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 op...
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| Format: | Article |
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Springer
2018
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| Online Access: | https://eprints.nottingham.ac.uk/51157/ |
| _version_ | 1848798430747426816 |
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| author | Cassidy, Jennifer Paradisi, Francesca |
| author_facet | Cassidy, Jennifer Paradisi, Francesca |
| author_sort | Cassidy, Jennifer |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T20:19:39Z |
| format | Article |
| id | nottingham-51157 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T20:19:39Z |
| publishDate | 2018 |
| publisher | Springer |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-511572020-05-04T19:50:51Z https://eprints.nottingham.ac.uk/51157/ Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) Cassidy, Jennifer Paradisi, Francesca 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. Springer 2018-06 Article PeerReviewed 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 Haloquadratum walsbyi; Alcohol dehydrogenase; Thermoactivity; Dual cofactor specificity https://link.springer.com/article/10.1007%2Fs12033-018-0083-6 doi:10.1007/s12033-018-0083-6 doi:10.1007/s12033-018-0083-6 |
| spellingShingle | Haloquadratum walsbyi; Alcohol dehydrogenase; Thermoactivity; Dual cofactor specificity Cassidy, Jennifer Paradisi, Francesca Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title | Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title_full | Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title_fullStr | Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title_full_unstemmed | Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title_short | Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH) |
| title_sort | haloquadratum walsbyi yields a versatile, nad+/nadp+ dual affinity, thermostable, alcohol dehydrogenase (hwadh) |
| topic | Haloquadratum walsbyi; Alcohol dehydrogenase; Thermoactivity; Dual cofactor specificity |
| url | https://eprints.nottingham.ac.uk/51157/ https://eprints.nottingham.ac.uk/51157/ https://eprints.nottingham.ac.uk/51157/ |