ABSTRACT
A general procedure has been developed to model the behaviour of enzymatic reactions in a membrane bioreactor. This procedure unifies the kinetics of the reaction and the adsorption of the enzyme or enzymatic complexes on the membrane, enabling the selection of the most appropriate kinetic model. The general procedure proposed has been particularized and applied to experimental results obtained with two enzymatic reactions carried out in a hollow-fibre reactor, enzymatic hydrolysis of lactose by beta-galactosidase and glucose-fructose isomerization by glucose isomerase. The application of the general model has allowed us to determine the mechanism of the reaction for both kinetic reactions, assuming the adsorption of the enzymatic complex EGa for lactose hydrolysis and the adsorption of the free enzyme onto the membrane for glucose-fructose isomerization.
