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Induction, purification, and characterization of two extracellular α-L-arabinofuranosidases from Fusarium oxysporum

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dc.contributor.author Panagiotou, G en
dc.contributor.author Topakas, E en
dc.contributor.author Economou, L en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:19:03Z
dc.date.available 2014-03-01T01:19:03Z
dc.date.issued 2003 en
dc.identifier.issn 0008-4166 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/15343
dc.subject α-L-arabinofuranosidase en
dc.subject Enzyme induction en
dc.subject Enzyme purification en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.classification Immunology en
dc.subject.classification Microbiology en
dc.subject.other Enzymes en
dc.subject.other Esters en
dc.subject.other pH effects en
dc.subject.other Phenols en
dc.subject.other Solubility en
dc.subject.other Enzyme purification en
dc.subject.other Molecular masses en
dc.subject.other Microbiology en
dc.subject.other 4 nitrophenyl alpha arabinofuranoside en
dc.subject.other alpha arabinofuranosidase en
dc.subject.other arabinose en
dc.subject.other arabinoxylan en
dc.subject.other benzene derivative en
dc.subject.other carbon en
dc.subject.other ferulic acid en
dc.subject.other fungal enzyme en
dc.subject.other phenol derivative en
dc.subject.other protein subunit en
dc.subject.other unclassified drug en
dc.subject.other enzyme en
dc.subject.other fungus en
dc.subject.other article en
dc.subject.other controlled study en
dc.subject.other enzyme activity en
dc.subject.other enzyme analysis en
dc.subject.other enzyme induction en
dc.subject.other enzyme purification en
dc.subject.other Fusarium oxysporum en
dc.subject.other Michaelis constant en
dc.subject.other molecular weight en
dc.subject.other nonhuman en
dc.subject.other pH en
dc.subject.other priority journal en
dc.subject.other stereospecificity en
dc.subject.other sugar beet en
dc.subject.other Arabinose en
dc.subject.other Biomass en
dc.subject.other Culture Media en
dc.subject.other Enzyme Induction en
dc.subject.other Fusarium en
dc.subject.other Glycoside Hydrolases en
dc.subject.other Polysaccharides en
dc.subject.other Substrate Specificity en
dc.subject.other Beta vulgaris subsp. vulgaris en
dc.subject.other Fungi en
dc.subject.other Fusarium en
dc.subject.other Fusarium oxysporum en
dc.subject.other Triticum aestivum en
dc.title Induction, purification, and characterization of two extracellular α-L-arabinofuranosidases from Fusarium oxysporum en
heal.type journalArticle en
heal.identifier.primary 10.1139/w03-077 en
heal.identifier.secondary http://dx.doi.org/10.1139/w03-077 en
heal.language English en
heal.publicationDate 2003 en
heal.abstract In the presence of L-arabinose as sole carbon source, Fusarium oxysporum produces two alpha-L-arabinofuranosidases (ABFs) named ABF1 and ABF2, with molecular masses of 200 and 180 kDa, respectively. The two F. oxysporum proteins have been purified to homogeneity. The purified enzymes are composed of three equal subunits and are neutral proteins with pIs of 6.0 and 7.3 for ABF1 and ABF2, respectively. With p-nitrophenyl alpha-L-arabinofuranoside (pNPA) as the substrate, ABF1 and ABF2 exhibited K-m values of 0.39 and 0.28 mmol.L-1, respectively, and V-max values of 1.6 and 4.6 mumol.min(-1).(mg of protein)(-1), respectively, and displayed optimal activity at pH 6.0 and 50-60degreesC. ABFs released arabinose only from sugar beet arabinan and not from wheat soluble and insoluble arabinoxylans. The enzymes were not active on substrates containing ferulic acid ester linked to C-5 and C-2 linkages of pNPA showing that phenolic substituents of pNPA sterically hindered the action of ABFs. en
heal.publisher NATL RESEARCH COUNCIL CANADA en
heal.journalName Canadian Journal of Microbiology en
dc.identifier.doi 10.1139/w03-077 en
dc.identifier.isi ISI:000187527100007 en
dc.identifier.volume 49 en
dc.identifier.issue 10 en
dc.identifier.spage 639 en
dc.identifier.epage 644 en


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