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Purification, characterization and mass spectrometric sequencing of transaldolase from Fusarium oxysporum

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dc.contributor.author Kourtoglou, E en
dc.contributor.author Mamma, D en
dc.contributor.author Topakas, E en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:29:04Z
dc.date.available 2014-03-01T01:29:04Z
dc.date.issued 2008 en
dc.identifier.issn 1359-5113 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/19106
dc.subject Fusarium oxysporum en
dc.subject transaldolase en
dc.subject purification en
dc.subject mass spectrometric sequencing en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.classification Engineering, Chemical en
dc.subject.other SACCHAROMYCES-CEREVISIAE en
dc.subject.other FERMENTATION PERFORMANCE en
dc.subject.other ACTIVE-SITE en
dc.subject.other METABOLISM en
dc.subject.other STRAINS en
dc.subject.other ETHANOL en
dc.subject.other ENZYMES en
dc.subject.other ENDO-1,4-BETA-D-GLUCANASE en
dc.subject.other ISOENZYMES en
dc.subject.other CELLULOSE en
dc.title Purification, characterization and mass spectrometric sequencing of transaldolase from Fusarium oxysporum en
heal.type journalArticle en
heal.identifier.primary 10.1016/j.procbio.2008.05.013 en
heal.identifier.secondary http://dx.doi.org/10.1016/j.procbio.2008.05.013 en
heal.language English en
heal.publicationDate 2008 en
heal.abstract Transaldolase (FoTal) was purified to homogeneity from the fungus Fusarium oxysporum. The native enzyme revealed a monomeric structure with molecular mass of 36 kDa. This FoTal depicted an optimal pH of 7.5 using imidazole buffer, while loss of activity was observed with Tris/HCl buffer. The optimal temperature was between 40 and 45 degrees C and the enzyme became unstable at temperatures above 50 degrees C. The isoelectric point of the purified enzyme was 4.5. The kinetics of the purified enzyme is consistent with a Ping Pong mechanism. The K-m values for D-eryth rose-4-phosphate and D-fructose-6-phosphate were 0.49 and 6.66 mM, while the k(cat) values were estimated at 4114 and 4151 min(-1), respectively. LC-MS/MS analysis provided peptide mass and sequence information that facilitated primary structure confirmation, allowing us to identify the FoTal gene (foxg_03074) from the genome of F. oxysporum. (C) 2008 Elsevier Ltd. All rights reserved. en
heal.publisher ELSEVIER SCI LTD en
heal.journalName PROCESS BIOCHEMISTRY en
dc.identifier.doi 10.1016/j.procbio.2008.05.013 en
dc.identifier.isi ISI:000259773100011 en
dc.identifier.volume 43 en
dc.identifier.issue 10 en
dc.identifier.spage 1094 en
dc.identifier.epage 1101 en


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