Digital simulation of homogeneous enzyme kinetics for amperometric redox-enzyme electrodes
β Scribed by F. Battaglini; E.J. Calvo
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 773 KB
- Volume
- 258
- Category
- Article
- ISSN
- 0003-2670
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β¦ Synopsis
An explmt pomt method IS described for dwtal snnulatlon of redox-enzyme catalysis and diffislon at soluble-enzyme electrodes Two experImenta conchtlons (chronopotentlometry and open-arcmt potential decay) were sunulated for a two-substrate enzyme (glucose oxldase) catalyzing the anaerobic oxidation of glucose, mechated by a soluble redox couple Tramlent and steady-state responses are compared to expernnental data and to prechctlons of the analyhcal solutions for selected cases Smmlated steady-state concentration profiles near the electrode surface are analyzed for dflerent values of KS/C, and K&C, The vahdlty of hnear Lmeweaver-Burk plots for the amperometnc response of enzyme electrodes IS &cussed &ywor& Amperometry, Enzyme electrodes, Glucose oxldase, DigItal slmulatlon
π SIMILAR VOLUMES
This paper describes an amperometric enzyme electrode for the rapid determination of theophylline in serum. The method is based on the catalysed oxidation of theophylline by the haem-containing enzyme theophylline oxidase. Results are presented for two approaches. First, ferrocene monocarboxylic aci