Effects of interaction between hesperetin/hesperidin and glutenin on the structure and functional properties of glutenin

Abstract

This research aimed to investigate the changes in the structure and functional properties of glutenin (Glu) induced by hesperetin (Ht) or hesperidin (Hd). Both Ht and Hd quenched the fluorescence of Glu through a static process and formed a Ht/Hd–Glu complex in one binding site. The binding constants between Glu and Ht and Hd were 4.20 × 104 L mol−1 and 3.59 × 104 L mol−1 at 25 °C, respectively. The computer simulations showed their bindings were dominated by hydrogen bonds and hydrophobic forces, and also provided the changes in particle motion and macroscopic properties of Glu induced by Ht/Hd. The presence of Ht/Hd promoted the exchange of sulfhydryl and disulfide bonds, resulting in the structural changes of Glu and the free sulfhydryl groups more exposed. Meanwhile, the increase in β-sheet content of Glu might cause the contraction of the carbon chain, thereby increasing the surface hydrophobicity. Due to the increase in rigid clusters and the decrease in flexibility, thermal stability of Glu was enhanced. Moreover, the emulsifying activity of Glu was significantly improved. This research lays the foundation for the application of Ht/Hd and Glu in healthy food or the optimization of Glu-based products.