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™ Ultra (LU). Immobilized preparations of the Lecitase™ 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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