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Int J Mol Sci. 2021 Dec 17;22(24). doi: 10.3390/ijms222413570.

Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection.

International journal of molecular sciences

Takenori Satomura, Kohei Uno, Norio Kurosawa, Haruhiko Sakuraba, Toshihisa Ohshima, Shin-Ichiro Suye

Affiliations

  1. Division of Engineering, Faculty of Engineering, University of Fukui, Fukui 910-8507, Japan.
  2. Life Science Innovation Center, University of Fukui, Fukui 910-8507, Japan.
  3. Department of Applied Chemistry Biotechnology, Graduate School of Engineering, University of Fukui, Fukui 910-8507, Japan.
  4. Department of Science and Engineering for Sustainable Innovation, Faculty of Science and Engineering, Soka University, Tokyo 192-8577, Japan.
  5. Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, Takamatsu 761-0795, Japan.
  6. Department of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.

PMID: 34948373 PMCID: PMC8704557 DOI: 10.3390/ijms222413570

Abstract

Flavoenzyme dye-linked l-lactate dehydrogenase (Dye-LDH) is primarily involved in energy generation through electron transfer and exhibits potential utility in electrochemical devices. In this study, a gene encoding a Dye-LDH homolog was identified in a hyperthermophilic archaeon,

Keywords: FMN; dye-linked l-lactate dehydrogenase; heterogeneous expression; hyperthermophilic archaeon; thermostable enzyme

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