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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/14479
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dc.contributor.authorSerefoglou, E.en
dc.contributor.authorLitina, K.en
dc.contributor.authorGournis, D.en
dc.contributor.authorKalogeris,E.en
dc.contributor.authorTzialla,A. A.en
dc.contributor.authorPavlidis, I. V.en
dc.contributor.authorStamatis, C.en
dc.contributor.authorMaccallini, E.en
dc.contributor.authorLubomska, M.en
dc.contributor.authorRudolf, P.en
dc.date.accessioned2015-11-24T17:38:20Z-
dc.date.available2015-11-24T17:38:20Z-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/14479-
dc.rightsDefault Licence-
dc.titleSmectite clays as solid supports for immobilization of β-glucosidase: Synthesis, Characterization and Biochemical propertiesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικώνel
heal.publicationDate2008-
heal.abstractNanomaterials as solid supports can improve the efficiency of immobilized enzymes by reducing diffusional limitation as well as by increasing the surface area per mass unit and therefore improving enzyme loading. In this work, β-glucosidase from almonds was immobilized on two smectite nanoclays. The resulting hybrid biocatalysts were characterized by a combination of powder X-ray diffraction, X-ray photoelectron spectroscopy, thermogravimetric analysis, differential thermal analysis, and infrared spectroscopy. Biochemical studies showed an improved thermostability of the immobilized enzyme as well as enhanced performance at higher temperatures and in a wider pH range.en
heal.publisherAmerican Chemical Societyen
heal.journalNameChem. Materen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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