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In particular, the model is applied to the enzymatic production of benzaldehyde from mandelonitrile by <jats:italic>Prunus amygdalus<\/jats:italic> hydroxynitrile lyase (pa\u2010Hnl) adsorbed at the diisopropyl ether (DIPE)\/aqueous buffer interface (pH = 5.5). We quantitatively describe our previously obtained experimental kinetic results (Hickel et al., 1999; 2001), and we successfully account for the aqueous\u2010phase enzyme concentration dependence of product formation rates and the observed reaction rates at early times. Multilayer growth explains the early time reversibility of enzyme adsorption at the DIPE\/buffer interface observed by both enzyme\u2010activity and dynamic\u2010interfacial\u2010tension washout experiments that replace the aqueous enzyme solution with a buffer solution. The postulated explanation for the unusual stability of pa\u2010Hnl adsorbed at the DIPE\/buffer interface is attributed to a two\u2010layer adsorption mechanism. In the first layer, slow conformational change from the native state leads to irreversible attachment and partial loss of catalytic activity. In the second layer, pa\u2010Hnl is reversibly adsorbed without loss in catalytic activity. The measured catalytic activity is the combined effect of the deactivation kinetics of the first layer and of the adsorption kinetics of each layer. For the specific case of pa\u2010Hnl adsorbed at the DIPE\/buffer interface, this combined effect is nearly constant for several hours resulting in no apparent loss of catalytic activity. Our proposed kinetic model can be extended to other interfacially active enzymes and other organic solvents. Finally, we indicate how interfacial\u2010tension lag times provide a powerful tool for rational solvent selection and enzyme engineering. \u00a9 2002 Wiley Periodicals, Inc. 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