Insight into the interaction mechanism of γ-aminobutyric acid with soybean protein isolate by in vitro, multi-spectral and in silico analyses

作者：Yifan Cui, Nan Ma, Xinxu Yan, Boya Zhang, Yuhan Lan, Xibo Wang, Qingshan Chen · 发表于：LWT · 年份：2025 · DOI：10.1016/j.lwt.2025.117996 · 被引用次数：6 · 研究领域：GABA and Rice Research、Food composition and properties、Probiotics and Fermented Foods

In this study, the mechanism of interaction between soybean protein isolate (SPI) and γ-aminobutyric acid (GABA) was investigated and its structural and functional properties were characterized. The findings demonstrated that the incorporation of GABA induced alterations in both the secondary and tertiary structures of SPI. The interaction between GABA and SPI is spontaneous and exothermic, primarily driven by hydrogen bonds and van der Waals forces. Compared to the 7S protein and GABA, the 11S protein forms a more compact and stable molecular structure than 7S and GABA, and the introduction of GABA increases the emulsification and foaming properties of SPI, while reducing particle size and improving antioxidant properties. These results provide new insights into the interaction mechanism between GABA and SPI and highlight the associated structural and functional modifications, thereby providing a theoretical basis for improving the application of plant proteins such as SPI and the development of GABA-rich protein products.