Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Application of mussel protein antihypertensive peptide

A technology for antihypertensive peptides and uses, which is applied in the application field of mussel protein antihypertensive peptides, can solve problems such as preparation of antihypertensive peptides, and achieve the effects of improving utilization rate, significant ACE inhibitory activity, and high activity

Inactive Publication Date: 2015-07-08
ZHEJIANG OCEAN UNIV
View PDF0 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the researchers found that there is no research on the preparation of antihypertensive peptides from mussel hydrolyzate by using this technology

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Application of mussel protein antihypertensive peptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0025] A rapid preparation method of mussel protein antihypertensive peptide, the preparation process is as follows: mussel meat "tissue crushing" enzymatic hydrolysis "ultrafiltration" agarose magnetic microspheres immobilized ACE adsorption "RP-HPLC purification" antihypertensive peptide.

[0026] ) Preparation and activation of agarose magnetic microspheres: According to the weight volume ratio of 1.5g: 30 mL, add agarose to water, boil together until the agarose is completely dissolved, add 1 ml Fe 3 o 4 Ferrofluid, fully mixed on a vortex mixer; drop the mixed liquid into the organic phase at 80°C (Span-80: liquid paraffin=1g:25mL) under stirring, and react at 80°C for 20 min; the organic phase Cool to 40°C and mechanically stir at 250 rpm for 15 min to shape the microspheres, and separate them in a magnetic field. The prepared microspheres were washed three times with petroleum ether and deionized water to remove the residual organic phase to obtain agarose magnetic M...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
molecular weightaaaaaaaaaa
Login to View More

Abstract

The invention discloses an application of a mussel protein antihypertensive peptide. The antihypertensive peptide has antihypertensive activity and is characterized in that an amino acid sequence of the antihypertensive peptide is Val-Ser-Trp-Pro-Cys-Arg-Trp(VSWPCRW); the molecular weight determined by ESI-MS (electrospray ionization mass spectrometry) is 935.07Da. The active peptide Val-Ser-Trp-Pro-Cys-Arg-Trp is obtained by shelling mussels, taking the meat of the mussels, carrying out enzymolysis on the meat, carrying out ultrafiltration on the enzymatic hydrolysate, adsorbing the enzymatic hydrolysate with an agarose magnetic microsphere immobilized ACE (angiotensin converting enzyme) and carrying out purification by RP-HPLC (reversed-phase high-performance liquid chromatography). The active peptide prepared by the invention has obvious ACE inhibitory activity and can be used in hypertension treatment related drugs.

Description

technical field [0001] The invention belongs to the application of bioengineering technology, and in particular relates to the application of mussel protein antihypertensive peptide. Background technique [0002] Angiotensin-converting enzyme (ACE), also known as peptidyl-carboxypeptidase or kininase II, has a molecular weight of 150,000 Da and belongs to the membrane-bound enzyme of vascular endothelial cells. ACE can hydrolyze the decapeptide angiotensin I into the octapeptide angiotensin II, which promotes further constriction of blood vessels, leading to an increase in blood pressure. At the same time, ACE can also promote the secretion of aldosterone by acting on the adrenal cortex. Therefore, ACE is an important component of renin-angiotensin-aldosterone (RAS). In addition, ACE can also catalyze the hydrolysis of bradykinin, which has antihypertensive effect, and make it inactive. Therefore, the purpose of lowering or controlling blood pressure can be achieved by fi...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A23L1/305A61K38/08A61P9/12
Inventor 王斌迟长凤赵玉勤孙坤来
Owner ZHEJIANG OCEAN UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com