Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/13877
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dc.contributor.authorTzialla, A. A.en
dc.contributor.authorKalogeris, E.en
dc.contributor.authorEnotiadis, A.en
dc.contributor.authorTaha, A. A.en
dc.contributor.authorGournis, D.en
dc.contributor.authorStamatis, H.en
dc.date.accessioned2015-11-24T17:33:35Z-
dc.date.available2015-11-24T17:33:35Z-
dc.identifier.issn0921-5107-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/13877-
dc.rightsDefault Licence-
dc.subjectsmectite claysen
dc.subjectadsorptionen
dc.subjectintercalationen
dc.subjectbiocatalysisen
dc.subjectoxidationen
dc.subjectenzyme immobilizationen
dc.subjectcatalyzed esterificationen
dc.subjectmediated epoxidationen
dc.subjecthydrogen-peroxideen
dc.subjectalpha-pineneen
dc.subjectnanocompositesen
dc.subjectelectrodesen
dc.subjectadsorptionen
dc.subjectsupportsen
dc.titleEffective immobilization of Candida antarctica lipase B in organic-modified clays: Application for the epoxidation of terpenesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1016/j.mseb.2009.09.003-
heal.identifier.secondary<Go to ISI>://000273157800009-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικώνel
heal.publicationDate2009-
heal.abstractThe use of three smectite nanoclays (Laponite, SWy-2 and Kunipia) organic-modified with octadecyl-trimethyl-ammonium surfactant, as suitable host matrices for the immobilization of lipase B from Candida antarctica (CaLB) was demonstrated. The resulting hybrid biocatalysts were characterized by a combination of powder X-ray diffraction, thermogravimetric analysis, differential thermal analysis, scanning electron microscopy and infrared spectroscopy. The experimental results confirmed the remarkable binding capacity of the three organoclays for CaLB. Activity and operational stability of immobilized CaLB were determined for the chemo-enzymatic epoxidation of terpenes (alpha-pinene and d-limonene) in organic media using various oxidizing agents. The immobilized enzyme retains a significant part of its activity after repeated use under drastic reaction conditions originating from the use of oxidants. (c) 2009 Elsevier B.V. All rights reserved.en
heal.publisherElsevieren
heal.journalNameMaterials Science and Engineering B-Advanced Functional Solid-State Materialsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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