The effect of temperature on enzyme activity: new insights and their implications
| Autor: | Michelle E. Peterson, Roy M. Daniel, Charles Kai-Wu Lee, Robert Eisenthal, Michael J. Danson |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
Hot Temperature biology Chemistry Stereochemistry Thermodynamics Environmental adaptation General Medicine Activation energy Adaptation Physiological Microbiology Enzyme assay Enzymes Evolution Molecular Enzyme Models Chemical biology.protein Molecular Medicine Denaturation (biochemistry) Thermal stability |
| Zdroj: | Extremophiles. 12:51-59 |
| ISSN: | 1433-4909 1431-0651 |
| DOI: | 10.1007/s00792-007-0089-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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