Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties

Abstract

In order to improve the functional properties of soybean protein isolates (SPI), microwave-assisted phosphorylation (MAP) was applied. The result showed that after microwaving at 600 W for 3 min, the phosphorylation level of SPI reached 35.72 mg/g, emulsifying activity and stability were increased 2 times and 1.4 times, respectively, the solubility was increased by 26.0% and the apparent viscosity was decreased by 13.5%. The charge density, content of sulfhydryl groups, and surface hydrophobicity increased significantly. The infra-red spectroscopic analysis indicated PO43-primary and lysine residues for phosphoric acid esterification. The change of amide bond É and fluorescence spectrum of variation suggested that the MAP made the secondary and tertiary structures of SPI into a compact conformation. Compared to the regular phosphorylation, the preparation time applied in MAP of SPI was much shorter. These results indicated that MAP can be used as an efficient method to improve the functional properties of SPI.