大豆蛋白的酶解聚集研究

Glycinin(11S), β-conglycinin(7S) and soy protein isolate (SPI) respectively were hydrolyzed using papain in this paper. The yield of the supernatant and the change of degree of hydrolysis were used to characterize the aggregation behavior during the hydrolysis. We analyzed some relevant properties of the supernatant and precipitation to investigate aggregation mechanism simply. The result showed that the yield of supernatant fluid was higher than that of 11S. Papain had stronger enzymatic hydrolysis ability to7S than 11S.The content of hydrophobic substance was higher than that of supernatant. Aggregates of 7S and SPI are mainly composed of peptides with molecular weight less than 5kDa while 11S main contains larger fraction more than 10kDa due to protein-peptide interaction. The findings of non-reducing and reducing pattern of tricine-SDS-PAGE also indicated the existence of disulfide bonds in the aggregates.The results can be used as a theoretical guidance for the regulation of the aggregation of soybean protein hydrolysates and the development of peptides.