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pubmed-article:12585481pubmed:abstractTextA technique based on liquid chromatography has been developed to facilitate studies of enantioselectivity in penicillin G acylase (PGA)-catalyzed hydrolysis of some 2-aryloxyalkanoic acid methyl esters and isosteric analogues. PGA was covalently immobilized on an aminopropyl monolithic silica support to create an immobilized HPLC-enzyme reactor. Two sets of experimental data were drawn to calculate the enantioselectivity (E) of the kinetically controlled enantiomer-differentiating reaction, the degree of substrate conversion and the enantiomeric excess of the product. The developed enzymatic reactor was coupled through a switching valve to an achiral analytical column for separation and quantitation of the hydrolysis products. The enantiomeric excess was determined off-line on a PGA-chiral stationary phase. In this way, highly precise E values were determined. A computational study related to the hydrolysis of the considered racemic esters was also carried out in order to unambiguously clarify both the substrate specificity and the enantioselectivity displayed by PGA.lld:pubmed
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pubmed-article:12585481pubmed:pagination535-42lld:pubmed
pubmed-article:12585481pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:12585481pubmed:articleTitleEnantioselective hydrolysis of some 2-aryloxyalkanoic acid methyl esters and isosteric analogues using a penicillin G acylase-based HPLC monolithic silica column.lld:pubmed
pubmed-article:12585481pubmed:affiliationDipartimento di Chimica Farmaceutica, Universita' di Pavia, Via Taramani 12, 1-27100 Pavia, Italy. g.massolini@unipv.itlld:pubmed
pubmed-article:12585481pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12585481pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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