NAD(P)-dependent glucose dehydrogenase: Applications for biosensors, bioelectrodes, and biofuel cells

Bioelectrochemistry. 2020 Oct:135:107574. doi: 10.1016/j.bioelechem.2020.107574. Epub 2020 May 23.

Abstract

This review discusses the physical and chemical properties of nicotinamide redox cofactor dependent glucose dehydrogenase (NAD(P) dependent GDH) and its extensive application in biosensors and bio-fuel cells. GDHs from different organisms show diverse biochemical properties (e.g., activity and stability) and preferences towards cofactors, such as nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+). The (NAD(P)+) play important roles in biological electron transfer, however, there are some difficulties related to their application in devices that originate from their chemical properties and labile binding to the GDH enzyme. This review discusses the electrode modifications aimed at immobilising NAD+ or NADP+ cofactors and GDH at electrodes. Binding of the enzyme was achieved by appropriate protein engineering techniques, including polymerisation, hydrophobisation or hydrophilisation processes. Various enzyme-modified electrodes applied in biosensors, enzymatic fuel cells, and biobatteries are compared. Importantly, GDH can operate alone or as part of an enzymatic cascade, which often improves the functional parameters of the biofuel cell or simply allows use of cheaper fuels. Overall, this review explores how NAD(P)-dependent GDH has recently demonstrated high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices.

Keywords: Biofuel cell; Biosensor; Glucose; Glucose dehydrogenase; NAD; NAD(P).

Publication types

  • Review

MeSH terms

  • Bioelectric Energy Sources*
  • Biosensing Techniques*
  • Electrodes*
  • Glucose 1-Dehydrogenase / metabolism*
  • Limit of Detection
  • NADP / metabolism*
  • Thermodynamics

Substances

  • NADP
  • Glucose 1-Dehydrogenase