Enzymic resolution of 2-substituted cyclohexanols through lipase-mediated esterification

Wimmer, Z; Skouridou, V; Zarevucka, M; Saman, D; Kolisis, FN

dc.contributor.author	Wimmer, Z	en
dc.contributor.author	Skouridou, V	en
dc.contributor.author	Zarevucka, M	en
dc.contributor.author	Saman, D	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T01:20:24Z
dc.date.available	2014-03-01T01:20:24Z
dc.date.issued	2004	en
dc.identifier.issn	0957-4166	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/15908
dc.subject	Enzyme	en
dc.subject	Kinetics	en
dc.subject	Enantiomeric Excess	en
dc.subject.classification	Chemistry, Inorganic & Nuclear	en
dc.subject.classification	Chemistry, Organic	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	2 (4 methoxybenzyl)cyclohexanol	en
dc.subject.other	3,3,3 trifluoromethyl 2 methoxy 2 phenylpropanoic acid	en
dc.subject.other	cyclohexanol derivative	en
dc.subject.other	propionic acid derivative	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	unclassified drug	en
dc.subject.other	article	en
dc.subject.other	chemical modification	en
dc.subject.other	chirality	en
dc.subject.other	cis isomer	en
dc.subject.other	cis trans isomerism	en
dc.subject.other	controlled study	en
dc.subject.other	enantiomer	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme mechanism	en
dc.subject.other	enzyme substrate	en
dc.subject.other	esterification	en
dc.subject.other	fungal strain	en
dc.subject.other	high performance liquid chromatography	en
dc.subject.other	nonhuman	en
dc.subject.other	nuclear magnetic resonance spectroscopy	en
dc.subject.other	priority journal	en
dc.subject.other	proton nuclear magnetic resonance	en
dc.subject.other	quantum yield	en
dc.subject.other	Rhizomucor	en
dc.subject.other	Rhizopus	en
dc.subject.other	trans isomer	en
dc.title	Enzymic resolution of 2-substituted cyclohexanols through lipase-mediated esterification	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.tetasy.2004.11.009	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.tetasy.2004.11.009	en
heal.language	English	en
heal.publicationDate	2004	en
heal.abstract	Several lipases were used for the kinetic resolution of the racemic cis- and trans-isomers of 2-(4-methoxybenzyl)cyclohexanol, by lipase-mediated esterification of the substrates to the corresponding acetate isomers. Lipase from Rhizomucor miehei was found to be the most efficient enzyme regarding enantiomeric excess (ee) and yield of the desired products. Several lipases were used for the kinetic resolution of the racemic cis- and trans-isomers of 2-(4-methoxybenzyl)cyclohexanol, by lipase-mediated esterification of the substrates to the corresponding acetate isomers. Conversion of the products and the remaining deracemized substrates into diastereoisomeric esters of 3,3,3-trifluoromethyl-2-methoxy-2-phenylpropanoic acid, their analysis by chiral HPLC and assignment of their absolute configurations through their1H and19F NMR spectra, were the basis of evaluation of the studied enzymic process. Lipase from Rhizomucor miehei (RML) was found to be the most efficient enzyme regarding enantiomeric excess (ee) and yield of the desired products, while resolution by lipase from Rhizopus arrhizus (RAL) resulted in satisfactory ee and lower yields. © 2004 Elsevier Ltd. All rights reserved.	en
heal.publisher	PERGAMON-ELSEVIER SCIENCE LTD	en
heal.journalName	Tetrahedron Asymmetry	en
dc.identifier.doi	10.1016/j.tetasy.2004.11.009	en
dc.identifier.isi	ISI:000225855100015	en
dc.identifier.volume	15	en
dc.identifier.issue	24	en
dc.identifier.spage	3911	en
dc.identifier.epage	3917	en