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Insight into the efficient loading and enhanced activity of enzymes immobilized on functionalized UiO-66
Fan Yang1, Hui-Hui Xie2, Fan Du1
1Shandong Province Key Laboratory of Applied Mycology, College of Life Sciences, Qingdao Agricultural University, Qingdao 266109, China.
International Journal of Biological Macromolecules
|September 12, 2024
Summary
Functionalized zirconium metal-organic frameworks (Zr-MOFs) enhance enzyme immobilization. Hydroxyl group functionalization on UiO-66 shows superior loading, activity, and stability for cytochrome c and catalase.
Area of Science:
- Materials Science
- Biocatalysis
- Nanotechnology
Background:
- Enzyme immobilization is crucial for efficient and sustainable biocatalysis.
- Zirconium-based metal-organic frameworks (Zr-MOFs) are promising enzyme carriers, but their immobilization performance requires further investigation.
- UiO-66 is a well-studied Zr-MOF with tunable properties.
Purpose of the Study:
- To systematically investigate the effect of surface functionalization on UiO-66 for enzyme immobilization.
- To evaluate the immobilization efficiency, enzyme stability, and catalysis kinetics of cytochrome c (Cyt c) and catalase (CAT) on functionalized UiO-66.
- To compare the affinity of Cyt c and CAT towards different UiO-66 derivatives.
Main Methods:
- UiO-66 was functionalized with various groups: -H, -NH2, -COOH, -OH, and -2OH.
- Cytochrome c and catalase were immobilized onto the functionalized UiO-66 materials.
- Enzyme loading capacity, activity, stability, and kinetic parameters were measured.
- Affinity constants between enzymes and carriers were determined.
Main Results:
- Hydroxyl group functionalization (-OH) on UiO-66 resulted in the highest enzyme loading capacity for both Cyt c and CAT.
- The -OH functionalized UiO-66 demonstrated enhanced enzyme activity and improved stability compared to other derivatives.
- Higher affinity constants were observed for Cyt c and CAT towards the -OH functionalized UiO-66, attributed to its surface area and microenvironment.
- The introduction of a single hydroxyl group significantly optimized the carrier properties for enzyme immobilization.
Conclusions:
- Surface functionalization of UiO-66, particularly with hydroxyl groups, significantly enhances enzyme immobilization.
- Hydroxyl-functionalized UiO-66 offers a superior platform for engineering biocatalysts with improved performance and stability.
- This study highlights the potential of MOFs as versatile materials for advanced enzyme immobilization applications.
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