Deactivation studies of immobilized glucose oxidase

✍ Scribed by S. Krishnaswamy; J. R. Kittrell

• Publisher: John Wiley and Sons
• Year: 1978
• Tongue: English
• Weight: 560 KB
• Volume: 20
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260200605

✦ Synopsis

Abstract

Studies have been performed in a tubular flow reactor to characterize the deactivation of immobilized glucose oxidase. The effects of oxygen concentration in the range of 0.09 to 0.467m__M__ and hydrogen peroxide concentrations in the range of 0.1 to 10m__M__ were studied. A simple mathematical model assuming first‐order reaction and deactivation was found to describe the deactivation behavior adequately. The deactivation rate constant was found to increase with increasing levels of feed oxygen. Hydrogen peroxide was found to deactivate the enzyme severely and the deactivation rate constants were higher than those for oxygen deactivation. The influence of external and internal diffusion effects on the deactivation rate constant were examined. Although diffusional restrictions were negligible for oxygen transfer to the pellet, they were significant for transfer of hydrogen peroxide to the bulk stream. Increasing deactivation rates. Severe internal diffusion limitations were observed for the glucose oxidase system. However, for particle sizes in the range of 500 to 2000 μm, no effect on the rate of deactivation of the enzyme was observed.