Abstract

Effects of limited enzymatic hydrolysis with pepsin and/or high-pressure homogenization in acid condition on the functional properties and structure characteristic of soybean protein isolate (SPI) were investigated. Functional properties, including protein solubility, surface hydrophobicity, particle size distribution, the ability of resisting freezing/thawing, foaming properties and dynamic surface properties were evaluated. Result showed that, single acid treatment could improve functional properties of SPI, but was not as effective as single or combined pepsin hydrolysis and high-pressure homogenization in acid condition. Emulsibility, the ability of resisting freezing/thawing and foaming capacity of soybean proteins were remarkably improved by the combination treatment, but no improvement of foaming stability was detected. Changes of structures were detected by surface hydrophobicity, and hydrodynamic diameter. It was found that aggregates existed in all treated samples. Besides, more flexible and soluble aggregates were observed in samples treated by limited pepsin proteolysis, high-pressure homogenization and the combination treatments, which might contribute to their functional properties.

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