CN110105430B - Ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof - Google Patents
Ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof Download PDFInfo
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- CN110105430B CN110105430B CN201910434383.6A CN201910434383A CN110105430B CN 110105430 B CN110105430 B CN 110105430B CN 201910434383 A CN201910434383 A CN 201910434383A CN 110105430 B CN110105430 B CN 110105430B
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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
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/485—Exopeptidases (3.4.11-3.4.19)
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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
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/15—Peptidyl-dipeptidases (3.4.15)
- C12Y304/15001—Peptidyl-dipeptidase A (3.4.15.1)
Abstract
The invention discloses a ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and a preparation method thereof. The method comprises the following specific steps: shelling fresh ginkgo nuts, and extracting crude protein after crushing treatment; carrying out enzymolysis on crude protein by protease; performing ultrafiltration on the enzymolysis liquid; subjecting the ultrafiltration permeate to Sephadex chromatography; separating the chromatographic solution by liquid chromatography to obtain the ginkgo protein peptide with the potential of reducing blood pressure, wherein the amino acid sequence of the ginkgo protein peptide is as follows: arginine-alanine-aspartic acid-phenylalanine-lysine (RADFK). The small peptide prepared by the invention has high Angiotensin Converting Enzyme (ACE) inhibitory activity, does not have cysteine residue in an amino acid sequence, does not need to be added with an additive for protecting active peptide, has simple preparation process, low cost and high product quality, and is suitable for industrial production.
Description
Technical Field
The invention relates to a ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and a preparation method thereof, belonging to the technical field of deep processing of agricultural products.
Background
According to the estimation of the world health organization, 1750 million people die from cardiovascular diseases every year, and hypertension is the key point for preventing and treating the cardiovascular diseases. Currently used hypotensive drugs such as captopril and enalapril are limited due to adverse reactions such as cough, rash and headache. However, the incidence of cardiovascular disease is increasing and new, safe alternatives, such as food-derived active peptides, are needed. Bioactive peptides are a generic term for a series of polypeptides of different sequences that constitute natural amino acids. They have multiple biological functions, such as antioxidant, immune-enhancing, hormone-regulating, antibacterial, antithrombotic, antiviral, antihypertensive, etc. The antihypertensive peptide, also called angiotensin converting enzyme inhibitory peptide, is a short-chain polypeptide substance which is separated from food protein and has obvious blood pressure reducing effect. The in vitro hypotensive activity of polypeptides is determined primarily by measuring the inhibitory activity of Angiotensin Converting Enzyme (ACE). Angiotensin Converting Enzyme (ACE) is a dipeptidyl carboxypeptidase located on the cell membrane and a key molecule in regulating blood pressure. The antihypertensive peptide has high food safety and bioavailability, and is a potential choice for developing functional peptide drugs and functional food additives.
Disclosure of Invention
The invention aims to provide a ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and a preparation method thereof.
In order to achieve the above objects and other related objects, the present invention provides the following technical solutions: a ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity is characterized in that: consists of the following amino acid residues: arginine-alanine-aspartic acid-phenylalanine-lysine.
In order to achieve the above objects and other related objects, the present invention provides the following technical solutions: a method for preparing ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity comprises the following steps:
step 1; soaking and degreasing the ginkgo nut powder to obtain degreased ginkgo nut powder;
step 2: extracting protein from defatted semen Ginkgo powder by alkali-dissolving and acid-precipitating method, dialyzing the obtained extractive solution, and lyophilizing to obtain semen Ginkgo protein;
and 3, step 3: preparing protein into aqueous solution, adding alkaline protease for enzymolysis, inactivating enzyme after enzymolysis, and centrifuging to obtain supernatant to obtain semen Ginkgo protease hydrolysate;
and 4, step 4: performing ultrafiltration treatment on the ginkgo protein hydrolysate, collecting ultrafiltration permeate and freeze-drying to obtain a ginkgo protein hydrolysate;
and 5: preparing a ginkgo protein hydrolysate into a ginkgo protein hydrolysate aqueous solution, carrying out chromatography on the ginkgo protein hydrolysate solution by using sephadex as a chromatography medium, and collecting a sample with the retention time of 87.36-102.23 min;
step 6: desalting the sample obtained in the step 5, freeze-drying, dissolving in trifluoroacetic acid aqueous solution again, and then adopting a C18 reverse phase chromatographic column, wherein a mobile phase a is formic acid aqueous solution with the volume fraction of 0.1%, a mobile phase b is acetonitrile aqueous solution containing formic acid with the mass fraction of 0.1%, and the volume fraction of acetonitrile is 84%; after the chromatographic column is balanced by the solution a, a sample is loaded by an automatic sample injector, and the detection wavelength is 228nm; collecting eluate with peak time of 25.13 min to obtain semen Ginkgo protein peptide solution with angiotensin converting enzyme inhibitory activity; the mass spectrometry analysis result shows that the amino acid sequence of the ginkgo protein peptide is as follows: arginine-alanine-aspartic acid-phenylalanine-lysine.
The preferable technical scheme is as follows: step 1, soaking the ginkgo nut powder in ethyl acetate for degreasing, performing suction filtration to remove a solvent after degreasing is finished, and drying to obtain degreased ginkgo nut powder; the particle size of the ginkgo nut powder is less than or equal to 40-80 meshes.
The preferable technical scheme is as follows: and 2, dissolving the defatted ginkgo nut powder in distilled water, regulating the pH value to 10, stirring overnight, centrifuging, taking supernatant, regulating the pH value of the supernatant to 4.62, centrifuging again, removing the supernatant, taking precipitate, dialyzing the precipitate in distilled water, and freeze-drying to obtain the defatted ginkgo protein.
The preferable technical scheme is as follows: in step 3, the defatted ginkgo protein is prepared into protein aqueous solution, the pH value is adjusted to 10, then alkaline protease is added, and the temperature is kept at 48-52 ℃ for 3.5-4.5 h.
The preferable technical scheme is as follows: and step 4, performing ultrafiltration treatment on the ginkgo biloba proteolytic liquid by adopting an ultrafiltration membrane with the molecular weight cutoff of 3000 Da.
The preferable technical scheme is as follows: in step 5, carrying out chromatography on the ginkgo protein hydrolysate solution by using a G-15 sephadex column, collecting a sample with the retention time of 87.36-102.23min, using ultrapure water as an eluent, and carrying out flow rate of 1mL/min and sample loading concentration of 80 mg/mL.
Due to the application of the technical scheme, compared with the prior art, the invention has the advantages that:
the ginkgo protein peptide prepared by the invention has high Angiotensin Converting Enzyme (ACE) inhibitory activity, does not have cysteine residue in an amino acid sequence, does not need to be added with an additive for protecting active peptide, has simple preparation process, low cost and high product quality, and is suitable for industrial production.
Drawings
FIG. 1 is a graph of the chromatography of ginkgo biloba proteolytic enzyme by Sephadex.
Detailed Description
The following description of the embodiments of the present invention is provided for illustrative purposes, and other advantages and effects of the present invention will become apparent to those skilled in the art from the present disclosure.
Please refer to fig. 1. It should be understood that the structures, ratios, sizes, and the like shown in the drawings and described in the specification are only used for matching with the disclosure of the specification, so as to be understood and read by those skilled in the art, and are not used to limit the conditions under which the present invention can be implemented, so that the present invention has no technical significance, and any structural modification, ratio relationship change, or size adjustment should still fall within the scope of the present invention without affecting the efficacy and the achievable purpose of the present invention. In addition, the terms "upper", "lower", "left", "right", "middle" and "one" used in the present specification are for clarity of description, and are not intended to limit the scope of the present invention, and the relative relationship between the terms and the terms is not to be construed as a scope of the present invention.
The detection method of the ACE inhibitory activity of the sample comprises the following steps:
the substrate, maleyl-histidine-leucine (HHL, 5 mM), and the sample were dissolved in 0.1M borate buffer (pH 8.3, containing 0.3M NaCl). Then, 50. Mu.L of the sample and 150. Mu.L of the substrate were added to the centrifuge tube, mixed and preheated in 37 ℃ water for 5 min. Then 0.1U of ACE solution was added and incubated at 37 ℃ for 60 min. At the end of the reaction, 250. Mu.L of 1M hydrochloric acid was added to terminate the reaction, and the solution was filtered through a 0.45 μ M filter and analyzed by reversed-phase high performance liquid chromatography on intsil ODS-3 (25X 4.6mm,5 μ M particle size). The mobile phase was distilled water acetonitrile =75 (v/v, 0.1% trifluoroacetic acid), flow rate 0.5 mL/min, detection wavelength 228 nm. The inhibition activity (%) was determined using captopril as a positive control and distilled water as a blank control as follows:
ACE inhibitory activity (%) = [ (a-B)/a ] × 100;
a is the peak area of hippuric acid when blank control is used, and B is the peak area of hippuric acid when sample is contained.
Example 1: ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof
(1) Pretreatment of raw materials: 500 g of fresh ginkgo fruits are subjected to shelling, seed peeling treatment and cutting, the fresh ginkgo fruits are dried for 24 hours in a constant-temperature drying oven at 45 ℃, and the ginkgo fruits are sieved by a 60-mesh sieve after being crushed.
(2) Degreasing: soaking 220 g of ginkgo nut powder in 400mL of ethyl acetate, stirring once every 10min, soaking for 2h, performing suction filtration to remove the solvent, and drying to obtain defatted ginkgo nut powder;
(3) Extracting ginkgo protein: dissolving 200g of defatted ginkgo powder in distilled water, adjusting the pH value to be 10.0 according to a material-liquid ratio of 1 to 15, stirring overnight, centrifuging 8000 g for 20 min, taking the supernatant, adjusting the pH value to be 4.62, centrifuging 8000 g for 20 min, removing the supernatant, taking the precipitate, taking the distilled water as a dialysate, dialyzing, and freeze-drying to obtain the ginkgo protein.
(4) Enzymolysis: preparing 200mL of 3% ginkgo protein aqueous solution, dissolving in 50 ℃ water bath, adjusting pH to 10.0, waiting for 5min, adding alkaline protease (enzyme activity 4000U), performing enzymolysis for 4h, adding NaOH solution during the enzymolysis, keeping the pH of the solution at 10.0, boiling for 5min to inactivate enzyme after enzymolysis is finished, cooling, adjusting pH to neutral, and centrifuging.
(5) And (3) ultrafiltration: and (3) carrying out ultrafiltration on 150 mL of enzymolysis liquid, wherein the interception amount is 3kDa, continuously collecting ultrafiltration components, and freeze-drying.
(6) Gel chromatography: preparing the product obtained in the step (5) into an aqueous solution, further purifying the ultrafiltration substance by using a G-15 sephadex column, taking ultrapure water as an eluent, wherein the flow rate is 1mL/min, the loading amount is 350mg, the loading volume is 4 mL, the loading concentration is 80 mg/mL, and collecting the chromatographic solution with the retention time of 87.36-102.23 min.
(7) The sample was desalted by chromatography on a DEAE cellulose column, then lyophilized and redissolved in 0.1% by volume trifluoroacetic acid solution. Then, a C18 reverse phase chromatography column was used, and the mobile phase a was 0.1% formic acid in water and the mobile phase b was acetonitrile in water containing 0.1% formic acid (84% acetonitrile). After the column was equilibrated with 95% solution a, a sample was applied by an autosampler, and the detection wavelength was 228nm and the flow rate was 1 mL/min. Collecting eluate with peak time of 25.13 min to obtain semen Ginkgo protein peptide solution with ACE inhibitory activity. Mixing 0.1 mL formic acid and 99.9 mL distilled water, wherein the solution a is 'mobile phase a' -0.1% formic acid aqueous solution; mobile phase b-0.1% formic acid in acetonitrile in water, with a volume fraction of acetonitrile of 84%. Acetonitrile and water are mixed according to the volume ratio of 84.
(8) The ACE inhibitory activity of the eluate is determined, and the amino acid sequence of the protein peptide is detected by LC-MS.
The ACE inhibitory activity detection result is 57.15% (2 mg/mL), and the composition sequence of 25.13 min peak substances is analyzed by liquid chromatography-mass spectrometry: arginine-alanine-aspartic acid-phenylalanine-lysine (RADFK).
Example 2: ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof
(1) Pretreatment of raw materials: 700g of fresh ginkgo fruits are subjected to shelling and seed peeling treatment, and then are placed in a constant temperature drying oven for drying for 30 hours, and are sieved by a 80-mesh sieve after being crushed.
(2) Degreasing: soaking 350 g of ginkgo nut powder in 100 mL of ethyl acetate, stirring once every 10min, soaking for 2h, performing suction filtration to remove the solvent, and drying to obtain defatted ginkgo nut powder;
(3) Protein extraction: dissolving 300 g of defatted ginkgo powder in distilled water, adjusting the pH to 10 according to a material-liquid ratio of 1.
(4) Enzymolysis: preparing 250 mL of 3% protein solution, dissolving at 45 ℃, adjusting the pH value to 10.0, adding 3500U of alkaline protease, carrying out enzymolysis for 5 h, adding NaOH solution during the enzymolysis, keeping the pH value of the solution at 10.0, boiling for 10min to inactivate the enzyme after the enzymolysis is finished, cooling, adjusting the pH value back to 7, centrifuging, and freeze-drying.
(5) And (3) ultrafiltration: and (3) performing ultrafiltration on 200mL of enzymolysis liquid, wherein the interception amount is 3kDa, continuously collecting ultrafiltration components, and performing freeze drying.
(6) Gel chromatography: the loading amount is 800 mg, the loading volume is 10 mL, and the chromatographic solution with the retention time of 87.36-102.23min is collected.
(7) After desalting and freeze-drying, the sample was redissolved in 0.1% trifluoroacetic acid solution. A C18 reverse phase chromatography column was used, mobile phase a being 0.1% aqueous formic acid and mobile phase b being 0.1% aqueous acetonitrile containing formic acid (84% acetonitrile). After the column was equilibrated with 95% solution a, a sample was applied by an autosampler, and the detection wavelength was 228nm and the flow rate was 1 mL/min. Collecting the eluate with peak time of 25.13 min;
(8) And (3) determining the ACE inhibitory activity of the eluent, and detecting the amino acid sequence of the protein peptide by liquid chromatography-mass spectrometry.
The ACE inhibitory activity detection result is 58.92% (1 mg/mL), and the composition sequence of 25.13 min peak substances is analyzed by liquid chromatography-mass spectrometry: arginine-alanine-aspartic acid-phenylalanine-lysine (RADFK).
Example 3: ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof
A Ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity comprises the following amino acid residues: arginine-alanine-aspartic acid-phenylalanine-lysine.
The preparation method comprises the following steps:
step 1; soaking and degreasing the ginkgo nut powder to obtain degreased ginkgo nut powder;
step 2: extracting protein from defatted ginkgo nut powder by an alkali-soluble acid precipitation method, dialyzing the obtained extracting solution, and freeze-drying to obtain ginkgo protein;
and step 3: preparing protein into aqueous solution, adding alkaline protease for enzymolysis, inactivating enzyme after enzymolysis, and centrifuging to obtain supernatant to obtain semen Ginkgo protease hydrolysate;
and 4, step 4: performing ultrafiltration treatment on the ginkgo protein hydrolysate, collecting ultrafiltration permeate and freeze-drying to obtain a ginkgo protein hydrolysate;
and 5: performing chromatography on the aqueous solution (80 mg/mL) of semen Ginkgo protein hydrolysate with dextran gel as chromatography medium, and collecting sample with retention time of 87.36-102.23 min;
step 6: subjecting the sample obtained in the step 5 to DEAE cellulose column chromatography desalination, freeze-drying, dissolving in trifluoroacetic acid aqueous solution with volume fraction of 0.1%, and adopting C18 reversed phase chromatographic column, wherein the mobile phase a is formic acid aqueous solution with mass fraction of 0.1%, the mobile phase b is acetonitrile aqueous solution containing formic acid with mass fraction of 0.1%, and the volume fraction of acetonitrile is 84%; after the chromatographic column is balanced by the solution a, a sample is loaded by an automatic sample injector; collecting eluate with peak time of 25.13 min to obtain semen Ginkgo protein peptide solution with ACE inhibitory activity. Mixing 0.1 mL formic acid and 99.9 mL distilled water, wherein the solution a is 'mobile phase a' -0.1% formic acid aqueous solution; mobile phase b-0.1% formic acid in acetonitrile water, with a volume fraction of acetonitrile of 84%. Acetonitrile and water are mixed according to the volume ratio of 84.
The preferred embodiment is: step 1, soaking the ginkgo nut powder in ethyl acetate for degreasing, performing suction filtration to remove a solvent after degreasing is finished, and drying to obtain degreased ginkgo nut powder; the particle size of the ginkgo nut powder is less than or equal to 40 meshes.
The preferred embodiment is: in the step 2, the defatted ginkgo nut powder is dissolved in distilled water, the pH value is adjusted to 10.0, the mixture is stirred overnight, the supernatant is taken after centrifugation, the pH value of the supernatant is adjusted to 4.62, the centrifugation is carried out again, the supernatant is discarded, the precipitate is taken, the precipitate is dialyzed in the distilled water and is freeze-dried, and the defatted ginkgo protein is obtained.
The preferred embodiment is: in step 3, the defatted ginkgo protein is prepared into a protein aqueous solution, the pH value is adjusted to 10, then alkaline protease is added, and the temperature is kept at 48 ℃ for 3.5 h.
And step 4, performing ultrafiltration treatment on the ginkgo biloba proteolytic liquid by adopting an ultrafiltration membrane with the molecular weight cutoff of 3000 Da.
The preferred embodiment is: in step 5, G-15 sephadex column is used for further purifying the ginkgo protein hydrolysate, ultrapure water is used as eluent, the flow rate is 1mL/min, and the sample concentration is 80 mg/mL.
Example 4: ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity and preparation method thereof
(1) Pretreatment: removing shell and peel of fresh semen Ginkgo, cutting, oven drying at 45 deg.C, pulverizing, and sieving with 50 mesh sieve;
(2) Degreasing: soaking in ethyl acetate, stirring once every 10min, soaking for 2 hr, vacuum filtering to remove solvent, and drying to obtain defatted semen Ginkgo powder;
(3) Extracting ginkgo protein: dissolving defatted semen Ginkgo powder in distilled water, adjusting pH to 10.0, stirring overnight, centrifuging, collecting supernatant, adjusting pH to 4.62, centrifuging again, removing supernatant, collecting precipitate, dialyzing the precipitate, and lyophilizing to obtain semen Ginkgo protein;
(4) Enzymolysis: preparing the ginkgo protein into a 3% protein solution, adjusting the pH to 10.0, adding alkaline protease, adjusting the enzyme activity to 4000U, and keeping the temperature at 50 ℃ for 4 hours;
(5) And (3) ultrafiltration: performing ultrafiltration with ultrafiltration membrane with molecular weight cutoff of 3000 Da, collecting ultrafiltration permeate, and lyophilizing;
(6) Gel chromatography: further purifying the ultrafiltered substance with G-15 sephadex column, eluting with ultrapure water at flow rate of 1mL/min and sample concentration of 80 mg/mL, and collecting the chromatographic solution with retention time of 87.36-102.23 min;
(7) Liquid chromatography separation of functional peptides: the sample was desalted and lyophilized and then redissolved in 0.1% trifluoroacetic acid solution. A C18 reverse phase chromatography column was used, mobile phase a being 0.1% aqueous formic acid and mobile phase b being 0.1% aqueous acetonitrile containing formic acid (84% acetonitrile). After the column was equilibrated with 95% solution a, a sample was applied by an autosampler, and the detection wavelength was 228nm and the flow rate was 1 mL/min. Collecting eluate with peak time of 25.13 min to obtain semen Ginkgo protein peptide solution with ACE inhibitory activity;
(8) The mass spectrometry analysis result shows that the amino acid sequence of the ginkgo protein peptide is as follows: arginine-alanine-aspartic acid-phenylalanine-lysine (RADFK).
While the invention has been described in connection with what is presently considered to be the most practical and preferred embodiment, it is to be understood that the invention is not to be limited to the disclosed embodiment, but on the contrary, is intended to cover various modifications and equivalent arrangements included within the spirit and scope of the appended claims.
Claims (1)
1. A ginkgo nut protein peptide with angiotensin converting enzyme inhibitory activity is characterized in that: consists of the following amino acid residues: arginine-alanine-aspartic acid-phenylalanine-lysine.
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