Effects of simultaneous internal and external mass transfer and product inhibition on immobilized enzyme-catalyzed reactor

A mathematical model has been developed for predicting the performance and simulation of a packed bed immobilized enzyme reactor performing lactose hydrolysis, which follows Michaelis-Menten kinetics with competitive product (galactose) inhibition. The performance characteristics of a packed bed immobilized enzyme reactor have been analyzed taking into account the simultaneous effects of internal and external mass transfer limitations. The model design equations are then solved by the method of weighted residuals such as Galerkin's method and orthogonal collocation on finite elements. The effects of simultaneous internal and external mass transfer coupled with product inhibition have been studied and their effects were shown to reduce internal effectiveness factor. The effects of product inhibition have been investigated at different operating conditions correlated at different regimes using dimensionless β_xo (St, Bi, θ, φ). Product inhibition was shown to reduce substrate conversion, and to decrease effectiveness factor when β_s > β_xo; however, it increases internal effectiveness factor when β_s < β_xo. The effectiveness factor is found to be independent of product inhibition at crossover point at which β_xo is defined. Effects of St and Bi have been investigated at different kinetic regimes and the results show their effects have a strong dependence on kinetic parameters θ, γ (i.e. K_m/K_p) and β_xo. The dimensionless residence time at crossover point, β_xo, has been correlated with kinetic and mass transfer parameters.