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Related Experiment Videos

Liquid phase enzyme reactor, a new bioreactor principle.

G Schmer1

  • 1Department of Laboratory Medicine, University of Washington, Seattle.

The International Journal of Artificial Organs
|November 1, 1992
PubMed
Summary

A novel liquid phase enzyme reactor overcomes low substrate affinity issues. Biotin-labeled L-Tryptophan side chain oxidase (TSO) was used in a rabbit plasma circuit, showing effective L-Tryptophan depletion and enzyme recovery.

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Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Biochemical Engineering

Background:

  • Solid phase enzyme reactors often suffer from reduced substrate affinity, indicated by increased Km app values.
  • This limitation hinders their efficiency in various biochemical applications.

Purpose of the Study:

  • To design and evaluate a liquid phase enzyme reactor system to overcome the substrate affinity limitations of solid phase systems.
  • To assess the efficacy of immobilizing biotin-labeled L-Tryptophan side chain oxidase (TSO) within a plasmapheresis circuit.

Main Methods:

  • A liquid phase enzyme reactor system was developed using biotin-labeled L-Tryptophan side chain oxidase (TSO).
  • The enzyme was directly injected into the plasma circuit of a filter plasmapheresis system in rabbits.
  • The enzyme was adsorbed onto an Avidin column before re-entering the animal's circulation.

Main Results:

  • Total L-Tryptophan depletion was observed within the plasma circuit over a 60-minute experimental period.
  • Complete readsorption of the enzyme to the Avidin column was achieved, indicating successful enzyme retention and recovery.
  • The liquid phase system demonstrated effective substrate depletion without the typical affinity loss seen in solid phase reactors.

Conclusions:

  • The developed liquid phase enzyme reactor system effectively addresses the substrate affinity drawbacks of solid phase systems.
  • This approach allows for efficient enzyme utilization and recovery in a biological milieu, such as a plasma circuit.
  • The system shows promise for applications requiring controlled enzymatic activity within circulating systems.

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