Analysis of immobilised multi-enzyme reaction systems with Michaelis-Menten kinetics

Abstract

The consecutive sequence of reactions S → P₁ → P₂ taking place inside a permeable spherical particle is analysed for the case in which the enzyme-catalysed steps in the reaction follow Michaelis-Menten type kinetics. The case in which each step in the reaction is inhibited by its product is also considered. The theoretical analysis takes into account both interparticle and intraparticle diffusional limitations and utilises an orthogonal collocation technique to obtain the effectiveness factor and selectivity of the reaction sequence. The orthogonal collocation method is found to be both convenient and simple and the analysis should prove useful in the design of immobilised multi-enzyme reactors.