Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (<i>E</i>)-4-Arylbut-3-en-2-yl Esters

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (<i>E</i>)-4-Arylbut-3-en-2-yl Esters

The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase&#8482; Ultra (LU). Immobilized preparations of the Lecitase&#8482; Ultra enzyme had significantly higher activity and...

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Bibliographic Details
Main Authors: Aleksandra Leśniarek, Anna Chojnacka, Radosław Drozd, Magdalena Szymańska, Witold Gładkowski
Format: Article
Language:English
Published: MDPI AG 2020-02-01
Series:Molecules
Subjects:
(<i>e</i>)-4-arylbut-3-en-2-ols
enantioselective hydrolysis
kinetic resolution
lecitase™ ultra
immobilization
cyanogen bromide-activated agarose
Online Access:https://www.mdpi.com/1420-3049/25/5/1067

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https://www.mdpi.com/1420-3049/25/5/1067

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