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Related Experiment Videos

Enzyme deactivation.

A Sadana1

  • 1Chemical Engineering Department, University of Mississippi, MS 38677-9740, USA.

Biotechnology Advances
|January 1, 1988
PubMed
Summary
This summary is machine-generated.

Enzyme deactivation often follows first-order kinetics, applicable to various enzymes and conditions. This study analyzes factors influencing this process, demonstrating its broad applicability and diverse mechanisms.

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Area of Science:

  • Biochemistry
  • Chemical Kinetics

Background:

  • Enzyme deactivation is a critical factor in enzyme stability and application.
  • First-order kinetics is a commonly observed deactivation pattern for many enzymes.

Purpose of the Study:

  • To comprehensively review and demonstrate the wide applicability of first-order enzyme deactivation kinetics.
  • To analyze the influence of various parameters and mechanisms on enzyme inactivation.

Main Methods:

  • Analysis of diverse experimental data from soluble and immobilized enzymes.
  • Examination of kinetic models, including reversible and complex deactivation pathways.
  • Investigation of substrate-dependent and time-dependent rate expressions.

Main Results:

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  • First-order deactivation kinetics is widely applicable across different enzymes and conditions.
  • Parameters like chemical modification, inhibitors, and substrates significantly influence inactivation rates.
  • Various mechanisms, including substrate involvement and grace periods, are presented for complex deactivations.

    • Conclusions:

    • First-order kinetics provides a robust framework for understanding enzyme deactivation.
    • The study highlights the versatility of kinetic modeling in predicting enzyme stability.
    • Understanding these kinetics is crucial for optimizing enzyme-based processes.