Document Detail


A comparison of two novel alcohol dehydrogenase enzymes (ADH1 and ADH2) from the extreme halophile Haloferax volcanii.
MedLine Citation:
PMID:  22526808     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Haloarchaeal alcohol dehydrogenases are exciting biocatalysts with potential industrial applications. In this study, two alcohol dehydrogenase enzymes from the extremely halophilic archaeon Haloferax volcanii (HvADH1 and HvADH2) were homologously expressed and subsequently purified by immobilized metal-affinity chromatography. The proteins appeared to copurify with endogenous alcohol dehydrogenases, and a double Δadh2 Δadh1 gene deletion strain was constructed to prevent this occurrence. Purified HvADH1 and HvADH2 were compared in terms of stability and enzymatic activity over a range of pH values, salt concentrations, and temperatures. Both enzymes were haloalkaliphilic and thermoactive for the oxidative reaction and catalyzed the reductive reaction at a slightly acidic pH. While the NAD(+)-dependent HvADH1 showed a preference for short-chain alcohols and was inherently unstable, HvADH2 exhibited dual cofactor specificity, accepted a broad range of substrates, and, with respect to HvADH1, was remarkably stable. Furthermore, HvADH2 exhibited tolerance to organic solvents. HvADH2 therefore displays much greater potential as an industrially useful biocatalyst than HvADH1.
Authors:
Leanne M Timpson; Ann-Kathrin Liliensiek; Diya Alsafadi; Jennifer Cassidy; Michael A Sharkey; Susan Liddell; Thorsten Allers; Francesca Paradisi
Related Documents :
8905088 - Genetically engineered synthesis of natural products: from alkaloids to corrins.
22428128 - Lycopene recovery from tomato peel under mild conditions assisted by enzymatic pre-trea...
15463728 - Atp versus pyrophosphate: glycolysis revisited in parasitic protists.
18037518 - Enzyme activation for organic solvents made easy.
2548618 - The rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group...
22538 - Purification and properties of nitroalkane oxidase from fusarium oxysporum.
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-4-25
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  -     ISSN:  1432-0614     ISO Abbreviation:  -     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-4-24     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Centre for Synthesis and Chemical Biology, UCD School of Chemistry and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Asymmetric bioreduction of activated alkenes by a novel isolate of Achromobacter species producing e...
Next Document:  Extracellular glutathione fermentation using engineered Saccharomyces cerevisiae expressing a novel ...