Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Designing a highly active soluble PQQ-glucose dehydrogenase for efficient glucose biosensors and biofuel cells.

Biochemical and biophysical research communications - 26 Nov 2010

Durand Fabien, Stines-Chaumeil Claire, Flexer Victoria, André Isabelle, Mano Nicolas

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biosensing Techniques
Share to Glucose

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis

Share to Mutation

Share to Protein Conformation

Share to Protein Engineering

Source

Identifiers

PMID: 21036156
DOI: 10.1016/j.bbrc.2010.10.102

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Designing a highly active soluble PQQ-glucose dehydrogenase for efficient glucose biosensors and biofuel cells.PMID 21036156Read ↗

Surface charge engineering of PQQ glucose dehydrogenase for downstream processing.Semantic proximity Read ↗

A mediator-adapted diaphorase variant for a glucose dehydrogenase-diaphorase biocatalytic system.Semantic proximity Read ↗

Does Acinetobacter calcoaceticus glucose dehydrogenase produce self-damaging H2O2?Semantic proximity Read ↗

Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values--site-directed mutagenesis studies on the putative active site.Semantic proximity Read ↗

Development of a Single Fluorescent Protein-Based Green Glucose Indicator by Semirational Molecular Design and Molecular Evolution.Semantic proximity Read ↗

A thermostable triple mutant of pyranose 2-oxidase from Trametes multicolor with improved properties for biotechnological applications.Semantic proximity Read ↗

Directed evolution of a formate dehydrogenase for increased tolerance to ionic liquids reveals a new site for increasing the stability.Semantic proximity Read ↗

Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design.Semantic proximity Read ↗

Engineering the respiratory complex I to energy-converting NADPH:ubiquinone oxidoreductase.Semantic proximity Read ↗

Enhanced catalytic performance and pH stability of Streptomyces Laccase Y230R and its degradation of malachite green.Semantic proximity Read ↗

Efficient direct electron transfer of PQQ-glucose dehydrogenase on carbon cryogel electrodes at neutral pH.Semantic proximity Read ↗

Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.