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

Cassidy, Jennifer; Paradisi, Francesca

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.

Citation

Cassidy, J., & Paradisi, F. (2018). Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH). Molecular Biotechnology, 60(6), 420-426. https://doi.org/10.1007/s12033-018-0083-6

• Journal Article Type: Article
• Acceptance Date: Apr 4, 2018
• Online Publication Date: Apr 13, 2018
• Publication Date: Jun 1, 2018
• Deposit Date: Apr 16, 2018
• Publicly Available Date: Apr 14, 2019
• Journal: Molecular Biotechnology
• Print ISSN: 1073-6085
• Electronic ISSN: 1559-0305
• Publisher: Springer Verlag
• Peer Reviewed: Peer Reviewed
• Volume: 60
• Issue: 6
• Pages: 420-426
• DOI: https://doi.org/10.1007/s12033-018-0083-6
• Keywords: Haloquadratum walsbyi; Alcohol dehydrogenase; Thermoactivity; Dual cofactor specificity
• Public URL: https://nottingham-repository.worktribe.com/output/961240
• Publisher URL: https://link.springer.com/article/10.1007%2Fs12033-018-0083-6
• 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