研究了温度和浓度对大豆分离蛋白(SPI)溶解性的影响,并用SDS-PAGE电泳分析了其可溶部分中亚基的组成及聚集方式。结果表明,热诱导大豆蛋白聚集生成了可溶聚集体,使得低浓度热处理后完全变性的SPI具有良好的溶解性。
The effects of tempetrature and concentration on the solubility of soy protein isolates (SPI) were studied, and then the subunit compositions and form of aggregation of soluble fractions obtained from treated SPI were analyzed by SDS-PAGE. The results showed that the totally denatured SPI after thermal treatment at low concentration have good solubility due to formation of heat-induced soluble protein aggregates.