A new method for determination of apparent kinetics parameters in recirculating packed-bed immobilized enzyme reactors

In this study, a simple and effective technique for characterizing Michaeli s-Menten apparent kinetic parameters in packed-bed immobilized enzyme react ors is presented. The apparent kinetic parameters of immobilized glucose ox idase on weak base ion exchanger resin (Duolite A 568) were determined for different substrate flow rates in a recirculation system and compared with those for soluble glucose oxidase. It was observed that, for the experiment al conditions, the immobilized enzyme K-m' values in a packed-bed reactor w ere less than the soluble enzyme K-m value and were flow dependent. The val ue of K-m' decreased with increasing flow rate. (C) 2001 Elsevier Science L td. AH rights reserved.