Ions-regulated aggregation kinetics for egg white protein: A promising formulation with controlled gelation and rheological properties.

This study aims to evaluate the structure of ions-regulated gelation of egg white protein (EWP) via aggregation kinetics model, which was built by monitoring turbidity. Results showed that compared with NaCl and KCl, the addition of NaSO increased free sulfhydryl content, surface hydrophobicity and particle size of EWP significantly, while weakened the order of secondary structure. Hence, strengthened gel network structure was observed with higher porosity, which improved the texture profiles and rheological properties of EWP gels. Based on these phenomena above, the relationship between aggregation behavior and gelling properties with ions was further investigated by aggregation kinetics model and principal component analysis. Because of the enhancement of protein interactions, the aggregation growth rate with NaSO was much faster than the samples with NaCl, which reflected over-aggregation due to the accelerated nucleation process and resulted in firmed gel network structure.