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The effect of temperature on enzyme activity: new insights and their implications
Roy M Daniel1, Michael J Danson, Robert Eisenthal
1Department of Biological Sciences, University of Waikato, Private Bag 3105, Hamilton 3240, New Zealand. r.daniel@waikato.ac.nz
Abstract:
The two established thermal properties of enzymes are their activation energy and their thermal stability. Arising from careful measurements of the thermal behaviour of enzymes, a new model, the Equilibrium Model, has been developed to explain more fully the effects of temperature on enzymes. The model describes the effect of temperature on enzyme activity in terms of a rapidly reversible active-inactive transition, in addition to an irreversible thermal inactivation. Two new thermal parameters, Teq and Delta Heq, describe the active-inactive transition, and enable a complete description of the effect of temperature on enzyme activity. We review here the Model itself, methods for the determination of Teq and Delta Heq, and the implications of the Model for the environmental adaptation and evolution of enzymes, and for biotechnology.
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Atoms, molecules, or ions must collide before they can react with each other. Atoms must be close together to form chemical bonds. This premise is the basis for a theory that explains many observations regarding chemical kinetics, including factors affecting reaction rates.
The collision theory is based on the postulates that (i) the reaction rate is proportional to the rate of reactant collisions, (ii) the reacting species collide in an orientation allowing contact between...

