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Enzyme immobilization based on reticular framework materials: Strategy, food applications, and prospect
Xiaorong Liu1, Manyan Qiu1, Yiyi Zhang1
1Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Immobilized enzymes using reticular framework materials (RFMs) enhance stability and reusability. This review covers RFM strategies, highlights, and food industry applications for improved enzyme technology.
Area of Science:
- Biocatalysis and Materials Science
- Focuses on enzyme immobilization using advanced porous materials.
Background:
- Natural enzymes offer high efficiency but suffer from poor stability and reusability.
- Immobilized enzyme technology addresses these limitations, enhancing enzyme performance and application scope.
Purpose of the Study:
- To comprehensively review strategies for enzyme immobilization on reticular framework materials (RFMs).
- To summarize research highlights and applications of RFM-based enzyme immobilization, particularly in the food industry.
- To identify future challenges and perspectives in this field.
Main Methods:
- Summarizes various immobilization strategies: physical adsorption, covalent linkage, diffusion, and in situ encapsulation.
- Reviews research on multi-enzyme systems, magnetic RFMs, and enzyme-mimicking RFMs.
- Compiles applications in the food industry.
Main Results:
- Reticular framework materials (RFMs) like MOFs, COFs, and HOFs offer high surface area, tunable porosity, and ordered structures ideal for enzyme carriers.
- Diverse immobilization techniques enable tailored enzyme integration onto RFMs.
- RFM-based enzyme immobilization shows promise for multi-enzyme systems and magnetic applications.
Conclusions:
- Enzyme immobilization on RFMs significantly improves enzyme stability and reusability, overcoming limitations of free enzymes.
- RFM-based systems present versatile platforms for advanced biocatalysis with broad industrial potential, especially in food processing.
- Further research is needed to address current challenges and unlock the full potential of RFM-enzyme conjugates.
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