Alcohol Selectivity in a Synthetic Thermophilic n-Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes
Abstract
n-Butanol is generated as a natural product of metabolism by several microorganisms, but almost all grow at mesophilic temperatures. In this paper, a synthetic pathway for n-butanol production from acetyl coenzyme A (acetyl-CoA) that functioned at 70°C was assembled in vitro from enzymes recruited from thermophilic bacteria to inform efforts for engineering butanol production into thermophilic hosts. Recombinant versions of eight thermophilic enzymes (β-ketothiolase [Thl], 3-hydroxybutyryl-CoA dehydrogenase [Hbd], and 3-hydroxybutyryl-CoA dehydratase [Crt] from Caldanaerobacter subterraneus subsp. tengcongensis; trans-2-enoyl-CoA reductase [Ter] from Spirochaeta thermophila; bifunctional acetaldehyde dehydrogenase/alcohol dehydrogenase [AdhE] from Clostridium thermocellum; and AdhE, aldehyde dehydrogenase [Bad], and butanol dehydrogenase [Bdh] from Thermoanaerobacter sp. strain X514) were utilized to examine three possible pathways for n-butanol. These pathways differed in the two steps required to convert butyryl-CoA to n-butanol: Thl-Hbd-Crt-Ter-AdhE (C. thermocellum), Thl-Hbd-Crt-Ter-AdhE (Thermoanaerobacter X514), and Thl-Hbd-Crt-Ter-Bad-Bdh. n-Butanol was produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, was used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70%more »
- Authors:
-
- North Carolina State Univ., Raleigh, NC (United States). Dept. of Chemical and Biomolecular Engineering
- North Carolina State Univ., Raleigh, NC (United States). Dept. of Chemical and Biomolecular Engineering
- Univ. of Georgia, Athens, GA (United States). Dept. of Biochemistry and Molecular Biology
- Publication Date:
- Research Org.:
- North Carolina State University, Raleigh, NC (United States); Univ. of Georgia, Athens, GA (United States)
- Sponsoring Org.:
- USDOE Advanced Research Projects Agency - Energy (ARPA-E); National Science Foundation (NSF); National Inst. of Health (NIH) (United States)
- OSTI Identifier:
- 1470144
- Grant/Contract Number:
- AR0000081; CBET-1264052; CBET-1264053; 2T32GM008776
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Applied and Environmental Microbiology
- Additional Journal Information:
- Journal Volume: 81; Journal Issue: 20; Journal ID: ISSN 0099-2240
- Publisher:
- American Society for Microbiology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Loder, Andrew J., Zeldes, Benjamin M., Garrison, G. Dale, Lipscomb, Gina L., Adams, Michael W. W., and Kelly, Robert M. Alcohol Selectivity in a Synthetic Thermophilic n-Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes. United States: N. p., 2015.
Web. doi:10.1128/AEM.02028-15.
Loder, Andrew J., Zeldes, Benjamin M., Garrison, G. Dale, Lipscomb, Gina L., Adams, Michael W. W., & Kelly, Robert M. Alcohol Selectivity in a Synthetic Thermophilic n-Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes. United States. https://doi.org/10.1128/AEM.02028-15
Loder, Andrew J., Zeldes, Benjamin M., Garrison, G. Dale, Lipscomb, Gina L., Adams, Michael W. W., and Kelly, Robert M. Fri .
"Alcohol Selectivity in a Synthetic Thermophilic n-Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes". United States. https://doi.org/10.1128/AEM.02028-15. https://www.osti.gov/servlets/purl/1470144.
@article{osti_1470144,
title = {Alcohol Selectivity in a Synthetic Thermophilic n-Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes},
author = {Loder, Andrew J. and Zeldes, Benjamin M. and Garrison, G. Dale and Lipscomb, Gina L. and Adams, Michael W. W. and Kelly, Robert M.},
abstractNote = {n-Butanol is generated as a natural product of metabolism by several microorganisms, but almost all grow at mesophilic temperatures. In this paper, a synthetic pathway for n-butanol production from acetyl coenzyme A (acetyl-CoA) that functioned at 70°C was assembled in vitro from enzymes recruited from thermophilic bacteria to inform efforts for engineering butanol production into thermophilic hosts. Recombinant versions of eight thermophilic enzymes (β-ketothiolase [Thl], 3-hydroxybutyryl-CoA dehydrogenase [Hbd], and 3-hydroxybutyryl-CoA dehydratase [Crt] from Caldanaerobacter subterraneus subsp. tengcongensis; trans-2-enoyl-CoA reductase [Ter] from Spirochaeta thermophila; bifunctional acetaldehyde dehydrogenase/alcohol dehydrogenase [AdhE] from Clostridium thermocellum; and AdhE, aldehyde dehydrogenase [Bad], and butanol dehydrogenase [Bdh] from Thermoanaerobacter sp. strain X514) were utilized to examine three possible pathways for n-butanol. These pathways differed in the two steps required to convert butyryl-CoA to n-butanol: Thl-Hbd-Crt-Ter-AdhE (C. thermocellum), Thl-Hbd-Crt-Ter-AdhE (Thermoanaerobacter X514), and Thl-Hbd-Crt-Ter-Bad-Bdh. n-Butanol was produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, was used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol was observed in vitro, but with a 60% decrease in the predicted pathway flux. With more-selective hypothetical versions of Bad and Bdh, >70% conversion to n-butanol is predicted, with a 19% increase in pathway flux. Finally and thus, more-selective thermophilic versions of Bad, Bdh, and AdhE are needed to fully exploit biocatalytic n-butanol production at elevated temperatures.},
doi = {10.1128/AEM.02028-15},
journal = {Applied and Environmental Microbiology},
number = 20,
volume = 81,
place = {United States},
year = {Fri Aug 07 00:00:00 EDT 2015},
month = {Fri Aug 07 00:00:00 EDT 2015}
}
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