Effects of conjugated interactions between Perilla seed meal proteins and different polyphenols on the structural and functional properties of proteins.

The study aims to perform alkali-induced covalent modification of perilla seed meal protein (PSMP) using different polyphenols: gallic acid (GA), protocatechuic acid (PCA), caffeic acid (CA), apigenin (API) and luteolin (LU). Covalent binding between different polyphenols and PSMP was found to occur, with PSMP-LU showing the highest binding rate of 90.89 ± 1.37 mg/g; the fluorescence spectrum of PSMP-CA showed a maximum blue shift of Δ13.4 nm; the solubility increased from 69.626 ± 1.39 % to 83.102 ± 0.98 %. In order to better understand how these covalent conjugates, stabilize -carotene in emulsions, they were utilized as emulsifiers in an emulsion delivery method. The work further reveals the formation of PSMP-polyphenol conjugates and develops a novel emulsification system to deliver readily decomposable functional factors, providing a potential scenario for the application of PSMP and bioactive conjugates.