Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/7622
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dc.contributor.authorSkouridou, V.en
dc.contributor.authorStamatis, H.en
dc.contributor.authorKolisis, F. N.en
dc.date.accessioned2015-11-24T16:33:08Z-
dc.date.available2015-11-24T16:33:08Z-
dc.identifier.issn1381-1177-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7622-
dc.rightsDefault Licence-
dc.subjectalpha-pineneen
dc.subjectcandida antarcticaen
dc.subjectoctanoic aciden
dc.subjectperoxycarboxylic acidsen
dc.titleLipase-mediated epoxidation of alpha-pineneen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000180290000016-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2003-
heal.abstractThis work describes the lipase-mediated synthesis of alpha-pinene oxide at ambient temperature. The immobilized lipase from Candida antarctica (Novozyme 435) is used to generate peroxyoctanoic acid directly from octanoic acid and hydrogen peroxide. The peroxy acid formed is then applied I for in situ oxidation of alpha-pinene. High conversion of alpha-pinene to alpha-pinene oxide (approximately 70%) was achieved when using a two-phase system of toluene and water. Various parameters affecting the conversion of alpha-pinene to alpha-pinene oxide were studied. (C) 2002 Elsevier Science B.V. All rights reserved.en
heal.journalNameJournal of Molecular Catalysis B-Enzymaticen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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