As the hydrolysis of starch by glucoamylase proceeds with stepwise removal of glucose units from the nonreducing ends of the starch chain, the number of available substrate molecules is essentially unchanged in the course of the degradation. In view of this aspect, a simple practical kinetic expression, which consists of a modified Michaelis-Menten form with product inhibition, is presented for the hydrolysis of soluble starch. It is assumed that the values of kinetic parameters V(m) and K(m) vary linearly from the values for starch toward those for maltose. The applicability of this kinetic expression is verified through the simulation with the experimental results for the hydrolysis of two soluble starches with different average molecular weights of 3 x 10(4) and 3 x 10(6).