Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates

Achouri, A.; Zhang, W.; Xu, S.Y.

Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates

1998

Achouri, A. | Zhang, W. | Xu, S.Y.

Commercial defatted soy meal was solubilized in an aqueous solution at pH 8.5 to prepare a soy protein isolate (SPI) with 90.45% protein and 95% solubility. Soy protein hydrolysate (SPH) was obtained by enzymatic hydrolysis of the SPI using a neutral proteinase at different degrees of hydrolysis (DH = 4, 6, 8 and 10). A previous heat treatment of native SPI at 80 degrees C for 10 and 30 min caused a gradual dissociation and/or unfolding of some fractions of the soy protein leading to a decrease in high molecular weight fractions. Gel filtration chromatography of SPH with DH = 8 indicated that the soluble fraction consisted mostly of low molecular weight peptides having a molecular weight less than 12.5 kDa. Combined hydrolysis and succinylation greatly increased protein solubility and caused marked changes in other functional properties depending on the degree of modification.

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