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n -Butanol is generated as a natural product of metabolism by several microorganisms, but almost all grow at mesophilic temperatures. A synthetic pathway forn -butanol production from acetyl coenzyme A (acetyl-CoA) that functioned at 70°C was assembledin 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] fromCaldanaerobacter subterraneus subsp.tengcongensis ;trans -2-enoyl-CoA reductase [Ter] fromSpirochaeta thermophila ; bifunctional acetaldehyde dehydrogenase/alcohol dehydrogenase [AdhE] fromClostridium thermocellum ; and AdhE, aldehyde dehydrogenase [Bad], and butanol dehydrogenase [Bdh] fromThermoanaerobacter sp. strain X514) were utilized to examine three possible pathways forn -butanol. These pathways differed in the two steps required to convert butyryl-CoA ton -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 toin vitro experiments, was used to determine relative enzyme ratios needed to maximizen -butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, &gt;70% conversion ton -butanol was observedin vitro , but with a 60% decrease in the predicted pathway flux. With more-selective hypothetical versions of Bad and Bdh, &gt;70% conversion ton -butanol is predicted, with a 19% increase in pathway flux. Thus, more-selective thermophilic versions of Bad, Bdh, and AdhE are needed to fully exploit biocatalyticn -butanol production at elevated temperatures.

applied and environmental microbiology

Alcohol Selectivity in a Synthetic Thermophilic <i>n</i> -Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes

Alcohol Selectivity in a Synthetic Thermophilic n -Butanol Pathway Is Driven by Biocatalytic and Thermostability Characteristics of Constituent Enzymes