CN102391361A - Chickpea peptide with antioxidation effect and separation and purification method and application - Google Patents
Chickpea peptide with antioxidation effect and separation and purification method and application Download PDFInfo
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Abstract
The invention discloses a chickpea peptide with antioxidation effect and a separation and purification method and an application; the chickpea peptide is expressed as CPe-III, and has a molecular weight of 1155 Da; the amino acid composition is Arg-Gln-Ser-His-Phe-Ala-Asn-Ala-Gln-Pro; and the secondary structure comprises 66% of alpha-helix. The method of the invention has a mild separation condition, a high sample recovery rate, high reproducibility of experimental results, and simple and economical equipment. The method of the invention has a simple process, and low energy consumption; the product has antioxidation effect; and basis is provided for artificial synthesis of antioxidant peptides.
Description
Technical field
The invention belongs to the preparing technical field of biologically active peptides, relate to a kind of garbanzo peptide and separation purification method and purposes with antioxygenation.
Background technology
The garbanzo peptide is the product that is obtained by the garbanzo proteolyze, and its amino acid is formed identical with garbanzo albumen, and indispensable amino acid reasonable ratio, the utilization that is prone to be absorbed by the body have the special and functional performance of the processing more superior than its albumen simultaneously.The garbanzo peptide molecular weight is little; Be easy to digest and assimilate; No protein denaturation, no fishy smell, soluble in water, under acidic conditions not coagulation, viscosity little, be heated and processing characteristics such as do not solidify, but also have the serum cholesterol content of reduction, promote metabolism of fat, hypotensive, resistance to reduction, functional performance such as alleviating fatigue rapidly.Antibacterial peptide, low irritability protein zymolyte, angiotensin inhibiting peptide or the like from garbanzo, have been isolated at present.
Anti-oxidation peptide is a kind of of biologically active peptides; People such as Yoshinori Mine think the oxidation-resistance of peptide at least can some effects other biological activity; Big quantity research has shown oxidation-resistance and the immunomodulatory of peptide, hypotensive, decreasing cholesterol, OPIOIDS antagonistic activity, antitumor etc. certain getting in touch has been arranged all, possibly be the basis of other physiological function.It passes through to reduce oxyradical, hydroxy radical qiao, thereby reaches antidotal function.Polypeptide with biological function all is an ordered structure, all forms, puts in order and special higher structure by certain amino acid per-cent.Therefore; From garbanzo, isolate polypeptide, and on structure, its activity is resolved, both to the applications expanding road of natural anti-oxidation peptide with oxidation-resistance; Also establish solid basis, demonstrate the advantage that it is used in fields such as medicine, food, feeds for the synthetic anti-oxidation peptide.
Gel filtration chromatography is to utilize the molecular sieve effect with cancellated gel, separates according to the molecular size of separated object.Separation condition is gentle, sample recovery rate is high, the experimental result circulation ratio is high, simple equipments economy.Mass spectroscopy is considered to measure the sensitive method of small molecules molecular weight at present.In recent years, along with each item technical development, the molecular weight ranges that mass spectrum can be measured improves greatly.The auxiliary laser desorption ionisation flight time mass spectrum of matrix becomes measures the especially effective tool of protein, polypeptide molecular weight and primary structure of biomacromolecule.The ir spectra of material has the characteristic of height; Absorption peak in the spectrogram is corresponding with the vibration mode of each group in the molecule; Can be used for studying the structure and the chemical bond of molecule, differentiate the secondary structure of polypeptide, is a kind of novel analysis and testing technology that developed recently gets up.
Summary of the invention
The purpose of this invention is to provide a kind of garbanzo peptide with antioxygenation.
Second purpose of the present invention provides a kind of separation purification method with garbanzo peptide of antioxygenation.
The 3rd purpose of the present invention provides a kind of purposes with garbanzo peptide of antioxygenation.
A kind of garbanzo peptide with antioxygenation representes that with the CPe-III molecular weight of said CPe-III is 1155Da, and amino acid consists of Arg-Gln-Ser-His-Phe-Ala-Asn-Ala-Gln-Pro, and secondary structure accounts for 66% with alpha-helix.
A kind of separation purification method with garbanzo peptide of antioxygenation comprises the steps:
(1) be 1 with olecranon bean powder after the degreasing and water by mass ratio: the mixed of 8-15, transfer pH=8.3 with the NaOH aqueous solution, stir and extract 0.5-1.5h; The centrifugal 15min-25min of 3500r/min-5000r/min, deposition is 1 in the solid-liquid mass ratio again: the ratio of 3-7 is extracted 2-3 time, merges supernatant; Transfer the pH=5.0 protein precipitation with the HCl aqueous solution, isolate supernatant, transfer pH=3.7 to carry out secondary sedimentation albumen with the HCl aqueous solution once more supernatant; Abandon supernatant, merge deposition twice, precipitate 2-3 time with deionized water wash; Transfer pH=7.0 with the NaOH aqueous solution, stir and make the deposition redissolution, lyophilize is the garbanzo white protein;
(2) said garbanzo white protein is dissolved in processes the garbanzo white protein aqueous solution that mass concentration is 3-5% in the zero(ppm) water; Is 0.3-0.4AU/g in Sumizyme MP Alcalase (Denmark NOVO company) with the albuminised ratio of garbanzo, and the Alcalase enzyme is put into the said garbanzo white protein aqueous solution, at pH=8.0, and under temperature of reaction 45-55 ℃ the condition, hydrolysis 50-70min; Is 50LAPU/g in Flavourzyme composite flavor enzyme (Denmark NOVO company) with the albuminised ratio of garbanzo, adds the Flavourzyme enzyme again, pH=7.0, and under the condition that temperature of reaction is 50 ℃, hydrolysis 90-120min; Enzymolysis solution is heated to boiling, the enzyme 10min that goes out, the centrifuging and taking supernatant lyophilize of cooling back promptly gets garbanzo peptide powder;
(3) with the polydextran gel Sephdex G-25 that handles well, dress post 1.6 * 50cm is with registering instrument recorded stream fluid absorbancy situation; Water elution to be distilled to baseline is steady; Get garbanzo peptide powder dissolution and join in the said polydextran gel Sephdex G-25 post after in zero(ppm) water, with the zero(ppm) water wash-out, flow velocity is 0.6mL/min; Detect the elutriant absorbancy at the 280nm place; Occur 3 elution peaks at times altogether, collect the 3rd elution peak liquid, promptly obtain having the garbanzo peptide of representing with the CPe-III of antioxygenation after the lyophilize.
Above-mentioned garbanzo peptide is in the purposes of preparation anti-oxidation health article.
The invention has the advantages that: utilize Sephdex G-25 can the peptide section of different molecular weight in the bullion garbanzo peptide be separated; Acquisition has the CPe-III of antioxidant effect, and separation condition is gentle, sample recovery rate is high, the experimental result circulation ratio is high, simple equipments economy.Utilize LC/MS, can be to the further separation and purification of CPe-III, and obtain information such as relative molecular mass and amino acid composition.Through ir spectra primary structure is verified at last, and drawn the information of secondary structure.Can resolve the anti-oxidant mechanism of CPe-III from structure level,, also establish solid basis for the synthetic anti-oxidation peptide to the application blaze the trail of natural anti-oxidation peptide.
Separation and purification anti-oxidation peptide and measure the method for its structure from the garbanzo peptide.This procedure is simple, and energy consumption is low, and product has oxidation resistant effect, and to the synthetic of anti-oxidation peptide foundation is provided.
Description of drawings
Fig. 1 is a garbanzo peptide chromatography collection of illustrative plates.
Fig. 2 is a CPe-III liquid phase collection of illustrative plates.
Fig. 3 is a CPe-III one-level mass-spectrogram.
Fig. 4 is a CPe-III second order ms collection of illustrative plates.
Fig. 5 is the infrared spectrogram of CPe-III.
Fig. 6 is the mensuration of each component reducing power of garbanzo peptide.
Fig. 7 is the ability that each component of garbanzo peptide is removed the DPPH radical.
Fig. 8 is the ability that each component of garbanzo peptide is removed the 0H radical.
Embodiment
Embodiments of the invention are in order to enable those skilled in the art to understand better the present invention, can not to do any restriction to the present invention.
Below in conjunction with specific embodiment the present invention is further described.
A kind of separation purification method with garbanzo peptide of antioxygenation comprises the steps:
(1) is 1: 10 mixed with the olecranon bean powder after the degreasing and water by mass ratio, transfers pH=8.3, stir and extract 1h with the NaOH aqueous solution; The centrifugal 20min of 4000r/min, deposition is that 1: 5 ratio is extracted 2 times in the solid-liquid mass ratio again, merges supernatant; Transfer the pH=5.0 protein precipitation with the HCl aqueous solution, isolate supernatant, transfer pH=3.7 to carry out secondary sedimentation albumen with the HCl aqueous solution once more supernatant; Abandon supernatant, merge deposition twice, precipitate 3 times with deionized water wash; Transfer pH=7.0 with the NaOH aqueous solution, stir and make the deposition redissolution, lyophilize 24h is the garbanzo white protein;
(2) said garbanzo white protein is dissolved in to process mass concentration in the zero(ppm) water be 4.87% the garbanzo white protein aqueous solution; In Alcalase enzyme and the albuminised ratio of garbanzo is 0.38AU/g, and the Alcalase enzyme is put into the said garbanzo white protein aqueous solution, at pH=8.0, and under the condition that temperature of reaction is 50 ℃, hydrolysis 70min; In Flavourzyme enzyme and the albuminised ratio of garbanzo is 50LAPU/g, adds the Flavourzyme enzyme again, at pH=7.0,50 ℃ of temperature of reaction, condition under, hydrolysis 100min; Enzymolysis solution is heated to boiling, the enzyme 10min that goes out, the centrifuging and taking supernatant lyophilize of cooling back promptly gets garbanzo peptide powder;
(3) with the polydextran gel Sephdex G-25 that handles well, dress post 1.6 * 50cm is with registering instrument recorded stream fluid absorbancy situation; Water elution to be distilled to baseline is steady, gets garbanzo peptide powder dissolution and joins in the said polydextran gel Sephdex G-25 post, with the zero(ppm) water wash-out after in zero(ppm) water; Flow velocity is 0.6mL/min, detects the elutriant absorbancy at the 280nm place, occurs 3 elution peaks at times altogether; Use the CPe-I respectively, CPe-II and CPe-III are represented, collect the 3rd elution peak liquid; Promptly obtain having the garbanzo peptide of representing with the CPe-III of antioxygenation after the lyophilize, see Fig. 1 chromatography collection of illustrative plates.
LC-MS (HLPC-MS) is confirmed the primary structure of CPe-III:
Chromatographic condition: sample size: 5 μ L; Moving phase: A liquid: water (0.1%TFA); B liquid: acetonitrile (0.1%TFA); Column temperature: room temperature; Flow velocity: 0.7mL/min.
Mass spectrum condition: adopt electron spray ionisation (ESI), spray voltage 4.5kv, atomization gas (N
2) 35 arbitrary value units of flow, auxiliary gas (N
2) 5 arbitrary value units of flow, 300 ℃ of capillary temperatures; Full scan scope: 150m/z-2000m/z; Carry out the positive ion detecting pattern; Carry out online MS/MS, intensity threshold values 10
5, ion width 2, collision normalized energy 30%.Application of B ioWorks3.3 software analysis fragment information, thereby the primary structure information of acquisition CPe-III, molecular weight: 1155Da, amino acid is formed: Arg-Gln-Ser-His-Phe-Ala-Asn-Ala-Gln-Pro.See Fig. 2 (RT is that corresponding peak, 3.55 places is the staple of CPe-III).See Fig. 3 (relative molecular mass that the one-level mass spectrum obtains the CPe-III is 1155Da).See that (second order ms is confirmed the amino acid composition of CPe-III to Fig. 4: Arg-Gln-Ser-His-Phe-Ala-Asn-Ala-Gln-Pro)
Ir spectra detects primary structure, and infers the secondary structure of oxidation-resistance CPe-III:
CPe-III and KBr mixed pressuring plate adopt total reflection spectrum assay method (ATR), European sampling thief sampling 32 times.At 4000cm
-1-400cm
-1Scan in the scope.See Fig. 5.(-2 pairs of acid amides I districts of Fig. 5-1 and Fig. 5 bands of a spectrum are composed Fourier from decurl with ask second derivative; Use Spectrum Analysis software OMNIC that CPe-III original spectrum band is carried out Gauss/Lorentz match; Calculate peak area, learn that CPe-III secondary structure is main with alpha-helix, accounts for 66%.
The mensuration of each component reducing power of garbanzo peptide
Reducing power measuring method: get the certain density garbanzo peptide solution of 1mL; Add the PBS buffered soln of 2.5mL 0.2mol/L pH6.6 and the potassium ferricyanide solution of 2.5mL 1%; Fully mixing behind the reaction 20min, cools off rapidly in 50 ℃ of water-baths; The trichoroacetic acid(TCA) that adds 2.5mL 10% again is in the centrifugal 10min of 3000r/min.Go deposition, get supernatant 2mL, add the FeCl of 2mL zero(ppm) water and 0.4mL 0.1% successively
3, thorough mixing, leave standstill 10min after, in 700nm wavelength colorimetric.
As can be seen from Figure 6, the reducing power of CPe-III is apparently higher than component CPe-I and II, and in the concentration range of 0.1～25mg/mL, along with concentration increases, reducing power significantly increases.
Each component of garbanzo peptide is removed the ability of DPPH radical:
Remove the measuring method of DPPH radical: the CPe solution of getting the 1mL different concns mixes with 1mL 0.1mmol/LDPPH reference liquid and concuss, at room temperature lucifuge reaction for some time (about 20min), surveys light absorption value A with the 517nm place then
iThe sample blank group replaces the DPPH reference liquid with the equal-volume absolute ethyl alcohol, surveying light absorption value with the 517nm place then, is designated as A
j, control group replaces sample solution with equal-volume zero(ppm) water, surveying light absorption value with the 517nm place then, is designated as A
0Clearance rate is according to computes:
Clearance rate (%)=[1-(A
i-A
j)/A
0] * 100%
A wherein
O, A
i, A
jRepresent control group respectively, the absorbancy of sample sets and sample blank group
Visible like Fig. 7, each collection part of garbanzo peptide all has significant scavenging(action) to the DPPH radical.In the scope of concentration 0.2～5mg/mL, along with the increase of concentration, the ability of removing the DPPH radical also increases to some extent.Under the same concentrations, the ability of the removing DPPH radical of each collection part of garbanzo peptide is following: CPe-III＞CPe-II＞CPe-I.The CPe-III increases with concentration in the scope of 0.1～1mg/mL, and clearance rate significantly increases, and shows tangible dose-effect relationship, and in the concentration range of 1～5mg/mL, clearance rate tends towards stability.
Each component of garbanzo peptide is removed the ability of 0H radical:
0H is removed the measuring method of ability: in the exsiccant test tube, add 0.4mL 50mmol/L phosphate buffered saline buffer (pH=7.5) successively; 0.1mL certain density garbanzo peptide solution (blank pipe replaces the garbanzo peptide solution with isopyknic zero(ppm) water); 0.1mL the EDTA solution of 1.04mmol/L, 0.1mL 10mmol/L H
2O
2, 0.1mL 2mmol/L VC, 0.1mL 60mmol/L ribodesose (DR) (control group does not add DR, replenishes zero(ppm) water), 0.1ml 1mmol/L FeC1
3, each manages final volume 1.0ml, takes out after placing 37 ℃ water bath with thermostatic control insulation 1h; Add 1mL 25% (v/v) HCI termination reaction rapidly; Add the 1mL1% thiobarbituricacid again, boiling water bath reaction 15min, cooling immediately after the taking-up; Measure light absorption value in wavelength 532nm place, be calculated as follows clearance rate:
0H clearance rate (%)={ [A
0-(A
1-A
2)]/A
0} * 100
A wherein
0, A
1, A
2Represent the absorbancy of control group, sample sets and sample blank group respectively
Visible from Fig. 8, each collection part of garbanzo peptide all has significant scavenging(action) to the 0H radical, and shows tangible dose-effect relationship, and in the concentration range of 0.1～20mg/mL, the removing ability of CPe-III all is higher than component CPe-I and II.
A kind of separation purification method with garbanzo peptide of antioxygenation comprises the steps:
(1) is 1: 8 mixed with the olecranon bean powder after the degreasing and water by mass ratio, transfers pH=8.3, stir and extract 1.5h with the NaOH aqueous solution; The centrifugal 15min of 5000r/min, deposition is that 1: 3 ratio is extracted 3 times in the solid-liquid mass ratio again, merges supernatant; Transfer the pH=5.0 protein precipitation with the HCl aqueous solution, isolate supernatant, transfer pH=3.7 to carry out secondary sedimentation albumen with the HCl aqueous solution once more supernatant; Abandon supernatant, merge deposition twice, precipitate 2 times with deionized water wash; Transfer pH=7.0 with the NaOH aqueous solution, stir and make the deposition redissolution, lyophilize 24h is the garbanzo white protein;
(2) said garbanzo white protein is dissolved in to process mass concentration in the zero(ppm) water be 3% the garbanzo white protein aqueous solution; In Alcalase enzyme and the albuminised ratio of garbanzo is 0.4AU/g, and the Alcalase enzyme is put into the said garbanzo white protein aqueous solution, at pH=8.0, and under the condition that temperature of reaction is 45 ℃, hydrolysis 60min; In Flavourzyme enzyme and the albuminised ratio of garbanzo is 50LAPU/g, adds the Flavourzyme enzyme, at pH=7.0,50 ℃ of temperature of reaction, condition under, hydrolysis 100min; Enzymolysis solution is heated to boiling, the enzyme 10min that goes out, the centrifuging and taking supernatant lyophilize of cooling back promptly gets garbanzo peptide powder.
(3) with embodiment 1.
A kind of separation purification method with garbanzo peptide of antioxygenation comprises the steps:
(1) is 1: 15 mixed with the olecranon bean powder after the degreasing and water by mass ratio, transfers pH=8.3, stir and extract 0.5h with the NaOH aqueous solution; The centrifugal 25min of 3500r/min, deposition is that 1: 7 ratio is extracted 2 times in the solid-liquid mass ratio again, merges supernatant; Transfer the pH=5.0 protein precipitation with the HCl aqueous solution, isolate supernatant, transfer pH=3.7 to carry out secondary sedimentation albumen with the HCl aqueous solution once more supernatant; Abandon supernatant, merge deposition twice, precipitate 3 times with deionized water wash; Transfer pH=7.0 with the NaOH aqueous solution, stir and make the deposition redissolution, lyophilize 24h is the garbanzo white protein;
(2) said garbanzo white protein is dissolved in to process mass concentration in the zero(ppm) water be 5% the garbanzo white protein aqueous solution; In Alcalase enzyme and the albuminised ratio of garbanzo is 0.3AU/g, and the Alcalase enzyme is put into the said garbanzo white protein aqueous solution, at pH=8.0, and under the condition that temperature of reaction is 55 ℃, hydrolysis 50min; In Flavourzyme enzyme and the albuminised ratio of garbanzo is 50LAPU/g, adds the Flavourzyme enzyme, at pH=7.0,50 ℃ of temperature of reaction, condition under, hydrolysis 90min; Enzymolysis solution is heated to boiling, the enzyme 10min that goes out, the centrifuging and taking supernatant lyophilize of cooling back promptly gets garbanzo peptide powder.
(3) with embodiment 1.
Claims (3)
1. the garbanzo peptide with antioxygenation is represented with the CPe-III, it is characterized in that the molecular weight of said CPe-III is 1155Da, and amino acid consists of Arg-Gln-Ser-His-Phe-Ala-Asn-Ala-Gln-Pro, and secondary structure accounts for 66% with alpha-helix.
2. a kind of separation purification method with garbanzo peptide of antioxygenation of claim 1 is characterized in that comprising the steps:
(1) be 1 with olecranon bean powder after the degreasing and water by mass ratio: the mixed of 8-15, transfer pH=8.3 with the NaOH aqueous solution, stir and extract 0.5-1.5h; The centrifugal 15min-25min of 3500r/min-5000r/min, deposition is 1 in the solid-liquid mass ratio again: the ratio of 3-7 is extracted 2-3 time, merges supernatant; Transfer the pH=5.0 protein precipitation with the HCl aqueous solution, isolate supernatant, transfer pH=3.7 to carry out secondary sedimentation albumen with the HCl aqueous solution once more supernatant; Abandon supernatant, merge deposition twice, precipitate 2-3 time with deionized water wash; Transfer pH=7.0 with the NaOH aqueous solution, stir and make the deposition redissolution, lyophilize is the garbanzo white protein;
(2) said garbanzo white protein is dissolved in processes the garbanzo white protein aqueous solution that mass concentration is 3-5% in the zero(ppm) water; In Sumizyme MP Alcalase and the albuminised ratio of garbanzo is 0.3-0.4AU/g, and the Alcalase enzyme is put into the said garbanzo white protein aqueous solution, at pH=8.0, and under temperature of reaction 45-55 ℃ the condition, hydrolysis 50-70min; In Flavourzyme composite flavor enzyme and the albuminised ratio of garbanzo is 50LAPU/g, adds the Flavourzyme enzyme again, pH=7.0, and under the condition that temperature of reaction is 50 ℃, hydrolysis 90-120min; Enzymolysis solution is heated to boiling, the enzyme 10min that goes out, the centrifuging and taking supernatant lyophilize of cooling back promptly gets garbanzo peptide powder;
(3) with the polydextran gel Sephdex G-25 that handles well, dress post 1.6 * 50cm is with registering instrument recorded stream fluid absorbancy situation; Water elution to be distilled to baseline is steady; Get garbanzo peptide powder dissolution and join in the said polydextran gel Sephdex G-25 post after in zero(ppm) water, with the zero(ppm) water wash-out, flow velocity is 0.6mL/min; Detect the elutriant absorbancy at the 280nm place; Occur 3 elution peaks at times altogether, collect the 3rd elution peak liquid, promptly obtain having the garbanzo peptide of representing with the CPe-III of antioxygenation after the lyophilize.
3. the described garbanzo peptide of claim 1 is in the purposes of preparation anti-oxidation health article.
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| CN103172706A (en) * | 2013-03-15 | 2013-06-26 | 中国科学院过程工程研究所 | Preparation method of chick-pea oligopeptide with antioxidation function |
| CN103194517A (en) * | 2013-04-11 | 2013-07-10 | 中国科学院过程工程研究所 | Chickpea short-peptide mixture and preparation method thereof |
| CN104789629A (en) * | 2015-04-30 | 2015-07-22 | 中国食品发酵工业研究院 | Chickpea oligopeptide and preparation method thereof |
| CN107223985A (en) * | 2016-03-23 | 2017-10-03 | 新疆丝路弘毅农业科技有限公司 | It is a kind of with the chick-pea composition of antioxidation and application |
| CN107361369A (en) * | 2017-07-18 | 2017-11-21 | 杏辉天力（杭州）药业有限公司 | A kind of chick pea extract and its production and use |
| CN108191961A (en) * | 2018-01-22 | 2018-06-22 | 山西师范大学 | The albuminised method and antioxidant that there is high scavenging capacity to superoxide anion are prepared from coconut cake |
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Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103172706A (en) * | 2013-03-15 | 2013-06-26 | 中国科学院过程工程研究所 | Preparation method of chick-pea oligopeptide with antioxidation function |
| CN103172706B (en) * | 2013-03-15 | 2015-05-20 | 中国科学院过程工程研究所 | Preparation method of chick-pea oligopeptide with antioxidation function |
| CN103194517A (en) * | 2013-04-11 | 2013-07-10 | 中国科学院过程工程研究所 | Chickpea short-peptide mixture and preparation method thereof |
| CN103194517B (en) * | 2013-04-11 | 2016-04-06 | 中国科学院过程工程研究所 | A kind of Chickpea short-peptide mixture and preparation method thereof |
| CN104789629A (en) * | 2015-04-30 | 2015-07-22 | 中国食品发酵工业研究院 | Chickpea oligopeptide and preparation method thereof |
| CN104789629B (en) * | 2015-04-30 | 2018-10-26 | 中国食品发酵工业研究院 | A kind of chick-pea oligopeptide and preparation method thereof |
| CN107223985A (en) * | 2016-03-23 | 2017-10-03 | 新疆丝路弘毅农业科技有限公司 | It is a kind of with the chick-pea composition of antioxidation and application |
| CN107361369A (en) * | 2017-07-18 | 2017-11-21 | 杏辉天力（杭州）药业有限公司 | A kind of chick pea extract and its production and use |
| CN107361369B (en) * | 2017-07-18 | 2021-02-05 | 杏辉天力（杭州）药业有限公司 | Chickpea extract and preparation method and application thereof |
| CN108191961A (en) * | 2018-01-22 | 2018-06-22 | 山西师范大学 | The albuminised method and antioxidant that there is high scavenging capacity to superoxide anion are prepared from coconut cake |
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