Flow calorimetry was used for investigation of kinetic properties of glucoamylase covalently bound to controlled-pore glass particles. Maltodextrin hydrolysis was measured in steady-state (single flow mode) and in non-steady-state conditions (total recycling of the reaction solution). The experimental data were treated by mathematical modeling based on material and heat balances of the reaction system. The proposed technique enables to determine intrinsic kinetic parameters of enzyme reactions influenced by internal particle diffusion directly from calorimetric data.