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Deactivation of TEM-1 beta-Lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methods

Abstract
The 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.
Type
Journal Article
Type of thesis
Series
Citation
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.
Date
2009
Publisher
WILEY-VCH Verlag GmbH & Co. KGaA
Degree
Supervisors
Rights
This 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.