Immobilization of membrane-bounded (S)-mandelate dehydrogenase in sol–gel matrix for electroenzymatic synthesis

Membrane-bounded (S)-mandelate dehydrogenase has been immobilized on the surface of glassy carbon and carbon felt electrodes by encapsulation in a silica film obtained by sol–gel chemistry. Such bioelectrochemical system has been used for the first time for electroenzymatic conversion of (S)-mandeli...

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Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2015-08, Vol.104, p.65-70
Main Authors: Mazurenko, Ievgen, Ghach, Wissam, Kohring, Gert-Wieland, Despas, Christelle, Walcarius, Alain, Etienne, Mathieu
Format: Article
Language:English
Subjects:
Alcohol Oxidoreductases - chemistry
Alcohol Oxidoreductases - metabolism
Bioelectrochemical system
Carbon - chemistry
Electrochemistry
Electrodes
Electrosynthesis
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Glass - chemistry
Glyoxylates - chemistry
Mandelic Acids - chemistry
Membrane protein
Membranes, Artificial
Silicon Dioxide - chemistry
Sol–gel
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Summary:Membrane-bounded (S)-mandelate dehydrogenase has been immobilized on the surface of glassy carbon and carbon felt electrodes by encapsulation in a silica film obtained by sol–gel chemistry. Such bioelectrochemical system has been used for the first time for electroenzymatic conversion of (S)-mandelic acid to phenylglyoxylic acid. Apparent Km in this sol–gel matrix was 0.7mM in the presence of ferrocenedimethanol, a value in the same order of magnitude as reported previously for vesicles in solution with other electron acceptors, i.e., Fe(CN)63− or 2,6-dichloroindophenol. The bioelectrode shows very good operational stability for more than 6days. This stability was definitively improved by comparison to a bioelectrode prepared by simple adsorption of the proteins on the electrode surface (fast activity decrease during the first 15h of experiment). Optimal electroenzymatic reaction was achieved at pH9 and 40°C. Apparent Km of the protein activity was 3 times higher in carbon felt electrode than on glassy carbon surface, possibly because of transport limitations in the porous architecture of the carbon felt. A good correlation was found between electrochemical data and chromatographic characterization of the reaction products in the bioelectrochemical reactor. [Display omitted] •First immobilization of membrane-bounded dehydrogenase in sol-gel film on electrode•Apparent Km in this silica gel film was 0.7mM in the presence of ferrocenedimethanol•Optimal electroenzymatic reaction was achieved at pH 9 and 40°C•The protein was active in the silica gel for more than 6days of continuous use•Bioelectrochemical reactor achieved 94% of (S)-mandelate conversion within 9hours
ISSN:1567-5394
1878-562X
DOI:10.1016/j.bioelechem.2015.03.004