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dc.contributor.authorTopakas, E.en
dc.contributor.authorVafiadi, C.en
dc.contributor.authorStamatis, H.en
dc.contributor.authorChristakopoulos, P.en
dc.date.accessioned2015-11-24T16:33:37Z-
dc.date.available2015-11-24T16:33:37Z-
dc.identifier.issn0141-0229-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7686-
dc.rightsDefault Licence-
dc.subjectsporotrichum thermophileen
dc.subjectferuloyl esteraseen
dc.subjectphenolic acid estersen
dc.subjecttransesterificationen
dc.subjectsurfactantless microemulsionsen
dc.subjectfluorescens subsp cellulosaen
dc.subjectorganic-solvent mixturesen
dc.subjectaspergillus-nigeren
dc.subjectdetergentless microemulsionsen
dc.subjectsubstrate-specificityen
dc.subjectcatalyten
dc.titleSporotrichum thermophile type C feruloyl esterase (StFaeC): purification, characterization, and its use for phenolic acid (sugar) ester synthesisen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1016/j.enzmictec.2004.12.020-
heal.identifier.secondary<Go to ISI>://000227781000017-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0141022904004041/1-s2.0-S0141022904004041-main.pdf?_tid=0fb8b26ac16ea54048ac930fd9b22268&acdnat=1335510792_d40b89159ac97ecf4eda0f54231f6b41-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2005-
heal.abstractA feruloyl esterase (StFaeC) produced by Sporotrichum thermophile was purified to homogeneity. The native StFaeC was homodimer with a subunit of M-r 23,000 and pI 3. 1. The enzyme activity was optimal at pH 6.0 and 55 degrees C. The esterase displayed remarkable stability at pH 10.0 and retained 50% of its activity after 133 and 55 min at 55 and 60 degrees C, respectively. Determination of k(cat)/K-m revealed that the enzyme had a broad spectrum of activity against the (hydroxyl) cinnamate esters indicating a type C feruloyl esterase. The enzyme was active on substrates containing ferulic acid ester linked to the C-5 and C-2 linkages of arabinofuranose and hydrolysed 4-nitrophenyl-5-O-trans-fer-uloyl-alpha-L-arabinofuranoside three times more efficiently than 4-nitrophenyl-2-O-trans-feruloyl-alpha-L-arabinofuranoside. Ferulic acid was efficiently released from wheat bran when the esterase was incubated together with xylanase from S. thermophile (a maximum of 41% total ferulic acid released after 1 h incubation). StFacC by itself could release FA but at a level almost 10-fold lower than that obtained in the presence of xylanase. The potential of StFaeC for the synthesis of various phenolic acid esters was examined using as a reaction system a ternary water-organic mixture consisting of n-hexane, 1-butanol and water. Also StFaeC catalyzed the transfer of the feruloyl group to L-arabinose in a similar system using t-butanol, with about a 40% conversion of L-arabinose to feruloylated derivative was achieved. This work is the first example of enzymatic feruloylation of a carbohydrate. (c) 2004 Elsevier Inc. All rights reserved.en
heal.journalNameEnzyme and Microbial Technologyen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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