Abstract: | The catalytic behaviors of α-chymotrypsin and of trypsin were studied in anionic AOT-isooctane-water and cationic CTAB-ROH-isooctane-water microemulsion systems. The effects of various parameters, such as the pH and the water content expressed in terms of the molar ratio wo = [H2O]/[Surfactant], on the enzyme activity, were examined. The kinetic constants were calculated and it was found that in the case of trypsin the enzyme exhibited a remarkable “superactivityrd, when studied in the CTAB microemulsion systems. The effect of the alcohol cosurfactant used in these cationic systems was investigated in relation to the polarity of the reaction medium. By using the hydrophilic probe 1-methyl-8-oxyquinolinium betaine the micropolarity of the water core was determined and related to the kinetic results. |