dc.contributor.author |
Christakopoulos, P |
en |
dc.contributor.author |
Katapodis, P |
en |
dc.contributor.author |
Hatzinikolaou, DG |
en |
dc.contributor.author |
Kekos, D |
en |
dc.contributor.author |
Macris, BJ |
en |
dc.date.accessioned |
2014-03-01T01:50:08Z |
|
dc.date.available |
2014-03-01T01:50:08Z |
|
dc.date.issued |
2000 |
en |
dc.identifier.issn |
0273-2289 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/26003 |
|
dc.subject |
Fusarium oxysporum |
en |
dc.subject |
alpha-L-arabinofuranosidase |
en |
dc.subject |
purification |
en |
dc.subject |
characterization |
en |
dc.subject |
synergism |
en |
dc.subject.classification |
Biochemistry & Molecular Biology |
en |
dc.subject.classification |
Biotechnology & Applied Microbiology |
en |
dc.subject.other |
ASPERGILLUS-AWAMORI |
en |
dc.subject.other |
XYLANASE |
en |
dc.subject.other |
SYSTEMS |
en |
dc.subject.other |
WALL |
en |
dc.title |
Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum |
en |
heal.type |
journalArticle |
en |
heal.language |
English |
en |
heal.publicationDate |
2000 |
en |
heal.abstract |
An alpha-L-arabinofuranosidase from Fusarium oxysporum Fusarium oxysporum F3 was purified to homogeneity by a two-step ion exchange intercalated by a gel filtration chromatography. The enzyme had a molecular mass of 66 kDa and was optimally active at pH 6.0 and 60 degrees C. It hydrolyzed aryl alpha-L-arabinofuranosides and cleaved arabinosyl side chains from arabinoxylan and arabinan. There was a marked synergistic effect between the alpha-L-arabinofuranosidase and an endo-(1-->4)-beta-D-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan. |
en |
heal.publisher |
HUMANA PRESS INC |
en |
heal.journalName |
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY |
en |
dc.identifier.isi |
ISI:000088567900006 |
en |
dc.identifier.volume |
87 |
en |
dc.identifier.issue |
2 |
en |
dc.identifier.spage |
127 |
en |
dc.identifier.epage |
133 |
en |