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完全热变性、可溶性大豆蛋白聚集物的溶解性质研究
引用本文:郑恒光,杨晓泉,林福珍.完全热变性、可溶性大豆蛋白聚集物的溶解性质研究[J].现代食品科技,2008,24(5):428-432.
作者姓名:郑恒光  杨晓泉  林福珍
作者单位:1. 华南理工大学食品蛋白研究工程中心,广东,广州,510640
2. 福建省粮油科学技术研究所,福建,福州,350002
摘    要:大豆分离蛋白在完全或部分热变性下仍可以保持较高的溶解性,这种类型的大豆蛋白在世界大豆蛋白工业中占据了重要地位.本研究发现:该类型的大豆分离蛋白的亚基之间是以共价键和非共价键相结合.其溶解性质与传统的低变性大豆分离相比:在饱和湿度加热条件下更容易丧失水溶性,在湿度为18%和50%下二者的变化趋势基本相同,盐溶性相对较差,含水乙醇对其溶解度的降低作用相对较弱,在65%乙醇溶液中加热溶解性非但不降低而且还大幅度升高.该研究成果对于大豆分离蛋白产品的开发以及大豆蛋白的基础研究都具有重要的借鉴意义.

关 键 词:热变性  完全热变性可溶性大豆蛋白聚集物  溶解性质
收稿时间:2008/1/21 0:00:00

Solubility of Fully Heat-denatured Soluble Soybean Protein Aggregates
ZHENG Heng-guang,YANG Xiao-quan,LIN Fu-zhen.Solubility of Fully Heat-denatured Soluble Soybean Protein Aggregates[J].Modern Food Science & Technology,2008,24(5):428-432.
Authors:ZHENG Heng-guang  YANG Xiao-quan  LIN Fu-zhen
Affiliation:(1.Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology, Guangzhou 510640, China); (2.Fujian Grain and Oil Science and Technology Research Institute, Fuzhou 350002, China)
Abstract:Fully or partially heat-denatured soybean protein isolate (DSPI) had high solubility, which took an important role in the soybean protein industry. Our research showed that the subunits of DSPI were combined with each other via covalent bands and non-covalent bands. The solubility of DSPI were reduced more easily than that of the traditional low denatured SPI by heating at 100% humidity But changes of their solubility were similar when they were heated at 18% or 50% humidity. The salt-solubility of DSPI was lower than that of the traditional low denatured SPI. Besides, aqueous ethanol could not obviously lower the solubility of DSPI. Heating DSPI in 65% ethanol may greatly improve its solubility. The results of this research had significant meaning for further basic researches and industrial application of soybean protein.
Keywords:heat-denature  fully denatured soluble soybean protein aggregates  solubility
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