ENZYME-MICROENVIRONMENT DYNAMIC INTERACTIONS IN MICROSTRUCTURED MEDIA

A new approach for the study of an enzyme's relationship with its own reaction medium is described. The microheterogeneous (micellar and liquid crystalline) media octyl-beta-D-glucoside/water (or glucose in water)/octanol plus the enzyme beta-D-Glucosidase were used to study enzyme-microenvironment dynamic interactions. Beta-D-Glucosidase hydrolyses octyl-beta-D-glucoside to form glucose and octanol. So doing, it could cause a transition from a one-phase domain of the diagram to a polyphasic system. Starting from each homogeneous region of the phase diagram, the enzyme, due to its catalytic activity, was responsible for different phase changes. The physicochemical properties of the medium changed in proportion to the progress of the enzymatic reaction. The modifications of the microenvironment were correlated with kinetic patterns specific for each phase exploration. Enzymatic reaction rate modifications occuring during the transitions were function of the different microstructured phases in presence but they were also dependent on local concentration and disponibility of octyl-beta-D-glucoside monomer.