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Method for preparing protein films by improving enzyme-promoting crosslinking modification of gluten proteins through multi-primary amide

A gluten protein and compound technology, applied in flexible coverings, packaging, wrapping paper, etc., can solve the problems of lack of lysine, limited physical and mechanical properties of gluten materials, and low number of free amino groups, etc. Mild conditions, environmentally friendly and easy to control, efficient operation effect

Inactive Publication Date: 2015-10-28
JIANGNAN UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] However, although glutamine residues are rich in gluten protein composition, lysine is severely lacking, resulting in a small number of free amino groups that can react with glutamine. The enzymatic reaction based on TGase improves the physical and mechanical properties of gluten protein materials. to a very limited extent

Method used

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  • Method for preparing protein films by improving enzyme-promoting crosslinking modification of gluten proteins through multi-primary amide
  • Method for preparing protein films by improving enzyme-promoting crosslinking modification of gluten proteins through multi-primary amide
  • Method for preparing protein films by improving enzyme-promoting crosslinking modification of gluten proteins through multi-primary amide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0015] Example 1 α-polylysine improves the activity of TGase in catalyzing the cross-linking reaction of gluten protein

[0016] Weigh the gluten protein and dissolve it in phosphate buffer (pH=7.0), the concentration is 3%, add a certain amount of α-polylysine, after the gluten protein is evenly dispersed in the solution, add a certain amount of transglutaminase (TGase), about 15u / g albumen, (the TGase that the present invention uses is widely present in plant, animal and microorganism, and the TGase of any source can realize identical effect in the present invention, and the TGase of different sources is all to gluten protein Catalyzed), reacted at 37°C for 3 hours under constant temperature stirring. Inactivated enzyme was added to the control sample, and the other conditions were the same. After the reaction was finished, it was freeze-dried and set aside. Before lyophilization, perform characterization tests. Get a certain amount of dispersion after the reaction, centr...

Embodiment 2

[0017] Modified gluten protein film after embodiment 2

[0018] Weigh the gluten protein and dissolve it in phosphate buffer (pH=7.0), the concentration is 3%, add a certain amount of α-polylysine, after the gluten protein is evenly dispersed in the solution, add a certain amount of transglutaminase (TGase), about 15u / g protein, reacted at 37°C for 3 hours under constant stirring. Inactivated enzyme was added to the control sample, and the other conditions were the same. After the reaction was finished, it was freeze-dried and set aside. Dissolve the modified gluten protein in formic acid, add a certain amount of glycerin, and stir at 40°C for 3 hours. After fully dissolving, place it in an ultrasonic oscillator for 5 minutes to remove internal air bubbles. The solution was poured onto a smooth polytetrafluoroethylene plate, dried at room temperature, and then the dried film was carefully peeled off from the plate to prepare a modified gluten film. The physical and mechanic...

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Abstract

The invention belongs to the field of biological materials, and relates to a method for preparing protein films by improving enzyme-promoting crosslinking modification of gluten proteins through multi-primary amide. The method aims to solve the problem that the improvement degree of physical and mechanical property of gluten protein films is low through an existing method that crosslinking is promoted only through enzymes. According to the method, the reaction capacity and reaction activity of a protein crosslinking reaction is enhanced by adding multi-primary amines while the gluten proteins are promoted to generate crosslinking modification through glutamine transaminase, the enzyme-promoting crosslinking degree among the proteins is increased remarkably under the bridging action of the multi-primary amines, and the physical and mechanical property of the protein films is further improved. Please see appended drawings. By means of the method, operation is conducted conveniently, reaction conditions are mild, the residue problems of chemical reagent are avoided, the method can replace traditional chemical crosslinking modification to a certain degree to prepare protein film materials, and the application field is broadened.

Description

technical field [0001] The invention relates to a method for preparing a protein film by improving enzymatic cross-linking modification of gluten protein by using a doubly amino compound, belonging to the field of biological materials. Background technique [0002] Gluten is a by-product of wheat starch production, with a wide range of sources, and its protein content is about 80%. Gluten protein can form a three-dimensional network structure after absorbing water, and has excellent extensibility, viscoelasticity, water absorption, etc. It is an ideal raw material for preparing protein films, and the obtained films have good biocompatibility, biodegradability and pathogen transmission Low-risk, it has broad application prospects in the fields of medicine, packaging materials and food. However, the mechanical properties of the gluten film prepared under general conditions are poor, and the dissolution rate in water is high, which affects its application effect. Cross-linkin...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C08L89/00C08K5/053C08J5/18C08J3/24B65D65/38
Inventor 崔莉孙红玉王平范雪荣王强刘刚
Owner JIANGNAN UNIV
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