Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates

Kalogeris, E; Christakopoulos, P; Kekos, D; Macris, BJ

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	2014-03-01T01:14:49Z
dc.date.available	2014-03-01T01:14:49Z
dc.date.issued	1999	en
dc.identifier.issn	1389-1723	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/13232
dc.subject	Family 10	en
dc.subject	Thermoascus aurantiacus	en
dc.subject	Xylanase	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Food Science & Technology	en
dc.subject.other	cellobioside	en
dc.subject.other	hymecromone glycoside	en
dc.subject.other	polysaccharide	en
dc.subject.other	unclassified drug	en
dc.subject.other	xylan endo 1,3 beta xylosidase	en
dc.subject.other	xylobiose	en
dc.subject.other	xylotriose	en
dc.subject.other	article	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme substrate	en
dc.subject.other	fermentation	en
dc.subject.other	fungus	en
dc.subject.other	fungus growth	en
dc.subject.other	molecular weight	en
dc.subject.other	nonhuman	en
dc.subject.other	Thermoascus	en
dc.subject.other	thin layer chromatography	en
dc.subject.other	Fungi	en
dc.subject.other	Thermoascus aurantiacus	en
dc.title	Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S1389-1723(99)80160-1	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S1389-1723(99)80160-1	en
heal.language	English	en
heal.publicationDate	1999	en
heal.abstract	The mode of action of a minor xylanase on a variety of polysaccharides and model substrates was investigated. The enzyme was excreted by Thermoascus aurantiacus grown in solid state fermentation (SSF). The purified enzyme had a molecular mass of 33,000. Thin laser chromatography analysis showed that the endo-xylanase liberated short fragments from polysaccharides. The enzyme hydrolysed aryl-beta-D-cellobioside and the chromogenic (fluorogenic) 4-methylumbelliferyl-beta-glycosides of xylobiose (MeUmbXyl(2)) and xylotriose (MeUmbXyl(3)) at the agluconic Linkage. The results suggested that the endoxylanase belonged to family 10.	en
heal.publisher	SOC BIOSCIENCE BIOENGINEERING JAPAN	en
heal.journalName	Journal of Bioscience and Bioengineering	en
dc.identifier.doi	10.1016/S1389-1723(99)80160-1	en
dc.identifier.isi	ISI:000082742300019	en
dc.identifier.volume	87	en
dc.identifier.issue	6	en
dc.identifier.spage	819	en
dc.identifier.epage	821	en