Abstract：
The present study was aimed to investigate the interactions between soybean protein isolate (SPI) with resveratrol (RESV) and lutein (LUT). The binding forces, molecular interactions and functional properties were explored by multi-spectroscopic analysis, molecular docking and functional property indexes between SPI and RESV/LUT. The RESV/LUT quenched SPI chromophore residues with static mechanism and the endothermic reaction. The SPI- RESV/LUT complexes were formed through hydrogen bond, electrostatic and hydrophobic interactions. Molecular docking confirmed van-der-Waals force as one of the important forces. The interaction of RESV/LUT led to SPI\'s secondary structure alterations with a decrease in α-helix and random coil and an increase in β-sheet and β-turns. RESV/LUT developed foaming and emulsifying properties of SPI and showed a significant decrease of the surface hydrophobicity with RESV/LUT concentrations increase attributed to SPI\'s partial unfolding. Our study exposed molecular mechanisms and confirmations to understand the interactions in protein- RESV/LUT complexes for protein industrial base promotion.
摘要：
本研究旨在研究大豆分离蛋白（SPI）与白藜芦醇（RESV）和叶黄素（LUT）之间的相互作用。约束力，通过多光谱分析探索分子相互作用和功能性质，SPI和RESV/LUT之间的分子对接和功能性质指标。RESV/LUT猝灭SPI发色团残基具有静态机理和吸热反响。SPI-RESV/LUT配合物通过氢键形成,静电和疏水相互作用。分子对接证实范德华力是重要的力量之一。RESV/LUT的相互作用导致SPI的二级结构改变，α螺旋和无规卷曲减少，β折叠和β转角增加。RESV/LUT开发了SPI的发泡和乳化性能，并显示出表面疏水性的显着降低，RESV/LUT浓度的增加归因于SPI的部分展开。我们的研究揭示了分子机制和确认，以了解蛋白质-RESV/LUT复合物中蛋白质工业基础促进的相互作用。
