Effects of mass-transfer resistance on apparent stability and performance of fixed-bed immobilized enzyme reactors: theory and experiments with immobilized invertase

Taking the hydrolysis of sucrose by invertase immobilized on anion-exchange resin as an example, the effects of mass-transfer resistance on the apparent stability of immobilized enzyme (IME) and the optimal policy for an IME reaction in a fixed-bed reactor have been studied theoretically and experimentally. The following results were obtained: (1) The effect of mass-transfer resistance on the effective deactivation rate of IME is summarized in two parameters concerning the intraparticle diffusion alpha(p) and the interparticle alpha(f). (2) At a constant processed amount of raw materials, there exists an optimal flow rate of reaction fluid to enhance the reactor performance while the mass-transfer resistance shifts the optimal point. (3) The intrinsic deactivation rate of IME has been estimated from the relationship between the fractional conversion at the reactor outlet and the operation time.