Molecular Mechanism of Egg White Protein for Strengthening the Cross-Linking Properties of Heat-Induced Wheat Gluten Gel

The chemical interaction between egg white protein (EWP) and wheat gluten (WG) is significantly influenced by the amount of EWP added. Therefore, the effects of EWP addition on the gelling properties and chemical interactions of heat-induced WG-EWP gels are thoroughly examined. The results demonstrate that the enhancement in gel strength of WG-EWP gels is positively correlated with the amount of EWP added. EWP addition improves protein-protein interactions by reducing the freedom of water. The enhanced aggregation between WG and EWP is likely due to a decrease in surface hydrophobicity and an increase in beta-sheet content. EWP enhances cross-linking with low molecular weight glutenin subunit (LMW-GS), high molecular weight glutenin subunit (HMW-GS), and gliadin (Gli). Specifically, EWP primarily cross-links with omega-, alpha-, and gamma-Glis through S-S bonds and interacts with GS through hydrophobic interactions and S-S bonds. This study provides a theoretical foundation for improving the WG network structure in wheat-based food production. Egg white protein (EWP) addition limits the fluidity of water in heat-induced wheat gluten (WG)-EWP gel. EWP addition improves the aggregation and cross-linking between WG and EWP. EWP mainly cross-links with omega-, alpha-, and gamma-gliadins through S-S bonds. EWP mainly cross-links with glutenin (Glu) through hydrophobic interaction and S-S bonds. image