The design equation for a packed-bed immobilized enzyme reactor is expressed in terms of apparent kinetic parameters and the relationship between the exit concentration of substrate consumed and the logarithm of the exit unconverted fraction of substrate is studied. Agreement of calculated values wi
Determination of apparent kinetic parameters for competitive product inhibition in packed-bed immobilized enzyme reactors
✍ Scribed by Ahmet R. Özdural; Deniz Tanyolaç; İsmail H. Boyacı; Mehmet Mutlu; Colin Webb
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 215 KB
- Volume
- 14
- Category
- Article
- ISSN
- 1369-703X
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✦ Synopsis
In this study, a simple and effective technique for characterizing Michaelis-Menten type kinetics with competitive product inhibition in packed-bed re-circulated immobilized enzyme reactors is presented, where the use of nonlinear regression techniques for multi-parameter estimation are not required. In order to demonstrate the new technique introduced in this work, enzymatic conversion of lactose in a recycling packed-bed reactor is envisaged where -galactosidase (lactase, EC 3.2.1.23) enzyme is immobilized on a weak base ion exchanger resin (Duolite A 568). For the experimental conditions used in this research, the total competitive inhibition by product (galactose) model is sufficient to represent the lactose hydrolysis kinetics in a packed-bed reactor.
📜 SIMILAR VOLUMES
A graphical method of determining the Michaelis-Menten constant free of the external mass transfer resistance for a packed bed immobilized enzyme system was illustrated with examples from 3 different enzyme reactions. The intercept at the ordinate obtained by the straight line extrapolation of data