Evaluation of intrinsic immobilized kinetics in hollow fiber reactor systems

摘要: Abstract Immobilized cell and enzyme hollow fiber reactors have been developed for a variety of biochemical biomedical applications. Reported mathematical models predicting substrate conversion in these limited accuracy because the use free-solution kinetic parameters. This paper describes method determining intrinsic kinetics enzymes immobilized reactor systems using model diffusion reaction porous media an optimization procedure to fit parameters experimental data. Two enzymes, thermophilic β-galactosidase that exhibits product inhibition L -lysine α-oxidase, were used analysis. The show immobilization enhanced activity while decreasing α-oxidase. Both had higher Km values than did soluble enzyme, indicating less affinity substrate. These results are illustrate significant improvement ability predict reactors.