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Reduction of furan derivatives by overexpressing NADH-dependent Adh1 improves ethanol fermentation using xylose as sole carbon source with Saccharomyces cerevisiae harboring XR-XDH pathway.
Appl Microbiol Biotechnol. 2013 Mar; 97(6):2597-607.AM

Abstract

Several alcohol dehydrogenase (ADH)-related genes have been identified as enzymes for reducing levels of toxic compounds, such as, furfural and/or 5-hydroxymethylfurfural (5-HMF), in hydrolysates of pretreated lignocelluloses. To date, overexpression of these ADH genes in yeast cells have aided ethanol production from glucose or glucose/xylose mixture in the presence of furfural or 5-HMF. However, the effects of these ADH isozymes on ethanol production from xylose as a sole carbon source remain uncertain. We showed that overexpression of mutant NADH-dependent ADH1 derived from TMB3000 strain in the recombinant Saccharomyces cerevisiae, into which xylose reductase (XR) and xylitol dehydrogenase (XDH) pathway of Pichia stipitis has been introduced, improved ethanol production from xylose as a sole carbon source in the presence of 5-HMF. Enhanced furan-reducing activity is able to regenerate NAD(+) to relieve redox imbalance, resulting in increased ethanol yield arising from decreased xylitol accumulation. In addition, we found that overexpression of wild-type ADH1 prevented the more severe inhibitory effects of furfural in xylose fermentation as well as overexpression of TMB3000-derived mutant. After 120 h of fermentation, the recombinant strains overexpressing wild-type and mutant ADH1 completely consumed 50 g/L xylose in the presence of 40 mM furfural and most efficiently produced ethanol (15.70 g/L and 15.24 g/L) when compared with any other test conditions. This is the first report describing the improvement of ethanol production from xylose as the sole carbon source in the presence of furan derivatives with xylose-utilizing recombinant yeast strains via the overexpression of ADH-related genes.

Authors+Show Affiliations

Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23001007

Citation

Ishii, Jun, et al. "Reduction of Furan Derivatives By Overexpressing NADH-dependent Adh1 Improves Ethanol Fermentation Using Xylose as Sole Carbon Source With Saccharomyces Cerevisiae Harboring XR-XDH Pathway." Applied Microbiology and Biotechnology, vol. 97, no. 6, 2013, pp. 2597-607.
Ishii J, Yoshimura K, Hasunuma T, et al. Reduction of furan derivatives by overexpressing NADH-dependent Adh1 improves ethanol fermentation using xylose as sole carbon source with Saccharomyces cerevisiae harboring XR-XDH pathway. Appl Microbiol Biotechnol. 2013;97(6):2597-607.
Ishii, J., Yoshimura, K., Hasunuma, T., & Kondo, A. (2013). Reduction of furan derivatives by overexpressing NADH-dependent Adh1 improves ethanol fermentation using xylose as sole carbon source with Saccharomyces cerevisiae harboring XR-XDH pathway. Applied Microbiology and Biotechnology, 97(6), 2597-607. https://doi.org/10.1007/s00253-012-4376-6
Ishii J, et al. Reduction of Furan Derivatives By Overexpressing NADH-dependent Adh1 Improves Ethanol Fermentation Using Xylose as Sole Carbon Source With Saccharomyces Cerevisiae Harboring XR-XDH Pathway. Appl Microbiol Biotechnol. 2013;97(6):2597-607. PubMed PMID: 23001007.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reduction of furan derivatives by overexpressing NADH-dependent Adh1 improves ethanol fermentation using xylose as sole carbon source with Saccharomyces cerevisiae harboring XR-XDH pathway. AU - Ishii,Jun, AU - Yoshimura,Kazuya, AU - Hasunuma,Tomohisa, AU - Kondo,Akihiko, Y1 - 2012/09/22/ PY - 2012/07/12/received PY - 2012/08/14/accepted PY - 2012/08/13/revised PY - 2012/9/25/entrez PY - 2012/9/25/pubmed PY - 2013/8/22/medline SP - 2597 EP - 607 JF - Applied microbiology and biotechnology JO - Appl Microbiol Biotechnol VL - 97 IS - 6 N2 - Several alcohol dehydrogenase (ADH)-related genes have been identified as enzymes for reducing levels of toxic compounds, such as, furfural and/or 5-hydroxymethylfurfural (5-HMF), in hydrolysates of pretreated lignocelluloses. To date, overexpression of these ADH genes in yeast cells have aided ethanol production from glucose or glucose/xylose mixture in the presence of furfural or 5-HMF. However, the effects of these ADH isozymes on ethanol production from xylose as a sole carbon source remain uncertain. We showed that overexpression of mutant NADH-dependent ADH1 derived from TMB3000 strain in the recombinant Saccharomyces cerevisiae, into which xylose reductase (XR) and xylitol dehydrogenase (XDH) pathway of Pichia stipitis has been introduced, improved ethanol production from xylose as a sole carbon source in the presence of 5-HMF. Enhanced furan-reducing activity is able to regenerate NAD(+) to relieve redox imbalance, resulting in increased ethanol yield arising from decreased xylitol accumulation. In addition, we found that overexpression of wild-type ADH1 prevented the more severe inhibitory effects of furfural in xylose fermentation as well as overexpression of TMB3000-derived mutant. After 120 h of fermentation, the recombinant strains overexpressing wild-type and mutant ADH1 completely consumed 50 g/L xylose in the presence of 40 mM furfural and most efficiently produced ethanol (15.70 g/L and 15.24 g/L) when compared with any other test conditions. This is the first report describing the improvement of ethanol production from xylose as the sole carbon source in the presence of furan derivatives with xylose-utilizing recombinant yeast strains via the overexpression of ADH-related genes. SN - 1432-0614 UR - https://www.unboundmedicine.com/medline/citation/23001007/Reduction_of_furan_derivatives_by_overexpressing_NADH_dependent_Adh1_improves_ethanol_fermentation_using_xylose_as_sole_carbon_source_with_Saccharomyces_cerevisiae_harboring_XR_XDH_pathway_ L2 - https://dx.doi.org/10.1007/s00253-012-4376-6 DB - PRIME DP - Unbound Medicine ER -