Enzymes are difficult to recycle, which limits their large-scale industrial applications. In this work, an ionic liquid-modified magnetic metal-organic framework composite, IL-Fe₃O₄@UiO-66-NH₂, was prepared and used as a support for enzyme immobilization. The properties of the support were characterized with X-ray powder diffraction (XRD), Fourier-transform infrared (FTIR) spectra, transmission electron microscopy (TEM), scanning electronic microscopy (SEM), and so on. The catalytic performance of the immobilized enzyme was also investigated in the hydrolysis reaction of glyceryl triacetate. Compared with soluble porcine pancreatic lipase (PPL), immobilized lipase (PPL-IL-Fe₃O₄@UiO-66-NH₂) had greater catalytic activity under reaction conditions. It also showed better thermal stability and anti-denaturant properties. The specific activity of PPL-IL-Fe₃O₄@UiO-66-NH₂ was 2.3 times higher than that of soluble PPL. After 10 repeated catalytic cycles, the residual activity of PPL-IL-Fe₃O₄@UiO-66-NH₂ reached 74.4%, which was higher than that of PPL-Fe₃O₄@UiO-66-NH₂ (62.3%). In addition, kinetic parameter tests revealed that PPL-IL-Fe₃O₄@UiO-66-NH₂ had a stronger affinity to the substrate and, thus, exhibited higher catalytic efficiency. The results demonstrated that Fe₃O₄@UiO-66-NH₂ modified by ionic liquids has great potential for immobilized enzymes.

#	Concept	H-Index	Publications	Citations
1	Engineering	2	2	47
2	Biochemistry	1	1	12
3	Biomolecular Engineering	1	1	12
4	Chemical Engineering	1	1	35
5	Biocatalysis	1	1	35

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