Determination of immobilized enzyme apparent kinetic parameters in packed-bed reactors: Presentation of a new methodology

Abstract

A new explicit equation is proposed for the determination of immobilized enzyme apparent Michaelis–Menten kinetic parameters in packed-bed reactors. The mathematical analysis is based on recycling systems. The present methodology is easily applicable for a wide range of operating conditions. It is free from the probable limitations of the single-pass apparent immobilized enzyme kinetic parameter estimation technique that requires simultaneous measurement of column substrate inlet and effluent concentrations at a specified time. The experimental system is composed of a substrate reservoir and a circulating flow packed-bed immobilized enzyme reactor. The experimental data is gathered for glucose decomposition reaction in a recirculation system with immobilized glucose oxidase on a weak base ion exchanger resin. The apparent kinetic parameter, K ′ m values were calculated with a new explicit equation, proposed in this work, and they are found to be 0.48 × 10 −3 and 0.60 × 10 −3 mmol cm −3 for the recirculation rates of 75 and 25 cm 3 min −1, respectively.