Modifying duck myofibrillar proteins using sodium bicarbonate under cold plasma treatment: Impact on the conformation, emulsification, and rheological properties

Abstract

This study aimed to explore the potential advantages of incorporating sodium bicarbonate to enhance the processing characteristics of duck myofibrillar proteins (MPs) during cold plasma treatment. Various concentrations of sodium bicarbonate (0%, 0.2%, 0.4%, and 0.6%) were examined for their impact on the structural, physicochemical, and functional properties of MPs under cold plasma treatment conditions (50 V, 3 min). Results indicated that sodium bicarbonate increased the unfolding of MPs, resulting in elevated active sulfhydryl content, enhanced surface hydrophobicity, intensified intrinsic fluorescence intensity, and reduced average particle size. Additionally, sodium bicarbonate significantly augmented (P < 0.05) α-helix and β-sheet content, leading to modifications in the microenvironments of tyrosine and tryptophan. Scanning electron microscopy and atomic force microscopy revealed that sodium bicarbonate effectively mitigated the protein aggregation induced by cold plasma treatment. Sodium bicarbonate induced secondary and tertiary structural alterations, enhancing the solubility of duck MPs, consequently improving their emulsifying and rheological properties. These findings suggest that sodium bicarbonate can effectively enhance the processing performance of duck MPs during cold plasma treatment, offering novel insights into the application of sodium bicarbonate in the cold plasma processing of duck products.