化学 杨梅素 石英晶体微天平 圆二色性 葡聚糖 色谱法 大豆蛋白 生物化学 有机化学 类黄酮 吸附 山奈酚 抗氧化剂
作者
Dan Lei,Junsheng Li,Chao Zhang,Shuyi Li,Zhenzhou Zhu,Feifei Wang,Qianchun Deng,Nabil Grimi
出处
期刊：Food Chemistry: X [Elsevier]
日期：2022-08-10 卷期号：15: 100426-100426 被引量：21
摘要
The complexation of soybean protein isolate (SPI) with β-glucan (DG) and myricetin (MC) was focused in this study. UV-Vis, circular dichroism and 3D fluorescence analysis jointly proved that interaction with DG and MC altered the structures of SPI, whose β-sheet decreased to 29 % and random coil increased to 35 %, respectively. Moreover, the microenvironment of tryptophan and tyrosine from protein were changed. The ternary complex performed a different molecular weight distribution, showing a larger molecular weight of 1.17×106 g/mol compared with SPI verified by gel permeation chromatography (GPC). And it was further evidenced by Quartz Crystal Microbalance with Dissipation (QCM-D) and molecular docking that glycinin (11S) possessed a better affinity toward DG and MC compared with β-conglycinin (7S), which indicated stronger binding ability through hydrogen bonds. The successful preparation of SPI-DG-MC complex will advance the application of soybean resource as a functional food ingredient.
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