Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/6226
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dc.creatorKoblitz, Maria Gabriela Bello-
dc.creatorPastore, Gláucia Maria-
dc.date2006-06-01-
dc.date.accessioned2015-04-30T13:33:47Z-
dc.date.available2015-04-30T13:33:47Z-
dc.date.issued2015-04-30-
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542006000300016-
dc.identifier.citationKOBLITZ, M. G. B.; PASTORE, G. M. Purification and biochemical characterization of an extracellular lipase produced by a new strain of Rhizopus sp. Ciência e Agrotecnologia, Lavras, v. 30, n. 3 , p. 494-502, maio 2006.-
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/6226-
dc.formattext/html-
dc.languageen-
dc.publisherEditora da Universidade Federal de Lavras-
dc.sourceCiência e Agrotecnologia v.30 n.3 2006-
dc.subjectLipase-
dc.subjectRhizopus sp.-
dc.subjectPurification-
dc.subjectBiochemical characterization-
dc.titlePurification and biochemical characterization of an extracellular lipase produced by a new strain of Rhizopus sp.-
dc.typejournal article-
dc.description.resumoThe present study had as a goal to purify and characterize the lipolytic fraction secreted by a strain of Rhizopus sp. Only 3 steps of purification were necessary to achieve SDS-PAGE homogeneity. One band with 37.5 KDa molecular mass and with 1446 U/mg specific activity was obtained. The purified fraction presented 2 lipase isoforms; both showed optimum activity at 50ºC, and were stable between 6.5 and 7.5 pH values and at temperatures below 50ºC and also kept their activity in hexane. The lipase was inactivated by Hg+2 and by n-bromosuccinimide and activated by Na+.-
Aparece nas coleções:Ciência e Agrotecnologia

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