Please use this identifier to cite or link to this item: https://doi.org/10.1007/s12155-012-9253-8
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dc.titleA Highly Efficient NADH-dependent Butanol Dehydrogenase from High-butanol-producing Clostridium sp. BOH3
dc.contributor.authorRajagopalan, G.
dc.contributor.authorHe, J.
dc.contributor.authorYang, K.-L.
dc.date.accessioned2014-10-09T06:42:28Z
dc.date.available2014-10-09T06:42:28Z
dc.date.issued2013
dc.identifier.citationRajagopalan, G., He, J., Yang, K.-L. (2013). A Highly Efficient NADH-dependent Butanol Dehydrogenase from High-butanol-producing Clostridium sp. BOH3. Bioenergy Research 6 (1) : 240-251. ScholarBank@NUS Repository. https://doi.org/10.1007/s12155-012-9253-8
dc.identifier.issn19391234
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/88451
dc.description.abstractButanol has been considered as a better alternative fuel and it can be produced from anaerobic Clostridial fermentation. Though several enzymes are involved in the biosynthesis of butanol in Clostridia, butanol dehydrogenase (BDH) is understood to play a major role, which catalyzes the conversion of butyraldehyde into butanol at the expenditure of a cofactor NAD(P)H. Recently, the strain Clostridium sp. BOH3 is reported to generate high level of butanol from monosugars. To investigate the BDH activity at various stages of fermentation, BOH3 was cultured in reinforced Clostridial medium with 30 g/l of glucose at 35 °C and the cells were harvested periodically from acid production and solvent production phases. During acid production, NADPH-dependent BDH activity is higher than NADH dependent BDH. Conversely, NADH-BDH activity is predominant during solvent production phase. The optimum pHs for NADH and NADPH-BDH are estimated as pH 6 and 8, respectively. By employing three steps of purification, NADH-BDH is purified to 102-fold with 36 % yield. Subsequent characterization reveals that NADH-BDH is a dimer composed of two subunits depicting the molecular weight of 44 kDa. The peptide finger printing analysis (MS/MS) suggests that the purified protein has higher homology with bifunctional acetaldehyde-CoA and alcohol dehydrogenase of Clostridium acetobutylicum. The extensive kinetic studies show that NADH-BDH follows an ordered sequential bi bi mechanism. The calculated values of Kbutyraldehyde and KNADH are 8. 35 ± 0. 25 and 0. 076 ± 0. 02 mM, respectively, whereas Vmax is 4. 02 ± 0. 07 μmol/(mg protein. min). The purified NADH-BDH retains 70 % of its initial activity after 7 days at 4 °C. © 2012 Springer Science+Business Media, LLC.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/s12155-012-9253-8
dc.sourceScopus
dc.subjectABE fermentation
dc.subjectButanol dehydrogenase
dc.subjectButanol production
dc.subjectClostridium sp
dc.subjectPurification
dc.typeArticle
dc.contributor.departmentCIVIL & ENVIRONMENTAL ENGINEERING
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1007/s12155-012-9253-8
dc.description.sourcetitleBioenergy Research
dc.description.volume6
dc.description.issue1
dc.description.page240-251
dc.identifier.isiut000314518300023
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