Lipase reaction in AOT-isooctane reversed micelles : effect of water on equilibria

Abstract

Equations corresponding to a two-substrate, second-order reversible model are derived and used for further analysis. The progress curves predicted from the rate equations agree very well with the experimental results under various reaction conditions. The values of the molar ratio of water to surfactant (R) which maximize the initial reaction rate and maximum fractional conversion is predictable from the derived rate equations and the resulting relationship between R and the kinetic constants. The effect of water on equilibria for hydrolytic reaction in reversed micelles has been investigated using lipase as a model enzyme.