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: Spelmezan, Cristina Georgiana, Bencze, László Csaba, Katona, Gabriel, Irimie, Florin Dan, Paizs, Csaba, Toșa, Monica Ioana
Format: Text
Language:English
Published: MDPI 2020
Subjects:
Article
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
http://www.ncbi.nlm.nih.gov/pubmed/31952168
https://doi.org/10.3390/molecules25020350
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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