消化(炼金术)
食品科学
化学
花青素
无规线圈
胃蛋白酶
热稳定性
猝灭(荧光)
大豆蛋白
颜料
疏水效应
生物化学
蛋白质二级结构
色谱法
荧光
酶
有机化学
物理
量子力学
作者
Zhen Ma,Jing Cheng,Shunshan Jiao,Pu Jing
摘要
Summary The interactions of anthocyanins and proteins might mutually influence each other on the physicochemical and functional properties. In this study, the interaction mechanism of soybean protein isolate (SPI) with mulberry anthocyanins (MA), and its effect on the thermal stability of anthocyanins and protein subunits’ digestibility were investigated through multiple spectroscopies and in vitro gastrointestinal models. Results showed that cyanidin‐3‐ O ‐glucoside (C3G), the main anthocyanin monomer in MA, could bind to SPI through hydrophobic interactions, resulting in static fluorescence quenching of SPI. The secondary structure of SPI changed by binding to C3G, with an increase of β‐sheet and a decrease of α‐helix and random coil. The formation of the SPI‐MA complexes improved the thermal stability of MA at 353 K, while, no significant protection occurred during heating at 368 K. Complexation with MA promoted the digestibility of SPI by pepsin, especially the α′ and α subunits of β‐conglycinin and the basic subunit of glycinin, and slightly delayed the digestibility of SPI under intestinal fluid. These results provide an in‐depth understanding of the influence of the protein‐anthocyanin interactions on the stability of anthocyanins and protein digestibility.
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