Consecutive immobilized enzymatic reactions with and without enzyme denaturation.

Consecutive biochemical reactions in an immobilized enzyme particle under the effects of internal and external diffusional resistances are analyzed. A rigorous nonlinear reaction kinetics is employed and the steady state effectiveness factor with negligible enzyme denaturation compared with the previous prediction by the first-order kinetics. It is found that the difference between them is rather substantial under most circumstances. The cases with significant enzyme denaturation are also investigated by using an unsteady state model. The substrate concentration responses to variation of the physical and kinetic parameters reveal many interesting characteristics of the reaction system.