Effects of salidroside on structural and functional properties of myofibrillar proteins in the Fenton system

This study used the Fenton reaction to simulate the oxidation process of porcine myofibrillar proteins (MPs), aiming to explore the regulatory effect of salidroside (SAL) on the structure and functional properties of MPs under oxidative conditions. Systematic characterization of MPs-SAL interactions through biochemical assays, physicochemical measurements, and multispectral structural analysis. The results demonstrated that SAL boosted the antioxidant prowess of MPs in a dose-dependent fashion. Oxidative stress caused a reduction in sulfhydryl levels and absolute Zeta potential values, while simultaneously increasing dimeric tyrosine formation. Compared to the control group, sulfhydryl and dimerized tyrosine levels decreased with increasing SAL concentration, while the absolute Zeta potential values exhibited a progressive augmentation. Furthermore, oxidation resulted in elevated surface hydrophobicity and reduced solubility, and SAL further promoted the exposure of hydrophobic residues, and SAL caused changes in both the secondary and tertiary structures of MPs. SDS-PAGE revealed no notable band variations in oxidized groups following SAL treatment. Scanning electron microscopy revealed that the pores of MPs became larger and the surface rough after oxidation, while the protein surface became less wrinkled and smoother after the addition of SAL. In summary, the interaction between MPs and SAL affects the structural and functional properties of proteins.