pH-Dependent enzyme deactivation models.
A pH-dependent "series-type" enzyme deactivation model using rapid protonation and deprotonation equilibria and the relatively slower inactivation rates is presented. From the enzyme activity-time trajectories at different pH the models presented permit the evaluation of some of the protonation and inactivation rate constants as well as the specific activities of the different enzyme forms. pH dependence of enzyme deactivations may also exhibit deactivation disguised kinetics. Three different examples of pH-dependent enzyme deactivations available in the literature are appropriately modeled to indicate the general applicability of the model. The model presented is consistent with the data and provides mechanistic insights into the pH-dependent deactivation of different enzymes.
Chitnis
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Chemical Engineering Department, University of Mississippi, University, Mississippi 38677-9740, USA.
Sadana
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