Abstract：
The interaction mechanism between soybean protein isolate (SPI) and furan flavor compounds with different structures is studied using spectroscopy, molecular docking, and MD simulation methods. The order of binding ability between SPI and furan flavor compounds is 2-acetylfuran>furfural>5-methylfurfural. The structural differences (position and quantity of methyl groups) of three furan flavor compounds are key factors leading to the different adsorption abilities of SPI for furan flavor compounds. The findings from spectroscopy analyses suggest that the interaction between SPI and furan flavor compounds involves both static and dynamic quenching mechanisms, with static quenching being the main factor. Molecular docking and MD simulations reveal the atomic-level mechanisms underlying the stable binding for SPI and furan flavor compounds at spatiotemporal multiscale. This study provides a theoretical framework for the production and adjustment of meat essence formula in the production of soybean protein-based meat products.
摘要：
利用光谱学研究了大豆分离蛋白(SPI)与不同结构的呋喃风味化合物的相互作用机理,分子对接,和MD模拟方法。SPI与呋喃风味化合物的结合能力顺序为2-乙酰呋喃>糠醛>5-甲基糠醛。3种呋喃风味化合物的结构差异(甲基的位置和数量)是导致SPI对呋喃风味化合物吸附能力不同的关键因素。光谱分析结果表明，SPI和呋喃风味化合物之间的相互作用涉及静态和动态猝灭机制。静态淬火是主要因素。分子对接和MD模拟揭示了SPI和呋喃风味化合物在时空多尺度上稳定结合的原子级机制。本研究为大豆蛋白基肉制品生产中肉精配方的生产和调整提供了理论框架。
