Spectroscopy combined with spatiotemporal multiscale strategy to study the adsorption mechanism of soybean protein isolate with meat flavor compounds (furan): Differences in position and quantity of the methyl
文献类型： 外文期刊
作者： Li, Yang 1 ; Xu, Jing 2 ; Sun, Fuwei 1 ; Guo, Yanan 1 ; Wang, Daoying 3 ; Cheng, Tianfu 1 ; Xu, Minwei 4 ; Wang, Zhongjiang 1 ; Guo, Zengwang 1 ;
作者机构： 1.Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China
2.Northeast Agr Univ, Coll Arts & Sci, Harbin 150030, Heilongjiang, Peoples R China
3.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Peoples R China
4.North Dakota State Univ, Dept Plant Sci, Fargo, ND 58108 USA
5.Hainan Acad Agr Sci, Agr Prod Proc Design & Res Inst, Haikou 571100, Hainan, Peoples R China
关键词： Soybean protein isolate; Furan flavor compounds; Flavor simulation; Interaction mechanism; Molecular dynamics simulations
期刊名称：FOOD CHEMISTRY （ 影响因子：8.8； 五年影响因子：8.6 ）
ISSN： 0308-8146
年卷期： 2024 年 451 卷
页码：
收录情况： SCI
摘要： 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.
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