Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases

Detalhes bibliográficos
Autor(a) principal: Rezende, Sebastião T.
Data de Publicação: 2010
Outros Autores: Viana, Pollyanna A., Meza, Andreia N., Gomide, Felipe T.F., Nagem, Ronaldo A.P., Santos, Alexandre M.C., Santoro, Marcelo M., Guimarães, Valéria M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi.org/10.1016/j.ijbiomac.2010.01.003
http://www.locus.ufv.br/handle/123456789/19855
Resumo: Spectroscopic 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.
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spelling Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidasesDebaryomyces hansenii UFV-1α-GalactosidasesCircular dichroismDifferential scanning calorimetryStabilitySpectroscopic 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.International Journal of Biological Macromolecules2018-05-29T10:32:03Z2018-05-29T10:32:03Z2010-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf01418130https://doi.org/10.1016/j.ijbiomac.2010.01.003http://www.locus.ufv.br/handle/123456789/19855engv. 46, n. 3, p. 298-303, Abril 2010Elsevier B.V.info:eu-repo/semantics/openAccessRezende, Sebastião T.Viana, Pollyanna A.Meza, Andreia N.Gomide, Felipe T.F.Nagem, Ronaldo A.P.Santos, Alexandre M.C.Santoro, Marcelo M.Guimarães, Valéria M.reponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T08:45:58Zoai:locus.ufv.br:123456789/19855Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T08:45:58LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.none.fl_str_mv Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
title Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
spellingShingle Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
Rezende, Sebastião T.
Debaryomyces hansenii UFV-1
α-Galactosidases
Circular dichroism
Differential scanning calorimetry
Stability
title_short Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
title_full Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
title_fullStr Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
title_full_unstemmed Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
title_sort Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
author Rezende, Sebastião T.
author_facet Rezende, Sebastião T.
Viana, Pollyanna A.
Meza, Andreia N.
Gomide, Felipe T.F.
Nagem, Ronaldo A.P.
Santos, Alexandre M.C.
Santoro, Marcelo M.
Guimarães, Valéria M.
author_role author
author2 Viana, Pollyanna A.
Meza, Andreia N.
Gomide, Felipe T.F.
Nagem, Ronaldo A.P.
Santos, Alexandre M.C.
Santoro, Marcelo M.
Guimarães, Valéria M.
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Rezende, Sebastião T.
Viana, Pollyanna A.
Meza, Andreia N.
Gomide, Felipe T.F.
Nagem, Ronaldo A.P.
Santos, Alexandre M.C.
Santoro, Marcelo M.
Guimarães, Valéria M.
dc.subject.por.fl_str_mv Debaryomyces hansenii UFV-1
α-Galactosidases
Circular dichroism
Differential scanning calorimetry
Stability
topic Debaryomyces hansenii UFV-1
α-Galactosidases
Circular dichroism
Differential scanning calorimetry
Stability
description Spectroscopic 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.
publishDate 2010
dc.date.none.fl_str_mv 2010-04-01
2018-05-29T10:32:03Z
2018-05-29T10:32:03Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv 01418130
https://doi.org/10.1016/j.ijbiomac.2010.01.003
http://www.locus.ufv.br/handle/123456789/19855
identifier_str_mv 01418130
url https://doi.org/10.1016/j.ijbiomac.2010.01.003
http://www.locus.ufv.br/handle/123456789/19855
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv v. 46, n. 3, p. 298-303, Abril 2010
dc.rights.driver.fl_str_mv Elsevier B.V.
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Elsevier B.V.
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv pdf
application/pdf
dc.publisher.none.fl_str_mv International Journal of Biological Macromolecules
publisher.none.fl_str_mv International Journal of Biological Macromolecules
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
instacron:UFV
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
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