Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry

Autores
Mobili, Pablo; Londero, Alejandra; Maria, T.M.R.; Eusébio, M.E.S.; de Antoni, Graciela Liliana; Fausto, R.; Gomez Zavaglia, Andrea
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
FTIR spectroscopy was used for the characterization of S-layer proteins extracted from microorganisms isolated from kefir grains. S-layer from Lactobacillus brevis ATCC 8287 has been already characterized [G. Vidgren, I. Palva, R. Pakkanen, K. Lounatmaa, A. Palva, J. Bacteriol. 174 (1992) 7419] and therefore it was used for the validation of FTIR as a method to investigate the secondary structure of the S-layer proteins of the studied kefir strains. A correlation between the secondary structures of S-layer proteins with surface properties of Lactobacillus kefir strains was found: a high percentage of b-sheet contents (40?50%) was found for non-aggregating strains, whereas this percentage decreased to 25?30% for aggregating ones. A quantitative comparison of the S-layers was performed by means of cluster analysis based on the obtained spectroscopic data. This analysis enabled the strains to be grouped in clusters according to the spectral diversity in the Amide I region. The non-aggregating strains of L. kefir cluster at Ssm > 0.943 and the aggregating strains form another cluster, with Ssm > 0.769. L. brevis ATCC 8287 appears clearly separated from these two clusters: the similarity with the aggregating strains is 0.658 and the similarity with the non-aggregating ones, 0.665. The thermal analysis of the lyophilized S-layer proteins was performed by means of differential scanning calorimetry (DSC) and FTIR. DSC analysis within the 30? 130 8C range showed two phase transitions with maxima located at ca. 58 and 98 8C for L. brevis and in the 67?70 and 110?119 8C ranges for the different strains of L. kefir (CIDCA 8344 only shows the lowest temperature phase transition). FTIR spectra obtained reveal that for all the L. kefir S-layer proteins the major secondary structure modifications upon heating occur nearly at the first phase transitions observed by DSC, with the thermal stability increasing with the percentage of b-sheets structures. The Slayer protein of L. brevis ATICC 8287, which among all protein studied is that with maximum b-sheet contents (and no a-helix structure) was then found to be the protein showing a greater thermal stability.
Fil: Mobili, Pablo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Londero, Alejandra. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Maria, T.M.R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: Eusébio, M.E.S.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: de Antoni, Graciela Liliana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Fausto, R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: Gomez Zavaglia, Andrea. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Materia
S-layer
Lactobacillus kefir
Lactobacillus brevis
FTIR
DSC
Secondary structure
Proteins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/154361
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/154361
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetryMobili, PabloLondero, AlejandraMaria, T.M.R.Eusébio, M.E.S.de Antoni, Graciela LilianaFausto, R.Gomez Zavaglia, AndreaS-layerLactobacillus kefirLactobacillus brevisFTIRDSCSecondary structureProteinshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2FTIR spectroscopy was used for the characterization of S-layer proteins extracted from microorganisms isolated from kefir grains. S-layer from Lactobacillus brevis ATCC 8287 has been already characterized [G. Vidgren, I. Palva, R. Pakkanen, K. Lounatmaa, A. Palva, J. Bacteriol. 174 (1992) 7419] and therefore it was used for the validation of FTIR as a method to investigate the secondary structure of the S-layer proteins of the studied kefir strains. A correlation between the secondary structures of S-layer proteins with surface properties of Lactobacillus kefir strains was found: a high percentage of b-sheet contents (40?50%) was found for non-aggregating strains, whereas this percentage decreased to 25?30% for aggregating ones. A quantitative comparison of the S-layers was performed by means of cluster analysis based on the obtained spectroscopic data. This analysis enabled the strains to be grouped in clusters according to the spectral diversity in the Amide I region. The non-aggregating strains of L. kefir cluster at Ssm > 0.943 and the aggregating strains form another cluster, with Ssm > 0.769. L. brevis ATCC 8287 appears clearly separated from these two clusters: the similarity with the aggregating strains is 0.658 and the similarity with the non-aggregating ones, 0.665. The thermal analysis of the lyophilized S-layer proteins was performed by means of differential scanning calorimetry (DSC) and FTIR. DSC analysis within the 30? 130 8C range showed two phase transitions with maxima located at ca. 58 and 98 8C for L. brevis and in the 67?70 and 110?119 8C ranges for the different strains of L. kefir (CIDCA 8344 only shows the lowest temperature phase transition). FTIR spectra obtained reveal that for all the L. kefir S-layer proteins the major secondary structure modifications upon heating occur nearly at the first phase transitions observed by DSC, with the thermal stability increasing with the percentage of b-sheets structures. The Slayer protein of L. brevis ATICC 8287, which among all protein studied is that with maximum b-sheet contents (and no a-helix structure) was then found to be the protein showing a greater thermal stability.Fil: Mobili, Pablo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Londero, Alejandra. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Maria, T.M.R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; PortugalFil: Eusébio, M.E.S.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; PortugalFil: de Antoni, Graciela Liliana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Fausto, R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; PortugalFil: Gomez Zavaglia, Andrea. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaElsevier Science2009-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/154361Mobili, Pablo; Londero, Alejandra; Maria, T.M.R.; Eusébio, M.E.S.; de Antoni, Graciela Liliana; et al.; Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry; Elsevier Science; Vibrational Spectroscopy; 50; 1; 5-2009; 68-770924-20311873-3697CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0924203108001392?via%3Dihubinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.vibspec.2008.07.016info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:36Zoai:ri.conicet.gov.ar:11336/154361instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:04:37.028CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
title Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
spellingShingle Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
Mobili, Pablo
S-layer
Lactobacillus kefir
Lactobacillus brevis
FTIR
DSC
Secondary structure
Proteins
title_short Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
title_full Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
title_fullStr Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
title_full_unstemmed Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
title_sort Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry
dc.creator.none.fl_str_mv Mobili, Pablo
Londero, Alejandra
Maria, T.M.R.
Eusébio, M.E.S.
de Antoni, Graciela Liliana
Fausto, R.
Gomez Zavaglia, Andrea
author Mobili, Pablo
author_facet Mobili, Pablo
Londero, Alejandra
Maria, T.M.R.
Eusébio, M.E.S.
de Antoni, Graciela Liliana
Fausto, R.
Gomez Zavaglia, Andrea
author_role author
author2 Londero, Alejandra
Maria, T.M.R.
Eusébio, M.E.S.
de Antoni, Graciela Liliana
Fausto, R.
Gomez Zavaglia, Andrea
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv S-layer
Lactobacillus kefir
Lactobacillus brevis
FTIR
DSC
Secondary structure
Proteins
topic S-layer
Lactobacillus kefir
Lactobacillus brevis
FTIR
DSC
Secondary structure
Proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv FTIR spectroscopy was used for the characterization of S-layer proteins extracted from microorganisms isolated from kefir grains. S-layer from Lactobacillus brevis ATCC 8287 has been already characterized [G. Vidgren, I. Palva, R. Pakkanen, K. Lounatmaa, A. Palva, J. Bacteriol. 174 (1992) 7419] and therefore it was used for the validation of FTIR as a method to investigate the secondary structure of the S-layer proteins of the studied kefir strains. A correlation between the secondary structures of S-layer proteins with surface properties of Lactobacillus kefir strains was found: a high percentage of b-sheet contents (40?50%) was found for non-aggregating strains, whereas this percentage decreased to 25?30% for aggregating ones. A quantitative comparison of the S-layers was performed by means of cluster analysis based on the obtained spectroscopic data. This analysis enabled the strains to be grouped in clusters according to the spectral diversity in the Amide I region. The non-aggregating strains of L. kefir cluster at Ssm > 0.943 and the aggregating strains form another cluster, with Ssm > 0.769. L. brevis ATCC 8287 appears clearly separated from these two clusters: the similarity with the aggregating strains is 0.658 and the similarity with the non-aggregating ones, 0.665. The thermal analysis of the lyophilized S-layer proteins was performed by means of differential scanning calorimetry (DSC) and FTIR. DSC analysis within the 30? 130 8C range showed two phase transitions with maxima located at ca. 58 and 98 8C for L. brevis and in the 67?70 and 110?119 8C ranges for the different strains of L. kefir (CIDCA 8344 only shows the lowest temperature phase transition). FTIR spectra obtained reveal that for all the L. kefir S-layer proteins the major secondary structure modifications upon heating occur nearly at the first phase transitions observed by DSC, with the thermal stability increasing with the percentage of b-sheets structures. The Slayer protein of L. brevis ATICC 8287, which among all protein studied is that with maximum b-sheet contents (and no a-helix structure) was then found to be the protein showing a greater thermal stability.
Fil: Mobili, Pablo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Londero, Alejandra. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Maria, T.M.R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: Eusébio, M.E.S.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: de Antoni, Graciela Liliana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Fausto, R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal
Fil: Gomez Zavaglia, Andrea. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
description FTIR spectroscopy was used for the characterization of S-layer proteins extracted from microorganisms isolated from kefir grains. S-layer from Lactobacillus brevis ATCC 8287 has been already characterized [G. Vidgren, I. Palva, R. Pakkanen, K. Lounatmaa, A. Palva, J. Bacteriol. 174 (1992) 7419] and therefore it was used for the validation of FTIR as a method to investigate the secondary structure of the S-layer proteins of the studied kefir strains. A correlation between the secondary structures of S-layer proteins with surface properties of Lactobacillus kefir strains was found: a high percentage of b-sheet contents (40?50%) was found for non-aggregating strains, whereas this percentage decreased to 25?30% for aggregating ones. A quantitative comparison of the S-layers was performed by means of cluster analysis based on the obtained spectroscopic data. This analysis enabled the strains to be grouped in clusters according to the spectral diversity in the Amide I region. The non-aggregating strains of L. kefir cluster at Ssm > 0.943 and the aggregating strains form another cluster, with Ssm > 0.769. L. brevis ATCC 8287 appears clearly separated from these two clusters: the similarity with the aggregating strains is 0.658 and the similarity with the non-aggregating ones, 0.665. The thermal analysis of the lyophilized S-layer proteins was performed by means of differential scanning calorimetry (DSC) and FTIR. DSC analysis within the 30? 130 8C range showed two phase transitions with maxima located at ca. 58 and 98 8C for L. brevis and in the 67?70 and 110?119 8C ranges for the different strains of L. kefir (CIDCA 8344 only shows the lowest temperature phase transition). FTIR spectra obtained reveal that for all the L. kefir S-layer proteins the major secondary structure modifications upon heating occur nearly at the first phase transitions observed by DSC, with the thermal stability increasing with the percentage of b-sheets structures. The Slayer protein of L. brevis ATICC 8287, which among all protein studied is that with maximum b-sheet contents (and no a-helix structure) was then found to be the protein showing a greater thermal stability.
publishDate 2009
dc.date.none.fl_str_mv 2009-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/154361
Mobili, Pablo; Londero, Alejandra; Maria, T.M.R.; Eusébio, M.E.S.; de Antoni, Graciela Liliana; et al.; Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry; Elsevier Science; Vibrational Spectroscopy; 50; 1; 5-2009; 68-77
0924-2031
1873-3697
CONICET Digital
CONICET
url http://hdl.handle.net/11336/154361
identifier_str_mv Mobili, Pablo; Londero, Alejandra; Maria, T.M.R.; Eusébio, M.E.S.; de Antoni, Graciela Liliana; et al.; Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry; Elsevier Science; Vibrational Spectroscopy; 50; 1; 5-2009; 68-77
0924-2031
1873-3697
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1016/j.vibspec.2008.07.016
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
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dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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