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

Screening method of functional peptide

A functional peptide and screening method technology, applied in the biological field, can solve the problems of large consumption of reagents, high cost, and long time consumption of functional peptides, and achieve the effects of reducing reagent consumption and pollution, increasing yield, and scientific methods

Pending Publication Date: 2022-04-29
时代生物科技(深圳)有限公司 +1
View PDF8 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] The present invention provides a screening method for functional peptides, which solves the technical problems of long time-consuming screening of functional peptides, large consumption of reagents, and high cost in the prior art. The specific technical solution is as follows:

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
  • Screening method of functional peptide
  • Screening method of functional peptide
  • Screening method of functional peptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0045] A method for screening sea cucumber anti-fatigue peptides, comprising the following steps performed in sequence:

[0046] S1: call the regulatory network related to the anti-fatigue function; find out the first gene target set related to the anti-fatigue function according to the regulatory network. The specific operation is: obtain sports training and fatigue-related transcriptome data sets from the GEO database; use the enrichment analysis clusterProfiler data package to perform the first GO analysis on the transcriptome data sets, and find out the significant differences in expressions involved in endurance training The biological process of the study was used as the first set of gene targets related to fatigue resistance. When performing the first GO analysis, it specifically includes: according to the transcriptome data set, using p<0.05 as the screening condition, classify the differential genes whose expression is up-regulated or down-regulated into the first gen...

Embodiment 2

[0057] The preparation process of the peptide collection of anti-fatigue sea cucumber peptide is as follows:

[0058] Sea cucumber protein is hydrolyzed by protease, and hydrolyzed at 37-50° C. for 3-7 hours to obtain sea cucumber peptide hydrolyzate, wherein the mass ratio of protease to sea cucumber protein is 0.4-0.9:1. The protease is one or more of trypsin, neutral protease and alkaline protease.

[0059] Preferably, when the protease is composed of alkaline protease, trypsin and neutral protease, the mass ratio of the alkaline protease, trypsin and neutral protease is (0.5~1):(1~2): (1~2). The enzyme activity of the alkaline protease is 50,000-500,000 U / g, the enzyme activity of the trypsin is 100,000-1,000,000 U / g, and the enzyme activity of the neutral protease is 100,000-650,000 U / g.

[0060] Next, the sea cucumber peptide hydrolyzate is ultrafiltered with a 2000D ultrafiltration membrane to obtain small molecule peptides with a molecular weight below 2000D.

[006...

Embodiment 3

[0068] Example 3 Zoological verification of sea cucumber anti-fatigue peptide

[0069] The weight-bearing swimming test was carried out on the adult mice who were orally synthesized candidate peptides for 3 to 5 weeks. group (1.4mg / g·d) and high sea cucumber peptide dose group (2.8mg / g·d). Specifically: the weight is fixed by adding 5% body weight lead skin to the tail of the mouse. The mouse is placed in a 50×50cm water tank with a water depth of 50cm and a water temperature of 28°C±0.5°C. Swim for 60 minutes. After swimming, each mouse is wiped dry. The body was anesthetized with pentobarbital sodium (50mg / kg BW, i.p.), and blood, heart, muscle, and liver tissues were collected; 10 rats in each group.

[0070] The candidate peptides include LPGSDDF, FD(Hyp)GA, APGLTY and G(Hyp)LQADY.

[0071] Test items include blood sugar before and after exercise, serum lactic acid before and after exercise, blood urea nitrogen before and after exercise, MtDNA content in heart and skelet...

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 a functional peptide screening method which is low in cost, efficient and environment-friendly and specifically comprises the following steps: calling a regulatory network related to the function type of a functional peptide needing to be screened; finding out a first gene target set related to the function type; performing functional target prediction on each sequenced peptide fragment, and screening to obtain a second gene target set related to the functional type; performing association processing on the second gene target set and the first gene target set to obtain a functional target; constructing a protein interaction network according to the functional targets, carrying out node graph visualization analysis to obtain a gene interaction network graph, and identifying to obtain a core module and a key gene; calculating node edge numbers of proteins and genes by using an R language, and performing normalization processing to obtain a first score of each target in the functional targets; multiplying the first score of each target point of the single peptide fragment by a corresponding similarity coefficient and then summing to obtain a functional score of the single peptide; and selecting the first 20 peptide fragments with hydrophobicity of 0-3 as candidate peptides.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to a screening method for functional peptides. Background technique [0002] Fatigue affects the quality of life, physical health and mental state of modern people. The development of nutritional regulation supplements with high-efficiency anti-fatigue functions is a current research and development hotspot. Many existing studies have shown that sea cucumber protein, especially the mixture of its hydrolyzed peptides, has good anti-fatigue effects, but when used as medicine or in the preparation of functional foods, high-purity anti-fatigue sea cucumber peptides are required, so it is usually necessary to fight fatigue after hydrolysis Sea cucumber peptides were purified. Searching for anti-fatigue sea cucumber peptides with specific functions in the hydrolyzed peptide mixture is tedious, time-consuming, and inefficient. The main reason is that there are many kinds of peptides, and dif...

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): G16B15/30G16B20/00G16B40/00G16B50/00
CPCG16B15/30G16B20/00G16B40/00G16B50/00
Inventor 刘会平蒋泽根乐国伟施用晖
Owner 时代生物科技(深圳)有限公司
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