dc.contributor.author |
Kalogeris, E |
en |
dc.contributor.author |
Christakopoulos, P |
en |
dc.contributor.author |
Kekos, D |
en |
dc.contributor.author |
MacRis, BJ |
en |
dc.date.accessioned |
2014-03-01T01:14:12Z |
|
dc.date.available |
2014-03-01T01:14:12Z |
|
dc.date.issued |
1998 |
en |
dc.identifier.issn |
0168-1656 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/12923 |
|
dc.subject |
Solid state cultivation |
en |
dc.subject |
Thermoascus aurantiacus |
en |
dc.subject |
Thermostability |
en |
dc.subject |
Xylanase |
en |
dc.subject.classification |
Biotechnology & Applied Microbiology |
en |
dc.subject.other |
Carbon |
en |
dc.subject.other |
Fungi |
en |
dc.subject.other |
Moisture |
en |
dc.subject.other |
Nitrogen |
en |
dc.subject.other |
Particle size analysis |
en |
dc.subject.other |
Separation |
en |
dc.subject.other |
Thermodynamic stability |
en |
dc.subject.other |
Isoelectric focusing |
en |
dc.subject.other |
Solid state culture (SSC) |
en |
dc.subject.other |
Xylanase |
en |
dc.subject.other |
Xylosidase |
en |
dc.subject.other |
Zymograms |
en |
dc.subject.other |
Enzymes |
en |
dc.subject.other |
carbon |
en |
dc.subject.other |
hymecromone |
en |
dc.subject.other |
xylan endo 1,3 beta xylosidase |
en |
dc.subject.other |
xylose |
en |
dc.subject.other |
article |
en |
dc.subject.other |
enzyme assay |
en |
dc.subject.other |
enzyme purification |
en |
dc.subject.other |
enzyme specificity |
en |
dc.subject.other |
enzyme synthesis |
en |
dc.subject.other |
fungus |
en |
dc.subject.other |
hydrolysis |
en |
dc.subject.other |
nonhuman |
en |
dc.subject.other |
priority journal |
en |
dc.subject.other |
Thermoascus |
en |
dc.subject.other |
thermostability |
en |
dc.subject.other |
Fungi |
en |
dc.subject.other |
Thermoascus aurantiacus |
en |
dc.title |
Studies on the solid-state production of thermostable endoxylanases from Thermoascus aurantiacus: Characterization of two isozymes |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1016/S0168-1656(97)00186-7 |
en |
heal.identifier.secondary |
http://dx.doi.org/10.1016/S0168-1656(97)00186-7 |
en |
heal.language |
English |
en |
heal.publicationDate |
1998 |
en |
heal.abstract |
Production of xylanases by the thermophilic fungus Thermoascus aurantiacus under solid state culture (SSC) was enhanced by optimization of the type of carbon and nitrogen source, inoculum type, moisture level and particle size of the carbon source. Under these conditions, yields as high as 6193 U g-1 of carbon source were obtained. Chromogenic (fluorogenic) 4-methylumbelliferyl-β-glycosides of xylose (MUX) and xylobiose (MUX2) were used to characterize xylanase multienzyme components, after separation by isoelectric focusing. The zymogram indicated one major and two minor xylanases and one β-xylosidase. The major (xylanase I) and one of the minor (xylanase II) xylanases were separated and characterized. Both xylanases exhibited remarkable thermostability. Copyright (C) 1998 Elsevier Science B.V.Production of xylanases by the thermophilic fungus Thermoascus aurantiacus under solid state culture (SSC) was enhanced by optimization of the type of carbon and nitrogen source, inoculum type, moisture level and particle size of the carbon source. Under these conditions, yields as high as 6193 U g-1 of carbon source were obtained. Chromogenic (fluorogenic) 4-methylumbelliferyl-β-glycosides of xylose (MUX) and xylobiose (MUX2) were used to characterize xylanase multienzyme components, after separation by isoelectric focusing. The zymogram indicated one major and two minor xylanases and one β-xylosidase. The major (xylanase I) and one of the minor (xylanase II) xylanases were separated and characterized. Both xylanases exhibited remarkable thermostability. |
en |
heal.publisher |
Elsevier Sci B.V., Amsterdam, Netherlands |
en |
heal.journalName |
Journal of Biotechnology |
en |
dc.identifier.doi |
10.1016/S0168-1656(97)00186-7 |
en |
dc.identifier.isi |
ISI:000073522800002 |
en |
dc.identifier.volume |
60 |
en |
dc.identifier.issue |
3 |
en |
dc.identifier.spage |
155 |
en |
dc.identifier.epage |
163 |
en |