Electrochemical and biosensing properties of an FAD-dependent glucose dehydrogenase from Trichoderma virens

Bioelectrochemistry. 2023 Oct:153:108480. doi: 10.1016/j.bioelechem.2023.108480. Epub 2023 May 29.

Abstract

We investigated the bioelectrochemical properties of an FAD-dependent glucose dehydrogenase from Trichoderma virens (TvGDH) and its electrochemical behaviour when immobilized on a graphite electrode. TvGDH was recently shown to have an unusual substrate spectrum and to prefer maltose over glucose as substrate, and hence could be of interest as recognition element in a maltose sensor. In this study, we determined the redox potential of TvGDH, which is -0.268 ± 0.007 V vs. SHE, and advantageously low to be used with many redox mediators or redox polymers. The enzyme was entrapped in, and wired by an osmium redox polymer (poly(1-vinylimidazole-co-allylamine)-{[Os(2,2'-bipyridine)2Cl]Cl}) with formal redox potential of +0.275 V vs. Ag|AgCl via poly(ethylene glycol) diglycidyl ether crosslinking onto a graphite electrode. When the TvGDH-based biosensor was tested with maltose it showed a sensitivity of 1.7 μA mM-1cm-2, a linear range of 0.5-15 mM, and a detection limit of 0.45 mM. Furthermore, it gave the lowest apparent Michaelis-Menten constant (KM app) of 19.2 ± 1.5 mM towards maltose when compared to other sugars. The biosensor is also able to detect other saccharides including glucose, maltotriose and galactose, these however also interfere with maltose sensing.

Keywords: Amperometry; FAD-dependent glucose dehydrogenase; GMC oxidoreductases; Maltose biosensor; Osmium polymer; Trichoderma virens.

MeSH terms

  • Biosensing Techniques*
  • Electrodes
  • Enzymes, Immobilized
  • Glucose
  • Glucose 1-Dehydrogenase / chemistry
  • Graphite*
  • Hypocrea*
  • Maltose
  • Oxidation-Reduction
  • Polymers / chemistry

Substances

  • Glucose 1-Dehydrogenase
  • Graphite
  • Maltose
  • Glucose
  • Polymers
  • Enzymes, Immobilized