Analysis of an immobilised enzyme reactor with catalysts activation

We investigate the behavior of a reaction described by Michaelis-Menten kinetics in an immobilized enzyme reactor (IER). The IER is treated as a well stirred flow reactor, in which the immobilized bounded and unbounded enzyme species are constrained to remain within the reaction vessel. The product species leaves the IER in the reactor outflow. Before the substrate can react with the enzyme, the enzyme must first be activated by absorption of an activator. We use steady state analysis to identify the best operating conditions or the reactor. To this end, we show that the concentration of product is maximized at low residence time whereas the productivity of the reactor is maximized at high residence times.