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

ACE inhibitory peptide P1 as well as application and preparation method thereof

A technology for inhibiting peptides and polypeptide sequences, which is applied in the field of ACE inhibitory peptide P1, can solve the problems of waste of fish skin resources, etc., and achieve the effects of good affinity, small toxic and side effects, and high specificity

Active Publication Date: 2020-08-07
FISHERIES RES INST OF FUJIAN
View PDF5 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] Pufferfish is a collective name for fish in the family Fuguidae of the bony fish class. With the opening and development of the pufferfish processing and utilization market, a large number of pufferfish processing and utilization by-products (such as fish skin, fish head, fish viscera, etc.) are used as Waste discarded or processed into animal feed will not only bring huge pressure to the environment, but also bring negative effects to society and a great waste of fish skin resources
At present, there is no relevant report on the extraction of ACE inhibitory peptides from puffer fish

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
  • ACE inhibitory peptide P1 as well as application and preparation method thereof
  • ACE inhibitory peptide P1 as well as application and preparation method thereof
  • ACE inhibitory peptide P1 as well as application and preparation method thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0037] In order to enable those skilled in the art to better understand the technical solution of the present invention, the present invention will be described in further detail below in conjunction with the accompanying drawings and specific embodiments.

[0038] The invention discloses an ACE inhibitory peptide P1, the amino acid sequence of which is: FNLRMQ.

[0039] The preparation method of ACE inhibitory peptide P1 comprises the following steps:

[0040] S1. Take fugu fish skin, add protease for enzymolysis, the enzymolysis temperature is controlled at 50°C-60°C, the enzyme-to-bottom ratio is 2%-4%, the pH is 11-12, and the enzymolysis time is 5h-7h. Preferably, the enzymolysis temperature is 55° C., the enzyme-to-substrate ratio is 2%, the pH is 12, and the enzymolysis time is 6 hours.

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

No PUM Login to View More

Abstract

The invention discloses an ACE (Angiotensin Converting Enzyme) inhibitory peptide P1 with the amino acid sequence is FNLRMQ, application of the ACE inhibitory peptide P1 in auxiliary antihypertensivedrugs or auxiliary antihypertensive functional foods, and a preparation method of the ACE inhibitory peptide P1. The ACE inhibitory peptide P1 obtained by the invention is extracted from puffer fish skin, has strong binding capacity with ACE enzyme and high activity, can be effectively used in antihypertensive drugs or functional foods to assist in reducing blood pressure, and has the advantages of high specificity and small toxic and side effects.

Description

technical field [0001] The present invention relates to the field of biotechnology, in particular to an ACE inhibitory peptide P1. The invention also relates to the application and preparation method of the ACE inhibitory peptide. Background technique [0002] The regulation of blood pressure in the human body is mainly controlled by the angiotensin system (renin-angiotensin system, RAS) and kinin system (kallikrein kinin system, KKS), and angiotensin converting enzyme (Angiotensinconverting enzyme, ACE) in these two systems plays a key role. ACE is a carboxyl dipeptidase widely distributed in mammalian tissues, mainly in vascular epithelial cells in the form of membrane-bound extracellular enzymes. In the RAS system, ACE can convert angiotensin Ⅰ (Angiotensin Ⅰ, Ang Ⅰ), which has no physiological activity, into angiotensin Ⅱ (Angiotensin Ⅱ, Ang Ⅱ), which has pressor activity. In the KKS system, ACE can degrade bradykinin into inactive fragments, resulting in vasoconstric...

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): C07K7/06C12P21/06C07K1/34C07K1/16C07K1/04C07K1/36A61K38/08A61P9/12A23L33/18
CPCC07K7/06C12P21/06A61P9/12A23L33/18A61K38/00A23V2002/00A23V2200/326A23V2250/55
Inventor 刘智禹蔡水淋苏永昌乔琨陈贝许旻
Owner FISHERIES RES INST OF FUJIAN
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