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

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dc.contributor.authorTimpson, Leanne M.
dc.contributor.authorAlsafadi, Diya
dc.contributor.authorMac Donnchadha, Cillin
dc.contributor.authorLiddell, Susan
dc.contributor.authorSharkey, Michael A.
dc.contributor.authorParadisi, Francesca
dc.date.accessioned2012-06-12T16:34:10Z
dc.date.available2012-06-12T16:34:10Z
dc.date.copyright2012 Springeren
dc.date.issued2012-01
dc.identifier.citationExtremophilesen
dc.identifier.urihttp://hdl.handle.net/10197/3635
dc.description.abstractHaloarchaeal 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.en
dc.description.sponsorshipScience Foundation Irelanden
dc.description.sponsorshipIrish Research Council for Science, Engineering and Technologyen
dc.format.extent615424 bytes
dc.format.extent321024 bytes
dc.format.mimetypeapplication/msword
dc.format.mimetypeapplication/msword
dc.language.isoenen
dc.publisherSpringeren
dc.relation.requiresBiomolecular and Biomedical Science Research Collectionen
dc.rightsThe final publication is available at springerlink.comen
dc.subjectAlcohol dehydrogenaseen
dc.subjectBiocatalysisen
dc.subjectExtremophileen
dc.subjectHalophileen
dc.subjectHaloarcula marismortuien
dc.subjectHaloferax volcaniien
dc.subjectOrganic solventsen
dc.subject.lcshAlcohol dehydrogenaseen
dc.subject.lcshEnzymesen
dc.subject.lcshExtreme environments--Microbiologyen
dc.subject.lcshHalophilic organismsen
dc.subject.lcshOrganic solventsen
dc.titleCharacterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Seaen
dc.typeJournal Articleen
dc.internal.availabilityFull text availableen
dc.statusPeer revieweden
dc.identifier.volume16en
dc.identifier.issue1en
dc.identifier.startpage57en
dc.identifier.endpage66en
dc.identifier.doi10.1007/s00792-011-0405-0-
dc.neeo.contributorTimpson|Leanne M.|aut|-
dc.neeo.contributorAlsafadi|Diya|aut|-
dc.neeo.contributorMac Donnchadha|Cillin|aut|-
dc.neeo.contributorLiddell|Susan|aut|-
dc.neeo.contributorSharkey|Michael A.|aut|-
dc.neeo.contributorParadisi|Francesca|aut|-
dc.description.othersponsorshipMercken
dc.description.othersponsorshipIslamic Development Banken
dc.description.adminEmbargo to 1 Jan 2013 --JGen
item.grantfulltextopen-
item.fulltextWith Fulltext-
Appears in Collections:Biomolecular and Biomedical Science Research Collection
Chemistry Research Collection
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