Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882

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dc.contributor.authorBennett, N. A.en
dc.contributor.authorRyan, J.en
dc.contributor.authorBiely, P.en
dc.contributor.authorVrsanska, M.en
dc.contributor.authorKremnicky, L.en
dc.contributor.authorMacris, B. J.en
dc.contributor.authorKekos, D.en
dc.contributor.authorChristakopoulos, P.en
dc.contributor.authorKatapodis, P.en
dc.contributor.authorClaeyssens, M.en
dc.contributor.authorNerinckx, W.en
dc.contributor.authorNtauma, P.en
dc.contributor.authorBhat, M. K.en
dc.date.accessioned2015-11-24T16:31:51Z
dc.date.available2015-11-24T16:31:51Z
dc.identifier.issn0008-6215-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7489
dc.rightsDefault Licence-
dc.subjectDisaccharides/metabolismen
dc.subjectEndo-1,4-beta Xylanasesen
dc.subjectEnzyme Stabilityen
dc.subjectFungal Proteins/chemistryen
dc.subjectHydrogen-Ion Concentrationen
dc.subjectIsoelectric Pointen
dc.subjectMitosporic Fungi/*enzymologyen
dc.subjectOligosaccharides/metabolismen
dc.subjectSubstrate Specificityen
dc.subjectTemperatureen
dc.subjectXylans/metabolien
dc.titleBiochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882en
heal.abstractAn endoxylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) from the culture filtrates of T. lanuginosus ATCC 46882 was purified to homogeneity by DEAE-Sepharose and Bio-Gel P-30 column chromatographies. The purified endoxylanase had a specific activity of 888.8 mumol min-1 mg-1 protein and accounted for approximately 30% of the total protein secreted by this fungus. The molecular mass of native (non-denatured) and denatured endoxylanase were 26.3 and 25.7 kD as, respectively. Endoxylanase had a pI of 3.7 and was optimally active between pH 6.0-6.5 and at 75 degrees C. The enzyme showed > 50% of its original activity between pH 5.5-9.0 and at 85 degrees C. The pH and temperature stability studies revealed that this endoxylanase was almost completely stable between pH 5.0-9.0 and up to 60 degrees C for 5 h and at pH 10.0 up to 55 degrees C for 5 h. Thin-layer chromatography (TLC) analysis showed that endoxylanase released mainly xylose (Xyl) and xylobiose (Xyl2) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methyl-D-glucuronoxylan and rhodymenan (a beta-(1-->3)-beta(1-->4)-xylan). Also, the enzyme released an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. The enzyme hydrolysed [1-3H]-xylo-oligosaccharides in an endofashion, but the hydrolysis of [1-3H]-xylotriose appeared to proceed via transglycosylation. since the xylobiose was the predominant product. Endoxylanase was not active on pNPX and pNPC at 40 and 100 mM for up to 6 h, but showed some activity toward pNPX at 100 mM after 20-24 h. The results suggested that the endoxylanase from T. lanuginosus belongs to family 11.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9648252-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0008621597100763/1-s2.0-S0008621597100763-main.pdf?_tid=0998d7f0-c389-11e2-9e50-00000aacb361&acdnat=1369300591_3b8208b967e26d2bf0b2751c1914c8e9-
heal.journalNameCarbohydr Resen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1998-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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