Abstract

The influence of microheterogeneity on enzyme inactivation kinetics is presented. Examples of different enzymes are given where microheterogeneity has been detected by different techniques. The different statistical models are presented which include the influence of microheterogeneity on enzyme inactivation kinetics and stability. As the microheterogeneity of the enzyme increases, there is a sharper decline in the normalized activity during the initial stages of the deactivation but a greater stability and activity, compared to similar homogeneous enzyme, as the deactivation proceeds. Microheterogeneity makes the deactivation reaction have a higher apparent order of reaction. The implications of microheterogeneity on enzyme inactivations are high lighted by different examples. The analysis provides fresh physical insights into the chemistry, subpopulations, structure, and function of enzymes.

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