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dc.contributor.authorRogers, Thomas A.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorBommarius, Andreas S.
dc.date.accessioned2010-02-22T23:10:03Z
dc.date.available2010-02-22T23:10:03Z
dc.date.issued2009
dc.identifier.citationRogers, T. A., Daniel, R. M. & Bommarius, A. S. (2009). Deactivation of TEM-1 beta-Lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methods. ChemCatChem, 1(1), 131-137.en
dc.identifier.urihttps://hdl.handle.net/10289/3635
dc.description.abstractThe thermal deactivation of TEM-1 β-lactamase was examined using two experimental techniques: a series of isothermal batch assays and a single, continuous, non-isothermal assay in an enzyme membrane reactor (EMR). The isothermal batch-mode technique was coupled with the three-state Equilibrium Model of enzyme deactivation, while the results of the EMR experiment were fitted to a four-state molten globule model . The two methods both led to the conclusions that the thermal deactivation of TEM-1 β -lactamase does not follow the Lumry-Eyring model and that the Teq of the enzyme (the point at which active and inactive states are present in equal amounts due to thermodynamic equilibrium) is at least 10 °C from the Tm (melting temperature), contrary to the idea that the true temperature optimum of a biocatalyst is necessarily close to the melting temperature.en
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherWILEY-VCH Verlag GmbH & Co. KGaA
dc.relation.urihttp://www3.interscience.wiley.com/journal/122512460/abstracten
dc.rightsThis is the pre-peer reviewed version of the following article: Rogers, T. A., Daniel, R. M. & Bommarius, A. S. (2009). Deactivation of TEM-1 beta-Lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methods. ChemCatChem, 1(1), 131-137, which has been published in final form at http://www3.interscience.wiley.com/journal/122512460/abstract.
dc.subjectbiocatalysisen
dc.subjectenzyme catalysisen
dc.subjectenzyme modelsen
dc.subjectEquilibrium Modelen
dc.subjectprotein foldingen
dc.titleDeactivation of TEM-1 beta-Lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methodsen
dc.typeJournal Articleen
dc.identifier.doi10.1002/cctc.200900120en
dc.relation.isPartOfChemCatChemen_NZ
pubs.begin-page131en_NZ
pubs.elements-id34725
pubs.end-page137en_NZ
pubs.issue1en_NZ
pubs.volume1en_NZ


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