An insight into the changes in conformation and emulsifying properties of soy β-conglycinin and glycinin as affected by EGCG: Multi-spectral analysis

Abstract

The binding mechanisms between soy β-conglycinin/glycinin and (−)-epigallocatechin-3-gallate (EGCG) were evaluated using multi-spectral techniques and molecular modeling. Additionally, the emulsifying properties of β-conglycinin/glycinin were investigated in their interactions with EGCG. Fluorescence analysis revealed that the quenching of β-conglycinin/glycinin by EGCG was static quenching. Specifically, EGCG to β-conglycinin/glycinin resulted in the conformation changes of the Trp and Tyr residues, around which the polarity toward more hydrophilic. The dominated binding between β-conglycinin and EGCG was hydrogen bonding, whereas was mainly hydrophobic force between glycinin and EGCG. Such affinity induced a more organized protein confirmation with decreased random coil and increased α-helix and β-structures. The docking data indicated the better affinity between glycinin and EGCG, compared to β-conglycinin. The emulsifying ability and capacity of β-conglycinin were enhanced with involvement EGCG, however no effect was found for glycinin. Our findings deliver insights in understanding of the interaction mechanisms between β-conglycinin/glycinin and EGCG.