Changes in structural, rheological, and gel properties of egg white protein induced by preheating in the dry state

The knowledge of fundamental rheological concepts is essential to understand the gelling process of egg white proteins (EWP), which can be used to further manipulate the gel performance with desired sensorial attributes. In this study, the rheological and gel properties of EWP as influenced by heating in the dry state were investigated. The structural changes in dry heated EWP (DEWP) were also characterized in terms of morphology, protein stability, and protein microenvironment. The results showed that moderate dry heating induced linear aggregation of DEWP and decreased the denaturation temperature (T_d) and enthalpy of denaturation (ΔH). Furthermore, the cross-linking on protein surface led to nonpolar microenvironment of hydrophobic groups, which lays the foundation of improved gel properties. The specific outcomes include the increase in the G'_max and the G''_max values, k'/k'' values of DEWP dispersions, gel hardness and gumminess of DEWP gels and a decrease in gelation temperature of DEWP dispersions. However, few changes were found in the springiness and cohesiveness of the DEWP gels with increasing dry heating time. Notably, gels prepared with DEWP also had better digestibility. Overall, these results can provide theoretical basis for quality control and sensory evaluation of DEWP in the food industry.