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。
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.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2006年第5期72-76,共5页
Food Science
基金
国家自然科学基金项目(20476040)
教育部留学回国人员基金资助项目(教外司留[2003]406号)
