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

TitleInduction, purification, and characterization of two extracellular α-L-arabinofuranosidases from Fusarium oxysporum
Authors
Issue Date2003
PublisherN R C Research Press. The Journal's web site is located at http://pubs.nrc-cnrc.gc.ca/cgi-bin/rp/rp2_desc_e?cjm
Citation
Canadian Journal Of Microbiology, 2003, v. 49 n. 10, p. 639-644 How to Cite?
AbstractIn the presence of L-arabinose as sole carbon source, Fusarium oxysporum produces two α-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 α-L-arabinofuranoside (pNPA) as the substrate, ABF1 and ABF2 exhibited Km values of 0.39 and 0.28 mmol·L-1, respectively, and Vmax values of 1.6 and 4.6 μmol·min-1·(mg of protein) -1, respectively, and displayed optimal activity at pH 6.0 and 50-60°C. 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.
Persistent Identifierhttp://hdl.handle.net/10722/181236
ISSN
2015 Impact Factor: 1.335
2015 SCImago Journal Rankings: 0.537
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPanagiotou, Gen_US
dc.contributor.authorTopakas, Een_US
dc.contributor.authorEconomou, Len_US
dc.contributor.authorKekos, Den_US
dc.contributor.authorMacris, BJen_US
dc.contributor.authorChristakopoulos, Pen_US
dc.date.accessioned2013-02-21T02:03:24Z-
dc.date.available2013-02-21T02:03:24Z-
dc.date.issued2003en_US
dc.identifier.citationCanadian Journal Of Microbiology, 2003, v. 49 n. 10, p. 639-644en_US
dc.identifier.issn0008-4166en_US
dc.identifier.urihttp://hdl.handle.net/10722/181236-
dc.description.abstractIn the presence of L-arabinose as sole carbon source, Fusarium oxysporum produces two α-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 α-L-arabinofuranoside (pNPA) as the substrate, ABF1 and ABF2 exhibited Km values of 0.39 and 0.28 mmol·L-1, respectively, and Vmax values of 1.6 and 4.6 μmol·min-1·(mg of protein) -1, respectively, and displayed optimal activity at pH 6.0 and 50-60°C. 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_US
dc.languageengen_US
dc.publisherN R C Research Press. The Journal's web site is located at http://pubs.nrc-cnrc.gc.ca/cgi-bin/rp/rp2_desc_e?cjmen_US
dc.relation.ispartofCanadian Journal of Microbiologyen_US
dc.subject.meshArabinose - Metabolismen_US
dc.subject.meshBiomassen_US
dc.subject.meshCulture Mediaen_US
dc.subject.meshEnzyme Inductionen_US
dc.subject.meshFusarium - Enzymology - Growth & Developmenten_US
dc.subject.meshGlycoside Hydrolases - Biosynthesis - Chemistry - Isolation & Purificationen_US
dc.subject.meshPolysaccharides - Metabolismen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleInduction, purification, and characterization of two extracellular α-L-arabinofuranosidases from Fusarium oxysporumen_US
dc.typeArticleen_US
dc.identifier.emailPanagiotou, G: gipa@hku.hken_US
dc.identifier.authorityPanagiotou, G=rp01725en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1139/w03-077en_US
dc.identifier.pmid14663498-
dc.identifier.scopuseid_2-s2.0-1042267963en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1042267963&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume49en_US
dc.identifier.issue10en_US
dc.identifier.spage639en_US
dc.identifier.epage644en_US
dc.identifier.isiWOS:000187527100007-
dc.publisher.placeCanadaen_US
dc.identifier.scopusauthoridPanagiotou, G=8566179700en_US
dc.identifier.scopusauthoridTopakas, E=6603178486en_US
dc.identifier.scopusauthoridEconomou, L=6701313581en_US
dc.identifier.scopusauthoridKekos, D=7003932669en_US
dc.identifier.scopusauthoridMacris, BJ=7006746072en_US
dc.identifier.scopusauthoridChristakopoulos, P=7006479823en_US

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