dc.creatorRezende, Sebastião T.
dc.creatorViana, Pollyanna A.
dc.creatorMeza, Andreia N.
dc.creatorGomide, Felipe T.F.
dc.creatorNagem, Ronaldo A.P.
dc.creatorSantos, Alexandre M.C.
dc.creatorSantoro, Marcelo M.
dc.creatorGuimarães, Valéria M.
dc.date2018-05-29T10:32:03Z
dc.date2018-05-29T10:32:03Z
dc.date2010-04-01
dc.date.accessioned2023-09-27T22:20:04Z
dc.date.available2023-09-27T22:20:04Z
dc.identifier01418130
dc.identifierhttps://doi.org/10.1016/j.ijbiomac.2010.01.003
dc.identifierhttp://www.locus.ufv.br/handle/123456789/19855
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8973769
dc.descriptionSpectroscopic and thermodynamic properties were determined for Debaryomyces hansenii UFV-1 extracellular and intracellular α-galactosidases. α-Galactosidases showed similar secondary structure compositions (α-helix, β-sheet parallel and β-turn). Effects of pH and temperature on the structure of α-galactosidases were investigated using circular dichroism spectroscopy. It was more pronounced at low pH. Microcalorimetry was employed for the determination of thermodynamic parameters. Immediate thermal denaturation reversibility was not observed for α-galactosidases; it occurred as a thermodynamically driven process. Extracellular α-galactosidase, at pH 5.5, showed lower Tm when compared to the intracellular enzyme. The CD and DSC data suggest that D. hansenii α-galactosidases have different behaviors although they possess some similar secondary structures.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherInternational Journal of Biological Macromolecules
dc.relationv. 46, n. 3, p. 298-303, Abril 2010
dc.rightsElsevier B.V.
dc.subjectDebaryomyces hansenii UFV-1
dc.subjectα-Galactosidases
dc.subjectCircular dichroism
dc.subjectDifferential scanning calorimetry
dc.subjectStability
dc.titleSpectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
dc.typeArtigo


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