymatic hydrolysis condition is：PH is 8.0, temperature 45 C, enzymolysis time 4.9h, concentration of substrate 3%, and enzyme additive amount is
9.6wt%；Enzymolysis product is detached using RP-HPLC reversed-phase high performance liquid chromatography, and monitors the antioxidant activity of separation component, is received
Collect the component with best antioxidant activity；The separation of reversed-phase HPLC is with the concentration gradient of 0.05% trifluoroacetic acid containing volume fraction
Linear elution is carried out as eluent for 0%~40% acetonitrile solution, chromatographic column used is 5 μ C18 of Gemini, and applied sample amount is
100 μ L, flow velocity 1mL/min, Detection wavelength 214nm measure the antioxidant activity of the corresponding eluent of each absorption peak, collect
Obtain the highest component of antioxidant activity.
Instrument that the present invention uses, detection means are as follows：
Present invention application RP-HPLC reversed-phase high performance liquid chromatography isolates and purifies means, realizes anti-oxidant more with remarkable activity
Peptide efficiently separates purifying.
The amino acid sequence of antioxidation polypeptide is identified using Q-TOF LC-MS.
In order to further appreciate that the content of present invention, feature and effect, the following examples are hereby given：
Embodiment 1
3 grams of black sharkskins are weighed, 100ml deionized waters are added, its pH is then adjusted to 8.0 with 1mol/L NaOH.First should
Solution water-bath is heated to 45 DEG C, and the enzyme of corresponding amount is then added according still further to the ratio that enzyme additive amount is 9.6wt.%, and enzymolysis time is
4.9 hour.Then enzyme deactivation 15 minutes in boiling water bath, 4000rpm is centrifuged 15 minutes again after cooling.It is spare to collect supernatant.
The black sharkskin enzymolysis product prepared is made into antioxidant activity identification, wherein ABTS 503nhibiting concentrations are 80 μ g/
mL（As shown in Figure 1）, DPPH 503nhibiting concentrations be 3.19mg/mL（As shown in Figure 2）, with certain lipid peroxidation inhibit to live
Property（As shown in Figure 3）With hydroxyl radical free radical scavenging capacity（As shown in Figure 4）, therefore, black sharkskin enzymolysis product has certain
Antioxidant activity.
Enzymolysis product is detached using RP-HPLC reversed-phase high performance liquid chromatography（As shown in Figure 5）, and monitor the anti-of separation component
Oxidation activity collects the component with best antioxidant activity；The separation of reversed-phase HPLC is to contain 0.05%（Volume）Trifluoroacetic acid
The acetonitrile solution that concentration gradient is 0%~40% carries out linear elution as eluent, and chromatographic column used is 5 μ C18 of Gemini,
Applied sample amount is 100 μ L, flow velocity 1mL/min, Detection wavelength 214nm, measures the anti-oxidant of the corresponding eluent of each absorption peak
Activity, collection obtain the highest component F19 of antioxidant activity（As shown in Figure 6）, DPPH free radical scavenging activities are 47.63%（Group
Divide a concentration of 1mg/mL）.
Utilize Q-TOF LC-MS identification components F19（Chromatography and Mass Spectrometry Conditions are as shown in table 1, table 2）, total ion current figure
As shown in fig. 7, MS/MS second order ms is recycled to identify 16.74min quasi-molecular ions, obtaining its overall amino acid sequence is（Such as Fig. 8-9
It is shown）：Ala-Thr-Val-Tyr（Molecular weight is 452 Da）, measure its antioxidant activity（As shown in table 3）, wherein ABTS is certainly
By base clearance rate（81.05±0.78）%, DPPH free radical scavenging activity（62.25±0.82）% and oxygen radical absorbability
（2606.05±77.49）μmol Trolox/g peptide.
Table 1 identifies F19 chromatographic condition parameters
Table 2 identifies F19 Mass Spectrometry Conditions parameters
The antioxidant activity of 3 anti-oxidation peptide of table
The foregoing is merely presently preferred embodiments of the present invention, all equivalent changes done according to scope of the present invention patent with repair
Decorations should all belong to the covering scope of the present invention.
Sequence table
<110>University of Fuzhou
<120>A kind of preparation of antioxidation polypeptide and isolation and purification method
<130> 1
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 4
<212> PRT
<213> 2 Ambystoma laterale x Ambystoma jeffersonianum
<400> 1
Ala Thr Val Tyr
1
Claims (3)
1. a kind of antioxidation polypeptide, it is characterised in that：The amino acid sequence of the antioxidation polypeptide is Ala-Thr-Val-Tyr.
2. a kind of antioxidation polypeptide preparation method as described in claim 1, it is characterised in that：Using black sharkskin as raw material, adopt
It is digested with alkali protease, isolated and purified, be freeze-dried and obtain antioxidation polypeptide；The enzymatic hydrolysis condition is：PH is
7.0 ~ 9.0,40 ~ 50 DEG C of temperature, enzymolysis time are 4.0 ~ 6.0h, concentration of substrate is 2.0 ~ 4.0%, enzyme additive amount be 9.0 ~
10.0wt.%。
3. antioxidation polypeptide preparation method according to claim 2, it is characterised in that：The specific steps isolated and purified
For：Enzymolysis product is detached using RP-HPLC reversed-phase high performance liquid chromatography, and monitors the antioxidant activity of separation component, collects tool
There is the component of best antioxidant activity；The separation of reversed-phase HPLC is with the concentration gradient of 0.05% trifluoroacetic acid containing volume fraction for 0%
~40% acetonitrile solution carries out linear elution as eluent, and chromatographic column used is 5 μ C18 of Gemini, and applied sample amount is 100 μ
L, flow velocity 1mL/min, Detection wavelength 214nm measure the antioxidant activity of the corresponding eluent of each absorption peak, and collection obtains
The highest component of antioxidant activity；The amino acid sequence of component is identified using Q-TOF LC-MS.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102219828A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidation polypeptide prepared from sharkskin collagen |
| CN102219830A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Oxidation resisting polypeptide and preparation method thereof |
| CN102219829A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease |
-
2018
- 2018-06-26 CN CN201810670244.9A patent/CN108484722B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102219828A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidation polypeptide prepared from sharkskin collagen |
| CN102219830A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Oxidation resisting polypeptide and preparation method thereof |
| CN102219829A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease |
Non-Patent Citations (1)
| Title |
|---|
| 颜阿娜 等: "鲨鱼皮蛋白肽的制备、分离纯化及抗氧化活性研究", 《2017中国食品科学技术学会第十四届年会暨第九届中美食品业高层论坛论文摘要集》 * |
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