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

Kourtoglou, E; Mamma, D; Topakas, E; Christakopoulos, P

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