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High-rate membrane supported aqueous-phase enzymatic conversion in organic solvent
1Howard P. Isermann Department of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Bioseparation
|June 1, 1994
Summary
Enzyme immobilization on microporous membranes using a supported aqueous-phase technique enables stable and efficient catalysis. This method enhances enzyme stability and reaction rates for industrial applications.
Area of Science:
- Biocatalysis
- Chemical Engineering
- Materials Science
Background:
- Enzyme immobilization is crucial for industrial biocatalysis, offering reusability and stability.
- Supported aqueous-phase immobilization presents a novel approach for enzyme stabilization within porous materials.
Purpose of the Study:
- To investigate the use of microporous membranes for enzyme immobilization via a supported aqueous-phase method.
- To evaluate the catalytic performance and stability of immobilized tyrosinase in a model reaction.
Main Methods:
- Microporous membranes were employed as support for enzyme immobilization.
- Tyrosinase was immobilized in a thin aqueous film on the membrane's inner surface.
- The immobilized enzyme catalyzed the oxidation of p-cresol in a chloroform environment.
Main Results:
- The immobilized tyrosinase exhibited stable catalytic activity for over 6 hours.
- Optimal operating conditions, including water content and permeation flux, were identified.
- Enzyme loading was critical for maintaining sustained enzyme activity and reaction rates.
Conclusions:
- Supported aqueous-phase immobilization on microporous membranes is a viable strategy for enzyme stabilization.
- This approach enhances enzyme reusability and catalytic efficiency, reducing mass transport limitations.
- The developed system offers high productivity for biocatalytic processes.