General theory of determining intraparticle active immobilized enzyme distribution and rate parameters.
A general theory is presented in this article for determining the intrinsic rate constants for the main reaction and deactivation reaction, the effective diffusivity of the substrate, and the active enzyme distribution within porous solid supports from deactivation study of a continuous stirred-basket reactor (CSBR). For the parallel deactivation five reaction kinetics are considered: (a) Michaelis-Menten, (b) substrate inhibition, (c) product inhibition (competitive), (d) product inhibition (anticompetitive), and (e) zero-order kinetics. The experimental results of the system of hydrogen-peroxide-immobilized catalase on controlled-pore glass particles are analyzed to demonstrate the application of the theory developed for parallel deactivation of active immobilized enzyme (IME). For series deactivation only first-order kinetics is treated, and a numerical procedure is proposed to deter mine the rate parameters and the internal active enzyme distribution. The experimental data of the system of glucose-immobilized glucose oxidase on silica-alumina and controlled-pore glass particles are used to verify the theory.
Hossain
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Department of Chemical Engineering, University of Queensland, St. Lucia, Queensland 4067, Australia.
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