Rogers, Thomas A.Daniel, Roy M.Bommarius, Andreas S.2010-02-222010-02-222009Rogers, 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.https://hdl.handle.net/10289/3635The 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.application/pdfenThis 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.biocatalysisenzyme catalysisenzyme modelsEquilibrium Modelprotein foldingJournal Article10.1002/cctc.200900120