食品科学 ›› 2008, Vol. 29 ›› Issue (7): 106-108.

• 基础研究 • 上一篇    下一篇

热变性和热聚集对大豆分离蛋白溶解性的影响

叶荣飞,杨晓泉,郑田要,郑恒光,朱建华,刘翀,司华静   

  1. 华南理工大学轻工与食品学院食物蛋白工程研究中心; 华南理工大学轻工与食品学院食物蛋白工程研究中心 广东广州510640; 广东广州510640
  • 出版日期:2008-07-15 发布日期:2011-07-28

Effects of Thermal Denaturation and Aggregation on Solubility of Soy Protein Isolates

YE  Rong-Fei, YANG  Xiao-Quan, ZHENG  Tian-Yao, ZHENG  Heng-Guang, ZHU  Jian-Hua, LIU  Chong, SI  Hua-Jing   

  1. Research and Development Center of Food Proteins, College of Light Industry and Food, South China University of Technology, Guangzhou 510640, China
  • Online:2008-07-15 Published:2011-07-28

摘要: 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。

关键词: 大豆分离蛋白, 热处理, 溶解性, 变性, 聚集

Abstract: 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.

Key words: soy protein isolates (SPI), thermal treatment, solubility, denaturation, aggregation