Isolation and purification of PQQ-dependent lactate dehydrogenase from Gluconobacter and use for direct electron transfer at carbon and gold electrodes

This research details the isolation and purification of a new type of lactate dehydrogenase that is dependent upon the coenzyme pyrroloquinoline quinone (PQQ). PQQ-dependent enzymes have been of interest in the literature over the last decade due to the fact that many of them can undergo direct elec...

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Bibliographic Details
Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2008-11, Vol.74 (1), p.73-77
Main Authors: Treu, Becky L., Minteer, Shelley D.
Format: Article
Language:English
Subjects:
Bioelectric Energy Sources
Biofuel cells
Biosensing Techniques - instrumentation
Biosensing Techniques - methods
Carbon
Direct electron transfer
Electrodes
Electron Transport
Gluconobacter
Gluconobacter - enzymology
Gluconobacter suboxydans
Gold
L-Lactate Dehydrogenase - isolation & purification
L-Lactate Dehydrogenase - metabolism
Lactate dehydrogenase
PQQ Cofactor
Pyrroloquinoline quinone
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Summary:This research details the isolation and purification of a new type of lactate dehydrogenase that is dependent upon the coenzyme pyrroloquinoline quinone (PQQ). PQQ-dependent enzymes have been of interest in the literature over the last decade due to the fact that many of them can undergo direct electron transfer (DET) at electrode surfaces which is of interest for biosensor and biofuel cell applications. In the paper, we detail the isolation of PQQ-dependent lactate dehydrogenase (PQQ-LDH) from two sources of Gluconobacter (Gluconobacter sp. 33 and Gluconobacter suboxydans). This paper also shows the first evidence that PQQ-LDH can undergo direct electron transfer at gold and carbon electrode surfaces for future use in biosensors and biofuel cells.
ISSN:1567-5394
1878-562X
DOI:10.1016/j.bioelechem.2008.07.005