Soy protein isolate was acylated with succinic anhydride and acetic anhydride. The functional properties are markedly improved by acylation of the $\varepsilon$-amino groups. Acylation of the available amino groups shifted the isoelectric point from 4.5 to 4.0 and enhanced the solubility between pH 4.0-6.0. In the 0.03M-$CaCl_2$ solution the solubility of the modified soy protein is much larger than that of the unmodified protein above the isoelectric point. The emulsion properties and foaming properties also improved by the modification and the effects of pH on the properties paralleled its effect on protein solubility. The changes of reduced viscosity with concentration followed Huggin's equation and by modification the intrinsic viscosity of the soy protein increased and the interaction coefficient decreased.