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Updated: Dec 24, 2025
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Synthesis and Characterization of Functionalized Metal-organic Frameworks
Published on: September 5, 2014
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Metal-Organic Frameworks: A New Platform for Enzyme Immobilization.
Niru Ye1, Xiaoxue Kou1, Jun Shen2
1MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China.
Chembiochem : a European Journal of Chemical Biology
|April 16, 2020
Summary
Metal-organic frameworks (MOFs) offer enhanced stability and recyclability for enzymes. This review explores MOF-based enzyme immobilization strategies and their applications in biocatalysis.
Area of Science:
- Materials Science
- Biochemistry
- Chemical Engineering
Background:
- Metal-organic frameworks (MOFs) possess high surface area, tunable porosity, and stability, making them ideal matrices for enzyme immobilization.
- Enzyme immobilization is crucial for enhancing enzyme stability, reusability, and application in biocatalysis.
- MOF-based enzyme immobilization offers a promising avenue for advanced biocatalytic systems.
Purpose of the Study:
- To review current strategies for immobilizing enzymes within MOFs.
- To highlight the advantages of MOF-immobilized enzymes (enzymes@MOFs).
- To discuss the potential applications of enzymes@MOFs in biocatalysis.
Main Methods:
- Surface immobilization of enzymes onto MOF materials.
- Post-synthetic infiltration of enzymes into pre-formed MOFs.
- In situ encapsulation of enzymes during MOF synthesis.
Main Results:
- Enzymes@MOFs exhibit significantly enhanced stability and recyclability compared to free enzymes.
- MOF matrices protect enzymes from harsh environmental conditions.
- MOF immobilization facilitates efficient cell-free biocatalysis.
Conclusions:
- MOFs provide a versatile platform for robust enzyme immobilization.
- Enzymes@MOFs demonstrate great potential for diverse industrial and biotechnological applications.
- Further research into MOF-enzyme interactions will unlock new biocatalytic possibilities.
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