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Enhanced acetyl esterase production by Fusarium oxysporum

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dc.contributor.author Christakopoulos, P en
dc.contributor.author Mamma, D en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.date.accessioned 2014-03-01T01:14:35Z
dc.date.available 2014-03-01T01:14:35Z
dc.date.issued 1999 en
dc.identifier.issn 0959-3993 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/13155
dc.subject Acetyl (xylan) esterase production, Fusarium oxysporum en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other 4 nitrophenylacetate en
dc.subject.other acetyl esterase en
dc.subject.other acetylxylan en
dc.subject.other deacetylation en
dc.subject.other enzyme synthesis en
dc.subject.other growth regulation en
dc.subject.other microbe metabolism en
dc.subject.other Fusarium oxysporum en
dc.title Enhanced acetyl esterase production by Fusarium oxysporum en
heal.type journalArticle en
heal.identifier.primary 10.1023/A:1008936204368 en
heal.identifier.secondary http://dx.doi.org/10.1023/A:1008936204368 en
heal.language English en
heal.publicationDate 1999 en
heal.abstract Production of acetyl esterase (EC 3.1.1.6) by Fusarium oxysporum strain F3 was enhanced by optimization of growth conditions. Under optimal conditions, activities as high as 0.89 U/ml of culture medium were obtained. The culture filtrate was equally active on p-nitrophenyl acetate and acetylxylan. The enzyme produced 71% deacetylation of acetylxylan in 2 h at 40 degrees C. Activity was optimized at pH 6.5 and at 55 degrees C. The respective K-m values for p-nitrophenyl acetate and acetylxylan were 0.25 mM and 1.05% (w/v) and the V-m values were 0.65 and 0.43 mu mol acetate/min/mg protein. en
heal.publisher KLUWER ACADEMIC PUBL en
heal.journalName World Journal of Microbiology and Biotechnology en
dc.identifier.doi 10.1023/A:1008936204368 en
dc.identifier.isi ISI:000082822900006 en
dc.identifier.volume 15 en
dc.identifier.issue 4 en
dc.identifier.spage 443 en
dc.identifier.epage 446 en


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