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

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...

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Bibliographic Details
Published in:Molecules
Main Authors: Cristina Georgiana Spelmezan, László Csaba Bencze, Gabriel Katona, Florin Dan Irimie, Csaba Paizs, Monica Ioana Toșa
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2020
Subjects:
lipase b from candida antarctica
magnetic nanoparticle
chitosan
covalent immobilization
enzymatic kinetic resolution
Organic chemistry
QD241-441
Antarc*
Antarctica
Online Access:https://doi.org/10.3390/molecules25020350
https://doaj.org/article/2a661d0f87be426d8c62a96fe1bcd4ef
Description
Summary: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.

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