Dataset Information

Dataset describing the amino acid catabolism of Thermoanaerobacter pseudethanolicus.

ABSTRACT: The dataset depicts the catabolism of branched-chain amino acids by Thermoanaerobacter pseudethanolicus in the presence of thiosulfate under different culture conditions. The results reveal that the strain can degrade all three branched-chain amino acids resulting in the production of their corresponding branched-chain fatty acids and branched-chain alcohols with the fatty acids always being the dominant product. The highest amounts of 2-methyl-1-butanol from isoleucine were at pH 6.5, liquid-gas ratio of 0.98, and at 20 mM thiosulfate concentration. A kinetic experiment of the branched-chain amino acids was done in the presence of thiosulfate as are data on selected enzyme activities related to alcohols and aldehydes. Finally, an NMR study using ¹³C1 methyl-1-butyrate during the degradation of leucine in the presence of thiosulfate was done to prove that the ¹³C1-methyl-1-butanol was indeed from its corresponding fatty acid.

SUBMITTER: Orlygsson J

PROVIDER: S-EPMC10792681 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature

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Dataset describing the amino acid catabolism of <i>Thermoanaerobacter pseudethanolicus</i>.

Orlygsson Johann J Scully Sean Michael SM

Data in brief 20231227

The dataset depicts the catabolism of branched-chain amino acids by <i>Thermoanaerobacter pseudethanolicus</i> in the presence of thiosulfate under different culture conditions. The results reveal that the strain can degrade all three branched-chain amino acids resulting in the production of their corresponding branched-chain fatty acids and branched-chain alcohols with the fatty acids always being the dominant product. The highest amounts of 2-methyl-1-butanol from isoleucine were at pH 6.5, li ...[more]

PMID: 38235181

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Project description:BackgroundChemical and physical pretreatment of lignocellulosic biomass improves substrate reactivity for increased microbial biofuel production, but also restricts growth via the release of furan aldehydes, such as furfural and 5-hydroxymethylfurfural (5-HMF). The physiological effects of these inhibitors on thermophilic, fermentative bacteria are important to understand; especially as cellulolytic strains are being developed for consolidated bioprocessing (CBP) of lignocellulosic feedstocks. Identifying mechanisms for detoxification of aldehydes in naturally resistant strains, such as Thermoanaerobacter spp., may also enable improvements in candidate CBP microorganisms.ResultsThermoanaerobacter pseudethanolicus 39E, an anaerobic, saccharolytic thermophile, was found to grow readily in the presence of 30 mM furfural and 20 mM 5-HMF and reduce these aldehydes to their respective alcohols in situ. The proteomes of T. pseudethanolicus 39E grown in the presence or absence of 15 mM furfural were compared to identify upregulated enzymes potentially responsible for the observed reduction. A total of 225 proteins were differentially regulated in response to the 15 mM furfural treatment with 152 upregulated versus 73 downregulated. Only 87 proteins exhibited a twofold or greater change in abundance in either direction. Of these, 54 were upregulated in the presence of furfural and 33 were downregulated. Two oxidoreductases were upregulated at least twofold by furfural and were targeted for further investigation. Teth39_1597 encodes a predicted butanol dehydrogenase (BdhA) and Teth39_1598, a predicted aldo/keto reductase (AKR). Both genes were cloned from T. pseudethanolicus 39E, with the respective enzymes overexpressed in E. coli and specific activities determined against a variety of aldehydes. Overexpressed BdhA showed significant activity with all aldehydes tested, including furfural and 5-HMF, using NADPH as the cofactor. Cell extracts with AKR also showed activity with NADPH, but only with four-carbon butyraldehyde and isobutyraldehyde.ConclusionsT. pseudethanolicus 39E displays intrinsic tolerance to the common pretreatment inhibitors furfural and 5-HMF. Multidimensional proteomic analysis was used as an effective tool to identify putative mechanisms for detoxification of furfural and 5-HMF. T. pseudethanolicus was found to upregulate an NADPH-dependent alcohol dehydrogenase 6.8-fold in response to furfural. In vitro enzyme assays confirmed the reduction of furfural and 5-HMF to their respective alcohols.

Dataset Information

Dataset describing the amino acid catabolism of Thermoanaerobacter pseudethanolicus.

Publications

Dataset describing the amino acid catabolism of <i>Thermoanaerobacter pseudethanolicus</i>.

Similar Datasets

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