Iwasa Hisanori, Hiratsuka Atsunori, Yokoyama Kenji, Uzawa Hirotaka, Orihara Kouhei, Muguruma Hitoshi
Nanomaterials Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 5-41, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan.
School of Bioscience and Biotechnology, Tokyo University of Technology, 1404-1 Katakura, Hachioji, Tokyo 192-0982, Japan.
ACS Omega. 2017 Apr 30;2(4):1660-1665. doi: 10.1021/acsomega.7b00277. Epub 2017 Apr 26.
Flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase (GDH) was identified and cloned from thermophilic filamentous fungi using the homology cloning method. A direct electron transfer bioanode composed of FAD-GDH and a single-walled carbon nanotube was produced. Enzymes from thermophilic microorganisms generally have low activity at ambient temperature; however, the FAD-GDH bioanode exhibits a large anodic current due to the enzymatic reaction (1 mA cm) at ambient temperature. Furthermore, the 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 FAD-GDHs expressed by various hosts influence the electrochemical properties of the bioanode.
采用同源克隆方法从嗜热丝状真菌中鉴定并克隆了黄素腺嘌呤二核苷酸（FAD）依赖性葡萄糖脱氢酶（GDH）。制备了一种由FAD-GDH和单壁碳纳米管组成的直接电子转移生物阳极。嗜热微生物的酶通常在环境温度下活性较低；然而，FAD-GDH生物阳极在环境温度下由于酶促反应（1 mA/cm²）而表现出较大的阳极电流。此外，FAD-GDH生物阳极在70℃下工作了12小时。这是首次报道具有来自嗜热微生物的葡萄糖催化酶的生物阳极，该生物阳极具有用于生物传感器和生物燃料电池应用的潜力。此外，我们展示了不同宿主表达的FAD-GDH糖型如何影响生物阳极的电化学性质。
