Haloquadratum walsbyi Yields a Versatile, NAD+/NADP+ Dual Affinity, Thermostable, Alcohol Dehydrogenase (HwADH)


This study presents the first example of an alcohol dehydrogenase (ADH) from the halophilic archaeum Haloquadratum walsbyi (HwADH). A hexahistidine-tagged recombinant HwADH was heterologously overexpressed in Haloferax volcanii. HwADH was purified in one step and was found to be thermophilic with optimal activity at 65 °C. HwADH was active in the presence of 10% (v/v) organic solvent. The enzyme displayed dual cofactor specificity and a broad substrate scope, and maximum activity was detected with benzyl alcohol and 2-phenyl-1-propanol. HwADH accepted aromatic ketones, acetophenone and phenylacetone as substrates. The enzyme also accepted cyclohexanol and aromatic secondary alcohols, 1-phenylethanol and 4-phenyl-2-butanol. H. walsbyi may offer an excellent alternative to other archaeal sources to expand the toolbox of halophilic biocatalysts.

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Alcohol dehydrogenase


Immobilised metal-affinity chromatography




Sodium dodecyl sulphate–polyacrylamide gel electrophoresis




Benzyl alcohol












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The authors wish to acknowledge the support from the Synthesis and Solid State Pharmaceutical Centre and Science Foundation Ireland, Grant Number 12/RC/2275, and Dr. Thorsten Allers for useful discussions.

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Correspondence to Francesca Paradisi.

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Cassidy, J., Paradisi, F. Haloquadratum walsbyi Yields a Versatile, NAD+/NADP+ Dual Affinity, Thermostable, Alcohol Dehydrogenase (HwADH). Mol Biotechnol 60, 420–426 (2018). https://doi.org/10.1007/s12033-018-0083-6

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  • Haloquadratum walsbyi
  • Alcohol dehydrogenase
  • Thermoactivity
  • Dual cofactor specificity