An Active Peptide with Bitter Taste Blocking Effect

A technology of blocking action and active peptides, which is applied in the directions of medical preparations, peptides, and applications of non-active ingredients, can solve limited problems, and achieve the effect of wide application prospects and good water solubility.

Active Publication Date: 2022-02-11
BOHAI UNIV
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In the prior art, the type reports of natural T2Rs blockers are very limited, therefore, it is very meaningful to develop novel natural T2Rs blockers

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
  • An Active Peptide with Bitter Taste Blocking Effect
  • An Active Peptide with Bitter Taste Blocking Effect
  • An Active Peptide with Bitter Taste Blocking Effect

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0027] This example screens and identifies a tetrapeptide DDNK that has a significant inhibitory effect on the combination of bitter substances and T2R14 from egg white, including the following steps:

[0028] (1) Virtual enzymolysis and preliminary screening of egg white protein.

[0029] Based on the online program ExPASy PeptideCutter, ovalbumin in egg whites was treated with typical digestive proteases of the gastrointestinal tract, namely pepsin (EC 3.4.23.1), trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1). , ovotransferrin and ovomucoid were subjected to simulated enzymatic hydrolysis, and their amino acid sequences were obtained through the NCBI website (https: / / www.ncbi.nlm.nih.gov / ), and their numbers were AAB59956.1, CAA26040.1 and ACJ04729.1. 219 dipeptides and above active peptides were obtained. Unreported dipeptides, tripeptides and tetrapeptides were selected to predict toxicity and water solubility properties using the ADMET program of DS 2017 software ...

Embodiment 2

[0035] Example 2. Determination of the Blocking Activity of Active Peptides to Bitter Substances

[0036]The bitter taste inhibitory activity of a certain concentration of peptide DDNK was determined by electronic tongue. Take a certain amount of peptide DDNK, add it to 30mL water and mix well, add 50mL quinine (1mM) to prepare the solution to be tested, use quinine as the blank control group, and use the peptides LELNQ and LEGSLE as the positive control group. After setting the number of cycles, data file name, sample quantity, sample name and test method, install the electrode and start the measurement.

[0037] The measurement process is as follows: (1) Clean the sensor in the positive and negative solutions for 90s, and then clean the sensor in the two reference solutions for 120s; (2) Balance the sensor in the conditioning solution for 30s; (3) Measure each sample for 30s; (4 ) After cleaning the sensor twice for 3s each, immerse it in the reference solution for 30s to m...

Embodiment 3

[0039] Example 3. DS software analyzes the interaction mode between peptide DDNK and T2R14.

[0040] The two-dimensional plan between peptide DDNK and T2R14 as figure 1 shown by figure 1 It can be seen that the tetrapeptide DDNK can interact with Asp168 residue, Trp89 residue, Ser167 residue, Gly158 residue, Asn157 residue, Cys165 residue, Tyr159 residue, Ser265 residue, Ile262 residue and Thr86 residue of T2R14 effect;

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 specifically relates to an active peptide with a bitterness blocking effect, the amino acid sequence of which is Asp-Asp-Asn-Lys (DDNK). The active peptide with bitter blocking effect provided by the present invention can effectively bind to the bitter taste receptor T2R14, has a sustained and stable masking effect on bitter substances, and has outstanding advantages such as safety, no toxic side effects, easy absorption, and industrialization. . The active peptide DDNK can be used in bitter foods, medicines and health products, and has broad application prospects and very important significance.

Description

technical field [0001] The invention belongs to the field of bioactive peptides, and in particular relates to an active peptide with bitterness blocking effect. Background technique [0002] After protein digestion, it is mainly absorbed directly in the form of peptides. Protein peptides can be used in many nutritional products or as flavor additives. However, in the process of preparing protein peptides, various degrees of bitterness will be produced. Studies have shown that although the insoluble proteins of soybeans and fish are modified by protease treatment, their solubility, thermal stability and anti-sedimentation properties in acidic environments are improved, but at the same time their hydrolyzed products have a bitter taste, which affects its use. The formation of bitter taste causes the flavor defect of food, which limits the application of protein hydrolyzate. Therefore, masking and removing the bitterness of protein hydrolyzates is a long-standing challenge ...

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): C07K5/113A23L27/00A23F3/14A23F3/34A23F5/14A23L19/00A23L33/18A61K47/18
CPCC07K5/1021A23L27/86A23F3/14A23F5/14A23F3/34A23L19/00A23L33/18A61K47/183A23V2002/00A23V2250/55A23V2200/16A23V2200/30A23V2200/328
Inventor 于志鹏阚若彤赵文竹王莹雪
Owner BOHAI UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products