Chapter 3. Characterization of Enzyme Activity

  1. Alejandro G. Marangoni
  1. Alejandro G. Marangoni

Published Online: 13 MAR 2003

DOI: 10.1002/0471267295.ch3

Enzyme Kinetics: A Modern Approach

Enzyme Kinetics: A Modern Approach

How to Cite

Marangoni, A. G. (2002) Characterization of Enzyme Activity, in Enzyme Kinetics: A Modern Approach (ed A. G. Marangoni), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/0471267295.ch3

Editor Information

  1. Department of Food Science, University of Guelph, Canada

Author Information

  1. Department of Food Science, University of Guelph, Canada

Publication History

  1. Published Online: 13 MAR 2003
  2. Published Print: 1 NOV 2002

ISBN Information

Print ISBN: 9780471159858

Online ISBN: 9780471267294

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Keywords:

  • progress curve;
  • initial velocity;
  • substrate affinity;
  • Vmax;
  • Km;
  • Kcat;
  • curve fitting

Summary

This chapter covers the principles and techniques used in the characterization of enzyme activity and the determination of the catalytic parameters Vmax and Km. Equilibrium and steady-state models are derived from first principles. The assumptions of enzyme catalysis models and the conditions for which they apply are discussed. Catalytic parameters are derived exclusively from fits of velocity versus substrate concentration data to the enzyme kinetic models using non-linear regression techniques. No linear transformations are used in this treatment. An example of the determination of enzyme catalytic parameters is presented in order to illustrate the principles discussed.