Chapter 3. Characterization of Enzyme Activity
- Alejandro G. Marangoni
Published Online: 13 MAR 2003
DOI: 10.1002/0471267295.ch3
Copyright © 2003 John Wiley & Sons, Inc.
Book Title
Enzyme Kinetics: A Modern Approach
Additional Information
How to Cite
Marangoni, A. G. (2003) 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
Department of Food Science, University of Guelph, Canada
Publication History
- Published Online: 13 MAR 2003
- Published Print: 1 NOV 2002
ISBN Information
Print ISBN: 9780471159858
Online ISBN: 9780471267294
- Summary
- Chapter
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.