Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/8270
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dc.contributor.authorStamatis, A.en
dc.contributor.authorMalandrinos, G.en
dc.contributor.authorButler, I. S.en
dc.contributor.authorHadjiliadis, N.en
dc.contributor.authorLouloudi, M.en
dc.date.accessioned2015-11-24T16:40:23Z-
dc.date.available2015-11-24T16:40:23Z-
dc.identifier.issn1381-1169-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8270-
dc.rightsDefault Licence-
dc.subjectthiamine catalysisen
dc.subjectdecarboxylationen
dc.subjectimmobilised biocatalystsen
dc.subjectmodified silicaen
dc.subject2-hydroxy-ketonesen
dc.subjectdiphosphate-dependent enzymesen
dc.subjectsol-gel materialsen
dc.subjectbenzoylformate decarboxylaseen
dc.subjectcrystal-structureen
dc.subjectmetal-complexesen
dc.subjectpyrophosphateen
dc.subjectmechanismen
dc.subjectmodelsen
dc.subjectcadmium(ii)en
dc.subjectresolutionen
dc.titleIntermediates of thiamine catalysis immobilized on silica surface as active biocatalysts for alpha-ketoacid decarboxylationen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1016/j.molcata.2006.11.049-
heal.identifier.secondary<Go to ISI>://000245880900017-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1381116906014075/1-s2.0-S1381116906014075-main.pdf?_tid=7c1b87479e8b7a862c552f056d00b985&acdnat=1333034662_fa5d43f85f387379c81307d9bc4dc3e0-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2007-
heal.abstractThiamine-dependent enzymes catalyse the decarboxylation of alpha-ketoacids, by both non-oxidative and oxidative mechanisms. Based on the ability of thiamine-cofactor to catalyse itself the decarboxylation of pyruvate to some extent, we have immobilized on a silica surface two 'active aldehyde' intermediates of thiamine catalysis, 2-alpha-hydroxybenzyl-thiamine pyrophosphate (HBTPP) and 2-alpha-hydroxyethyl-thiamine pyrophosphate (HETPP). The two intermediates have been tethered by a convenient method on silica support via their phosphate groups providing the covalently heterogenised biomolecules [HBTh-OP2O6-SiO3/2](n)center dot xSiO(2), and [HETh-OP2O6-SiO3/2](n)center dot xSiO(2). These bio-composite materials have been evaluated as catalysts for pyruvate and benzoyl-formate decarboxylation in either the presence or not of an aldehyde additive. Our data show that they are stable, very effective and recyclable catalysts for the production of 2-hydroxy-ketones, acetoine and benzoin. Their catalytic behavior is much better than the corresponding behavior of the homogeneous thiamine-systems due to the selected immobilization mode which bears similarities to that of the thiamine-cofactor binding to the protein. Considering our results, possible catalytic pathways of the prepared bio-composite materials are suggested. (C) 2006 Elsevier B.V. All rights reserved.en
heal.publisherElsevieren
heal.journalNameJournal of Molecular Catalysis a-Chemicalen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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