大豆蛋白
化学
乳状液
色氨酸
酪氨酸
蛋白质三级结构
二硫键
荧光
色谱法
生物化学
氨基酸
量子力学
物理
作者
Jiang Jiang,Jie Chen,Youling L. Xiong
摘要
Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h) in acidic (pH 1.5−3.5) and alkaline (pH 10.0−12.0) pH solutions, followed by refolding (1 h) at pH 7.0, was analyzed. Changes in emulsifying properties of treated SPI were then examined. The pH-shifting treatments resulted in a substantial increase in protein surface hydrophobicity, intrinsic tryptophan fluorescence intensity, and disulfide-mediated aggregation, along with the exposure of tyrosine. After the pH-shifting processes, soy protein adopted a molten globule-like conformation that largely maintained the original secondary structure and overall compactness but lost some tertiary structure. These structural modifications, consequently, led to markedly improved emulsifying activity of SPI as well as the emulsion stability.
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