Amperometric determinations of reducing enzyme activities in living whole S. cerevisiae cells immobilized on micro-band electrodes
|Jenny Emnéus 1, Christer Spegel 5, Arto Heiskanen 1, Ted Johansson 2, Marie-Francoise Gorwa-Grauslund 2, Milena Koudelka 3, Tautgirdas Ruzgas 4|
1. Lund University, Department of Analytical Chemistry, Lund SE-221 00, Sweden
It was found that the amplitude of the yeast-catalysed amperometric signal was dependent on the metabolic pathway supplying the NAD(P)H, in the order; ethanol oxidation pathway(EOP) > pentose phosphate pathway (PPP) > glycolytic pathway (GP). An optimum in the apparent electrochemical Michaelis-Menten (MM) constants for intracellular DkR was found for an M concentration of 200 mM, i.e. a minimum in the apparent KM and optimum in apparent imax.
 A. Heiskanen, J. Yakovleva, C. Spégel, R. Taboryski, M. Koudelka-Hep, J, Emnéus, T, Ruzgas, Electrochem. Com., 6 (2004) 219.
Presentation: Poster at SMCBS'2005 Workshop, by Jenny Emnéus
See On-line Journal of SMCBS'2005 Workshop
Submitted: 2005-08-02 08:24 Revised: 2009-06-07 00:44
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