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      The temperature optima of enzymes: a new perspective on an old phenomenon

      Daniel, Roy M.; Danson, Michael J.; Eisenthal, Robert
      DOI
       10.1016/S0968-0004(01)01803-5
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      Daniel, R.M., Danson, M.J. & Eisenthal, R. (2001). The temperature optima of enzymes: a new perspective on an old phenomenon. Trends in Biochemical Sciences, 26(4), 223-225.
      Permanent Research Commons link: https://hdl.handle.net/10289/4455
      Abstract
      Careful analysis of the dependence of enzyme activity on assay temperature has revealed that some enzymes might have real temperature optima in which the decrease in catalytic rate at temperatures above the optimum is not primarily a result of irreversible thermal inactivation. The ‘equilibrium model’ has been formulated to describe genuine temperature optima, and to suggest a simple experimental method by which to distinguish these cases from those in which enzyme instability is the major determinant of temperature optima.
      Date
      2001-04
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3124]
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