Analysis of a lipase-catalyzed kinetic resolution by chiral normal-phase liquid chromatography.
As part of our investigation of structure-activity relationships in a Candida rugosa lipase-catalyzed ester hydrolysis reaction, methyl 2-(octylsulfinyl)benzoate has been studied, with respect to rate and enantioselectivity behaviour, using two different lipase preparations. A chiral normal-phase liquid chromatography method has been developed for determination of the experimental data, degree of conversion (c) and enantiomeric excess of the substrate (ees) or the product (eep), needed for calculation of the enantioselectivity in a kinetic resolution of this kind. A recently developed new class of network-polymeric chiral stationary phases, giving baseline-resolution with high selectivities for the ester substrates as well as their corresponding carboxylic acid products, permits, without any derivatization, an accurate and direct determination of the rate of the hydrolysis reaction and of the enantioselectivity from one and the same chromatogram.
Löwendahl
C
C
Department of Organic Chemistry, Göteborg University, Sweden.
Allenmark
S
S
D001565:Benzoates / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D002175:Candida / Q000201:enzymology; D002853:Chromatography, Liquid / Q000379:methods*; D004952:Esters / Q000302:isolation & purification; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013454:Sulfoxides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D001565:Benzoates; D004952:Esters; D013454:Sulfoxides; C108701:methyl 2-(octylsulfinyl)benzoate; D008049:Lipase