Abstract
It is essential to understand the mechanism of action of ultrasound synergistic free radical oxidation to promote covalent reactions between proteins and polyphenols. (-)-epigallo-catechin 3-gallate (EGCG) with rich bioactivity could be used to increase the functional properties of cereal protein-gliadin (GL). This study systematically explored the role of ultrasound treatment (US) on the binding mechanisms of GL and EGCG. Electrophoresis and high-performance liquid chromatography (HPLC) confirmed the greater molecular mass of the covalent complexes in the ultrasound environment. Quantitative analysis by the phenol content revealed that the ultrasound environment increased the EGCG content in the covalent complex by 15.08 mg/g of protein. The changes in the spatial structure of the proteins were indicated by Fourier infrared and ultraviolet spectroscopy. Additionally, scanning electron microscopy (SEM) and atomic force microscopy (AFM) found that US disrupted the aggregation of GL and the clustered structure of the covalent complexes. The results demonstrated that the water solubility of ultrasonic conjugates was significantly increased by 8.8-64.19%, the digestion rate was more efficient, and the radical scavenging capacity was twice that of GL. This research contributes to the theoretical basis for broadening the application of polyphenols in modifying protein.