Protein-Protein Interactions and Structure of Heat-Set Gels Based on Pea Protein and Egg White Mixtures

This study examined the thermal gelation of mixtures of laboratory-prepared pea protein isolate (PPI) and egg white proteins (EWP) at different PPI/EWP weight ratios (100/0, 75/25, 50/50, 25/75, 0/100) at pH 7.5 and 9.0.Viscoelastic and texture properties of the composite gels, along with the microstructure and molecular interactions involved in the gel network, were investigated.Except PPI-EWP 100/0 at pH 9.0, all systems gelled with increasing gel hardness, springiness and cohesiveness when EWP content increased.This phenomenon was explained by the microstructure of the gels, wherein the presence of PPI enhanced the formation of aggregates embedded in the EWP network, thus loosening it.The rheological properties of the mixed gels were primarily influenced by the EWP network, significantly involving disulfide bonds.However, upon the addition of PPI, hydrogen bonds and hydrophobic interactions predominated and the structure of the gel became more sensitive to pH as electrostatic repulsions interfered.Playing on the ratio of PPI/EWP allows for the production of gels with varying textures, and the data suggest the possibility of partially substituting egg white with pea proteins in food gel formulation.