Abstract
The rate of aminopyrine oxidation in the presence of H2O2 by the hydroperoxidase activity of soybean lipoxygenase was studied as a function of micelle size (ω0) 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 (ω0 or θ) has to be changed at a time in order to avoid artefactual enzymatic behaviour.
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