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Ethyl cinnamate, an ester known asflavor and fragrance compound,has been synthesized using two immobilized bioreactor systems, batchand fluidized bed bioreactors. The enzyme used for this synthesisis a commercial lipase B preparation, Novozyme 435. Initial kineticstudies were conducted in both employed bioreactor configurations,and kinetic constants were obtained. Several models were tried forfitting of experimental data, but the best fit, for both bioreactors,was obtained when the ping-pong bi-bi mechanism was used. Interestinglyenough, ethanol inhibition occurred in batch bioreactor, but it didnot exist in the fluidized bed bioreactor. Solid–liquid masstransfer coefficients were calculated for both bioreactors to determinewhether mass transfer limitations existed in either of these systems.The calculation of Damköhler numbers and Thiele modulus confirmedthat mass transfer limitations had no effect on the overall reactionin both bioreactors. [ABSTRACT FROM AUTHOR]