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, T eq and ΔH eq, 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 T eq and ΔH eq, and the implications of the Model for the environmental adaptation and evolution of enzymes, and for biotechnology.
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Acknowledgements
We thank the Royal Society of New Zealand’s Marsden Fund and the National Science Foundation (Biocomplexity 0120648) for financial support.
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Communicated by D.A. Cowan.
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Daniel, R.M., Danson, M.J., Eisenthal, R. et al. The effect of temperature on enzyme activity: new insights and their implications. Extremophiles 12, 51–59 (2008). https://doi.org/10.1007/s00792-007-0089-7
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DOI: https://doi.org/10.1007/s00792-007-0089-7