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

dc.contributor.authorKontogianni, A.en
dc.contributor.authorSkouridou, V.en
dc.contributor.authorSereti, V.en
dc.contributor.authorStamatis, H.en
dc.contributor.authorKolisis, F. N.en
dc.date.accessioned2015-11-24T16:33:03Z
dc.date.available2015-11-24T16:33:03Z
dc.identifier.issn1381-1177-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7611
dc.rightsDefault Licence-
dc.subjectWater activityen
dc.subjectMonoesteren
dc.subjectAcylation rateen
dc.titleLipase-catalyzed esterification of rutin and naringin with fatty acids of medium carbon chainen
heal.abstractFlavonoids 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 (aw) 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.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1016/s1381-1177(02)00139-x-
heal.identifier.secondaryhttp://www.sciencedirect.com/science/article/pii/S138111770200139X-
heal.journalNameJournal of Molecular Catalysis B: Enzymaticen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2003-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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