CN115197309A - Amygdalus communis protein-derived ACE inhibitory peptide, and preparation method and application thereof - Google Patents
Amygdalus communis protein-derived ACE inhibitory peptide, and preparation method and application thereof Download PDFInfo
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- CN115197309A CN115197309A CN202210830278.6A CN202210830278A CN115197309A CN 115197309 A CN115197309 A CN 115197309A CN 202210830278 A CN202210830278 A CN 202210830278A CN 115197309 A CN115197309 A CN 115197309A
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- badam
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
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- 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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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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Abstract
The invention discloses an ACE inhibitory peptide derived from badam protein, and a preparation method and application thereof. The invention prepares the amygdalus amurensis ACE inhibitory peptide by performing ultrafiltration, gel chromatography and amino acid sequence identification on an enzymolysis product of the amygdalus amurensis protein by taking ACE enzyme inhibition rate as an index, wherein the ACE inhibitory peptide has higher ACE inhibitory activity and NO cytotoxicity, and can increase the content of endogenous relaxing factor NO in HUVEC cells and reduce the content of endogenous shrinking factor ET-1, so that the ACE inhibitory peptide can be used as a potential natural antihypertensive drug or functional food, and simultaneously opens up a new idea for development of the amygdalus amurensis polypeptide and high-valued development of processing byproducts.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to an ACE inhibitory peptide derived from badam protein, and a preparation method and application thereof.
Background
Hypertension, which is one of the most important public health problems in the world and threatens the life health and safety of more and more people, is the most important risk factor of cardiovascular diseases and is also an important cause of death of patients with cardiovascular diseases. Hypertension can cause headache, dizziness, vomit, palpitation, short breath, chest distress and hypodynamia, and also can cause risks of life and health hazards such as stroke, myocardial infarction, chronic nephropathy, obesity, atherosclerosis and the like, the occurrence of hypertension is closely related to the fibrosis and remodeling process of various cardiovascular diseases, and the hypertension can also cause damage to the physiological functions of various hypertension target organs such as heart, brain, kidney and the like.
The regulation mechanism of blood pressure is complex and includes ACE, renin, endothelin I, endothelin converting enzyme,Calcium channels and the like are all associated with the regulation of blood pressure. The Kallikrein-Kinin System (KKS) and the Renin-Angiotensin System (RAS) are currently considered to be the most major blood pressure regulating systems. In RAS system, angiotensinogen N-terminal released by liver is explained by renin water to release angiotensin-1 (Ang-I), angiotensin I is further hydrolyzed into angiotensin-II (Ang-II) with vasoconstriction function under the action of angiotensin converting enzyme-I (ACE), thereby increasing body blood pressure, simultaneously, angiotensin-II can stimulate adrenal cortex zona cell synthesis and promote cells to release aldosterone, and the released aldosterone promotes convoluted tubule and collecting duct K + -Na + Exchange and reabsorption of water cause an increase in sodium concentration and an increase in blood volume, resulting in an increase in blood pressure in the body. At present, the commonly used angiotensin converting enzyme inhibitors are mainly pril drugs, are suitable for patients with obesity and diabetes hypertension, but may have side effects of severe cough and angioedema, and may have aldosterone escape after long-term administration, so that the drug effect is reduced. Therefore, with the increasing demand for high-nutrition and functional foods, people are more concerned about natural animals and plants, and the enzymolysis of ACE inhibitory peptide from food-derived protein becomes a focus of attention.
Badam is one of the characteristic dried fruits in China, and the planting history of badam in China is long. The badam has high nutritional value, is rich in a large amount of amino acids, unsaturated fatty acids, polyphenols, trace elements and the like, and is found to be beneficial to preventing hypertension and heart diseases by related researches. The resource of the badam in China is relatively rich, and the development of the processed products of the badam is mainly focused on the aspect of milk protein beverages, so that the research and development of the production and preparation of the ACE inhibitory peptides of the badam can improve the effective utilization of the badam protein, increase the added value of the badam and realize the comprehensive utilization of the resource.
At present, polypeptides with ACE inhibitory activity are separated from animal and plant proteins such as medlar, corn, oyster, broccoli and the like, but researches on the ACE inhibitory activity of badam polypeptides are rarely reported.
Disclosure of Invention
The present invention is directed to solving at least one of the problems of the prior art described above. Therefore, the invention provides an ACE inhibitory peptide derived from badam protein, and a preparation method and application thereof.
According to one aspect of the present invention, there is provided an ACE inhibiting peptide derived from badam protein, the ACE inhibiting peptide comprising a peptide having the amino acid sequence LR, LYH, LY, TF, VF, LF, LW, FF.
The invention also provides a preparation method of the ACE inhibitory peptide, which comprises the following steps:
s1: taking badam defatted powder as a raw material, and extracting badam protein by an alkali-dissolving and acid-precipitating method;
s2: adding water into the badam protein, stirring, adding a protease enzymolysis combination for enzymolysis reaction, inactivating enzyme, centrifuging, removing precipitate, and taking supernatant to obtain an enzymolysis product;
s3: performing ultrafiltration on the enzymolysis product by using a 3kDa ultrafiltration centrifugal tube to obtain a permeate;
s4: and (3) carrying out gel chromatography on the permeate, eluting to obtain a plurality of components, selecting a target component by taking the ACE enzyme inhibition rate as an index, and freeze-drying to obtain the ACE inhibitory peptide.
In some embodiments of the present invention, in step S2, the protease enzymatic combination includes alkaline protease and complex protease, and the complex protease is produced by deep liquid fermentation of bacillus subtilis, and is formed by concentration, extraction, refining and compounding, and is a bacillus protease complex. The activity of the compound protease is more than or equal to 120units/mg.
In some embodiments of the present invention, in step S2, the mass ratio of the alkaline protease to the complex protease is 1: (0.5-2.0), and the addition amount of the protease enzymolysis combination is 3000-5000U/g badam protein.
In some embodiments of the present invention, in step S2, before adding the protease enzymatic combination, the badam protein and water are mixed in a mass ratio of 1: (9-12) mixing, and keeping for 8-12min in a water bath at the temperature of 75-85 ℃.
In some embodiments of the present invention, in step S2, the enzymatic hydrolysis reaction is performed at a pH of 7.0 to 8.0 and a temperature of 40 to 50 ℃.
In some embodiments of the present invention, in step S2, the time of the enzymatic hydrolysis reaction is 2-4h.
In some embodiments of the present invention, in step S2, the temperature of the enzyme deactivation is 95-105 ℃, and the time of the enzyme deactivation is 10-12min.
In some embodiments of the invention, the temperature of the ultrafiltration is 0-5 ℃ and the centrifugal force of the ultrafiltration is 5000-8000Xg in step S3. Further, the ultrafiltration time is 20-40min.
In some embodiments of the invention, in step S4, the gel chromatography is performed using a Sephadex G-25 Sephadex column, and the amount of the permeate separated by the Sephadex G-25 Sephadex column is 2 to 3% of the volume of the Sephadex G-25 Sephadex column.
In some embodiments of the invention, in step S4, the elution is performed with water, a sample loading of 40-60mg/mL, and a flow rate of 0.4-0.6mL/min.
In some embodiments of the invention, in step S4, the target component is determined for its amino acid sequence using high performance liquid mass spectrometry.
The invention also provides application of the ACE inhibitory peptide in preparation of a medicine or a health product for promoting NO release in HUVEC cells and inhibiting ET-1 generation in HUVEC cells.
The invention also provides application of the ACE inhibitory peptide in preparation of health-care food or medicine for regulating blood pressure.
According to a preferred embodiment of the present invention, at least the following advantages are provided:
the invention prepares the amygdalus amurensis ACE inhibitory peptide by performing ultrafiltration, gel chromatography and amino acid sequence identification on an enzymolysis product of the amygdalus amurensis protein by taking ACE enzyme inhibition rate as an index, wherein the ACE inhibitory peptide has higher ACE inhibitory activity, has 90 percent of ACE inhibition rate when the concentration is 1mg/mL, has NO cytotoxicity, can increase the content of endogenous relaxing factor NO in HUVEC cells and reduce the content of endogenous contraction factor ET-1, and therefore, the ACE inhibitory peptide can be used as a potential natural antihypertensive drug or functional food, and simultaneously opens up a new idea for development of the amygdalus amurensis polypeptide and high-valued development of a processing byproduct.
Drawings
The invention is further described with reference to the following figures and examples, in which:
FIG. 1 is a graph of the ACE inhibition rate of a badam protein double-enzyme combined enzymolysis product;
FIG. 2 is a graph of the ACE inhibition ratio of the ultrafiltration component of a badam proteolysis product;
FIG. 3 is a Sephadex G-25 gel filtration chromatogram of an ultrafiltration fraction with a molecular weight of <3 kDa;
FIG. 4 is a graph of ACE inhibition of 3 fractions prepared in example 1;
FIG. 5 is a mass spectrum of component III obtained in example 1;
FIG. 6 shows the results of the effect of gel chromatography elution fraction III on the viability of HUVEC cells (note:' indicates a significant difference from the Control group, where p is < 0.05;. Indicates p < 0.01;. Indicates p < 0.001).
FIG. 7 shows the effect of gel chromatography elution fraction III on the amount of NO released from HUVEC cells (note: 'indicates a significant difference from the Control group, wherein' indicates that p <0.05; indicates p <0.01, '#' indicates a significant difference from the positive Control group, wherein # indicates p <0.05 and # # indicates p < 0.01).
FIG. 8 shows the effect of gel chromatography elution fraction III on the release of ET-1 from HUVEC cells (note: ' indicates a significant difference from the Control group, where p <0.05; and ' # ' indicates a significant difference from the positive Control group, where # indicates p < 0.05).
Detailed Description
The concept and technical effects of the present invention will be clearly and completely described below in conjunction with the embodiments to fully understand the objects, features and effects of the present invention. It is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all embodiments, and those skilled in the art can obtain other embodiments without inventive effort based on the embodiments of the present invention, and all embodiments are within the protection scope of the present invention.
Example 1
This example prepares an ACE inhibitory peptide derived from badam protein by the following specific process:
(1) Preparing raw materials: mixing badam degreased powder in a ratio of 1:10 adding water and stirring, adjusting pH to 10 with NaOH, heating to 45 ℃, keeping the temperature for 4h, centrifuging, taking supernatant, adding HCl to adjust pH to 4.5, centrifuging, adding a small amount of water and stirring, adjusting pH to 7 with NaOH, freeze-drying into powder, and storing at-20 ℃ to obtain the badam protein.
(2) Preparation of almond protease: taking badam protein as a raw material, and mixing the raw material with the feed liquid according to the mass ratio of 1:10, adding distilled water, keeping the mixture in a water bath kettle at the temperature of 80 ℃ for 10 minutes, and then adding distilled water into the mixture according to the mass ratio of 1:1, adding alkaline protease and compound protease (Shanghai-sourced leaf biotechnology, inc., S10155, compound protease, batch number: J04GS150440, activity is more than or equal to 120 units/mg), keeping the total enzyme amount of 4000U/g badam protein for enzymolysis for 4h, keeping the temperature at 100 ℃ for 10 minutes for enzyme inactivation, cooling to normal temperature, then using a refrigerated centrifuge for 4 ℃, centrifuging at 10000rpm for 10 minutes, taking supernatant enzymatic hydrolysate, discarding precipitated protein residues, freezing the enzymatic hydrolysate in a refrigerator at minus 80 ℃, and then freeze-drying to obtain enzymatic hydrolysate powder.
(3) Dissolving the enzymolysis solution powder with water, and performing refrigerated centrifugation for 30 minutes at 4 ℃ under the centrifugal force of 6000Xg by using an ultrafiltration centrifugal tube with the molecular weight cutoff of 3kDa to obtain supernatant and permeate; the inhibition rates of the supernatant and the permeate were determined by taking the ACE inhibition rate as an index, and the results are shown in fig. 2, and the components of the badam polypeptide extract with the molecular weight of less than 3kDa had higher ACE inhibition activity.
(4) Separating and purifying the permeate by gel chromatography with Sephadex G-25 Sephadex column, wherein the elution conditions are as follows: eluting with distilled water at flow rate of 0.4mL/min and sample loading of 50mg/mL, collecting one tube every 6min, measuring absorbance at 230nm of the eluate, collecting desired peak according to absorbance value, collecting 3 fractions, and freeze drying 3 fractions as shown in FIG. 3.
The method for detecting the inhibitory activity of Angiotensin Converting Enzyme (ACE) comprises the following steps: mu.L of ACE solution and 10. Mu.L of badam enzymolysis solution are added into a centrifuge tube in sequence, and then the mixture is placed into an incubator at 37 ℃ for incubation for 6min, then 30. Mu.L of HHL is added, the mixture is incubated in the incubator at 37 ℃ for 30min, and 60. Mu.L of HCl (0.1M) is added to stop the reaction. Wherein the blank group was substituted with 10. Mu.L of borate buffer solution instead of the enzymatic hydrolysate. Three sets of parallel experiments were performed and peak areas were measured at 228nm by high performance liquid chromatography, mobile phase (acetonitrile: water =25, 0.05% tfa), wherein the blank set replaced the enzymatic hydrolysate with 10 μ L of borate buffer solution. ACE was prepared at 0.1U/mL and HHL at 10mmol/L, all solutions were borate buffered (0.1M, 0.3M NaCl, pH 8.3).
ACE inhibition ratio (%) = (A1-A0)/A1
Wherein A1 is the area of HA peak of enzymolysis liquid group, A0 is the area of HA peak of blank group.
The results are shown in fig. 1, 2 and 4, wherein fig. 1 shows the ACE inhibition rate of the enzymolysis product obtained by the enzymolysis of the alkaline protease, the trypsin, the neutral protease, the compound protease and the papain in a mass ratio of 1. As can be seen from FIG. 2, the ACE inhibitory rate was 79.03% + -2.52% at an ultrafiltration fraction concentration of less than 3kDa of 1 mg/mL. As can be seen from figure 4, when the concentration of the component III is 1mg/mL, the ACE inhibitory rate can reach 90.19% +/-1.61%, and the ACE inhibitory peptide can be obtained after the component III is frozen and dried.
(5) Structural identification of gel chromatography elution component III with highest ACE inhibitory activity
Precisely weighing 0.02-2 mg of sample in a 2-5 mL centrifuge tube, adding 1.5mL of ultrapure water, filtering with a 0.22 mu m filter membrane, and then loading on a computer for analysis. The polypeptide sequence analysis is carried out by using a model U3000 RSLC-QEAX ultra-high resolution liquid chromatograph-mass spectrometer, the mass spectrum works in a fullMS/DD-MS2 mode (positive ion acquisition), the primary resolution is set to 35000, the mass-to-charge ratio range is 100-1500 m/z, topN is set to 4, the bombardment energy is step energy (20-40-60), the secondary resolution is set to 35000, and the dynamic mass-to-charge ratio acquisition range is obtained.
The results are shown in FIG. 5, and fraction III is composed of LR, LYH, LY, TF, VF, LF, LW, FF.
Test examples
Culture of Human Umbilical Vein Endothelial Cells (HUVEC): cell recovery followed by 5% CO at 37% 2 Culturing under 95% humidity condition, and replacing endothelial cell culture medium once after 24 h. After the cell growth confluence reached 80% or more, discard the medium, 0.9% nacl wash twice, then add pancreatin-digested cells, add endothelial cell medium to stop digestion, centrifuge and discard supernatant, add medium resuspension, 1: passage 2 to culture flask. HUVEC cells in logarithmic growth phase were taken as experimental material.
1. HUVEC cytotoxicity assay (MTT method):
cells in the logarithmic growth phase were digested by the passage method to prepare a cell suspension of 1X 104 cells/well. Inoculating the cell suspension in a 96-well plate, 100. Mu.L/well, at 37 ℃,5% 2 Culturing in an incubator. After 24h, adding 100 mu L of serum-free DMEM cell culture solution into the control wells; mu.L of complete culture medium containing sample concentrations of 0.5,1.0,1.5,2.0,2.5, 3.0 and 3.5mg/mL is added into the sample wells respectively, and the samples are cultured for 24h, 48h and 72h respectively, and then the liquid is discarded. Washing with PBS twice, adding 100 μ L complete culture medium containing MTT, culturing for 4 hr, removing culture medium, adding 150 μ L DMSO solution, shaking at 37 deg.C in dark for 10min, and measuring OD570nm under enzyme labeling instrument.
Cell viability (%) = [ (experiment group-a blank)/(control group a-a blank) ] × 100%
The experimental group A is a group added with ACE inhibitory peptides with different concentrations, the control group A is a group without the ACE inhibitory peptides, and the blank group A is a blank hole of an ELISA plate.
The results are shown in FIG. 6. As can be seen, the polypeptide had no significant difference in HUVEC growth inhibition at concentrations ranging from 0.5 to 2.5mg/mL for 72h, and the cell activity at concentrations above 3.0mg/mL was decreased at 72h, compared to the blank group. Indicating that within a certain concentration range, the badam polypeptide component III has no significant toxic effect on HUVEC.
2. Determination of NO content:
HUVEC cells were seeded at 2X 105 cells/well in 6-well plates, 2 mL/well. Culturing for 24h in a special medium containing 10% FBS, discarding the culture solution, washing twice with PBS, adding 2mL of serum-free culture solution into a control well, adding 2mL of serum-free culture solution containing samples with the concentration of 0.5,1.0,1.5,2.0 and 2.5mg/mL into a sample well, adding 2mL of serum-free culture solution containing captopril with the concentration of 0.5mg/mL into a positive control well, culturing for 48h, and detecting by using an NO kit.
The results are shown in fig. 7, and the increase of NO content in HUVEC cells can be promoted by the badam polypeptide component III, thereby demonstrating that the badam polypeptide component III prepared in example 1 has good blood pressure lowering effect.
3. Determination of ET-1 content:
HUVEC cells were seeded at 2X 106 cells/well in 6-well plates, 2 mL/well. Culturing for 24h in a special medium containing 10% FBS, discarding the culture solution, washing twice with PBS, adding 2mL of serum-free culture solution into the control wells, adding 2mL of serum-free culture solution containing samples with concentration of 0.5,1.0,1.5,2.0,2.5mg/mL into the sample wells, adding 2mL of serum-free culture solution containing captopril with concentration of 0.5mg/mL into the positive control wells, and culturing for 48h in each group for 3 wells. The kit adopts a double-antibody one-step sandwich method enzyme-linked immunosorbent assay kit (ELISA).
As a result, as shown in FIG. 8, almond polypeptide fraction III can reduce the amount of ET-1 in HUVEC cells, indicating that Almond polypeptide fraction III prepared in example 1 has a good blood pressure lowering effect.
In conclusion, the elution component III with better amygdalus ACE inhibitory activity has a promotion effect on the NO release amount in HUVEC cells and can also inhibit the generation of ET-1, so that the amygdalus ACE inhibitory peptide can realize the effect of reducing blood pressure by influencing the functions of human umbilical vein endothelial cells in a cell environment, and has the prospect of further research.
The embodiments of the present invention have been described in detail with reference to the drawings, but the present invention is not limited to the embodiments, and various changes can be made within the knowledge of those skilled in the art without departing from the gist of the present invention. Furthermore, the embodiments of the present invention and features of the embodiments may be combined with each other without conflict.
Claims (10)
1. An ACE inhibiting peptide derived from a badam protein, wherein the ACE inhibiting peptide comprises a peptide having the amino acid sequence LR, LYH, LY, TF, VF, LF, LW, FF.
2. The process for the preparation of ACE inhibiting peptides according to claim 1, comprising the steps of:
s1: extracting badam protein by using badam defatted powder as a raw material through an alkali dissolution and acid precipitation method;
s2: adding water into the badam protein, stirring, adding a protease for enzymolysis, performing enzymolysis reaction, inactivating enzyme, centrifuging, removing precipitate, and taking supernatant to obtain an enzymolysis product;
s3: performing ultrafiltration on the enzymolysis product by using a 3kDa ultrafiltration centrifugal tube to obtain a permeate;
s4: and (3) carrying out gel chromatography on the permeate, eluting to obtain a plurality of components, selecting a target component by taking the ACE enzyme inhibition rate as an index, and freeze-drying to obtain the ACE inhibitory peptide.
3. The method according to claim 2, wherein in step S2, the protease enzymatic composition comprises alkaline protease and complex protease, and the complex protease is produced by deep liquid fermentation of bacillus subtilis, and is prepared by concentration, extraction, refining and compounding, and is a bacillus protease complex.
4. The method according to claim 3, wherein in step S2, the mass ratio of the alkaline protease to the complex protease is 1: (0.5-2.0); the addition amount of the protease enzymolysis combination is 3000-5000U/g badam protein.
5. The method of claim 2, wherein in step S3, the temperature of ultrafiltration is 0-5 ℃; the centrifugal force of the ultrafiltration is 5000-8000Xg.
6. The method according to claim 2, wherein the gel chromatography is performed using a Sephadex G-25 Sephadex column in step S4, and the amount of the permeate separated by the Sephadex G-25 Sephadex column is 2 to 3% by volume of the Sephadex G-25 Sephadex column.
7. The method according to claim 2, wherein in step S4, water is used for the elution, the amount of the sample is 40 to 60mg/mL, and the flow rate is 0.4 to 0.6mL/min.
8. The method according to claim 2, wherein in step S4, the target component is subjected to amino acid sequencing by high performance liquid mass spectrometry.
9. Use of the ACE inhibiting peptide of claim 1 in the manufacture of a medicament or health product for promoting NO release in HUVEC cells and inhibiting ET-1 production in HUVEC cells.
10. Use of the ACE inhibiting peptide of claim 1 in the manufacture of a health food or a medicament for regulating blood pressure.
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