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Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols

Cristina Georgiana Spelmezan, László Csaba Bencze, Gabriel Katona, Florin Dan Irimie, Csaba Paizs, Monica Ioana Toșa

2020Molecules27 citationsDOIOpen Access PDF

Abstract

Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.

Topics & Concepts

Candida antarcticaKinetic resolutionLipaseChemistryChitosanEnzymeBiochemistryEnantioselective synthesisCatalysisEnzyme Catalysis and ImmobilizationCarbohydrate Chemistry and SynthesisClick Chemistry and Applications
Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols | Litcius