Lipase-catalyzed esterification of rutin and naringin with fatty acids of medium carbon chain

Kontogianni, A; Skouridou, V; Sereti, V; Stamatis, H; Kolisis, FN

dc.contributor.author	Kontogianni, A	en
dc.contributor.author	Skouridou, V	en
dc.contributor.author	Sereti, V	en
dc.contributor.author	Stamatis, H	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T02:42:17Z
dc.date.available	2014-03-01T02:42:17Z
dc.date.issued	2003	en
dc.identifier.issn	1381-1177	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/30908
dc.subject	Acylation rate	en
dc.subject	Monoester	en
dc.subject	Water activity	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	Carbon	en
dc.subject.other	Catalysis	en
dc.subject.other	Esterification	en
dc.subject.other	Esters	en
dc.subject.other	Fatty acids	en
dc.subject.other	Regioselectivity	en
dc.subject.other	Enzymes	en
dc.subject.other	aurantiin	en
dc.subject.other	carbon	en
dc.subject.other	fatty acid	en
dc.subject.other	flavonoid	en
dc.subject.other	rutoside	en
dc.subject.other	solvent	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	acylation	en
dc.subject.other	Candida antarctica	en
dc.subject.other	catalysis	en
dc.subject.other	conference paper	en
dc.subject.other	enzyme immobilization	en
dc.subject.other	esterification	en
dc.subject.other	molecular biology	en
dc.subject.other	nonhuman	en
dc.subject.other	Candida antarctica	en
dc.title	Lipase-catalyzed esterification of rutin and naringin with fatty acids of medium carbon chain	en
heal.type	conferenceItem	en
heal.identifier.primary	10.1016/S1381-1177(02)00139-X	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S1381-1177(02)00139-X	en
heal.language	English	en
heal.publicationDate	2003	en
heal.abstract	Flavonoids rutin and naringin were acylated with fatty acids of medium carbon chain (with 8-12 carbon atoms on their molecule) in a reaction catalyzed by immobilized lipase from Candida antarctica (Novozyme) in various solvent systems. The reaction parameters affecting the acylation rate and the conversion of the enzymatic process, such as the nature of the organic solvent and acyl donor used, the water activity (a(w)) of the system, as well as the kinetic of the reaction have been investigated. In all cases studied, only flavonoid monoester is identified as the product, which indicates that this lipase-catalyzed esterification is regioselective. The enzymatic acylation of flavonoids seems to follow Michaelis-Menten kinetics. (C) 2002 Elsevier Science 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/S1381-1177(02)00139-X	en
dc.identifier.isi	ISI:000180290000014	en
dc.identifier.volume	21	en
dc.identifier.issue	1-2	en
dc.identifier.spage	59	en
dc.identifier.epage	62	en