Applied Microbiology and Biotechnology

, Volume 100, Issue 6, pp 2685–2692 | Cite as

FudC, a protein primarily responsible for furfural detoxification in Corynebacterium glutamicum

  • Yota Tsuge
  • Motonori Kudou
  • Hideo Kawaguchi
  • Jun Ishii
  • Tomohisa Hasunuma
  • Akihiko KondoEmail author
Biotechnologically relevant enzymes and proteins


Lignocellulosic hydrolysates contain compounds that inhibit microbial growth and fermentation, thereby decreasing the productivity of biofuel and biochemical production. In particular, the heterocyclic aldehyde furfural is one of the most toxic compounds found in these hydrolysates. We previously demonstrated that Corynebacterium glutamicum converts furfural into the less toxic compounds furfuryl alcohol and 2-furoic acid. To date, however, the genes involved in these oxidation and reduction reactions have not been identified in the C. glutamicum genome. Here, we show that Cgl0331 (designated FudC) is mainly responsible for the reduction of furfural into furfuryl alcohol in C. glutamicum. Deletion of the gene encoding FudC markedly diminished the in vivo reduction of furfural to furfuryl alcohol. Purified His-tagged FudC protein from Escherichia coli was also shown to convert furfural into furfuryl alcohol in an in vitro reaction utilizing NADPH, but not NADH, as a cofactor. Kinetic measurements demonstrated that FudC has a high affinity for furfural but has a narrow substrate range for other aldehydes compared to the protein responsible for furfural reduction in E. coli.


Corynebacterium glutamicum Furfural Furfuryl alcohol Alcohol dehydrogenase NADPH 



We are grateful to Shoko Miyazaki, Yoshimi Hori, and Kumiko Yoshihara for providing technical assistance on the construction of plasmids and strains, GC-MS analysis, and protein purification and enzyme assay, respectively. This work was supported by the Commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade, and Industry (METI), Japan, and was also supported in part by Special Coordination Funds for Promoting Science and Technology, Creation of Innovation Centers for Advanced Interdisciplinary Research Areas (Innovative Bioproduction, Kobe). This work was also supported in part by Grant-in-Aid for Young Scientists (B) to YT from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan.

Compliance with ethical standards

Conflict of Interests

All the authors declare that they have no conflict of interests.

Ethical approval

This study does not contain any studies with human participants or animals performed by any of the authors.


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Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  • Yota Tsuge
    • 1
  • Motonori Kudou
    • 1
  • Hideo Kawaguchi
    • 2
  • Jun Ishii
    • 1
  • Tomohisa Hasunuma
    • 1
  • Akihiko Kondo
    • 2
    • 3
    Email author
  1. 1.Organization of Advanced Science and TechnologyKobe UniversityKobeJapan
  2. 2.Department of Chemical Science and Engineering, Graduate School of EngineeringKobe UniversityKobeJapan
  3. 3.Biomass Engineering Program, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-kuYokohamaJapan

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