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Porphyra haitanensis antihypertensive peptide, porphyra haitanensis antihypertensive peptide extract and application

A technology of antihypertensive peptides and extracts, applied in the field of bioactive peptides, to achieve good antihypertensive effect and good ACE inhibitory activity

Active Publication Date: 2018-11-20
INST OF OCEANOLOGY - CHINESE ACAD OF SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0008] At present, there have been a variety of peptides with angiotensin-converting enzyme (ACE) inhibitory effects screened from marine algae, such as Ulva, Chlorella, Water Enteromorpha, etc., but very few ACE-inhibitory peptides have been isolated from laver. to report

Method used

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  • Porphyra haitanensis antihypertensive peptide, porphyra haitanensis antihypertensive peptide extract and application
  • Porphyra haitanensis antihypertensive peptide, porphyra haitanensis antihypertensive peptide extract and application
  • Porphyra haitanensis antihypertensive peptide, porphyra haitanensis antihypertensive peptide extract and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] (1) Take 40g of seaweed powder, add 1200ml of water to soak at room temperature for 3 hours, add 800mg of trypsin, stir and control the temperature at 40°C during enzymolysis, adjust the pH of the solution to 7.8, after 3 hours of enzymolysis, inactivate the enzyme at 100°C for 10 minutes .

[0024] (2) Impurities were removed by filtration, the supernatant was precipitated with ethanol with a final volume concentration of 75%, the precipitate was removed by centrifugation, the supernatant was concentrated to 20 ml, and freeze-dried.

[0025] (3) The components obtained by alcohol precipitation were further separated and purified using Sephadex G-25, distilled water was used as the mobile phase, and the flow rate was controlled at 0.8ml / min. The components with a retention time of 35min-36min were collected and concentrated to freeze-dry.

[0026] (4) The above chromatographically purified components were identified using UPLC-ESI-Q-Exactive Focus-MS / MS. Mascot2.2 compa...

Embodiment 2

[0028] (1) Take 40g of laver powder, add 1600ml of water and soak at room temperature for 2h, adjust the pH to 8.0, and the temperature at 37°C, add 1200mg of trypsin to start the enzymolysis reaction, after 2h, boil water for 10min to terminate the reaction.

[0029] (2) Remove impurities by filtration, use ethanol with a final volume concentration of 80% to precipitate impurities, remove impurities by filtration, concentrate to 20 ml and lyophilize.

[0030] (3) The above components were separated and purified by Sephadex G-25 gel chromatography, the mobile phase was distilled water, the flow rate was 0.8ml / min, the components with a retention time of 35min-36min were collected, concentrated and freeze-dried.

[0031] (4) Use UPLC-ESI-Q-Exactive Focus-MS / MS to identify the collected components. Mascot2.2 compares the mass spectrum information with the Porphyra transcriptome (SRX1016678, downloaded to NCBI), and selects the top 20 and Polypeptides with polar or large group re...

Embodiment 3

[0033] The sequence of the polypeptide is identified above, the artificially synthesized polypeptide TGAPCR with a purity >98% is described below, and the physicochemical properties and antihypertensive activity in vivo of TGAPCR are evaluated below.

[0034] (1) Determination of ACE inhibitory activity of peptides in vitro by high performance liquid chromatography (HPLC)

[0035] The medicines and instruments used in this example can be obtained commercially unless otherwise specified.

[0036] The principle of high performance liquid chromatography (HPLC) assaying ACE inhibitory activity is: ACE can hydrolyze the substrate hippuryl-histidyl-leucine (Hip-His-Leu, HHL, Sigma Company of the United States) into hippuric acid, When an enzyme inhibitor is added, the amount of hippuric acid generated is correspondingly reduced, and the inhibition rate of the inhibitor on ACE can be determined by detecting the absorption peak area of ​​hippuric acid at an ultraviolet wavelength of 2...

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Abstract

The invention discloses angiotensin converting enzyme (ACE) inhibitory peptide which has specific sequence and is screened from porphyra haitanensis enzymolysis products. The sequence of the polypeptide is Thr-Gly-Ala-Pro-Cys-Arg (TGAPCR), and through mass spectrum identification, the molecular weight of the polypeptide is 603.69 Da. The polypeptide has the characteristics of stable structure, notoxicity, high water solubility and the like; and through in-vitro high-performance liquid chromatography (HPLC) identification, the polypeptide has low IC50. Significant effect of reducing the systolic pressure of spontaneously hypertensive rats in vivo is achieved; and the diastolic pressure can be reduced for a long time. The ACE inhibitory peptide with specific sequence can be applied to development of an ACE inhibitor and also can be applied to health-care products and medicine products related to hypertensive therapy.

Description

technical field [0001] The invention relates to the technical field of bioactive peptides, and relates to the screening and identification of laver trypsin hydrolyzed polypeptides and its application in angiotensin-converting enzyme (ACE) inhibitors, medicines related to hypertension treatment, health care products and the like. Background technique [0002] Bioactivity peptides, also known as functional peptides, are a class of polypeptides with certain physiological activities and functions. Their molecular weight is usually below 10KDa and contain 2-20 amino acids. It has a variety of biological functions, including anti-tumor, anti-bacterial, anti-viral, anti-fatigue, anti-aging, lowering blood pressure, lowering blood sugar and other biological activities. Compared with protein, its molecular weight is small, low antigenicity, and can be absorbed. Therefore, bioactive peptides can be widely used in the development of food, health products, cosmetics and drugs. [0003...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K7/06C07K1/36C07K1/30C07K1/16C12P21/06A61K38/08A61P9/12A23L33/18
CPCA23V2002/00A61K38/00A23L33/18A61P9/12C07K7/06C12P21/06A23V2200/326
Inventor 张全斌邓真真刘英娟王晶耿丽华岳洋
Owner INST OF OCEANOLOGY - CHINESE ACAD OF SCI
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