Related Experiment Video
Updated: Jul 8, 2026

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
Published on: August 15, 2016
Effect of Heat Treatment Combined with TG Enzyme Cross-Linking on the Zein-Pea Protein Complex: Physicochemical and
Yan Li1,2,3, Chi Wang1, Nannan Hu3
1College of Food Science and Engineering, Ocean University of China, Qingdao 266100, China.
Abstract:
Plant proteins have the advantages of low cost and high yield, but they are still not comparable to animal proteins in processing due to factors such as gelation and solubility. How to enhance the processing performance of plant proteins by simple and green modification means has become a hot research topic nowadays. Based on the above problems, we studied the effect of gel induction on its properties. In this study, a pea protein-zein complex was prepared by the pH cycle method, and the effects of different induced gel methods on the gel properties of the complex protein were studied. The conclusions are as follows: All three gel induction methods can make the complex protein form a gel system, among which the gel strength of heat treatment and the TG enzyme-inducted group is the highest (372.84 g). Through the observation of the gel microstructure, the gel double network structure disappears and the structure becomes denser, which leads to a stronger water-binding state of the gel sample in the collaborative treatment group. In the simulated digestion experiment, heat treatment and enzyme-induced samples showed the best slow-release effect. This study provides a new method for the preparation of multi-vegetable protein gels and lays a theoretical foundation for their application in food processing.

