Determination of the inherent deactivation characteristics for the parallel poisoning of immobilized catalase

✍ Scribed by Nguyen M. Tai; P. F. Greenfield

• Publisher: John Wiley and Sons
• Year: 1981
• Tongue: English
• Weight: 715 KB
• Volume: 23
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260230411

✦ Synopsis

Abstract

An approximate analytical solution which describes the deactivation of catalase immobilized on porous supports is provided. Catalase was chosen as an example of an enzyme which undergoes parallel poisoning. The solution incorporates the effects of pore diffusion and of the parallel poisoning. The solution incorporates the effects of pore diffusion and of the parallel poisoning of catalase by its substrate hydrogen peroxide into a time dependent effectiveness factor which can then be inserted into the appropriate reactor equations. The model was tested by measuring experimentally the deactivation of immobilized catalase in both a packed bed reactor and a continuous stirred basket reactor and was found to be very satisfactory at inlet substrate concentrations of less than 0.02__M__. Values of the deactivation rate constant obtained by regression analysis were independent of particle type and size and reactor description indicating that they were in fact inherent characteristics of the immobilized enzymes which are immobilized on supports and which undergo substrate or parallel poisoning.