Abstract
The combination of polyphenols and protein can improve the functional characteristics of protein. How to effectively promote the binding of polyphenols to protein is still a difficult topic. In this study, hydrodynamic cavitation (HC) was used to induce the fabrication of complexes between soy protein isolate (SPI) and different polyphenols (tannic acid (TA), chlorogenic acid (CGA), ferulic acid (FA), caffeic acid (CA), and gallic acid (GA)). The effect of HC on the interaction between polyphenols and SPI was investigated, and the structural and functional properties of the formed complexes were characterized. The results showed that HC treatment led to SPI structure stretching, which increased the binding level of polyphenols, especially that of TA (increased from 35.08 ± 0.73% to 66.42 ± 1.35%). The increase in ultraviolet-visible absorption intensity and quenching of fluorescence intensity confirmed that HC enhanced the interaction between polyphenols and protein. HC treatment reduced the contents of free sulfhydryl and amino groups in SPI-polyphenol complexes and altered their Fourier transform infrared spectroscopy, indicating that HC treatment promoted the formation of C-N and C-S bonds between SPI and polyphenols. Circular dichroism spectroscopy indicated that HC treatment altered the secondary structure of SPI-polyphenol complexes, inducing an increase in α-helix and random coil contents and a decrease in β-sheet content. Regarding functional properties, HC treatment improved the emulsification and antioxidant activity of SPI-polyphenol complexes. Therefore, HC is an effective technique for promoting the binding of polyphenols to protein.