Understanding interactions among flavor compounds from spices and myofibrillar proteins by multi-spectroscopy and molecular docking simulation

Influence of the constant heating treatment on structural and adsorption properties of myofibrillar proteins (MPs) of chicken was investigated. The results showed that heat treatment enhanced the exposure of sulfhydryl groups and improved hydrophobicity of MPs surface. Particle size distribution of MPs significantly varied depending on heat treatment duration. Also, heat treatments resulted in significant changes in the alpha-helix and beta-sheet structures of MPs. Besides, the MPs formed larger, irregular, and cluster-like aggregates after heat treatments. Moreover, heat treatments increased viscosity and surface roughness of MPs, while zeta potential value was reduced after heat treatments. Furhthermore, binding interactions between the MPs and spices flavors signifcanlty varied relying on nature of MPs and flavor compounds, as well as heat treatments duration. Amino acid residues were interacted with flavor compounds of spices via a variety of bonds and a stable MPs-flavors complex was per-formed. The obtained results provide a basis for understanding structural and physicochemical changes that occur in MPs during cooking and the interactions between MPs and flavors of spices.

Automated summary

This study investigated the influence of constant heating treatment on the structural and adsorption properties of chicken myofibrillar proteins (MPs). The results showed that heat treatment increased the exposure of sulfhydryl groups and improved the hydrophobicity of MPs' surface. The particle size distribution, alpha-helix and beta-sheet structures, as well as the formation of aggregates, viscosity, surface roughness, and zeta potential of MPs were significantly affected by heat treatments. Additionally, the binding interactions between MPs and flavors of spices varied depending on the nature of MPs, flavor compounds, and heat treatment duration.