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Effects of thermal sterilization on soy protein isolate/polyphenol complexes: Aspects of structure, in vitro digestibility and antioxidant activity
Food Research International ( IF 7.0 ) Pub Date : 2018-06-19 , DOI: 10.1016/j.foodres.2018.06.034
Cong Ren , Wenfei Xiong , Dengfeng Peng , Yun He , Peiyuan Zhou , Jing Li , Bin Li

The main purpose of this work was to investigate the influence of typical thermal sterilization approaches (pasteurization, high-temperature sterilization) on the structure, in vitro digestibility, and antioxidant activity of soy protein isolate (SPI)/black soybean seed coat extract (BE) complexes at pH 7.0. The results of zeta potential and particle size demonstrated that the addition of BE was contributed to inhibit protein thermal aggregation. Heat sterilization resulted in protein unfolding revealed by UV–Vis, circular dichroism, and fluorescence spectroscopy analysis. The increase of BE led to the reduction of fluorescence intensity and surface hydrophobicity of SPI. Moreover, the formation of SPI/BE complexes inhibited protein digestion in vitro, while thermal sterilization promoted protein digestion. The SPI/BE complexes showed a strong radical scavenging ability both before and after thermal treatment.



中文翻译:

热灭菌对大豆分离蛋白/多酚复合物的影响:结构,体外消化率和抗氧化活性方面

这项工作的主要目的是研究典型的热灭菌方法(巴氏灭菌,高温灭菌)对大豆分离蛋白(SPI)/黑大豆种皮提取物(BE)的结构,体外消化率和抗氧化活性的影响。 )pH 7.0下的络合物。zeta电位和粒径的结果表明,BE的添加有助于抑制蛋白质的热聚集。加热灭菌导致蛋白质的展开,这是通过紫外可见光谱,圆二色性和荧光光谱分析得出的。BE的增加导致SPI的荧光强度和表面疏水性降低。此外,SPI / BE复合物的形成抑制了体外蛋白质的消化,而热灭菌促进了蛋白质的消化。

更新日期:2018-06-19
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