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

Peptide calcium chelate and preparation method and application thereof

A chelate and chelation reaction technology, which is applied in the preparation methods of peptides, chemical instruments and methods, peptides, etc., can solve the problems of low development and utilization of bonito flakes protein.

Inactive Publication Date: 2020-07-28
GUANGDONG OCEAN UNIVERSITY
View PDF13 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Aiming at the development trend of the above-mentioned calcium supplement products and the practical problem of low development and utilization of bonito protein, the present invention provides a calcium peptide chelate and its preparation method and application to explore the high value of bonito protein source Chemical utilization and development of new peptide-calcium products

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
  • Peptide calcium chelate and preparation method and application thereof
  • Peptide calcium chelate and preparation method and application thereof
  • Peptide calcium chelate and preparation method and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0055] Example 1, Preparation and Characteristic Analysis of Bonito Protein Peptide Powder

[0056] 1. The preparation method of bonito protein peptide powder

[0057] The present embodiment provides a preferred method for preparing Auxis thazard, and the specific operations are as follows. The meat of the flat rudder skipjack is taken, minced, homogenized, and then enzymatically hydrolyzed by papain and flavor protease. The enzymatic hydrolysis conditions are: temperature 50°C, papain addition amount 500U / g, flavor protease addition amount 200U / g, pH 6.5 , Enzymolysis time 3h. The enzymolyzed product was centrifuged for 15min (3500g, 4°C) after the enzyme was inactivated in a water bath, and the obtained supernatant was deoiled by a tubular centrifuge, decolorized by perlite (addition amount was 3%), and then passed through a ceramic membrane (pore size 0.2μm) and ultra Filtrate with a filter membrane (5000U), and finally obtain the bonito oligopeptide powder through concen...

Embodiment 2

[0070] Example 2, preparation and structural characterization of bonito protein peptide chelated calcium

[0071] The preparation yield of protein peptide chelated calcium is closely related to the amino acid composition and molecular weight of the peptide source, as well as the type of calcium source and preparation conditions. The bonito protein peptide chelated calcium prepared in this embodiment selects the bonito protein peptide described in Example 1 as a protein source, and there are many types of calcium sources, among which calcium chloride and hydroxide are the most widely used. Calcium, calcium chloride is selected as the calcium source of the present embodiment. It should be noted that the type of calcium source is not particularly limited in this embodiment. Based on the technical ideas of the present invention, those skilled in the art can prepare the calcium source described in this embodiment by selecting one or more specific calcium sources. Skipjack protein ...

Embodiment 3

[0089] Embodiment three, separation and purification of calcium binding peptide

[0090] In this example, Sephadex G-15 gel chromatography and RP-HPLC were used to separate and purify protein peptides with high calcium binding activity from bonito protein peptides, and to study its binding characteristics with calcium ions by infrared spectroscopy and mass spectrometry .

[0091] Skipjack oligopeptides were separated by Sephadex G-15 gel ( Figure 12 ), to obtain 5 different fractions, respectively denoted as F1, F2, F3, F4, F5, the calcium binding activity of which is as follows Figure 13 shown. As the molecular weight decreases, the calcium-binding ability of the peptide gradually increases. The first four components have strong calcium-binding activity, and component F4 shows the strongest calcium-binding ability (73.6±4.6mg / g). The calcium-binding activity of F5 was significantly lower than that of the other four components. It was speculated that the main components o...

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
pore sizeaaaaaaaaaa
Login to View More

Abstract

The invention discloses a preparation method of a peptide calcium chelate. The preparation method comprises the step of performing a chelation reaction between a protein source and a calcium source inwater, wherein the protein source is Auxis thazard protein peptide, and the parameter setting of the chelation reaction is as follows: a mass ratio of the protein source to the calcium source is 1:3-3:1, a chelation temperature is 30-70 DEG C, a chelation time is 10-50 min, and pH is 7-11. The Auxis thazard protein peptide is prepared by enzymatically hydrolyzing Auxis thazard with papain and flavor protease, a product of enzymatic hydrolysis is centrifuged after enzyme-inactivation, a supernatant is de-oiled, decolorized, filtered through a ceramic membrane and an ultrafiltration membrane, and then concentrated and dried to obtain the Auxis thazard protein peptide with a molecular weight no more than 5000 U, and the Auxis thazard protein peptide contains calcium-binding active peptides Glu-Pro-Ala-His and Tyr-Asp-Thr. A binding manner between Glu-Pro-Ala-His and calcium ion is as follows: the carboxylic acid group of Glu binds to calcium ion in a bidentate mode, and the carboxylic acid group and amino group of His chelate with calcium ion in an alpha mode to form a five-membered ring structure. The peptide calcium chelate of the invention has the function of promoting the growthand development of rat bones, and a new idea is provided for the high-value utilization of Auxis thazard and the development of novel peptide-calcium products.

Description

technical field [0001] The invention belongs to the technical field of biotechnology and aquatic product processing, and relates to a deep processing technology of bonito, in particular to a calcium peptide chelate and its preparation method and application. Background technique [0002] Calcium is an indispensable constant mineral for the human body. It plays a very important role in various stages of human infancy, growth and old age, and has various physiological functions. Calcium deficiency is very common among people in underdeveloped areas, and infants, young children, pregnant women and the elderly are the main groups prone to calcium deficiency. Calcium deficiency presents different health problems at different growth stages. When the supply of calcium continues to be insufficient, the metabolism of the human body will be disturbed, which will affect the normal life activities of the human body, and even lead to clinical symptoms in severe cases. Long-term calcium...

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): C07K14/46C07K5/113C07K5/087C07K1/107C07K1/14C07K1/34C12P21/06A61K38/17A61K38/06A61K38/07A61K33/14A61P19/08
CPCC07K14/461C07K5/0812C07K5/1021C12P21/06A61K33/14A61P19/08A61K38/00A61K2300/00
Inventor 吉宏武陈铭苏伟明刘书成郝记明
Owner GUANGDONG OCEAN UNIVERSITY
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