Mostrar el registro sencillo del ítem

dc.contributor.author
Mobili, Pablo  
dc.contributor.author
Londero, Alejandra  
dc.contributor.author
Maria, T.M.R.  
dc.contributor.author
Eusébio, M.E.S.  
dc.contributor.author
de Antoni, Graciela Liliana  
dc.contributor.author
Fausto, R.  
dc.contributor.author
Gomez Zavaglia, Andrea  
dc.date.available
2022-04-05T13:17:20Z  
dc.date.issued
2009-05  
dc.identifier.citation
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  
dc.identifier.issn
0924-2031  
dc.identifier.uri
http://hdl.handle.net/11336/154361  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
S-layer  
dc.subject
Lactobacillus kefir  
dc.subject
Lactobacillus brevis  
dc.subject
FTIR  
dc.subject
DSC  
dc.subject
Secondary structure  
dc.subject
Proteins  
dc.subject.classification
Alimentos y Bebidas  
dc.subject.classification
Otras Ingenierías y Tecnologías  
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS  
dc.title
Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2022-03-14T16:42:01Z  
dc.identifier.eissn
1873-3697  
dc.journal.volume
50  
dc.journal.number
1  
dc.journal.pagination
68-77  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
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  
dc.description.fil
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  
dc.description.fil
Fil: Maria, T.M.R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal  
dc.description.fil
Fil: Eusébio, M.E.S.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal  
dc.description.fil
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  
dc.description.fil
Fil: Fausto, R.. Universidad de Coimbra. Facultad de Ciencias E Tecnología. Department Of Chemistry; Portugal  
dc.description.fil
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  
dc.journal.title
Vibrational Spectroscopy  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0924203108001392?via%3Dihub  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.vibspec.2008.07.016