Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH)

Cassidy, Jennifer and Paradisi, Francesca (2018) Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH). Molecular Biotechnology, 60 (6). pp. 420-426. ISSN 1559-0305

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Abstract

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, 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.

Item Type: Article
RIS ID: https://nottingham-repository.worktribe.com/output/961240
Additional Information: This is a post-peer-review, pre-copyedit version of an article published in Molecular Biotechnology. The final authenticated version is available online at: http://dx.doi.org/10.1007/s12033-018-0083-6
Keywords: Haloquadratum walsbyi; Alcohol dehydrogenase; Thermoactivity; Dual cofactor specificity
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Chemistry
Identification Number: https://doi.org/10.1007/s12033-018-0083-6
Depositing User: Smith, Ruth
Date Deposited: 16 Apr 2018 13:20
Last Modified: 04 May 2020 19:50
URI: http://eprints.nottingham.ac.uk/id/eprint/51157

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