Formation mechanism of giant squid myofibrillar protein aggregates induced by egg white protein during heat treatment

Abstract

In order to solve the problem of poor performance of giant squid gel, this study proposed a method to induce the aggregation of giant squid protein molecules by exogenous additives to improve its gel performance. The particle size, zeta potential, free sulfhydryl group, carbonyl group and hydrophobic index of protein solution were characterized by laser light scattering, fluorescence spectrum and ultraviolet spectrum, and the effect of egg white protein (EWP) on myofibrillar protein (MP) aggregation was analyzed. In the presence of EWP, the density and Rg/Rh value of protein particles decreased significantly after mixing for 600 min, indicating that the interaction between MP and EWP protein could be enhanced by embedding appropriate amount of EWP in the middle of MP protein. With the increase of the proportion of egg white protein, the blue shift of the maximum absorption wavelength of endogenous fluorescence in the mixed protein solution decreased. In the range of 25–65 °C, the change rates of surface charge, free sulfhydryl group, carbonyl group and surface hydrophobicity decreased, which proved that EWP inhibited the self-aggregation rate of MP molecules during the heating process, and induced its gel by interspersing between MP molecules to improve the formation of three-dimensional network during protein thermal gel process. Finally, the addition of EWP improved the gel properties of giant squid surimi. This study offered new direction for improving gel properties and promotes the development and application of giant squid.