食品科学 ›› 2006, Vol. 27 ›› Issue (5): 72-76.

• 基础研究 • 上一篇    下一篇

两种大豆分离蛋白的比较研究

 黄友如, 华欲飞,  裘爱泳   

  1. 江南大学食品学院食品科学与安全教育部重点实验室
  • 出版日期:2006-05-15 发布日期:2011-09-16

Characteristics Comparative Study on Two Extraction Types of Soy Protein Isolates

 HUANG  You-Ru, HUA  Yu-Fei,   Qiu-Ai-Yong   

  1. Key Laboratory of Food Science and Safety, Ministry of Education, School of Food Science and Engineering, Southern Yangtze University, Wuxi 214036, China
  • Online:2006-05-15 Published:2011-09-16

摘要:  本文以醇洗豆粕为原料制备大豆分离蛋白(SPI-A),并将之与传统的碱溶酸沉工艺制备的大豆分离蛋白(SPI-C)作比较,发现脱脂豆粕经醇洗之后所制备的大豆分离蛋白,其功能性质明显优于传统的大豆分离蛋白。凝胶性能研究表明样品SPI-A的凝胶强度是385.4g,明显高于样品CSPI(85.4g);样品SPI-A的乳化和起泡性能也有明显的改善;HPLC研究表明SPI-A和SPI-C两种样品几乎在同一时间出峰,但激光光散射分析表明样品SPI-A的流体动力学半径远比样品SPI-C的大,说明样品SPI-A形成的聚集体体积较大,结构较为疏松,而样品SPI-C所形成的聚集体体积较小且结构较为致密。

关键词: 大豆分离蛋白, 乙醇, 功能性质, 凝胶, HPLC, 光散射

Abstract: Defatted soy flakes were washed with aqueous alcohol and the resultant material was extracted with water to prepare soy protein isolate (SPI-A) with improved functional properties in comparing with the conventional soy protein isolate(SPI-C)extracted directly from the alkaline low-denatured soy flakes. Gelling property was determined by rheometer at the protein concentration of 12% (W/W) while the gel fracture force of SPI-A was 385.4g, substantially higher than that of SPI-C (85.4g). Emulsifying and foaming stability were also found to be improved through alcohol washing. High performance size exclusion chromatography showed that when SPI-A and SPI-C were both eluted around the same time, the laser light scattering analysis indicated that SPI-A solution contains particles with larger hydrodynamic radius than SPI-C, suggesting that SPI-A forms larger protein aggregates with more flexible structure whereas SPI-C forms smaller and more compacted aggregates.

Key words: soy protein isolate, ethanol, functionality, gelation, HPLC, light scattering