Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance

This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA₁₅₀ complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.