Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 100, Issue 6, Pages 2685-2692Publisher
SPRINGER
DOI: 10.1007/s00253-015-7115-y
Keywords
Corynebacterium glutamicum; Furfural; Furfuryl alcohol; Alcohol dehydrogenase; NADPH
Categories
Funding
- Commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from Ministry of Economy, Trade, and Industry (METI), Japan
- Special Coordination Funds for Promoting Science and Technology
- Creation of Innovation Centers for Advanced Interdisciplinary Research Areas (Innovative Bioproduction, Kobe)
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan
- Grants-in-Aid for Scientific Research [26870363] Funding Source: KAKEN
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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.
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