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

ACE inhibitory peptide and preparation method and application

A technology for inhibiting peptides and inhibiting activity, which is applied in the field of ACE inhibitory peptides and preparations, and can solve problems such as taste disorders

Inactive Publication Date: 2019-10-25
JIMEI UNIV
View PDF4 Cites 10 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Although these drugs are effective in controlling blood pressure, they can have many side effects such as: cough, taste disturbance, rash, kidney failure, etc.

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 and preparation method and application
  • ACE inhibitory peptide and preparation method and application
  • ACE inhibitory peptide and preparation method and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0025] Embodiment 1: Preparation of natural ACE inhibitory peptide

[0026] 1. Extraction of sea cucumber protein: Take 200g sea cucumber and dissolve it in 2000mL pre-cooled 0.1mol / L NaOH solution. After the tissue is homogenized, centrifuge (12000g, 4°C, 20min), and the obtained precipitate continues to be dissolved in NaOH buffer. After stirring overnight, centrifuge (12000g, 4°C, 20min) to collect the precipitate. After repeated 4 times, the precipitate collected after the last centrifugation was repeatedly rinsed with distilled water until the pH of the eluate was neutral. After washing with water, the protein was dissolved in 10 times the volume of 0.5 mol / L acetic acid, stirred overnight and then centrifuged (12000g, 4°C, 20min), the obtained supernatant was the sea cucumber protein solution.

[0027] 2. Enzymatic hydrolysis of sea cucumber protein: Preheat the sea cucumber protein solution in a 37°C water bath for 5 minutes, add 0.5% by weight of pepsin and place it a...

Embodiment 2

[0030] Example 2: Preparation of artificially synthesized ACE inhibitory peptides

[0031] 1. Weigh 0.3mmol of Fmoc-Pro-Wang Resin (for P1900520) or Fmoc-Arg(Pbf)-Wang Resin (for P1900521) with a substitution degree of 0.35mmol / g, place it in a medium-sized reaction column, soak in DMF for 120min ;

[0032] 2. Drain the DMF, add 20% Pip / DMF which is 3 times the volume of the resin, and blow nitrogen for 30 minutes to remove Fmoc, wash with DMF 5 times, and the ninhydrin detection shows dark blue;

[0033] 3. Put in the raw materials in proportion (AA:HBTU:NMM=3:2.85:6), add an appropriate amount of DMF, and blow nitrogen to react until the ninhydrin detection is transparent;

[0034] 4. Repeat steps 2-3 to complete the sequence synthesis;

[0035] 5. Drain the resin in the reactor, transfer it to a cutting tube, add 40ml of F solution, and control the temperature on a shaking table for 1.5h;

[0036] 6. Suction filtration, collect the cutting filtrate into a centrifuge tube...

Embodiment 3

[0039] Example 3: Detection of natural ACE inhibitory activity

[0040]The permeate obtained after the enzymolysis solution is separated by ultrafiltration with a 3kDa ultrafiltration membrane is lyophilized and concentrated to obtain a lyophilized powder. After diluting into different concentrations with water, the ACE inhibitory activity was detected, and the results were as follows: figure 1 shown. It can be seen from the figure that the ACE inhibitory activity IC of the permeate 50 It was 81.37 μg / mL. The naturally-prepared ACE inhibitory peptide is obtained by enzymatic hydrolysis with gastrointestinal protease, which can prevent the active peptide from being degraded and inactivated by the digestive juice of the gastrointestinal tract after being ingested by the human body.

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 inhibitory peptide and a preparation method and application. The amino acid sequence of the ACE inhibitory peptide is GPPGP and is derived from natural animal proteins,the IC50 of the ACE inhibitory peptide is 190.43 micromole per liter, the molecular weight is small, and the ACE inhibitory peptide has the advantages of being stable, safe, easy to absorb by the human body and the like and can be used for industrial production. The ACE inhibitory peptide with the amino acid sequence of GPPGP can be used for preparing hypertension treatment / prevention medicine orserving as a functional food additive for long-term treatment and health care of hypertension patients.

Description

technical field [0001] The invention relates to the technical field of bioactive peptides, in particular to ACE inhibitory peptides, preparation methods and uses. Background technique [0002] With the rapid development of my country's economy and the change of people's living habits, chronic non-communicable diseases have become public health problems affecting people's health. Hypertension is a non-communicable chronic disease and is a very important risk factor for patients with stroke, heart failure and coronary artery disease. In 2015, 874 million adults were estimated to have a systolic blood pressure (SBP) of 140 mm Hg or higher, based on data from 195 countries and territories. It is estimated that by 2025, approximately 1.56 billion people worldwide will suffer from hypertension. Hypertension is now a major health problem worldwide. [0003] Angiotensin I-converting enzyme (ACE) is a carboxypeptidase (EC 3.4.15.1) widely present in mammalian tissues, in the renin...

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): C07K7/06C12P21/06C07K1/36C07K1/34C07K1/30C07K1/16A23L33/18A61K38/08A61P9/12
CPCA23L33/18A23V2002/00A61K38/00A61P9/12C07K7/06C12P21/06A23V2200/326A23V2250/55
Inventor 曹敏杰肖盼盼章骞翁凌刘光明
Owner JIMEI 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