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Published May 15, 2012 | Accepted Version + Supplemental Material
Journal Article Open

Bilirubin oxidase from Bacillus pumilus: a promising enzyme for the elaboration of efficient cathodes in biofuel cells

Abstract

A CotA multicopper oxidase (MCO) from Bacillus pumilus, previously identified as a laccase, has been studied and characterized as a new bacterial bilirubin oxidase (BOD). The 59 kDa protein containing four coppers, was successfully over-expressed in Escherichia coli and purified to homogeneity in one step. This 509 amino-acid enzyme, having 67% and 26% sequence identity with CotA from Bacillus subtilis and BOD from Myrothecium verrucaria, respectively, shows higher turnover activity towards bilirubin compared to other bacterial MCOs. The current density for O(2) reduction, when immobilized in a redox hydrogel, is only 12% smaller than the current obtained with Trachyderma tsunodae BOD. Under continuous electrocatalysis, an electrode modified with the new BOD is more stable, and has a higher tolerance towards NaCl, than a T. tsunodae BOD modified electrode. This makes BOD from B. pumilus an attractive new candidate for application in biofuel cells (BFCs) and biosensors.

Additional Information

© 2012 Elsevier. Received 24 November 2011, Revised 6 February 2012, Accepted 16 February 2012, Available online 25 February 2012. This work was supported by a European Young Investigator Award (EURYI), la Région Aquitaine, a France-Stanford grant, and by National Institutes of Health grant no. DK-31450.

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Accepted Version - nihms-491697.pdf

Supplemental Material - 1-s2.0-S0956566312001121-mmc1.doc

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August 22, 2023
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