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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/7758
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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, H.en
dc.contributor.authorMaccallini, E.en
dc.contributor.authorLubomska, M.en
dc.contributor.authorRudolf, P.en
dc.date.accessioned2015-11-24T16:34:06Z-
dc.date.available2015-11-24T16:34:06Z-
dc.identifier.issn0897-4756-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7758-
dc.rightsDefault Licence-
dc.subjectray photoelectron-spectroscopyen
dc.subjectpyrococcus-furiosusen
dc.subjectcrystal-structureen
dc.subjectenzyme-activityen
dc.subjectmontmorilloniteen
dc.subjectstabilityen
dc.subjectadsorptionen
dc.subjectbiosensoren
dc.subjectoxidaseen
dc.subjectbindingen
dc.titleSmectite clays as solid supports for immobilization of beta-glucosidase: Synthesis, characterization, and biochemical propertiesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1021/Cm800486u-
heal.identifier.secondary<Go to ISI>://000256854800045-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdfplus/10.1021/cm800486u-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
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, beta-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.journalNameChemistry of Materialsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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