Abstract
Isothermal titration Calorimetry (ITC) has become a powerful method for evaluating enzyme kinetics, as it provides a way to detect catalytic reaction heat as a function of time with high sensitivity and reproducibility. This review focuses on both established and newly emerging methodologies for evaluating the kinetics of enzyme-catalyzed reactions. Because it allows direct determination of the reaction rate, which itself indicates enzyme activity, ITC is expected to provide a general and effective way to evaluate enzyme activity. The theoretical basis of ITC for evaluating enzyme kinetics is reviewed, as demonstrates the advantages of this method.
