Modeling of enzymatic esterification kinetics with respect to the substrates ratio

Enzymatic esterification in reversed micelle system is presented. The initial reaction rate has its local maximum at equimolar initial ratio of alcohol to acid for each one of the studied acid concentrations. Modelling of this phenomenon is made based on Michaelis-Menten equation for Ping-Pong Bi-Bi mechanism. One variable in this equation changes with the initial acid concentration while the other is set to alter with the ratio of alcohol to acid and its deviation from the determined optimal value of 1. The observed inhibition by the acid is considered. The effect of acid dilution when the initial water concentration in the reversed micelle system is increased is also taken into account. The kinetic parameters are determined graphically. The modelled rate dependences on the substrates ratio are compared to the measured data. Suggestions for further model development are made.