4.7 Article

Lipase-based MIL-100(Fe) biocomposites as chiral stationary phase for high-efficiency capillary electrochromatographic enantioseparation

Journal

MICROCHIMICA ACTA
Volume 190, Issue 3, Pages -

Publisher

SPRINGER WIEN
DOI: 10.1007/s00604-023-05647-9

Keywords

Chiral separation; Lipase; Metal-organic frameworks; Immobilization; Capillary electrochromatography

Ask authors/readers for more resources

A novel chiral porous column was fabricated by immobilizing lipase on MIL-100(Fe) biocomposites, which were used as a chiral stationary phase for capillary electrochromatographic enantioseparation. The lipase biocomposites based on MOFs not only improved the stereoselective activities, but also enhanced the stability and applicability of the enzyme. The performance of the porous column was characterized and evaluated, showing high resolution and excellent stability for enantioseparation.
A novel chiral porous column was fabricated by lipase immobilized MIL-100(Fe) biocomposites as chiral stationary phase through covalent coupling and applied to capillary electrochromatographic enantioseparation. MOF-based lipase biocomposites not only enhance stereoselective activities but also improve the stability and applicability of the enzyme. The functionalized porous columns were characterized by Fourier transform infrared spectroscopy, scanning electron microscopy, and powder X-ray diffraction. The performance of the porous column was evaluated by enantioseparating amino acid enantiomers, affording high resolution over 2.0. Besides, the enantio-resolutions of phenylephrine, phenylsuccinic acid, chloroquine, and zopiclone were also greater than 2.0. The relative standard deviations of run-to-run, intra-, and inter-day repeatability were within 4.0% in terms of resolution and retention time, exhibiting excellent stability of the column. Conceivably, the results show that MOF-based lipase composites as chiral stationary phase offer a highly efficient means for enantioseparation in capillary electrochromatography, attributing to the enhanced enantioselective activities of lipase by highly ordered frameworks.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available