Transient response of bienzyme electrodes.
A mathematical model of the transient response of amperometric bienzyme electrodes with a consecutive, cyclic and parallel substrate conversion is developed. At high catalytic activity the kinetic behavior of consecutive and parallel conversion is close to the substance diffusion through the inert membrane, and the kinetics of cyclic conversion are 3.54 times slower. At low substrate conversion rates the electrodes' response is markedly retarded. Mathematical modeling results are compared with the experimental data on the kinetic behavior of amperometric enzyme electrodes in the membranes of which the consecutive and cyclic conversions of glucose and nicotinamide adenine dinucleotide, respectively, take place.
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D004566:Electrodes; D004800:Enzymes, Immobilized / Q000378:metabolism; D000431:Ethanol / Q000032:analysis*; D005947:Glucose / Q000032:analysis*; D005949:Glucose Oxidase / Q000378:metabolism*; D008433:Mathematics; D008962:Models, Theoretical; D010544:Peroxidases / Q000378:metabolism
D004800:Enzymes, Immobilized; D000431:Ethanol; D000426:Alcohol Dehydrogenase; D005949:Glucose Oxidase; D010544:Peroxidases; D005947:Glucose