Kinetic and modelling studies on the lipase catalysed enantioselective esterification of (±)-perillyl alcohol

Skouridou, V; Chrysina, ED; Stamatis, H; Oikonomakos, NG; Kolisis, FN

dc.contributor.author	Skouridou, V	en
dc.contributor.author	Chrysina, ED	en
dc.contributor.author	Stamatis, H	en
dc.contributor.author	Oikonomakos, NG	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T02:42:51Z
dc.date.available	2014-03-01T02:42:51Z
dc.date.issued	2004	en
dc.identifier.issn	1381-1177	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/31102
dc.subject	AoL	en
dc.subject	Aspergillus oryzae lipase	en
dc.subject	CALB	en
dc.subject	Candida antarctica lipase B	en
dc.subject	Candida cylindracea lipase	en
dc.subject	Candida lipolytica lipase	en
dc.subject	CcL	en
dc.subject	ClL	en
dc.subject	MjL	en
dc.subject	Mucor javanicus lipase	en
dc.subject	PcL	en
dc.subject	Penicillium roqueforti lipase	en
dc.subject	porcine pancreas lipase	en
dc.subject	PPL	en
dc.subject	PrL	en
dc.subject	Rhizomucor miehei lipase	en
dc.subject	RmL	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	Alcohols	en
dc.subject.other	Conformations	en
dc.subject.other	Crystal structure	en
dc.subject.other	Enzymes	en
dc.subject.other	Esterification	en
dc.subject.other	Organic acids	en
dc.subject.other	Decanoic acid	en
dc.subject.other	Enantioselectivity	en
dc.subject.other	Stereopreferences	en
dc.subject.other	Catalysis	en
dc.subject.other	decanoic acid	en
dc.subject.other	ester	en
dc.subject.other	perillyl alcohol	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	Burkholderia cepacia	en
dc.subject.other	calculation	en
dc.subject.other	Candida	en
dc.subject.other	candida cylindracea	en
dc.subject.other	catalysis	en
dc.subject.other	conference paper	en
dc.subject.other	crystal structure	en
dc.subject.other	enantiomer	en
dc.subject.other	enantioselectivity	en
dc.subject.other	energy	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme conformation	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme structure	en
dc.subject.other	esterification	en
dc.subject.other	model	en
dc.subject.other	structure analysis	en
dc.subject.other	X ray analysis	en
dc.subject.other	Aspergillus	en
dc.subject.other	Aspergillus oryzae	en
dc.subject.other	Burkholderia cepacia	en
dc.subject.other	Candida	en
dc.subject.other	Candida antarctica	en
dc.subject.other	Candida cylindracea	en
dc.subject.other	Mucor	en
dc.subject.other	Mucor javanicus	en
dc.subject.other	Penicillium	en
dc.subject.other	Penicillium roquefortii	en
dc.subject.other	Pseudomonas	en
dc.subject.other	Rhizomucor	en
dc.subject.other	Rhizomucor miehei	en
dc.subject.other	Suidae	en
dc.subject.other	Yarrowia lipolytica	en
dc.title	Kinetic and modelling studies on the lipase catalysed enantioselective esterification of (±)-perillyl alcohol	en
heal.type	conferenceItem	en
heal.identifier.primary	10.1016/j.molcatb.2004.02.011	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.molcatb.2004.02.011	en
heal.language	English	en
heal.publicationDate	2004	en
heal.abstract	Several lipases were kinetically studied with the aim to exploit their enantioselectivity in the esterification of (S)-(-) and (R)-(+)-perillyl alcohol with decanoic acid. Most of the lipases studied exhibited stereopreference towards the R-enantiomer with apparent E-values from 3.8 to 0.6, calculated as the initial esterification rates ratio for the individual enantiomers. In an attempt to interpret the structural basis of enantioselectivity, modelling studies were performed with two of these lipases, Candida cylindracea lipase (CcL) and Pseudomonas cepacia lipase (PcL) based on their previously determined X-ray crystal structures. The results derived from modelling studies confirm their stereopreferences towards the R-enantiomer, since increased conformational energy of the S-ester was found compared to the R-ester. (C) 2004 Elsevier B.V. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Journal of Molecular Catalysis B: Enzymatic	en
dc.identifier.doi	10.1016/j.molcatb.2004.02.011	en
dc.identifier.isi	ISI:000221882900003	en
dc.identifier.volume	29	en
dc.identifier.issue	1-6	en
dc.identifier.spage	9	en
dc.identifier.epage	12	en