In this study, a simple and effective technique for characterizing Michaelis-Menten apparent kinetic parameters in packed-bed immobilized enzyme reactors is presented. The apparent kinetic parameters of immobilized glucose oxidase 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 experimental conditions, the immobilized enzyme Klmvalues in a packed-bed reactor were less than the soluble enzyme K1mvalue and were flow dependent. The value of Klmdecreased with increasing flow rate. © 2001 Elsevier Science Ltd. All rights reserved.
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