Immobilization to improve the properties of Pseudomonas fluorescens lipase for the kinetic resolution of 3-aryl-3-hydroxy esters

Abstract

Lipase AK “Amano” 20 from Pseudomonas fluorescens (PFL) was immobilized using diverse immobilization techniques. The methods developed, especially the optimized sol–gel procedure, enabled the fine tuning of enzymatic activity and enantioselectivity for the kinetic resolution of racemic ethyl 3-aryl-3-hydroxypropanoates. The aryl moieties of the racemates include furan-2 and 3-yl, thiophen-2 and 3-yl, benzofuran-2-yl, benzo[ b]thiophen-2-yl, as well as phenyl and 4-chloro- and 4-methoxyphenyl groups. The optimized PFL sol–gel preparation (encapsulation from the aqueous solution of PFL, sucrose and Celite in situ) was shown to be efficiently reusable in ten cycles and highly enantioselective with E > 200 to all other substrates except furan-2 and 3-yl and thiophen-2 and 3-yl substituted compounds with E 108–184.