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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/123456789/7627
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dc.contributor.authorVardakou, M.en
dc.contributor.authorKatapodis, P.en
dc.contributor.authorSamiotaki, M.en
dc.contributor.authorKekos, D.en
dc.contributor.authorPanayotou, G.en
dc.contributor.authorChristakopoulos, P.en
dc.date.accessioned2015-11-24T16:33:11Z-
dc.date.available2015-11-24T16:33:11Z-
dc.identifier.issn0141-8130-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7627-
dc.rightsDefault Licence-
dc.subjectBiochemistry/methodsen
dc.subjectChromatography, Gel/methodsen
dc.subjectChromatography, Ion Exchange/methodsen
dc.subjectCoumaric Acids/analysis/metabolismen
dc.subjectEndo-1,4-beta Xylanases/chemistry/*metabolismen
dc.subjectEurotiales/*enzymologyen
dc.subjectHydrolysisen
dc.subjectOligosaccharides/analysis/metabolismen
dc.subjectSpectroen
dc.titleMode of action of family 10 and 11 endoxylanases on water-unextractable arabinoxylanen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/14599595-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0141813003000771/1-s2.0-S0141813003000771-main.pdf?_tid=fbc38d3c-c388-11e2-872c-00000aacb361&acdnat=1369300568_dc77f55e2d07d8b4707a97e599917999-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2003-
heal.abstractMicrobial endo-beta-1,4-xylanases (EXs, EC 3.2.1.8) belonging to glycanase families 10 and 11 differ in their action on water-unextractable arabinoxylan (WU-AX). WU-AX was incubated with different levels of a Thermoascus aurantiacus family 10 and a Sporotrichum thermophile family 11 endoxylanases. At 10 g l(-1) arabinoxylan, enzyme concentrations (KE values) needed to obtain half-maximal hydrolysis rates (V(max) values) were 4.4 nM for the xylanase from T. aurantiacus and 7.1 nM for the xylanase from S. thermophile. Determination of Vmax/KE revealed that the family 10 enzyme hydrolysed two times more efficiently WU-AX than the family 11 enzyme. Molecular weights of the products formed were assessed and separation of feruloyl-oligosaccharides was achieved by anion-exchange and size-exclusion chromatography (SEC). The main difference between the feruloylated products by xylanases of family 10 and 11 concerned the length of the products containing feruloyl-arabinosyl substitution. The xylanase from T. aurantiacus liberated from WU-AX a feruloyl arabinoxylodisaccharide (FAX2) as the shortest feruloylated fragment in contrast with the enzyme from S. thermophile, which liberated a feruloyl arabinoxylotrisaccharide (FAX3). These results indicated that different factors govern WU-AX breakdown by the two endoxylanases.en
heal.journalNameInt J Biol Macromolen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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