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

Method for preparing active peptide metal chelate by enzymatic hydrolysis of laver

A metal chelate and active peptide technology, applied in the field of laver enzymatic hydrolysis to prepare active peptide metal chelate, can solve problems such as low utilization rate, and achieve product safety, improved glycosidase inhibitory activity, and good gastrointestinal stability. Effect

Active Publication Date: 2020-11-06
JIANGNAN UNIV
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The utilization rate of iron, zinc and other metal elements in food by the human body is very low. Therefore, finding a safe and effective nutritional supplement product is of great significance to human health

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
  • Method for preparing active peptide metal chelate by enzymatic hydrolysis of laver
  • Method for preparing active peptide metal chelate by enzymatic hydrolysis of laver
  • Method for preparing active peptide metal chelate by enzymatic hydrolysis of laver

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0046] Example 1 Enzymolysis and preparation of laver α-glucosidase inhibitory active peptide

[0047] Take Porphyra zebra as raw material, dry, pulverize, sieve, take 40-mesh laver protein dry powder and add it to 20mmol / L, pH8.5 NaHCO 3 -NaH 2 CO 3 In the buffer solution, the mass ratio of the laver protein dry powder to the buffer solution is 1:33g / mL. Then add alkaline protease E / S=8×10 4 U / g, neutral protease 8×10 4 U / g dry substrate, aminopeptidase 28U / g, hydrolyze at 50°C for 6h. Alkaline protease was purchased from Pangbo Company, neutral protease was purchased from Su Kehan ​​Company, and its model was SUKAPro NE. Aminopeptidase was independently developed and prepared by the inventor. The preparation method is described in patent CN104293749A. The enzyme was inactivated in a boiling water bath, and the supernatant was obtained by centrifugation. After diluting the supernatant 1.6 times, pass the filter membranes of 10kDa ultrafiltration membrane and 1kDa nanofi...

Embodiment 2

[0049] Embodiment 2 ZnCl alone 2 Effect of Solution on Inhibitory Activity of α-Glucosidase

[0050] Prepare ZnCl with a concentration of 0.1-0.5mmol / L respectively 2 solution, to measure the influence of different concentrations of metal solutions on the inhibitory rate of α-glucosidase, such as figure 2 As shown, with ZnCl 2 With the increase of solution concentration, the inhibition rate of α-glucosidase gradually increased, indicating that ZnCl alone 2 The solution has inhibitory effect on α-glucosidase.

Embodiment 3

[0051] Example 3 Preparation of laver enzymatic hydrolysis product α-glucosidase inhibitory activity polypeptide zinc chelate

[0052] 0.18g laver enzymatic hydrolyzate α-glucosidase inhibitory activity polypeptide was dissolved in 30mL ZnCl concentration of 0.5mmol / L 2 solution, so that the concentration of the laver enzymatic hydrolysis product α-glucosidase inhibitory activity polypeptide in the solution is 6 mg / ml. Adjust the pH of the solution to 4.5, and then place it in a oscillating water-bath shaker at 37° C. for 1.5 h to obtain a zinc chelate of a laver enzymatic hydrolysis product α-glucosidase inhibitory active polypeptide. Its chelation degree was measured to be 25.6%. The product was made into a solution with a concentration of 1 mg / ml, and its α-glucosidase inhibition rate was measured according to the method in the above specification, and the result was 79.8%.

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
Chelation degreeaaaaaaaaaa
Login to View More

Abstract

The invention relates to a method for preparing active peptide metal chelate through nori enzymolysis. The method comprises the following steps: performing enzymolysis reaction on crushed nori and protease in a buffer solution, and performing centrifugation and taking supernatant liquid after enzymolysis; filtering the supernatant liquid, concentrating and drying filtrate to obtain solid polypeptide powder; dissolving the solid polypeptide powder in a metal salt aqueous solution and performing chelation reaction to obtain nori enzymolysis active peptide metal chelate. The invention also discloses application of the nori enzymolysis active peptide metal chelate to preparation of an alpha-glucosaccharase inhibitor. The invention discloses novel natural raw material enzymolysis active peptide. The novel natural raw material enzymolysis active peptide has the inhibition activity of target enzyme and can chelate trace metal elements, and the prepared active peptide metal chelate can be absorbed by a human body quickly, so that the effects of supplementing iron and zinc and treating diabetes are achieved.

Description

technical field [0001] The invention relates to the technical field of production of marine active substance biological products, in particular to a method for preparing active peptide metal chelates by enzymatic hydrolysis of laver. Background technique [0002] Diabetes mellitus is a hyperglycemic metabolic disease caused by multiple factors, and its pathogenesis is mainly insulin resistance, oxidative stress, impaired β-cell function, and cytokine inflammation. The current mechanism of action for treating diabetes is mainly to improve insulin secretion and resistance, and to maintain the stability of pancreatic β-cell content. In addition, the use of various enzyme inhibitors in the process of glycolysis is also a treatment for diabetes. Due to the controllable conditions and mild reaction conditions for the preparation of natural α-glucosidase inhibitors by enzymatic hydrolysis, the products have strong inhibitory activity and strong safety, so they have attracted wides...

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 Patents(China)
IPC IPC(8): C12P21/06C07K1/34
CPCC07K1/34C12P21/06
Inventor 田亚平胡春芹龙婧周楠迪杜琴
Owner JIANGNAN 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