AbstractThe kinetics of the maltose hydrolysis by means of free and immobilized in polyacrylamide gel glucoamylase has been investigated. The kinetic constants in theMichaelis‐Menten'sequation have been determined. In the case of immobilized enzyme two different methods have been used, the one giving intrinsic constant values and the other – affected by the diffusion resistances. The obtained kinetic parameters were compared with these determined for free enzyme system.A mathematical model of the process has been constructed. The inhibition effect of the product and the reversibility of the reaction have been taken into account. The model has been solved using already determined kinetics parameters. Very good correlation between calculated and experimental data was fo