A model was developed to describe the conversion degree in a membrane bioreactor (MBR) for the synthesis of short-chain esters as a function of the flow rate. The transesterification reaction was catalyzed by a recombinant cutinase of Fusarium solani pisi microencapsulated in reversed micelles of AOT/isooctane. The differences of product concentration in permeate and retentate together with the deactivation profiles led to an enzyme distribution evaluation that describes the experimental values attained. The model considers the bioreactor design as well as its hydrodynamics and the enzyme kinetics. The approach included the analysis of the MBR operation as a CSTR, a PFR, and a series of continuous reactors. The comparative efficiency of these reactor types is discussed. The enzyme distribution was estimated for all the cases. The best description was obtained considering a series of two CSTRs. The modeling results led to a re-evaluation of cutinase operational stability. Deactivation rates correlated very well with the hydrodynamic aspects of biocatalyst location. (C) 2000 John Wiley & Sons, Inc.