Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , , , |
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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LOCUS Repositório Institucional da UFV |
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2145 |
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 |
_version_ |
1817560041763373056 |