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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

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
2012-01
Date Available
2012-06-12T16:34:10Z
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
Subjects

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/
File(s)
No Thumbnail Available
Name

HmADH12 Multiple Sequence Alignment.doc

Description
Supporting information
Size

601 KB

Format

Microsoft Word

Checksum (MD5)

1403e193fdd360c58f0956ee64f033f4

No Thumbnail Available
Name

HmADH12 Extremophiles 2012.doc

Size

313.5 KB

Format

Microsoft Word

Checksum (MD5)

00c235bcb8043c1ebe1f9888958afea1

Owning collection
Chemistry Research Collection
Mapped collections
Biomolecular and Biomedical Science Research Collection

Item descriptive metadata is released under a CC-0 (public domain) license: https://creativecommons.org/public-domain/cc0/.
All other content is subject to copyright.

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