Treatment method and application of gluten protein

A processing method and technology of gluten protein, applied in the fields of application, plant protein processing, packaging, etc., can solve the problems of poor water solubility, unsatisfactory functional properties, hindering the application of gluten protein, etc., to achieve improved solubility and emulsification properties, and enhance solubility Effect

Active Publication Date: 2022-07-01
NORTHWEST A & F UNIV
View PDF7 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0010] The technical problem solved by this application is that, as a high-quality vegetable protein, gluten has high nutritional value, but due to its own structural characteristics, its poor water solubility leads to unsatisfactory functional properties, which hinders the use of gluten in food and Applications in other industries

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
  • Treatment method and application of gluten protein
  • Treatment method and application of gluten protein
  • Treatment method and application of gluten protein

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0035] Protein sample preparation:

[0036] At room temperature, gluten protein was dissolved in distilled water to prepare a gluten protein aqueous solution with a protein concentration of 5 mg / mL.

[0037]Among them, the gluten protein aqueous solution without any treatment was used as the control group. Take three gluten protein aqueous solutions for heat treatment only: heat treatment at 40°C, 60°C, and 80°C for 30 min, and stir at room temperature for 1 h; adjust the pH to 12.0 with 1M NaOH solution, and the three gluten protein aqueous solutions are respectively heated at 40°C, 60°C , heat treatment at 80°C for 30 min, stir at room temperature for 1 h, then adjust the pH to 7.0 with 1M HCl solution (pH cycle method), and continue stirring at room temperature for 1 h. At the same time, three gluten protein aqueous solutions were taken and heat-treated at 40° C., 60° C., and 80° C. for 30 min, respectively, and stirred for 1 h at room temperature. All processed gluten pr...

Embodiment 2

[0039] Solubility determination

[0040] Pour the centrifuged gluten protein supernatant into a petri dish, keep the precipitate in a centrifuge tube, and dry it in a 55°C oven overnight. After drying, weigh the centrifuge tube and the precipitate together, and subtract the original centrifuge tube from the obtained mass. The mass is the precipitation mass, and the gluten protein solubility calculated from the obtained gluten protein precipitation mass is Solubility 1. After 48h freeze-drying of the gluten protein supernatant, the gluten protein freeze-dried sample was carefully taken out and weighed, and the gluten protein solubility calculated according to the mass of the obtained gluten protein supernatant sample was solubility 2.

[0041]

[0042]

[0043] like figure 1 As shown, all 9 treatments had some effect on the solubility of gluten protein. Among them, compared with the control, the improvement of the solubility of gluten protein by single heat treatment wa...

Embodiment 3

[0047] Determination of average particle size of emulsions

[0048] To measure the average particle size of protein molecules, choose a dynamic laser light scattering (DLS) with a λ=633nm He / Ne laser particle size potential analyzer and set the scattering angle to 173°. Pipette 1 mL of different gluten protein sample solutions with a concentration of 5 mg / mL into a special material cuvette (polystyrene) (refractive index 1.33) to determine the average particle size. The measurement temperature is set at 25±0.1°C, and the temperature is kept for 3 minutes. Three parallel experiments were performed for each protein sample, each parallel sample was scanned three times, and the final results were averaged.

[0049] The size of protein particle size has a great influence on protein structure and functional properties, and has important application value for improving the utilization rate of protein resources.

[0050] like figure 2 As shown, all 9 treatments had a certain effec...

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 provides a treatment method of gluten protein. The solubility and emulsification characteristics of the gluten protein are improved. After the gluten protein solution is subjected to heat treatment and pH cycle treatment, disulfide bonds of gluten protein molecules are broken, the content of free sulfydryl is increased, the surface hydrophobicity is increased, and the particle size is reduced, so that the solubility and the emulsifying property of the gluten protein are remarkably improved. Therefore, a solution is provided for expanding the application market of the gluten protein.

Description

technical field [0001] The present application relates to the field of food processing, in particular to a gluten protein processing method and application thereof. Background technique [0002] Wheat gluten protein, commonly known as Wheat gluten (WG), is a common high-quality vegetable protein in daily life. ) and the smaller molecular weight gliadin (Gliadin). The gliadin molecule is non-polar, mainly due to the presence of disulfide bonds in the molecule; while gliadin has both intermolecular disulfide bonds and intramolecular disulfide bonds, and the formation of intermolecular disulfide bonds is normal. It is formed by the interaction between protein subunits. [0003] Wet gluten refers to dispersing gluten in water, the starch in it is dissolved, and the gluten protein molecules interact with water to form protein aggregates with a unique network structure. Wet gluten has excellent properties such as extensibility, viscoelasticity, water absorption, and film formin...

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): A23J3/18A23L2/38A23G9/38B65D65/46
CPCA23J3/18A23L2/38A23G9/38B65D65/463A23V2002/00A23V2250/5486
Inventor 段翔熊丹丹徐倩倩刘学波付钰坤
Owner NORTHWEST A & F 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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap