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Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3

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dc.contributor.author Christakopoulos, P en
dc.contributor.author Nerinckx, W en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, B en
dc.contributor.author Claeyssens, M en
dc.date.accessioned 2014-03-01T01:12:13Z
dc.date.available 2014-03-01T01:12:13Z
dc.date.issued 1996 en
dc.identifier.issn 0168-1656 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/12011
dc.subject Enzyme purification en
dc.subject Fusarium oxysporum en
dc.subject Partial amino acid sequence en
dc.subject Xylanase en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other Cellulose en
dc.subject.other Chemical bonds en
dc.subject.other Enzyme kinetics en
dc.subject.other Enzymes en
dc.subject.other High pressure liquid chromatography en
dc.subject.other Hydrolysis en
dc.subject.other Ion exchange en
dc.subject.other Molecular weight en
dc.subject.other pH en
dc.subject.other Purification en
dc.subject.other Reaction kinetics en
dc.subject.other Thermodynamic stability en
dc.subject.other Isoelectric points en
dc.subject.other Partial amino acid sequence en
dc.subject.other Xylanase en
dc.subject.other Biotechnology en
dc.subject.other alkaline xylanase en
dc.subject.other unclassified drug en
dc.subject.other xylan endo 1,3 beta xylosidase en
dc.subject.other amino acid sequence en
dc.subject.other article en
dc.subject.other controlled study en
dc.subject.other enzyme analysis en
dc.subject.other enzyme purification en
dc.subject.other fusarium oxysporum en
dc.subject.other nonhuman en
dc.subject.other priority journal en
dc.subject.other Amino Acid Sequence en
dc.subject.other Biotechnology en
dc.subject.other Chromatography, Gel en
dc.subject.other Chromatography, Ion Exchange en
dc.subject.other Enzyme Stability en
dc.subject.other Fusarium en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Isoelectric Point en
dc.subject.other Molecular Sequence Data en
dc.subject.other Molecular Weight en
dc.subject.other Sequence Homology, Amino Acid en
dc.subject.other Substrate Specificity en
dc.subject.other Xylan Endo-1,3-beta-Xylosidase en
dc.subject.other Xylosidases en
dc.subject.other Fusarium en
dc.subject.other Fusarium oxysporum en
dc.title Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3 en
heal.type journalArticle en
heal.identifier.primary 10.1016/0168-1656(96)01619-7 en
heal.identifier.secondary http://dx.doi.org/10.1016/0168-1656(96)01619-7 en
heal.language English en
heal.publicationDate 1996 en
heal.abstract Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55°C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11.Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55 °C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11. en
heal.publisher Elsevier Science B.V., Amsterdam, Netherlands en
heal.journalName Journal of Biotechnology en
dc.identifier.doi 10.1016/0168-1656(96)01619-7 en
dc.identifier.isi ISI:A1996VU83500010 en
dc.identifier.volume 51 en
dc.identifier.issue 2 en
dc.identifier.spage 181 en
dc.identifier.epage 189 en


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