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Enzymatic catalysis via liquid-liquid interfaces.

Adrie J J Straathof1

  • 1Kluyver Laboratory for Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands.

Biotechnology and Bioengineering
|June 12, 2003
PubMed
Summary
This summary is machine-generated.

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Enzymes in water-organic solvent mixtures can have activity affected by the interface. Both substrate mass transfer and enzyme adsorption at the interface can explain this, often with similar effects.

Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Interfacial phenomena

Background:

  • Enzymes in biphasic systems can exhibit activity dependent on the available phase interface.
  • Potential mechanisms include substrate mass transfer limitations and enzyme adsorption onto the interface.

Purpose of the Study:

  • To analyze the consequences of substrate mass transfer and enzyme adsorption on enzyme activity in biphasic systems.
  • To compare the mathematical descriptions of these two mechanisms.

Main Methods:

  • Theoretical analysis of enzyme kinetics in biphasic systems.
  • Comparison of mathematical models for substrate mass transfer and enzyme adsorption.

Main Results:

  • Both substrate mass transfer and enzyme adsorption can lead to similar qualitative effects on enzyme activity.

Related Experiment Videos

  • Reaction rates show linear dependence at low concentrations and saturation at high concentrations regarding substrate, enzyme, and interfacial area.

    • Conclusions:

    • Distinguishing between substrate mass transfer and enzyme adsorption requires quantitative comparison of their respective models.
    • Both mechanisms may operate concurrently in enzymatic reactions within biphasic liquid systems.