Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters
Aleksandra Leśniarek , Anna Chojnacka , Radosław Drozd , Magdalena Szymańska , Witold Gładkowski
AbstractThe 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 enantioselectivity than the free enzyme, particularly for 4-phenylbut-3-en-2-yl butyrate as the substrate. Moreover, the kinetic resolution with the immobilized enzyme was achieved in a much shorter time (24–48 h). Lecitase™ Ultra, immobilized on cyanogen bromide-activated agarose, was particularly effective, producing, after 24 h of reaction time in phosphate buffer (pH 7.2) with acetone as co-solvent, both (R)-alcohols and unreacted (S)-esters with good to excellent enantiomeric excesses (ee 90–99%). These conditions and enzyme were also suitable for the kinetic separation of racemic (E)-4-phenylbut-3-en-2-yl butyrate analogs containing methyl substituents on the benzene ring (4b,4c), but they did not show any enantioselectivity toward (E)-4-(4’-methoxyphenyl)but-3-en-2-yl butyrate (4d).
|Journal series||Molecules, ISSN 1420-3049, (N/A 100 pkt)|
|Publication size in sheets||0.85|
|Keywords in English||(E)-4-arylbut-3-en-2-ols, Lecitase™ Ultra, cyanogen bromide-activated agarose, enantioselective hydrolysis, immobilization, kinetic resolution|
|License||Journal (articles only); published final; ; with publication|
|Score||= 100.0, 14-09-2020, ArticleFromJournal|
|Publication indicators||= 0; = 0; : 2017 = 1.146; : 2018 = 3.06 (2) - 2018=3.38 (5)|
|Citation count*||3 (2020-09-17)|
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.