Gluten protein colloid granules and preparation method and application of gluten protein colloid granules

Abstract

The invention discloses gluten protein colloid granules and a preparation method and application of the gluten protein colloid granules. The preparation method comprises the following steps: gluten protein is subjected to crosslinking reaction under the effect of glutamine transaminase so as to form gluten protein colloid granules; micro hydrophilic molecules with primary amine groups are added into the reaction system, and are at least one of L-lysine, glucosamine and L-glutamic acid, and the mass ratio of micro hydrophilic molecules with primary amine groups to the gluten protein is 1 to (10-100). According to the invention, the micro hydrophilic molecules with primary amine groups are added into the reaction system; the gluten protein is subjected to crosslinking among molecules and within molecules, and crosslinking reaction is performed together with the micro hydrophilic molecules with primary amine groups; on one hand, glutamine or asparaginate in the gluten protein can be prevented from being subjected to deamidation reaction by glutamine transaminase, and on the other hand, because the micro hydrophilic molecules with the primary amine groups contains electrified groups, relatively high surface electric charge is given to the gluten protein.

Description

technical field [0001] The invention relates to the field of protein emulsifiers, in particular to a gluten protein colloid particle and its preparation method and application. Background technique [0002] Wheat gluten is a by-product of wheat starch processing. Wheat gluten contains about 80% gluten protein, and its main components are gliadin and glutenin. Gliadin is a globulin, which is highly viscous but inelastic after hydration. Glutenin is a fibrous macromolecule with good elasticity after hydration, but no stickiness. These two proteins endow gluten with its viscous network structure properties and give baked goods their unique texture properties. However, gluten protein contains many hydrophobic amino acids and uncharged amino acids, and its intramolecular hydrophobic interaction area is relatively large, so it is easy to aggregate into agglomerates in aqueous solution, which hinders the application of gluten protein in aqueous solution environment. At present, ...

AI Technical Summary

Problems solved by technology

[0009] The invention provides a preparation method of gluten protein colloidal particles, to solve the shortage of primary amines in the existing method, causing transglutaminase to catalyze glutamine or asparagine for deamidation reaction and inter-molecular and intra-molecular cross-linking Various reactions such as gluten protein colloidal particle point modification are insufficient, the product purity is low, and the particle size difference is large.