Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/3842
DC FieldValueLanguage
dc.contributor.authorGonçalves, A. M.-
dc.contributor.authorSchacht, E.-
dc.contributor.authorMatthijs, G.-
dc.contributor.authorBarros, M. R. Aires-
dc.contributor.authorCabral, J. M. S.-
dc.contributor.authorGil, M. H.-
dc.date.accessioned2008-08-29T15:27:20Z-
dc.date.available2008-08-29T15:27:20Z-
dc.date.issued1999en_US
dc.identifier.citationEnzyme and Microbial Technology. 24:1-2 (1999) 60-66en_US
dc.identifier.urihttps://hdl.handle.net/10316/3842-
dc.description.abstractRecombinant cutinase from Fusarium solani pisi was covalently attached to dextran and two derivatized silica supports, Biosil-NH2 and Biosil-Dextran-NH2. Kinetic parameters were determined for all three systems as well as for soluble cutinase. Long-term stability in aqueous media was studied; dextran may have a stabilizing role not only due to the covalent links involved but also in the same way as other polyhydroxides in aqueous media. Differential scanning calorimetry analysis suggests an enhancement of conformational stability of the immobilized forms.en_US
dc.description.urihttp://www.sciencedirect.com/science/article/B6TG1-4165DGC-9/1/b62e6c1431e1ea508958b86755959198en_US
dc.format.mimetypeaplication/PDFen
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectConformational stabilityen_US
dc.subjectcutinaseen_US
dc.subjectdextranen_US
dc.subjectimmobilizationen_US
dc.subjectthermostabilityen_US
dc.titleStability studies of a recombinant cutinase immobilized to dextran and derivatized silica supportsen_US
dc.typearticleen_US
dc.identifier.doi10.1016/S0141-0229(98)00089-1-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.openairetypearticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:FCTUC Eng.Química - Artigos em Revistas Internacionais
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