Abstract
A series-type model is utilized to show the influence of pH on enzyme inactivation kinetics and stability. Examples of enzyme inactivations involving both single-step and series-type mechanisms are presented. Empirical relations for the inactivation rate constant for the first step and the residual activity as a function of pH are presented. This provides physical insights into the enzyme inactivation processes. The analysis forms the beginning of a framework within which one could quantitatively manipulate the inactivation rate constants and the residual activity for enzymes in desired directions as a function of pH.
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