Relationship of co-gelation and co-aggregation on egg white ovalbumin-lysozyme heteroprotein complex: Formation and thermodynamics

This study aimed to establish binary protein system on egg white ovalbumin (OVA)-lysozyme (LYS), and investigated the relationship between co-aggregation and co-gelation. We focused on the formation of OVA-LYS complex, the typical thermo-dynamically favored coacervation process, in terms of gelling properties, microstructure and thermodynamics. Benefited from synergistic effects during co-gelation, the thermally induced gels of OVA-LYS complex formed at extremely low protein concentration (18 mg/mL) and showed higher storage modulus with increasing LYS concentration. Moreover, the rising particle size, reduced zeta potential, unordered secondary structure and strengthened protein chain were observed with the addition of LYS. Remarkably, the divalent ions enhanced thermodynamic stability of OVA-LYS complex, although the growth of aggregates units were prevented by ions at room temperature. ITC and molecular docking analyses revealed the binding affinity stoichiometry and combination phase, which were closely related to the decrease of minimum energy resulted from the formation of hydrogen bond.

Automated summary

This study established a binary protein system using ovalbumin (OVA) and lysozyme (LYS) in egg white, and investigated the relationship between co-aggregation and co-gelation. The addition of LYS enhanced the thermodynamic stability and storage modulus of OVA-LYS complex, and also influenced its microstructure and protein chain properties. Furthermore, divalent ions enhanced the thermal stability of the complex.