University of Natural Resources and Life Sciences, Vienna (BOKU) - Research portal

Logo BOKU Resarch Portal

Selected Publication:

Stoica, L; Ruzgas, T; Ludwig, R; Haltrich, D; Gorton, L.
(2006): Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.
Langmuir. 2006; 22(25):10801-10806 FullText FullText_BOKU

Abstract:
This paper presents some functional differences as well as similarities observed when comparing the newly discovered cellobiose dehydrogenase (CDH) from Trametes Villosa (T.v) with the well-characterized one from Phanerochaete chrysosporium (P.c.). The enzymes were physically adsorbed on spectrographic graphite electrodes placed in an amperometric flow through cell connected to a flow system. In the case of T.v.-CDH-modified graphite electrodes, a high direct electron transfer (DET) current was registered at the polarized electrode in the presence of the enzyme substrate reflecting a very efficient internal electron transfer (IET) process between the reduced FAD-cofactor and the oxidized heme-cofactor. In the case of P.c.-CDH-modified graphite electrodes, the DET process is not as efficient, and the current will greatly increase in the presence of a mediator (mediated electron transfer, MET). As a consequence, when comparing the two types of enzyme-modified electrodes an inverted DET/MET ratio for T.v.-CDH is shown, in comparison with P.c.-CDH. The rates of the catalytic reaction were estimated to be comparable for both enzymes, by measuring the combined DET + MET currents. The inverted DET/MET ratio for T.v.-CDH-modified electrodes might suggest that probably there is a better docking between the two domains of this enzyme and that the linker region of P.c.-CDH might have an active role in modulating the rate of the IET (by changing the interdomain distance), with respect to pH. Based on the new properties of T.v.-CDH emphasized in the present study, an analytical application of a third-generation biosensor for lactose was recently published.
Authors BOKU Wien:
Haltrich Dietmar
Ludwig Roland
Find related publications in this database (using NML MeSH Indexing)
Adsorption -
Basidiomycota - enzymology
Biosensing Techniques - enzymology
Carbohydrate Dehydrogenases - chemistry
Electrons - chemistry
Graphite - chemistry
Hydrogen-Ion Concentration - chemistry
Models, Molecular - chemistry
Phanerochaete - enzymology
Sensitivity and Specificity - enzymology
Surface Properties - enzymology



Altmetric:
© BOKU Wien Imprint