l-Arginine and l-lysine improve the emulsifying and dissolution properties of pale, soft, exudative-like chicken myofibrillar proteins by modifying their conformations.

Herein, we investigated the effect and potential mechanisms of l-arginine (Arg) and l-lysine (Lys) on the emulsifying and dissolution properties of pale, soft, exudative (PSE)-like chicken myofibrillar proteins (MPs). The findings revealed that Arg/Lys effectively enhanced the emulsion activity and emulsion stability indexes of PSE-like MPs, resulting in smaller and more uniform PSE-like MP-soybean oil emulsions. Arg/Lys increased the solubility, absolute potential, hydrophobicity, fluorescence intensity, and β-sheet content and decreased the turbidity, particle size, and β-turn and random coil content of PSE-like MPs. Additionally, Arg/Lys did not significantly affect the Schiff base, carbonyl group, and total sulfhydryl contents, but caused a red shift of the band near 299 nm, indicating conformational rather than primary structural changes. Altogether, these findings indicate that Arg/Lys improves the emulsifying and dissolution performances of PSE-like MPs by adjusting conformation and contributes to a better understanding of how Arg/Lys enhances the physicochemical properties of PSE-like sausages.