Experimental evaluation of the usefulness of equations describing the apparent maximum reaction rate and apparent Michaelis constant of an immobilized enzyme reaction.

To determine the usefulness of equations previously proposed for the apparent maximum reaction rate and apparent Michaelis constant of an immobilized enzyme, starch hydrolysis by glucoamylase immobilized on a porous ceramic support was considered as a model system. Initial reaction rates, v0, were measured for a wide range of initial starch concentrations, Sb0, to make a nonlinear plot of Sb0/v0 versus Sb0, and the apparent kinetic parameters were determined from the slopes and intercepts of tangents to the nonlinear plot at given values of Sb0. The equations were found to accurately express the diffusional effect on the kinetic parameters.