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  5. Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea
 
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Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea

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Download HmADH12 Extremophiles 2012.doc313.5 KB
Download HmADH12 Multiple Sequence Alignment.docSupporting information601 KB
Author(s)
Timpson, Leanne M. 
Alsafadi, Diya 
Mac Donnchadha, Cillin 
Liddell, Susan 
Sharkey, Michael A. 
Paradisi, Francesca 
Uri
http://hdl.handle.net/10197/3635
Date Issued
January 2012
Date Available
12T16:34:10Z June 2012
Abstract
Haloarchaeal alcohol dehydrogenases are of increasing interest as biocatalysts in the field of white biotechnology. In this study, the gene adh12 from the extreme halophile Haloarcula marismortui (HmADH12), encoding a 384 residue protein, was cloned into two vectors: pRV1 and pTA963. The resulting constructs were used to transform host strains Haloferax volcanii (DS70) and (H1209), respectively. Overexpressed His-tagged recombinant HmADH12 was purified by immobilized metal-affinity chromatography (IMAC). The His-tagged protein was visualized by SDS-PAGE, with a subunit molecular mass of 41.6 kDa, and its identity was confirmed by mass spectrometry. Purified HmADH12 catalyzed the interconversion between alcohols and aldehydes and ketones, being optimally active in the presence of 2 M KCl. It was thermoactive, with maximum activity registered at 60°C. The NADP(H) dependent enzyme was haloalkaliphilic for the oxidative reaction with optimum activity at pH 10.0. It favored a slightly acidic pH of 6.0 for catalysis of the reductive reaction. HmADH12 was significantly more tolerant than mesophilic ADHs to selected organic solvents, making it a much more suitable biocatalyst for industrial application.
Sponsorship
Science Foundation Ireland
Irish Research Council for Science, Engineering and Technology
Other Sponsorship
Merck
Islamic Development Bank
Type of Material
Journal Article
Publisher
Springer
Journal
Extremophiles
Volume
16
Issue
1
Start Page
57
End Page
66
Copyright (Published Version)
2012 Springer
Keywords
  • Alcohol dehydrogenase...

  • Biocatalysis

  • Extremophile

  • Halophile

  • Haloarcula marismortu...

  • Haloferax volcanii

  • Organic solvents

Subject – LCSH
Alcohol dehydrogenase
Enzymes
Extreme environments--Microbiology
Halophilic organisms
Organic solvents
DOI
10.1007/s00792-011-0405-0
Language
English
Status of Item
Peer reviewed
This item is made available under a Creative Commons License
https://creativecommons.org/licenses/by-nc-sa/1.0/
Owning collection
Chemistry Research Collection
Scopus© citations
26
Acquisition Date
Mar 30, 2023
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