Catalytic properties of the endoxylanase I from Thermoascus aurantiacus

Kalogeris, E; Christakopoulos, P; Vrsanska, M; Kekos, D; Biely, P; Macris, BJ

dc.contributor.author	Kalogeris, E	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Vrsanska, M	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Biely, P	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T02:41:45Z
dc.date.available	2014-03-01T02:41:45Z
dc.date.issued	2001	en
dc.identifier.issn	1381-1177	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/30613
dc.subject	Endoxylanase	en
dc.subject	Family 10	en
dc.subject	Thermoascus aurantiacus	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	arabinoxylan	en
dc.subject.other	xylan	en
dc.subject.other	xylan endo 1,3 beta xylosidase	en
dc.subject.other	conference paper	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme purification	en
dc.subject.other	gel filtration	en
dc.subject.other	hydrolysis	en
dc.subject.other	molecular weight	en
dc.subject.other	polyacrylamide gel electrophoresis	en
dc.subject.other	Thermoascus	en
dc.subject.other	thin layer chromatography	en
dc.title	Catalytic properties of the endoxylanase I from Thermoascus aurantiacus	en
heal.type	conferenceItem	en
heal.identifier.primary	10.1016/S1381-1177(00)00178-8	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S1381-1177(00)00178-8	en
heal.language	English	en
heal.publicationDate	2001	en
heal.abstract	Endo-beta -1,4-xylanase I previously purified from Thermoascus aurantiacus solid state culture was further characterized. The enzyme had a molecular weight of 33 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 31 kDa by gel filtration. Thin layer chromatography (TLC) analysis showed that endoxylanase liberates aldotetrauronic acid MeGlcA alpha -1,2-Xyl beta -1,4-Xyl beta -1,4-Xyl as the shortest acidic fragment from glucuronoxylan and an isomeric xylotriose (Xyl(3)) of the structure Xyl beta1-3Xyl beta1-4Xyl from rhodymenan. The enzyme performed ideally on O-acetyl-4-O-methyl-glucuronoxylan, Liberating large amounts of shea acetylated and non-acetylated fragments. Also, the enzyme was capable to hydrolyse arabinoxylan to arabinose (Arab), xylose (Xyl) and xylobiose (Xyl(2)). The enzyme degraded pNPX (4-nitrophenyl beta -D-xylopyranoside) by a complex reaction pathway that involved both hydrolysis and glycosyl transfer reactions. The enzyme tolerates the replacement of beta -xylopyranosyl units in several artificial substrates by beta -glucopyranosyl, alpha -L-arabinopyranosyl and alpha -L-arabinofuranosyl units and was active on pNPC (4-nitrophenyl beta -D-cellobioside), pNP-Arap (4-nitrophenyl alpha -L-arabinopyranoside) and pNPAraf (4-nitrophenyl alpha -L-arabinofuranoside). The enzyme also hydrolysed the 4-methylumbelliferyl glycosides of beta -D-xylobiose and beta -D-xylotriose at the agluconic linkage. The results suggested that the xylanase I from T. aurantiacus has catalytic properties similar to those belonging to family 10. (C) 2001 Elsevier Science B.V. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Journal of Molecular Catalysis - B Enzymatic	en
dc.identifier.doi	10.1016/S1381-1177(00)00178-8	en
dc.identifier.isi	ISI:000167014100049	en
dc.identifier.volume	11	en
dc.identifier.issue	4-6	en
dc.identifier.spage	491	en
dc.identifier.epage	501	en