On the basis of hydrogen peroxide decomposition process occurring in the bioreactor with fixed-bed of commercial catalase the optimal feed temperature was determined. This feed temperature was obtained by maximizing the time-average substrate conversion under constant feed flow rate and temperature constraints. In calculations, convection-diffusion-reaction immobilized enzyme fixed-bed bioreactor described by a coupled mass and energy balances as well as general kinetic equation for rate of enzyme deactivation was taken into consideration. This model is based on kinetic, hydrodynamic and mass-transfer parameters estimated in earlier work. The simulation showed that in the biotransformation with thermal deactivation of catalase optimal feed temperature is only affected by kinetic parameters for enzyme deactivation and decreases with increasing value of activation energy for deactivation. When catalase undergoes parallel deactivation the optimal feed temperature is strongly dependent on hydrogen peroxide feed concentration, feed flow rate and diffusional resistances expressed by biocatalyst effectiveness factor. It has been shown that the more significant diffusional resistances and the higher hydrogen peroxide conversions, the higher the optimal feed temperature is expected.
Optimal feed temperature was determined for a non-isothermal fixed-bed reactor performing hydrogen peroxide decomposition by immobilized Terminox Ultra catalase. This feed temperature was obtained by maximizing the average substrate conversion under constant feed flow rate and temperature constraints. In calculations, convection-diffusion-reaction immobilized enzyme fixed-bed reactor described by a set of partial differential equations was taken into account. It was based on kinetic, hydrodynamic and mass transfer parameters previously obtained in the process of H2O2 decomposition. The simulation showed the optimal feed temperature to be strongly dependent on hydrogen peroxide concentration, feed flow rate and diffusional resistances expressed by biocatalyst effectiveness factor.
It is known that external diffusional resistances are significant in immobilized enzyme packed-bed reactors, especially at large scales. Thus, the external mass transfer effects were analyzed for hydrogen peroxide decomposition by immobilized Terminox Ultra catalase in a packed-bed bioreactor. For this purpose the apparent reaction rate constants, kP, were determined by conducting experimental works at different superficial velocities, U, and temperatures. To develop an external mass transfer model the correlation between the Colburn factor, JD, and the Reynolds number, Re, of the type JD = K Re(n-1) was assessed and related to the mass transfer coefficient, kmL. The values of K and n were calculated from the dependence (am kp-1 - kR-1) vs. Re-1 making use of the intrinsic reaction rate constants, kR, determined before. Based on statistical analysis it was found that the mass transfer correlation JD = 0.972 Re-0.368 predicts experimental data accurately. The proposed model would be useful for the design and optimization of industrial-scale reactors.