Abstract
ABSTRACTThe mass transfer and kinetic properties of both soluble and immobilized β‐galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading.
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