Thermophilic Talaromyces emersonii Flavin Adenine Dinucleotide-Dependent Glucose Dehydrogenase Bioanode for Biosensor and Biofuel Cell Applications

Hisanori Iwasa; Atsunori Hiratsuka; Kenji Yokoyama; Hirotaka Uzawa; Kouhei Orihara; Hitoshi Muguruma

doi:10.1021/acsomega.7b00277

Thermophilic Talaromyces emersonii Flavin Adenine Dinucleotide-Dependent Glucose Dehydrogenase Bioanode for Biosensor and Biofuel Cell Applications

ACS Omega. 2017 Apr 30;2(4):1660-1665. doi: 10.1021/acsomega.7b00277. Epub 2017 Apr 26.

Authors

Hisanori Iwasa¹, Atsunori Hiratsuka¹, Kenji Yokoyama^{1

2}, Hirotaka Uzawa¹, Kouhei Orihara³, Hitoshi Muguruma³

Affiliations

¹ Nanomaterials Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 5-41, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan.
² School of Bioscience and Biotechnology, Tokyo University of Technology, 1404-1 Katakura, Hachioji, Tokyo 192-0982, Japan.
³ Graduate School of Engineering and Science, Shibaura Institute of Technology, 3-7-5 Toyosu, Koto, Tokyo 135-8548, Japan.

Abstract

Flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase (GDH) was identified and cloned from thermophilic filamentous fungi Talaromyces emersonii using the homology cloning method. A direct electron transfer bioanode composed of T. emersonii FAD-GDH and a single-walled carbon nanotube was produced. Enzymes from thermophilic microorganisms generally have low activity at ambient temperature; however, the T. emersonii FAD-GDH bioanode exhibits a large anodic current due to the enzymatic reaction (1 mA cm^-2) at ambient temperature. Furthermore, the T. emersonii FAD-GDH bioanode worked at 70 °C for 12 h. This is the first report of a bioanode with a glucose-catalyzing enzyme from a thermophilic microorganism that has potential for biosensor and biofuel cell applications. In addition, we demonstrate how the glycoforms of T. emersonii FAD-GDHs expressed by various hosts influence the electrochemical properties of the bioanode.