Hydroperoxidase activity of soybean lipoxygenase in reverse micelles
Abstract The rate of aminopyrine oxidation in the presence of H 2 O 2 by the hydroperoxidase activity of soybean lipoxygenase was studied as a function of micelle size ( ω 0 ) and water content ( θ ) in sodium dioctyl sulfosuccinate (AOT) reverse micelles in isooctane. When the micelle size was changed at a fixed water content a saturation activity profile was obtained, but when both micelle size and water content were changed at the same time, a bell-shaped profile was observed. These results indicate that only one micellar parameter ( ω 0 or θ ) has to be changed at a time in order to avoid artefactual enzymatic behaviour.