CN104530187A - Saury antioxidative peptide as well as separation and extraction method and application thereof - Google Patents
Saury antioxidative peptide as well as separation and extraction method and application thereof Download PDFInfo
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Abstract
The invention belongs to the field of food biological techniques, and discloses a saury antioxidative peptide as well as a separation and extraction method and application thereof. The saury antioxidative peptide has an amino acid sequence as shown in Ser-Gly-Ala-Ala-Met. The separation and extraction method comprises the following steps: performing enzymolysis on saury by using protease, thereby obtaining a saury proteolysis product; separating the saury proteolysis product by using macroporous adsorption resin, thereby obtaining peptide powder I; separating the peptide powder I by using a sephadex chromatographic column, thereby obtaining peptide powder II; further purifying the peptide powder II by using a high efficiency liquid chromatogram column, thereby obtaining saury antioxidative peptide. The saury antioxidative peptide disclosed by the invention is relatively high in antioxidation property, and can be used in fields such as food, cosmetics and medicines.
Description
Technical field
The invention belongs to technical field of food biotechnology, be specifically related to a kind of saury anti-oxidation peptide and separating and extracting method thereof and application.
Background technology
Saury belongs to pelagic fishes, cheap, and its meat contains rich in protein.Indispensable amino acid not only containing needed by human body in saury albumen and enzymolysis product thereof, and containing having the amino acid of better nutritivity value in a large number, as His, Tyr and Met etc. have the amino acid of anti-oxidant activity, therefore, saury albumen can be used as the good source of preparing antioxidation active peptides.At present, storage mainly concentrated on to the research of saury both at home and abroad and fish for aspect, although also have the investigator of minority to improve the added value of saury, its processing byproduct is studied, and the effective constituent being extracted different sites is in industry, but be also only concentrate on fish scale and internal organ two aspect, the research being prepared by saury albumen to anti-oxidation peptide is then little.
The external prostatitis walked in antioxidation active peptides research in the world, and have marine fishes protein source antioxidation active peptides and study widely, as Kim Se-Kwon etc. has isolated the antioxidation active peptides section of different molecular weight and amino acid structure from tilapia, salmon, tuna, cod and walleye pollack, these peptide classes embody activity mainly through inhibited oxidation reaction, minimizing hydroperoxide, chelated metal ions and scavenging free radicals; SRM university of India is isolated tetrapeptide, pentapeptide, six peptides and seven peptides from scad, Herba Antenoronis filiformis, two-Wing flyingfiss and black butterfish respectively, all have stronger anti-oxidant activity and significant free radical scavenging activity.The research of China to antioxidation active peptides is then started late, and mostly is vegetable-protein to the research of antioxidation active peptides.Therefore, in the process finding antioxidation active peptides, the sight of increasing domestic scholars turns to animal proteinum, especially marine fishes albumen.In recent years, along with the raising of the deep and development technique studied marine organisms, from marine fishes albumen, prepare safety, efficiently bioactive peptide has become the study hotspot of society.Saury albumen is rich in the multiple amino acid with nutritive value, and these amino acid are not yet fully used at present, causes the waste of resource.
Summary of the invention
In order to solve the shortcoming and defect part of above prior art, primary and foremost purpose of the present invention is to provide a kind of saury anti-oxidation peptide.
Another object of the present invention is to the separating and extracting method that above-mentioned saury anti-oxidation peptide is provided.
Another object of the present invention is the application providing above-mentioned saury anti-oxidation peptide.
The object of the invention is achieved through the following technical solutions:
A kind of saury anti-oxidation peptide, described anti-oxidation peptide has the aminoacid sequence of Ser-Gly-Ala-Ala-Met.
The separating and extracting method of above-mentioned saury anti-oxidation peptide, comprises following operation steps:
(1) being decaptitated and internal organ by saury, be twisted into fish gruel after watery blood cleans up, is 1:(2 ~ 4 by fish gruel and water in mass ratio) mix, add protease hydrolyzed 4 ~ 12h, go out enzyme, and centrifuging and taking supernatant liquor after cooling, obtains saury protein hydrolysate (PSPHs);
(2) with macroporous adsorbent resin, PSPHs is separated, be the ethanolic soln gradient elution of 10% ~ 29%, 30% ~ 49%, 50% ~ 69% and 70% ~ 90% successively by distilled water and volume fraction, collect the component of 30% ~ 49% ethanolic soln wash-out, lyophilize, obtains Gly-His-Lys I;
(3) Gly-His-Lys I sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, be further purified with Reversed Phase High Performance, be that moving phase carries out wash-out with acetonitrile-trifluoroacetic acid aqueous solution that the volume percent of acetonitrile is respectively 2% ~ 9%, 10% ~ 19%, 20% ~ 39% and 40% ~ 55% successively, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 10% ~ 19%, lyophilize, obtains saury anti-oxidation peptide.
Proteolytic enzyme described in step (1) is one or both in flavor protease or pancreatin, and proteolytic enzyme addition is 500 ~ 1500U/g albumen; The pH of described enzymolysis is 6.5 ~ 8.5, and hydrolysis temperature is 45 ~ 55 DEG C.
The enzyme that goes out described in step (1) refers to insulation 10 ~ 30min at 85 ~ 100 DEG C; Described centrifugally refer to centrifugal 10 ~ 30min under the centrifugal force of 1500 ~ 4000g.
The preferred HP-20 resin of macroporous adsorbent resin described in step (2).
Sephadex chromatography post preferred Sephadex G-25 sephadex chromatography post described in step (3).
The preferred C18 post of Reversed Phase High Performance described in step (4); Described trifluoroacetic acid aqueous solution refers to that volume fraction is the trifluoroacetic acid aqueous solution of 0.1% ~ 0.2%.
The application of above-mentioned saury anti-oxidation peptide in food, makeup and field of medicaments.
Had the following advantages and beneficial effect by preparation method of the present invention and the product tool that obtains:
(1) saury anti-oxidation peptide of the present invention is small peptide, molecular weight is 435Da, easily be absorbed by the body, and there is stronger anti-oxidant activity, its oxyradical receptivity is 4.47 times of gsh, for about 10 times of thick peptide, safe, nontoxic and efficient saury anti-oxidation peptide can replace some chemosynthesis antioxidants to be applied in foodstuffs industry improving food stability;
(2) the present invention utilizes zymolysis technique and particular separation purification techniques to obtain a kind of high reactivity anti-oxidation peptide, not only improves the economic benefit of saury industry, and improves utilization ratio and the added value of saury resource;
(3) the present invention has used macroporous adsorbent resin separation and purification saury polypeptide, different from the past conventional separating and purifying technology, macroporous adsorbent resin effectively can remove the inorganic salt in enzymolysis product, and a large amount of existence of salt not only have influence on the security of peptide as food, also have influence on activity and the local flavor of peptide; The anti-oxidation peptide solution that the present invention prepares is without bitter taste, fishy smell, and good mouthfeel, the local flavor of thicker peptide has clear improvement, and solves because bioactive peptide to limit the problem of saury albumen application with bitter taste in various degree.
Accompanying drawing explanation
The absorbancy of five components obtained after the HP-20 macroporous adsorbent resin separation of Fig. 1 embodiment 5;
Fig. 2 is the absorbancy of three components obtained after the SephadexG-25 sephadex chromatography post of embodiment 5 is separated;
Fig. 3 is the Reversed Phase High Performance XBridge of embodiment 5
tMthe spectrogram of five components that prep C18 post is separated;
Fig. 4 is the mass spectroscopy figure of the aminoacid sequence of the saury anti-oxidation peptide that embodiment 5 obtains;
Fig. 5 is the Antioxidative Activity Determination figure of three components obtained after the SephadexG-25 sephadex chromatography post of embodiment 5 is separated;
Fig. 6 is the Reversed Phase High Performance XBridge of embodiment 5
tMprep C18 post is separated the Antioxidative Activity Determination figure of five components obtained.
Embodiment
Below in conjunction with embodiment, the present invention is described in further detail, but embodiments of the present invention are not limited thereto.
Embodiment 1
(1) saury is decaptitated and internal organ, after watery blood cleans up, is twisted into fish gruel, by rotten for fish with water in mass ratio 1:2 mix, add flavor protease, addition is 1500U/g albumen, pH be 6.5, temperature be 45 DEG C of conditions under enzymolysis 4h; Be incubated 30min at 85 DEG C, under the centrifugal force of 1500g, centrifugal 30min, gets supernatant liquor, obtains saury protein hydrolysate (PSPHs), and degree of hydrolysis is 13.10% ± 0.72%;
(2) with HP-20 macroporous adsorbent resin, PSPHs is separated, be 10%, 30%, 50% and 70% ethanolic soln gradient elution by distilled water and volume fraction successively after loading, collect the component of 30% ethanolic soln wash-out, lyophilize, obtain Gly-His-Lys I;
(3) Gly-His-Lys I Sephadex G-25 sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, Reversed Phase High Performance XBridge is used
tMprep C18 post is further purified, acetonitrile-the trifluoroacetic acid aqueous solution (0.1%V/V trifluoroacetic acid aqueous solution) being respectively 2%, 10%, 20% and 40% successively by the volume percent of acetonitrile carries out wash-out for moving phase, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 10%, lyophilize, obtains saury anti-oxidation peptide.
The saury anti-oxidation peptide that the present embodiment obtains, carry out sequential analysis by mass spectroscopy, from the molion that first mass spectrometric produces, select m/z to be 436.4338 as parent ion, enter second order ms, through sequential analysis, the aminoacid sequence obtaining this peptide is Ser-Gly-Ala-Ala-Met.
Embodiment 2
(1) saury is decaptitated and internal organ, after watery blood cleans up, is twisted into fish gruel, by rotten for fish with water in mass ratio 1:2 mix, add pancreatin, addition is 500U/g albumen, pH be 8.5, temperature be 55 DEG C of conditions under enzymolysis 8h; Be incubated 10min at 100 DEG C, under the centrifugal force of 4000g, centrifugal 10min, gets supernatant liquor, obtains saury protein hydrolysate (PSPHs), and degree of hydrolysis is 15.58% ± 0.55%;
(2) with HP-20 macroporous adsorbent resin, PSPHs is separated, be 29%, 49%, 69% and 90% ethanolic soln gradient elution by distilled water and volume fraction successively after loading, collect the component of 49% ethanolic soln wash-out, lyophilize, obtain Gly-His-Lys I;
(3) Gly-His-Lys I Sephadex G-25 sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, Reversed Phase High Performance XBridge is used
tMprep C18 post is further purified, acetonitrile-the trifluoroacetic acid aqueous solution (0.2%V/V trifluoroacetic acid aqueous solution) being respectively 9%, 19%, 39% and 55% successively by the volume percent of acetonitrile carries out wash-out for moving phase, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 19%, lyophilize, obtains saury anti-oxidation peptide.
The saury anti-oxidation peptide that the present embodiment obtains, carry out sequential analysis by mass spectroscopy, from the molion that first mass spectrometric produces, select m/z to be 436.4388 as parent ion, enter second order ms, through sequential analysis, the aminoacid sequence obtaining this peptide is Ser-Gly-Ala-Ala-Met.
Embodiment 3
(1) saury is decaptitated and internal organ, be twisted into fish gruel after watery blood cleans up, by rotten for fish with water in mass ratio 1:4 mix, add the mixed enzyme of flavor protease and pancreatin, addition is 1000U/g albumen, pH be 7.5, temperature be 50 DEG C of conditions under enzymolysis 12h; Be incubated 15min at 95 DEG C, under the centrifugal force of 2500g, centrifugal 20min, gets supernatant liquor, obtains saury protein hydrolysate (PSPHs), and degree of hydrolysis is 18.72% ± 0.95%;
(2) with HP-20 macroporous adsorbent resin, PSPHs is separated, be 20%, 40%, 60% and 80% ethanolic soln gradient elution by distilled water and volume fraction successively after loading, collect the component of 40% ethanolic soln wash-out, lyophilize, obtain Gly-His-Lys I;
(3) Gly-His-Lys I Sephadex G-25 sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, Reversed Phase High Performance XBridge is used
tMprep C18 post is further purified, acetonitrile-the trifluoroacetic acid aqueous solution (0.1%V/V trifluoroacetic acid aqueous solution) being respectively 5%, 10%, 30% and 50% successively by the volume percent of acetonitrile carries out wash-out for moving phase, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 10%, lyophilize, obtains saury anti-oxidation peptide.
The saury anti-oxidation peptide that the present embodiment obtains, carry out sequential analysis by mass spectroscopy, from the molion that first mass spectrometric produces, select m/z to be 436.4388 as parent ion, enter second order ms, through sequential analysis, the aminoacid sequence obtaining this peptide is Ser-Gly-Ala-Ala-Met.
Embodiment 4
(1) saury is decaptitated and internal organ, after watery blood cleans up, is twisted into fish gruel, by rotten for fish with water in mass ratio 1:4 mix, add the mixed enzyme of flavor protease and pancreatin, addition is 1000U/g albumen, pH be 8, temperature be 50 DEG C of conditions under enzymolysis 8h; Be incubated 15min at 95 DEG C, under the centrifugal force of 3500g, centrifugal 15min, gets supernatant liquor, obtains saury protein hydrolysate (PSPHs), and degree of hydrolysis is 17.92% ± 0.95%;
(2) with HP-20 macroporous adsorbent resin, PSPHs is separated, be 20%, 40%, 60% and 80% ethanolic soln gradient elution by distilled water and volume fraction successively after loading, collect the component of 40% ethanolic soln wash-out, lyophilize, obtain Gly-His-Lys I;
(3) Gly-His-Lys I Sephadex G-25 sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, Reversed Phase High Performance XBridge is used
tMprep C18 post is further purified, acetonitrile-the trifluoroacetic acid aqueous solution (0.1%V/V trifluoroacetic acid aqueous solution) being respectively 5%, 15%, 30% and 45% successively by the volume percent of acetonitrile carries out wash-out for moving phase, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 15%, lyophilize, obtains saury anti-oxidation peptide.
The saury anti-oxidation peptide that the present embodiment obtains, carry out sequential analysis by mass spectroscopy, from the molion that first mass spectrometric produces, select m/z to be 436.4388 as parent ion, enter second order ms, through sequential analysis, the aminoacid sequence obtaining this peptide is Ser-Gly-Ala-Ala-Met.
Embodiment 5
(1) saury is decaptitated and internal organ, after watery blood cleans up, is twisted into fish gruel, by rotten for fish with water in mass ratio 1:3 mix, add the mixed enzyme of flavor protease and pancreatin, addition is 1000U/g albumen, pH be 8, temperature be 50 DEG C of conditions under enzymolysis 8h; Be incubated 15min at 95 DEG C, under the centrifugal force of 3500g, centrifugal 15min, gets supernatant liquor, obtains saury protein hydrolysate (PSPHs), and degree of hydrolysis is 17.03% ± 0.32%;
(2) with HP-20 macroporous adsorbent resin, PSPHs is separated, be 20%, 40%, 60% and 80% ethanolic soln gradient elution by distilled water and volume fraction successively after loading, each component is detected under determined wavelength is 214nm condition, as shown in Figure 1, obtain five component PSPHs-I, PSPHs-II, PSPHs-III, PSPHs-IV, PSPHs-V successively, collect the component PSPHs-III of 40% ethanolic soln wash-out, lyophilize, obtain Gly-His-Lys I;
(3) Gly-His-Lys I Sephadex G-25 sephadex chromatography post is separated, be that moving phase carries out wash-out with distilled water, each component is detected under determined wavelength is 214nm condition, as shown in Figure 2, three component A, B and C are obtained successively by the time order and function of wash-out, collect the component C of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, Reversed Phase High Performance XBridge is used
tMprep C18 post is further purified, be that moving phase carries out wash-out with acetonitrile-trifluoroacetic acid aqueous solution that the volume percent of acetonitrile is respectively 5%, 15%, 30% and 45% successively, each component is detected under determined wavelength is 214nm condition, as shown in Figure 3, obtain five component C1, C2, C3, C4 and C5 successively, collect the component C3 of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 15%, lyophilize, obtains saury anti-oxidation peptide.
The saury anti-oxidation peptide that the present embodiment obtains, sequential analysis is carried out by mass spectroscopy, result as shown in Figure 4, from the molion that first mass spectrometric produces, select m/z to be 436.4388 as parent ion (can show that from spectrogram the mass percent of this parent ion is about 86%), enter second order ms, through sequential analysis, the aminoacid sequence obtaining this peptide is Ser-Gly-Ala-Ala-Met.
The anti-oxidant activity of five components obtained in the enzymolysis product (PSPHs) obtained the present embodiment step (1) and step (2) detects, result is as shown in table 1, as can be seen from Table 1, the anti-oxidant activity of component PSPHs-III is the highest.
Table 1 each component anti-oxidant activity detected result
Detect the anti-oxidant activity of three components obtained in the present embodiment step (3), as shown in Figure 5, as seen from Figure 5, the anti-oxidant activity of component C is the highest for result.
The anti-oxidant activity of five components obtained in the present embodiment step (4) is detected, result as shown in Figure 6, as seen from Figure 6, the anti-oxidant activity of the saury anti-oxidation peptide (component C3) that the present embodiment obtains is the highest, and its oxyradical receptivity is 4.47 times of gsh (GSH); For about 10 times of thick peptide (PSPHs).
In the present invention, ORAC (Oxygen radical absorbance capacity, oxyradical receptivity) ORAC method, reducing power and scavenging ability of DPPH free radical is adopted to measure the activity of anti-oxidation peptide.
ORAC method: the method with reference to people such as Blanca Hernndez Ledesma also slightly changes.In each micropore of 96 hole fluorescent plate, add testing sample 20 μ L respectively (each enzymolysis product 75mmol/L phosphate buffered saline buffer is done suitable dilution, each sample liquid concentration to be measured is 0.04-0.06mg/mL) add 70nmol/L fluorescein (FL) 120 μ L afterwards, be incubated 15min at 37 DEG C after, in each hole, add rapidly 12mmol/L AAPH60 μ L with multichannel pipettor and start reaction, and microwell plate is placed in microplate reader at 37 DEG C with excitation wavelength 485nm, emission wavelength 520nm carries out METHOD FOR CONTINUOUS DETERMINATION, every 2min measures 1 each hole fluorescence intensity, minute be set in fluorescence decay be after baseline till, namely 2h is set to.Fluorescence intensity is designated as f respectively
0, f
1, f
2... f
100, by the absolute fluorescence intensity data f of each micropore different time points of record
nwith initial fluorescent intensity f
0compare, be converted to relative intensity of fluorescence, and according to formula AUC=f
1/ f
0+ f
2/ f
0+ f
3/ f
0+ ... f
i/ f
0+ ... f
100/ f
0, statistics fluorescence quenching area under curve (AUC
sample) value, then according to formula net AUC=AUC
sample-AUC
blank, calculate the net AUC value of different concns Trolox and sample respectively, wherein AUC
blankthe AUC value of Free Radical contrast during for not having an antioxidant.
The mensuration of reducing power: the method with reference to people such as Sampath Kumar also slightly changes.Certain density PSPHs and GSH contrast solution is prepared with deionized water, getting each sample 2mL joins in the mixture of the potassium ferricyanide solution of 2mL0.2mol/L phosphate buffered saline buffer (pH6.6) and 2mL1%, the TCA of 2mL10% is added again after 50 DEG C of insulation 20min, then with the centrifugal 10min of 3000r/min, get supernatant liquor 2mL and 2mL distilled water and 0.4mL0.1% iron(ic) chloride to react, after 10min, measure its light absorption value at 700nm place.
The mensuration of scavenging ability of DPPH free radical: the method with reference to people such as Xie Zhengjun also slightly changes.Accurately take 7.92mg DPPH, with 95% dissolve with ethanol and constant volume to 100mL, be mixed with 0.2mmol DPPH ethanolic soln.Certain density PSPHs and GSH contrast solution is prepared with deionized water.Get each sample liquid and contrast liquid 2.0mL to mix with 2.0mL DPPH ethanolic soln and shake up, ambient temperatare surveys the light absorption value at 517nm place after putting 30min, count A
i; Get each sample liquid and contrast liquid 2.0mL and mix with 2.0mL95% ethanolic soln the light absorption value shaking up and measure 517nm place, reading counts A
j; Get 2ml DPPH ethanolic soln and add that the mixing of 2ml distilled water shakes up the light absorption value measuring 517nm place, reading counts A
c; The blank ethanol for 2ml95% adds the zeroing of 2ml distilled water.All measured values are three mean values, and the clearance rate calculation formula of DPPH free radical is: R=[1-(A
i-A
j)/A
c] × 100%.
Above-described embodiment is the present invention's preferably embodiment; but embodiments of the present invention are not restricted to the described embodiments; change, the modification done under other any does not deviate from spirit of the present invention and principle, substitute, combine, simplify; all should be the substitute mode of equivalence, be included within protection scope of the present invention.
Claims (9)
1. a saury anti-oxidation peptide, is characterized in that described anti-oxidation peptide has the aminoacid sequence of Ser-Gly-Ala-Ala-Met.
2. the separating and extracting method of saury anti-oxidation peptide according to claim 1, is characterized in that comprising following operation steps:
(1) being decaptitated and internal organ by saury, be twisted into fish gruel after watery blood cleans up, is 1:(2 ~ 4 by fish gruel and water in mass ratio) mix, add protease hydrolyzed 4 ~ 12h, go out enzyme, and centrifuging and taking supernatant liquor after cooling, obtains saury protein hydrolysate;
(2) with macroporous adsorbent resin, PSPHs is separated, be the ethanolic soln gradient elution of 10% ~ 29%, 30% ~ 49%, 50% ~ 69% and 70% ~ 90% successively by distilled water and volume fraction, collect the component of 30% ~ 49% ethanolic soln wash-out, lyophilize, obtains Gly-His-Lys I;
(3) Gly-His-Lys I sephadex chromatography post is separated, is that moving phase carries out wash-out with distilled water, obtains three components successively by the time order and function of wash-out, collect the component of last wash-out, lyophilize, obtain Gly-His-Lys II;
(4) by after water-soluble for Gly-His-Lys II, be further purified with Reversed Phase High Performance, be that moving phase carries out wash-out with acetonitrile-trifluoroacetic acid aqueous solution that the volume percent of acetonitrile is respectively 2% ~ 9%, 10% ~ 19%, 20% ~ 39% and 40% ~ 55% successively, collect the component of the acetonitrile-trifluoroacetic acid aqueous solution wash-out of 10% ~ 19%, lyophilize, obtains saury anti-oxidation peptide.
3. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: the proteolytic enzyme described in step (1) is one or both in flavor protease or pancreatin; The addition of proteolytic enzyme is 500 ~ 1500U/g albumen.
4. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: described in step (1), the pH of enzymolysis is 6.5 ~ 8.5, and hydrolysis temperature is 45 ~ 55 DEG C.
5. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: the enzyme that goes out described in step (1) refers to insulation 10 ~ 30min at 85 ~ 100 DEG C; Described centrifugally refer to centrifugal 10 ~ 30min under the centrifugal force of 1500 ~ 4000g.
6. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: the macroporous adsorbent resin described in step (2) refers to HP-20 resin.
7. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: the sephadex chromatography post described in step (3) refers to Sephadex G-25 sephadex chromatography post.
8. the separating and extracting method of saury anti-oxidation peptide according to claim 2, is characterized in that: the Reversed Phase High Performance described in step (4) refers to C18 post; Described trifluoroacetic acid aqueous solution refers to that volume fraction is the trifluoroacetic acid aqueous solution of 0.1% ~ 0.2%.
9. the application of saury anti-oxidation peptide according to claim 1 in food, makeup and field of medicaments.
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| CN107927623A (en) * | 2017-12-12 | 2018-04-20 | 苏州卫生职业技术学院 | A kind of preparation method of anti-fatigue health-caring preparation |
| CN108059662A (en) * | 2018-02-02 | 2018-05-22 | 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 |
| CN108117589A (en) * | 2018-02-13 | 2018-06-05 | 中国科学院海洋研究所 | A kind of isolation and purification method of Optimization of Low Value Fish anti-oxidation peptide |
| 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 |
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| 赵强忠 等: "秋刀鱼抗氧化肽制备及其抗氧化活性的研究", 《现代食品科技》 * |
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| CN108059662A (en) * | 2018-02-02 | 2018-05-22 | 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 |
| CN108117589A (en) * | 2018-02-13 | 2018-06-05 | 中国科学院海洋研究所 | A kind of isolation and purification method of Optimization of Low Value Fish anti-oxidation peptide |
| CN108117589B (en) * | 2018-02-13 | 2020-12-29 | 中国科学院海洋研究所 | Separation and purification method of low-value fish antioxidant peptide |
| 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 |
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