pH feedback control of enzyme membranes

pH feedback on immobilized enzymes is theoretically examined with respect to substrate and pH levels, strength of acids produced by the reaction, buffering and asymmetry of the system. All the productions of proton by the different reactions are taken into account by using a 'symbolic species' H. The system of differential diffusion-reaction equations is then integrated using numerical methods. The local 'effective enzyme activity' modulated by an acidity factor enables us to predict and quantify evolutions of the systems: NonMichaelian behavior of an immobilized Michaelis-Menten-type enzyme is shown, even when pH back-actions are excluded; the analysis of intramembrane pH profiles shows that the shift of the optimal pH is a complex function of the substrate and pH levels, the intrinsic pH dependence of the enzyme, and the membrane characteristics. This study may easily be transposed to other types of effector such as divalent cations and used in examining self-regulations of multienzyme systems where pH-active reactions are involved.