Analysis of the coupled transport, reaction, and deactivation phenomena in the immobilized glucose oxidase and catalase system.
In a previous paper, the overall or macrokinetics of the immobilized glucose oxidase--catalase system has been presented. In this paper a detailed analysis of the interaction of diffusion and reaction in this system will be presented. The mathematical treatment includes two consecutive reactions with two-substrate kinetics. Furthermore, the deactivation of both enzymes due to the intermediate product peroxide is taken into account. The predicted results suggest that the efficiency of the glucose oxidase reaction depends on the concentration ranges of the two substrates. Furthermore, the external mass-transfer rate may cause a shift from glucose limitation to oxygen limitation. The efficiency of the coupled system is always higher than that predicted for the uncoupled reaction path. The calculations show that the economics of the coupled system depend a great deal on the deactivation of the enzymes.
D001692:Biological Transport; D002374:Catalase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005949:Glucose Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008956:Models, Chemical
D004800:Enzymes, Immobilized; D006861:Hydrogen Peroxide; D005949:Glucose Oxidase; D002374:Catalase