Solubility of Fully Heat-denatured Soluble Soybean Protein Aggregates
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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.
