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Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile

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dc.contributor.author Katapodis, P en
dc.contributor.author Vrsanska, M en
dc.contributor.author Kekos, D en
dc.contributor.author Nerinckx, W en
dc.contributor.author Biely, P en
dc.contributor.author Claeyssens, M en
dc.contributor.author Macris, BJ en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:18:44Z
dc.date.available 2014-03-01T01:18:44Z
dc.date.issued 2003 en
dc.identifier.issn 0008-6215 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/15167
dc.subject Endoxylanase en
dc.subject Family 11 en
dc.subject Sporotrichum thermophile en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Chemistry, Applied en
dc.subject.classification Chemistry, Organic en
dc.subject.other Biochemical engineering en
dc.subject.other Cell culture en
dc.subject.other Enzymes en
dc.subject.other High performance liquid chromatography en
dc.subject.other Molecular mass en
dc.subject.other Polysaccharides en
dc.subject.other 1,4 beta dextro xylan xylanoxydrolase en
dc.subject.other 4 o methyl dextro glucuronoxylan en
dc.subject.other arabinoxylan en
dc.subject.other carbohydrate derivative en
dc.subject.other enzyme en
dc.subject.other fungal enzyme en
dc.subject.other o acetyl 4 o methylglucuronoxylan en
dc.subject.other oligosaccharide en
dc.subject.other reducing agent en
dc.subject.other rhodymenan en
dc.subject.other unclassified drug en
dc.subject.other xylan en
dc.subject.other xylobiose en
dc.subject.other xyloexaose en
dc.subject.other xylopentaose en
dc.subject.other xylose en
dc.subject.other xylotetraose en
dc.subject.other xylotriose en
dc.subject.other article en
dc.subject.other catalysis en
dc.subject.other chemical bond en
dc.subject.other enzyme activity en
dc.subject.other enzyme degradation en
dc.subject.other enzyme purification en
dc.subject.other enzyme release en
dc.subject.other high performance liquid chromatography en
dc.subject.other hydrolysis en
dc.subject.other isoelectric point 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 Sporothrix en
dc.subject.other thin layer chromatography en
dc.subject.other viscosity en
dc.subject.other Catalysis en
dc.subject.other Catalytic Domain en
dc.subject.other Chromatography, Gel en
dc.subject.other Chromatography, High Pressure Liquid en
dc.subject.other Chromatography, Ion Exchange en
dc.subject.other Chromatography, Thin Layer en
dc.subject.other Culture Media, Conditioned en
dc.subject.other Electrophoresis, Polyacrylamide Gel en
dc.subject.other Endo-1,4-beta Xylanases en
dc.subject.other Enzyme Inhibitors en
dc.subject.other Glucosides en
dc.subject.other Glycosides en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Hymecromone en
dc.subject.other Isoelectric Point en
dc.subject.other Kinetics en
dc.subject.other Magnetic Resonance Spectroscopy en
dc.subject.other Molecular Weight en
dc.subject.other Oligosaccharides en
dc.subject.other Sporothrix en
dc.subject.other Substrate Specificity en
dc.subject.other Temperature en
dc.subject.other Viscosity en
dc.subject.other Xylans en
dc.subject.other Corynascus heterothallicus en
dc.subject.other Sporotrichum en
dc.title Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile en
heal.type journalArticle en
heal.identifier.primary 10.1016/S0008-6215(03)00291-X en
heal.identifier.secondary http://dx.doi.org/10.1016/S0008-6215(03)00291-X en
heal.language English en
heal.publicationDate 2003 en
heal.abstract An endo-beta-1,4-xylanase (1,4-beta-D-xylan xylanoxydrolase, EC 3.2.1.8) present in culture filtrates of Sporotrichum thermophile ATCC 34628 was purified to homogeneity by Q-Sepharose Lind Sephacryl S-200 column chromatographies. The enzyme has a molecular mass of 25,000 Da, an isoelectric point of 6.7, and is optimally active at pH 5 and at 70 degreesC. Thin-layer chromatography (TLC) analysis showed that endo-xylanase liberates mainly xylose (Xyl) and xylobiose (Xyl,) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methylglucuronoxylan and rhodymenan (a beta-(1-->4)-beta(1-->3)-xylan). Also, the enzyme releases an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. Analysis of reaction mixtures by high performance liquid chromatography (HPLC) revealed that the enzyme cleaves preferentially the internal glycosidic bonds of xylooligosaccharides, [1-H-3]-xylooligosaccharides and xylan. The enzyme also hydrolyses the 4-methylumbelliferyl glycosides of beta-xylobiose and beta-xylotriose at the second glycosidic bond adjacent to the aglycon. The endoxylanase is not active on pNPX and pNPC. The enzyme mediates a decrease in the viscosity of xylan associated with a release of only small amounts of reducing sugar. The enzyme is irreversibly inhibited by series of omega-epoxyalkyl glycosides of D-Xylopyranose. The results suggest that the endoxylanase from S. thermophile has catalytic properties similar to the enzymes belonging to family 11. (C) 2003 Elsevier Ltd. All rights reserved. en
heal.publisher ELSEVIER SCI LTD en
heal.journalName Carbohydrate Research en
dc.identifier.doi 10.1016/S0008-6215(03)00291-X en
dc.identifier.isi ISI:000185122500009 en
dc.identifier.volume 338 en
dc.identifier.issue 18 en
dc.identifier.spage 1881 en
dc.identifier.epage 1890 en


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