Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture

Christakopoulos, P; Kekos, D; Kolisis, FN; Macris, BJ

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Kolisis, FN	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T01:10:53Z
dc.date.available	2014-03-01T01:10:53Z
dc.date.issued	1995	en
dc.identifier.issn	0141-5492	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/11478
dc.subject	Carbon Source	en
dc.subject	Enzyme	en
dc.subject	fusarium oxysporum	en
dc.subject	High Temperature	en
dc.subject	Kinetics	en
dc.subject	Submerged Culture	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	beta glucosidase	en
dc.subject.other	carbon	en
dc.subject.other	glucan synthase	en
dc.subject.other	article	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme synthesis	en
dc.subject.other	fungus culture	en
dc.subject.other	fungus growth	en
dc.subject.other	fusarium oxysporum	en
dc.subject.other	nonhuman	en
dc.subject.other	ph	en
dc.subject.other	temperature	en
dc.subject.other	thermostability	en
dc.subject.other	Fungi	en
dc.subject.other	Fusarium	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/BF00129023	en
heal.identifier.secondary	http://dx.doi.org/10.1007/BF00129023	en
heal.language	English	en
heal.publicationDate	1995	en
heal.abstract	The simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum was investigated in submerged culture Consecutive optimization of growth conditions resulted in the correction of large activity differences, observed during production of enzymes, and substantially enhanced low enzyme yields At optimum growth conditions yields as high as 1650 and 232 U per g of carbon source of endoglucanase and beta-glucosidase were obtained respectively competing favourably with those reported for microorganisms grown on the same carbon source. The most important kinetic characteristics of the enzymes were the high temperature optima of endoglucanase (60 degrees C) and beta-glucosidase (65 degrees C) and the exceptionally high thermostability of endoglucanase. Tire latter enzyme retained 50% of the activity at pH 5.0 after approximately 6.5 h at 70 degrees C.	en
heal.publisher	CHAPMAN HALL LTD	en
heal.journalName	Biotechnology Letters	en
dc.identifier.doi	10.1007/BF00129023	en
dc.identifier.isi	ISI:A1995RQ90900020	en
dc.identifier.volume	17	en
dc.identifier.issue	8	en
dc.identifier.spage	883	en
dc.identifier.epage	888	en