[Kinetic patterns of reactions with immobilized enzymes in open systems].

For studying the properties of immobilized enzyme, a flow reactor is suggested which provides ideal mixing of the reaction components with the granules of immobilized enzyme. To elucidate the mechanism of the reaction and to determine the effective values of maximal rates and Michaelis constants, an analysis of formal kinetic relationships describing the behaviour of the reactor in the stationary and non-stationary regimes has been carried out. The non-stationary kinetics is analyzed both for the case of step-wise and continuous supply of the substrate. A number of equations has been evolved which describe the time dependences of the concentrations of the substrate and reaction products; relationships have been found allowing determination of maximal rates and Michaelis constants from experimental data.