PURIFICATION AND MODE OF ACTION OF A LOW-MOLECULAR-MASS ENDO-1,4-BETA-D-GLUCANASE FROM FUSARIUM-OXYSPORUM

CHRISTAKOPOULOS, P; KEKOS, D; MACRIS, BJ; CLAEYSSENS, M; BHAT, MK

dc.contributor.author	CHRISTAKOPOULOS, P	en
dc.contributor.author	KEKOS, D	en
dc.contributor.author	MACRIS, BJ	en
dc.contributor.author	CLAEYSSENS, M	en
dc.contributor.author	BHAT, MK	en
dc.date.accessioned	2014-03-01T01:44:04Z
dc.date.available	2014-03-01T01:44:04Z
dc.date.issued	1995	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/24273
dc.subject	FUSARIUM OXYSPORUM	en
dc.subject	ENDO-1,4-BETA-D-GLUCANASE	en
dc.subject	PURIFICATION	en
dc.subject	MODE OF ACTION	en
dc.subject	TRANSGLYCOSYLATION	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	TRICHODERMA-REESEI	en
dc.subject.other	CLOSTRIDIUM-CELLULOLYTICUM	en
dc.subject.other	PENICILLIUM-PINOPHILUM	en
dc.subject.other	NEUROSPORA-CRASSA	en
dc.subject.other	BETA-GLUCOSIDASE	en
dc.subject.other	ESCHERICHIA-COLI	en
dc.subject.other	CELLULASE	en
dc.subject.other	ENDOGLUCANASES	en
dc.subject.other	SPECIFICITY	en
dc.subject.other	KONINGII	en
dc.title	PURIFICATION AND MODE OF ACTION OF A LOW-MOLECULAR-MASS ENDO-1,4-BETA-D-GLUCANASE FROM FUSARIUM-OXYSPORUM	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	1995	en
heal.abstract	A low molecular mass (23.2 kDa) endo-1,4,beta-D-glucanase from Fusarum oxysporum was purified to homogeneity by gel-filtration and ion-exchange chromatographies. The enzyme was optimally active at pH 6.0 and at 50 degrees C. It had a pI value of 8.6 and was stable at 55 degrees C for 1 h. It hydrolyzed carboxymethylcellulose, cello-oligosaccharides (Glc(n)) and 4-methylumbelliferylcello-oligosaccharides but did not hydrolyze cellobiose, p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-xyloside, Avicel, filter paper and xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that this enzyme cleaved preferentially the internal glycoside bonds of higher cello-oligosaccharides. The enzyme also catalyzed the formation of transfer products in the presence of cellotriose, cellotetraose and 4-methylumbelliferylglucoside (MeUmbGlc).	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	JOURNAL OF BIOTECHNOLOGY	en
dc.identifier.isi	ISI:A1995QK37500011	en
dc.identifier.volume	39	en
dc.identifier.issue	1	en
dc.identifier.spage	85	en
dc.identifier.epage	93	en