Complexation of thermally-denatured soybean protein isolate with anthocyanins and its effect on the protein structure and in vitro digestibility
Complexation of thermally-denatured soybean protein isolate with anthocyanins and its effect on the protein structure and in vitro digestibility
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热变性大豆分离蛋白与花青素的络合及其对蛋白质结构和体外消化率的影响
DOI：
10.1016/j.foodres.2018.01.040
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发表时间：
2018-04-01
影响因子：
8.1
通讯作者：
Jiang, Lianzhou
中科院分区：
文献类型：
--
作者：
Zhang, Yan;Chen, Si;Jiang, Lianzhou
研究了富含花青素的黑米提取物（ARBRE）与大豆分离蛋白（SPI）在0、70、85和100℃下的络合作用及其对蛋白质消化率的影响。利用傅里叶变换红外光谱、圆二色光谱和荧光光谱研究了SPI与ARBRE相互作用过程中的结构变化。与ARBRE络合后，所有样品的SPI二级结构变化均表现为a-螺旋显著增加，β -sheet含量显著降低。结果还表明，ARBRE通过单个结合位点的静态猝灭来猝灭SPI荧光（在未加热和加热的样品中）。与ARBRE络合后，未加热和加热SPI的消化率均有所提高。SPI-ARBRE复合物的形成有利于大豆蛋白制品在食品中的应用，提高了其蛋白质的消化率和营养质量。
The complexation of anthocyanin-rich black rice extracts (ARBRE) with soybean protein isolate (SPI) heated at 0, 70, 85, and 100 degrees C and its effect on protein digestibility were studied. The structural changes of SPI during its interaction with ARBRE in all the samples were studied by Fourier transform infrared, circular dichroism, and fluorescence spectroscopy. The secondary structure changes of SPI in all the samples after complexation with ARBRE showed a significant increase in a-helix and a significant decrease in beta-sheet contents. Results also showed that ARBRE quenched the SPI fluorescence (in both unheated and heated samples) via static quenching with a single binding site. The digestibility of unheated and heated SPI was improved upon complexing with ARBRE. The formation of the SPI-ARBRE complexes is beneficial for the application of soy protein-based products in foods by increasing their protein digestibility and nutritional quality.