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

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

Lipase B from 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 transesteri...

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Veröffentlicht in:Molecules (Basel, Switzerland) Switzerland), 2020-01, Vol.25 (2), p.350
Hauptverfasser: Spelmezan, Cristina Georgiana, Bencze, László Csaba, Katona, Gabriel, Irimie, Florin Dan, Paizs, Csaba, Toșa, Monica Ioana
Format: Artikel
Sprache:eng
Schlagworte:
Acetic acid
Adsorption
Biocatalysts
Chemical synthesis
Chitosan
covalent immobilization
enzymatic kinetic resolution
Enzymes
Glycerol
Hexanes
Lipase
lipase b from candida antarctica
magnetic nanoparticle
Nanoparticles
Transesterification
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Zusammenfassung:Lipase B from 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, -hexane, 45 °C), the biocatalyst remains active after 10 cycles.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules25020350