| Literature DB >> 21036156 |
Fabien Durand1, Claire Stines-Chaumeil, Victoria Flexer, Isabelle André, Nicolas Mano.
Abstract
We report for the first time a soluble PQQ-glucose dehydrogenase that is twice more active than the wild type for glucose oxidation and was obtained by combining site directed mutagenesis, modelling and steady-state kinetics. The observed enhancement is attributed to a better interaction between the cofactor and the enzyme leading to a better electron transfer. Electrochemical experiments also demonstrate the superiority of the new mutant for glucose oxidation and make it a promising enzyme for the development of high-performance glucose biosensors and biofuel cells.Entities:
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Year: 2010 PMID: 21036156 DOI: 10.1016/j.bbrc.2010.10.102
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575