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。

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.