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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/123456789/7625
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dc.contributor.authorTopakas, E.en
dc.contributor.authorStamatis, H.en
dc.contributor.authorBiely, P.en
dc.contributor.authorKekos, D.en
dc.contributor.authorMacris, B. J.en
dc.contributor.authorChristakopoulos, P.en
dc.date.accessioned2015-11-24T16:33:10Z-
dc.date.available2015-11-24T16:33:10Z-
dc.identifier.issn0168-1656-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7625-
dc.rightsDefault Licence-
dc.subjectfusarium oxysporumen
dc.subjectferuloyl esteraseen
dc.subjectpurificationen
dc.subjectesterificationen
dc.subjectmicroemulsionsen
dc.subjectprimary-cell wallen
dc.subjectaspergillus-nigeren
dc.subjectwheat branen
dc.subjectdetergentless microemulsionsen
dc.subjectenzymatic-synthesisen
dc.subjectfae-iiien
dc.subjectreleaseen
dc.subjectlipaseen
dc.subjectpolysaccharidesen
dc.subjectantioxidantsen
dc.titlePurification and characterization of a feruloyl esterase from Fusarium oxysporum catalyzing esterification of phenolic acids in ternary water-organic solvent mixturesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1016/S0168-1656(02)00363-2-
heal.identifier.secondary<Go to ISI>://000182299400004-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0168165602003632/1-s2.0-S0168165602003632-main.pdf?_tid=925cae66c6aebc1515dcb058694d368c&acdnat=1335509962_e53393034142162d3c088ec3eacae592-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2003-
heal.abstractAn extracellular feruloyl esterase (FAE-II) from the culture filtrates of Fusarium oxysporum F3 was purified to homogeneity by SP-Sepharose, t-butyl-HIC and Sephacryl S-200 column chromatography. The protein corresponded to molecular mass and pI values of 27 kDa and 9.9, respectively. The enzyme was optimally active at pH 7 and 45 degreesC. The purified esterase was fully stable at pH 7.0-9.0 and temperature up to 45 degreesC after 1 h incubation. Determination of k(cat)/K-m revealed that the enzyme hydrolysed methyl sinapinate 6, 21 and 40 times more efficiently than methyl ferulate, methyl coumarate and methyl caffeate, respectively. The enzyme was active on substrates containing ferulic acid ester linked to the C-5 but inactive to the C-2 positions of arabinofuranose such as 4-nitrophenyl 5-O-transferuloyl-alpha-L-arabinofuranoside and 4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside. In the presence of Sporotrichum thermophile xylanase, there was a significant release of ferulic acid from destarched wheat bran by FAE-II, indicating a synergistic interaction between FAE-II and S. thermophile xylanase. FAE-II by itself could release only little ferulic acid from destarched wheat bran. The potential of FAE-II for the synthesis of various phenolic acid esters was tested using as a reaction system a surfactantless microemulsion formed in ternary mixture consisting of n-hexane, 1-propanol and water. (C) 2003 Elsevier Science B.V. All rights reserved.en
heal.journalNameJournal of Biotechnologyen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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