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Exploring the interaction mechanism between yeast protein and soybean Isoflavones before and after high-pressure
Zihuan Wang1, Xiuli Xu2, Caixia Chen3
1School of Light Industry Science and Engineering; Key Laboratory of Geriatric Nutrition and Health, Ministry of Education of China; Beijing Technology and Business University, Beijing 100048, China.
Abstract:
This study investigated the binding mechanism between soybean isoflavones (SIF) and yeast protein (YP), subject to high-pressure homogenization (60 MPa, YP60). SIF at varying concentrations ranging from 2.1 to 3.0 mg/mL interacted non-covalently with both YP and YP60, as confirmed by total phenol content analysis. UV-Vis, FTIR and fluorescence spectroscopy indicated that SIF binding induced slight conformational changes in the protein structure. Fluorescence quenching analysis revealed a static quenching mechanism, with hydrogen bonding and van der Waals forces as the primary stabilizing interactions. High-pressure homogenization effectively altered the structure of YP by partially unfolding the protein, thereby exposing additional hydrophobic sites and enhancing its binding affinity for SIF. Molecular docking and dynamics simulations further demonstrated that stable YP-SIF complexes are formed through multiple hydrogen bonds, as well as electrostatic, and van der Waals interactions at specific amino acid residues, leading to increased structural stability and compactness of the protein.
