CN114805490B - Antioxidant peptide prepared from tilapia skin and preparation method thereof - Google Patents
Antioxidant peptide prepared from tilapia skin and preparation method thereof Download PDFInfo
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- CN114805490B CN114805490B CN202210237803.3A CN202210237803A CN114805490B CN 114805490 B CN114805490 B CN 114805490B CN 202210237803 A CN202210237803 A CN 202210237803A CN 114805490 B CN114805490 B CN 114805490B
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/06—Free radical scavengers or antioxidants
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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 invention discloses an antioxidant peptide prepared from tilapia skin and a preparation method thereof, wherein the amino acid sequence of the antioxidant peptide is Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu. The preparation method sequentially comprises the following steps: washing and crushing tilapia skin, adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 8.0-12.0, the temperature is 35-65 ℃, the enzyme adding amount is 1-6% of the total mass, and the feed-liquid ratio is 1: 20-80 g/ml, and the enzymolysis time is 5.0-15.0 h; inactivating enzyme in a boiling water bath of the tilapia skin enzymolysis liquid, rapidly cooling, centrifuging for 10-20 min at 10000r/min at 4 ℃, and taking supernatant; filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000; separating the components with molecular weight less than or equal to 1000 by using a reversed-phase high performance liquid chromatograph to obtain the tilapia skin antioxidant peptide with molecular weight of 1007Da and amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to an antioxidant peptide prepared from tilapia skin and a preparation method thereof.
Background
When the organism is stimulated by harmful substances, the organism can generate excessive active oxygen free radicals, and then the living organism can develop and attack cells and mitochondria in the body, so that the structure and the function of the living organism are changed, and diseases such as aging and the like are caused. Antioxidants can scavenge excessive reactive oxygen radicals through enzymatic or non-enzymatic reactions, and existing antioxidants are both synthetic and natural. The synthetic antioxidant has low price and high antioxidant activity, but researches show that the synthetic antioxidant has the adverse effects of carcinogenesis, teratogenesis, mutation and the like; the natural antioxidant is mainly antioxidant peptide, not only can remove free radicals, but also has the functions of body defense, immunoregulation, mineral absorption promotion and the like.
Tilapia is a freshwater fish which is widely cultivated, only tilapia is widely accepted at present, but bones, viscera, skin and the like of the tilapia are not developed. In particular, tilapia skin contains abundant collagen, but no report has been made so far on the preparation of antioxidant peptide from tilapia skin as a raw material.
Disclosure of Invention
The invention aims to solve the technical problems in the prior art and provides an antioxidant peptide prepared from tilapia skin and a preparation method thereof.
The technical scheme of the invention is as follows: an antioxidant peptide prepared from tilapia skin has an amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu.
The preparation method of the antioxidant peptide prepared by utilizing tilapia skin sequentially comprises the following steps:
a. washing and crushing tilapia skin, adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 8.0-12.0, the temperature is 35-65 ℃, the enzyme adding amount is 1-6% of the total mass, and the feed-liquid ratio is 1: 20-80 g/ml, and the enzymolysis time is 5.0-15.0 h;
b. inactivating enzyme in a boiling water bath of the tilapia skin enzymolysis liquid, rapidly cooling, centrifuging for 10-20 min at 10000r/min at 4 ℃, and taking supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. the components with the molecular weight less than or equal to 1000 are separated by using a reversed-phase high performance liquid chromatograph to obtain the antioxidant peptide with the molecular weight of 1007Da and the amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu.
The preparation method is preferably carried out according to the following steps:
a. washing and crushing tilapia skin, and then adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 10.0, the temperature is 51 ℃, the enzyme adding amount is 2.51% of the total mass, and the feed-liquid ratio is 1: 5.0 g/ml, and the enzymolysis time is 9.0h;
b. inactivating enzyme in boiling water bath for 15min, rapidly cooling, centrifuging at 4deg.C for 15min at 10000r/min, and collecting supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. the components with the molecular weight less than or equal to 1000 are separated by using a reversed-phase high performance liquid chromatograph to obtain the antioxidant peptide with the molecular weight of 1007Da and the amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu.
The separation conditions of the step d are as follows: the chromatographic column is PREP-ODS (H) KIT,250×20mmI.D; the mobile phase is acetonitrile solution with 5% of A phase-mass concentration, the acetonitrile solution with 80% of B phase-mass concentration, and the acetonitrile solutions of A phase and B phase both contain 0.1% of TFA by mass percent; gradient elution is carried out for 10 percent of phase B, 0 to 10 minutes, 10 to 80 percent of phase B, 10 to 15 minutes and 80 to 10 percent of phase B for 30 to 40 minutes; the sample loading was 700. Mu.L, the flow rate was 7ml/min, and the detection wavelength was 220nm.
The invention takes tilapia skin as raw material, and active polypeptide with specific peptide chain length is obtained by controlling enzymolysis conditions of alkaline protease, and the active polypeptide has low price and higher antioxidationActivity, DPPH, ABTS and hydroxyl radical IC 50 (semi-inhibitory concentration) was 2.56.+ -. 0.15, 15.14.+ -. 0.01, 16.38.+ -. 0.68 mg/ml, respectively. Meanwhile, the invention improves the utilization rate of the tilapia skin and increases the added value of tilapia byproducts.
Drawings
FIG. 1 is a schematic representation of antioxidant activity of various ultrafiltration components in accordance with an embodiment of the present invention.
FIG. 2 is a RP-HPLC elution profile of the product H1-H8 isolated in accordance with the present invention.
FIG. 3 is a schematic representation of the antioxidant activity of the isolated products H1-H8 according to the example of the present invention.
FIG. 4 is a total ion flow diagram of the separation product H8 according to an embodiment of the present invention.
FIG. 5 is a mass spectrum of an antioxidant peptide according to an embodiment of the present invention.
Detailed Description
Example 1:
the invention relates to a preparation method of antioxidant peptide prepared from tilapia skin, which comprises the following steps of:
a. washing and crushing 5g of tilapia skin, adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are pH10.0 (regulated by 1mol/L NaOH), temperature of 51 ℃, enzyme addition amount of 2.51% of total mass and feed-liquid ratio of 1 g:50ml and enzymolysis time of 9.0h;
b. inactivating enzyme in boiling water bath for 15min, rapidly cooling, centrifuging at 4deg.C for 15min at 10000r/min, and collecting supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. the components with the molecular weight less than or equal to 1000 are separated by using a reversed-phase high performance liquid chromatograph to obtain the antioxidant peptide with the molecular weight of 1007Da and the amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu. The separation condition is that the chromatographic column is PREP-ODS (H) KIT,250×20mmI.D; the mobile phase is acetonitrile solution with 5% of A phase-mass concentration, the acetonitrile solution with 80% of B phase-mass concentration, and the acetonitrile solutions of A phase and B phase both contain 0.1% of TFA by mass percent; gradient elution is carried out for 10 percent of phase B, 0 to 10 minutes, 10 to 80 percent of phase B, 10 to 15 minutes and 80 to 10 percent of phase B for 30 to 40 minutes; the sample loading was 700. Mu.L, the flow rate was 7ml/min, and the detection wavelength was 220nm.
Example 2:
the invention relates to a preparation method of antioxidant peptide prepared from tilapia skin, which comprises the following steps of:
a. washing and crushing 5g of tilapia skin, and adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 8.0 (regulated by 1mol/L NaOH), the temperature is 65 ℃, the enzyme adding amount is 1% of the total mass, and the feed-liquid ratio is 1 g:80ml, enzymolysis time is 15.0h;
b. inactivating enzyme in boiling water bath for 15min, rapidly cooling, centrifuging at 4deg.C for 20min at 10000r/min, and collecting supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. the components with the molecular weight less than or equal to 1000 are separated by using a reversed-phase high performance liquid chromatograph to obtain the antioxidant peptide with the molecular weight of 1007Da and the amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu. The separation condition is that the chromatographic column is PREP-ODS (H) KIT,250×20mmI.D; the mobile phase is acetonitrile solution with 5% of A phase-mass concentration, the acetonitrile solution with 80% of B phase-mass concentration, and the acetonitrile solutions of A phase and B phase both contain 0.1% of TFA by mass percent; gradient elution is carried out for 10 percent of phase B, 0 to 10 minutes, 10 to 80 percent of phase B, 10 to 15 minutes and 80 to 10 percent of phase B for 30 to 40 minutes; the sample loading was 700. Mu.L, the flow rate was 7ml/min, and the detection wavelength was 220nm.
Example 3:
the invention relates to a preparation method of antioxidant peptide prepared from tilapia skin, which comprises the following steps of:
a. washing and crushing 5g of tilapia skin, and adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 12.0 (regulated by 1mol/L NaOH), the temperature is 35 ℃, the enzyme adding amount is 6% of the total mass, and the feed-liquid ratio is 1 g:20ml and enzymolysis time of 5.0h;
b. inactivating enzyme in boiling water bath for 15min, rapidly cooling, centrifuging at 4deg.C for 10min at 10000r/min, and collecting supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. the components with the molecular weight less than or equal to 1000 are separated by using a reversed-phase high performance liquid chromatograph to obtain the antioxidant peptide with the molecular weight of 1007Da and the amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu. The separation condition is that the chromatographic column is PREP-ODS (H) KIT,250×20mmI.D; the mobile phase is acetonitrile solution with 5% of A phase-mass concentration, the acetonitrile solution with 80% of B phase-mass concentration, and the acetonitrile solutions of A phase and B phase both contain 0.1% of TFA by mass percent; gradient elution is carried out for 10 percent of phase B, 0 to 10 minutes, 10 to 80 percent of phase B, 10 to 15 minutes and 80 to 10 percent of phase B for 30 to 40 minutes; the sample loading was 700. Mu.L, the flow rate was 7ml/min, and the detection wavelength was 220nm.
The alkaline protease used in examples 1 to 3 was purchased from Shanghai Yuan Yeast Biotechnology Co., ltd (China Shanghai), and the enzyme activity unit was 200U/mg.
Experiment:
the steps a and b in the example 1 are carried out enzymolysis on tilapia skin to obtain supernatant, the supernatant is filtered by an ultrafiltration membrane to obtain components with molecular weights of more than or equal to 5000Da, 3500-5000Da, 1000-3500Da and less than or equal to 1000Da, and the antioxidant activity of each component is measured, and the result is shown in figure 1.
FIG. 1 shows that component (M4) with molecular weight less than or equal to 1000Da has higher antioxidant activity.
Separating the component with molecular weight less than or equal to 1000Da by using reversed phase high performance liquid chromatography according to the method of step d to obtain the elution components H1-H8 corresponding to each absorption peak as shown in figure 2. The antioxidant activity of each of the components H1 to H8 was measured, and the results are shown in FIG. 3, which shows that the antioxidant activity of the component H8 is the highest.
Component H8 is identified by MALDILC-MS/MS, and the total ion flow diagram is shown in figure 4, wherein one amino acid sequence is Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu; the mass spectrum is shown in FIG. 5, and the molecular weight is 1007 Da.
The protein peptide with the amino acid sequence Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu is synthesized and prepared according to the prior art, and the antioxidant activity is detected,DPPH, ABTS and hydroxyl radical IC 50 (semi-inhibitory concentration) was 8.52.+ -. 0.69, 9.14.+ -. 0.08, 23.44.+ -. 1.60. 1.60 mg/ml, respectively.
The method for testing the antioxidant activity comprises the following steps:
(1) DPPH free radical scavenging ability
Samples of different concentrations were each taken and mixed well with 100uL DPPH solution (0.05 mg/ml, ethanol preparation) and incubated at room temperature for 30 minutes in the absence of light, and absorbance at 517nm was measured. Ethanol was used as a control instead of DPPH solution and ethanol was used as a blank instead of sample. Glutathione (GSH) was used as a positive control. The DPPH radical scavenging activity of the samples was calculated as follows:
wherein A is s 、A c And A b The absorbance of the sample group, the control group and the blank group are represented, respectively.
(2) ABTS radical scavenging ability
Preparation of stock solution containing 7mmol/L ABTS and 2.45mmol/L Potassium persulfate as ABTS solution, at room temperature overnight protected from light to give ABTS + . The ABTS working solution was diluted in distilled water with an absorbance at 734nm of 0.70±0.02. 100uL samples with different concentrations are fully mixed with 400 uLABSS working solution respectively, incubated for 10 minutes at room temperature in a dark place, and absorbance at 734nm is measured. Distilled water was used instead of the sample as a blank. GSH was used as a positive control. ABTS radical scavenging activity of the samples was calculated as follows:
wherein A is s And A b The absorbance of the sample and blank groups, respectively.
(3) Scavenging ability of hydroxyl radical
Samples with different concentrations are respectively taken to be 100uL and 100uL 9mmol/L FeSO 4 100uL 9mmol/L salicylic acid ethanolSolution, 100uL8.8mmol/LH 2 O 2 The mixture was thoroughly mixed and incubated in a 37℃water bath for 30 minutes, and the absorbance at 510nm was measured. Distilled water replaces H 2 O 2 And samples were used as control and blank. GSH was used as a positive control. The hydroxyl radical scavenging activity of the samples was calculated as follows:
wherein A is s 、A c And A b The absorbance of the sample group, the control group and the blank group are represented, respectively.
Sequence listing
<110> university of Dalian ocean
<120> an antioxidant peptide prepared from tilapia skin and preparation method thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 12
<212> PRT
<213> Tilapia (Oreochromis mossambicus)
<400> 1
Gly Asn Ala Gly Pro Thr Gly Pro Ala Gly Pro Leu
1 5 10
Claims (2)
1. An antioxidant peptide prepared from tilapia skin is characterized in that: the amino acid sequence of the antioxidant peptide is Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu.
2. A method for preparing an antioxidant peptide prepared from tilapia skin according to claim 1, which comprises the following steps in sequence:
a. washing and crushing tilapia skin, and then adding alkaline protease for enzymolysis to obtain tilapia skin enzymolysis liquid, wherein the enzymolysis conditions are that the pH is 10.0, the temperature is 51 ℃, the enzyme adding amount is 2.51% of the total mass, and the feed-liquid ratio is 1: 5.0 g/ml, and the enzymolysis time is 9.0h;
b. inactivating enzyme in boiling water bath for 15min, rapidly cooling, centrifuging at 4deg.C for 15min at 10000r/min, and collecting supernatant;
c. filtering the supernatant with ultrafiltration membrane to obtain component with molecular weight less than or equal to 1000;
d. separating the components with molecular weight less than or equal to 1000 by using a reversed-phase high performance liquid chromatograph to obtain antioxidant peptide with molecular weight of 1007Da and amino acid sequence of Gly-Asn-Ala-Gly-Pro-Thr-Gly-Pro-Ala-Gly-Pro-Leu;
the separation conditions of the step d are as follows: the chromatographic column is PREP-ODS (H) KIT,250×20mmI.D; the mobile phase is acetonitrile solution with 5% of A phase-mass concentration, the acetonitrile solution with 80% of B phase-mass concentration, and the acetonitrile solutions of A phase and B phase both contain 0.1% of TFA by mass percent; gradient elution is carried out for 10 percent of phase B, 0 to 10 minutes, 10 to 80 percent of phase B, 10 to 15 minutes and 80 to 10 percent of phase B for 30 to 40 minutes; the sample loading was 700. Mu.L, the flow rate was 7ml/min, and the detection wavelength was 220nm.
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2022
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| CN102219829A (en) * | 2011-05-18 | 2011-10-19 | 福州大学 | Antioxidant polypeptide prepared by enzymatic hydrolysis of sharkskin collagen with acid protease |
| CN107441479A (en) * | 2017-08-08 | 2017-12-08 | 广东海洋大学 | Marine active peptide/chitin burn ointment for treating scald and preparation method thereof |
| CN108794576A (en) * | 2018-06-26 | 2018-11-13 | 福州大学 | The method for preparing antioxidation polypeptide as raw material using black sharkskin |
| CN112280816A (en) * | 2020-09-18 | 2021-01-29 | 自然资源部第三海洋研究所 | Large-scale preparation method of marine source type I collagen subunit |
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