Elucidating the effect of protonation-amplified pulsed electric field processes on flavor-controlled release behavior of goose meat

This study aimed to investigate the cooperative effects of protonation combined with pulsed electric field (PEF) treatment on the conformational changes of goose myofibrillar proteins (MPs) and their flavor-controlled release behavior. Structural variations in MPs were characterized by circular dichroism, Fourier transform infrared spectroscopy, and surface hydrophobicity (H 0 ) detection. The binding mechanism between MPs and typical flavor compounds was further explored via molecular docking. Results demonstrated that protonation disrupted the intramolecular ionic bonds and hydrogen bonds of MPs, increasing their sensitivity to subsequent PEF treatment. The synergistic protonation-PEF treatment induced a significant transition from α-helix to β-sheet structure, accompanied by a remarkable increase in surface hydrophobicity. Molecular docking confirmed that key amino acid residues (Asp97, Gln95) were primarily responsible for the enhanced binding capacity of MPs to hydrophobic flavor compounds. This work provides mechanism insights into the cooperative regulation of protonation and PEF on the structure and flavor-binding capacity of goose MPs, providing scientific support for the control of flavor release in processed goose products.