ArticleExtremophiles : life under extreme conditions2010
Gene cloning and characterization of an aldehyde dehydrogenase from long-chain alkane-degrading Geobacillus thermoleovorans B23.
Article in Extremophiles : life under extreme conditions, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- Screening of molecular elements and improvement of heat resistance in a thermophilic bacterium.Engineering microbiology · 2025Article
- Extremozyme-Based Biosensors for Environmental Pollution Monitoring: Recent Developments.Biosensors · 2024Review
- Study of ALDH fromCells · 2021Article
- Effectiveness of3 Biotech · 2019Article
- Biodegradation of sulfamethazine by an isolated thermophile-Geobacillus sp. S-07.World journal of microbiology & biotechnology · 2017Article
- Cloning and expression of three ladA-type alkane monooxygenase genes from an extremely thermophilic alkane-degrading bacterium Geobacillus thermoleovorans B23.Extremophiles : life under extreme conditions · 2014Article
- Draft Genome Sequence of Geobacillus thermoleovorans Strain B23.Genome announcements · 2013Article
- Polysaccharide-degrading thermophiles generated by heterologous gene expression in Geobacillus kaustophilus HTA426.Applied and environmental microbiology · 2013Article
- Refolding of a thermostable glyceraldehyde dehydrogenase for application in synthetic cascade biomanufacturing.PloS one · 2013Article
- A toolkit to enable hydrocarbon conversion in aqueous environments.Journal of visualized experiments : JoVE · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Geobacillus thermoleovorans B23 is capable of degrading long-chain alkanes at 70 degrees C. Bt-aldh, an aldehyde dehydrogenase gene in B23, was located in the upstream region of p21 whose expression level was dramatically increased when alkane degradation was started (Kato et al. 2009, BMC Microbiol 9:60). Like p21, transcription level of Bt-aldh was also increased upon alkane degradation. Bt-Aldh (497 aa, MW = 53,886) was overproduced in Escherichia coli, purified, and characterized biochemically. Bt-Aldh acted as an octamer, required NAD(+) as a coenzyme, and showed high activity against aliphatic long-chain aldehydes such as tetradecanal. The optimum condition for activity was 50-55 degrees C and pH 10.0. The activity was elevated to two- to threefold in the presence of 2 mM Ba(2+), Ca(2+), or Sr(2+), while Mg(2+) and Zn(2+) inhibited the enzyme activity. Bt-Aldh represents thermophilic aldehyde dehydrogenases responsible for degradation of long-chain alkanes.
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