ArticleExtremophiles : life under extreme conditions2013
Effect of organic solvents on the activity and stability of halophilic alcohol dehydrogenase (ADH2) from Haloferax volcanii.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 46 citations in OpenAlex.
- Biochemical properties of glycerol kinase from the hypersaline-adapted archaeonApplied and environmental microbiology · 2025Article
- Potassium binding by carbonyl clusters, halophilic adaptation and catalysis of Haloferax mediterranei D-2-hydroxyacid dehydrogenase.Communications biology · 2025Article
- Pharmaceutical applications of halophilic enzymes.Heliyon · 2025Review
- Ion-combination specific effects driving the enzymatic activity of halophilic alcohol dehydrogenase 2 fromRSC sustainability · 2024Article
- Exploring Oxidoreductases from Extremophiles for Biosynthesis in a Non-Aqueous System.International journal of molecular sciences · 2023Review
- Directed evolution engineering to improve activity of glucose dehydrogenase by increasing pocket hydrophobicity.Frontiers in microbiology · 2022Article
- Halophilic archaea and their potential to generate renewable fuels and chemicals.Biotechnology and bioengineering · 2021Review
- Haloferax volcanii for biotechnology applications: challenges, current state and perspectives.Applied microbiology and biotechnology · 2020Review
- Biosynthesis of butyl esters from crude oil of palm fruit and kernel using halophilic lipase secretion by3 Biotech · 2019Article
- Haloferax volcanii as immobilised whole cell biocatalyst: new applications for halophilic systems.Applied microbiology and biotechnology · 2019Article
- Haloquadratum walsbyi Yields a Versatile, NADMolecular biotechnology · 2018Article
- Engineering substrate promiscuity in halophilic alcohol dehydrogenase (HvADH2) by in silico design.PloS one · 2017Article
- Bioinspired Immobilization of Glycerol Dehydrogenase by Metal Ion-Chelated Polyethyleneimines as Artificial Polypeptides.Scientific reports · 2016Article
- Asymmetric reduction of ketones and β-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum.Applied microbiology and biotechnology · 2015Article
- Effect of organic solvents on the structure and activity of moderately halophilic Bacillus sp. EMB9 protease.Extremophiles : life under extreme conditions · 2014Article
- Covalent immobilization of alcohol dehydrogenase (ADH2) from Haloferax volcanii: how to maximize activity and optimize performance of halophilic enzymes.Molecular biotechnology · 2014Article
- Protective role of salt in catalysis and maintaining structure of halophilic proteins against denaturation.Frontiers in microbiology · 2014Review
- Heterologous overexpression, purification and characterisation of an alcohol dehydrogenase (ADH2) from Halobacterium sp. NRC-1.Molecular biotechnology · 2013Article
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2 authors at 1 institution in 1 country.
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Abstract
The effect of various organic solvents on the catalytic activity, stability and substrate specificity of alchohol dehydrogenase from Haloferax volcanii (HvADH2) was evaluated. The HvADH2 showed remarkable stability and catalysed the reaction in aqueous-organic medium containing dimethyl sulfoxide (DMSO) and methanol (MeOH). Tetrahydrofuran and acetonitrile were also investigated and adversely affected the stability of the enzyme. High concentration of salt, essential to maintain the enzymatic activity and structural integrity of the halophilic enzyme under standard conditions may be partially replaced by DMSO and MeOH. The presence of organic solvents did not induce gross changes in substrate specificity. DMSO offered a protective effect for the stability of the enzyme at nonoptimal pHs such as 6 and 10. Salt and solvent effects on the HvADH2 conformation and folding were examined through fluorescence spectroscopy. The fluorescence findings were consistent with the activity and stability results and corroborated the denaturing properties of some solvents. The intrinsic tolerance of this enzyme to organic solvent makes it highly attractive to industry.
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