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Block copolymer microdomains: a novel medium for enzymatic reactions
A Gupte1, R Nagarajan, A Kilara
1Department of Chemical Engineering, Pennsylvania State University, University Park 16802.
Biotechnology Progress
|July 1, 1991
Summary
Block copolymers form microdomains that immobilize enzymes for reactions. This microheterogeneity offers potential for biocatalysis with water-insoluble substrates.
Area of Science:
- Polymer Science
- Biochemistry
- Materials Science
Background:
- Block copolymers self-assemble into microdomains, creating microheterogeneous environments.
- These microheterogeneous media can influence chemical and biological processes.
Purpose of the Study:
- To investigate the use of hydrophobic-hydrophilic block copolymer microdomains as media for enzyme immobilization and reactions.
- To explore the impact of the microenvironment's hydrophobicity on enzymatic activity.
Main Methods:
- Formation of block copolymer microdomains.
- Immobilization of enzymes (cholesterol oxidase, horseradish peroxidase) within these microdomains.
- Assessing enzymatic activity in the microdomains compared to aqueous media.
Main Results:
- Block copolymer microdomains effectively immobilized enzymes.
- Enzymatic activity was altered within the microdomains, influenced by the microenvironment's hydrophobicity.
- The microdomains were easily generated, well-defined, and reproducible.
Conclusions:
- Hydrophobic-hydrophilic block copolymer microdomains are effective media for enzyme immobilization.
- These systems show significant potential for enzymatic biosynthetic reactions, especially with water-insoluble substrates or products.