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An assay method in a reversed micellar system, which can be better characterized in physicochemical terms than that in an emulsion system, was investigated. The first-order rate constant when [S] « Km and the zero-order rate constant when [S]» Km for lipase reaction in the system show a linear relationship with enzyme concentration over a twenty-fold range, which is an important criterion for an enzyme assay. Based on the results, a three-point assay of lipase in reversed micelles was established. To ensure the initial rate, the assay time should be limited to the time during which about 4.5% of the substrate is utilized.

Determination of lipase activity in AOT-isooctane reversed micelles.