Exploring the Interactions of Soybean 7S Globulin with Gallic Acid, Chlorogenic Acid and (-)-Epigallocatechin Gallate

In this study, the noncovalent interaction mechanisms between soybean 7S globulin and three polyphenols (gallic acid (GA), chlorogenic acid (CA) and (-)-epigallocatechin gallate (EGCG)) were explored and compared using various techniques. Fluorescence experiments showed that GA and EGCG had strong static quenching effects on 7S fluorescence, and that of CA was the result of multiple mechanisms. The interactions caused changes to the secondary and tertiary structure of 7S, and the surface hydrophobicity was decreased. Thermodynamic experiments showed that the combinations of polyphenols with 7S were exothermic processes. Hydrogen bonds and van der Waals forces were the primary driving forces promoting the binding of EGCG and CA to 7S. The combination of GA was mainly affected by electrostatic interaction. The results showed that the structure and molecular weight of polyphenols play an important role in their interactions. This work is helpful for developing products containing polyphenols and soybean protein.

Automated summary

This study investigates the noncovalent interaction mechanisms between soybean 7S globulin and three polyphenols and finds that different compounds have different effects on the protein. Various techniques, such as thermodynamic experiments and fluorescence experiments, provide strong evidence for explaining these interactions.