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dc.contributor.author
Pescuma, Micaela
dc.contributor.author
Hebert, Elvira Maria
dc.contributor.author
Rabesona, Hanitra
dc.contributor.author
Drouet, Martine
dc.contributor.author
Choiset, Yvan
dc.contributor.author
Haertlé, Thomas
dc.contributor.author
Mozzi, Fernanda Beatriz
dc.contributor.author
Font, Graciela Maria
dc.contributor.author
Chobert, Jean-Marc
dc.date.available
2018-08-27T18:34:10Z
dc.date.issued
2011-07-15
dc.identifier.citation
Pescuma, Micaela; Hebert, Elvira Maria; Rabesona, Hanitra; Drouet, Martine; Choiset, Yvan; et al.; Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin; Elsevier; Food Chemistry; 127; 2; 15-7-2011; 487-492
dc.identifier.issn
0308-8146
dc.identifier.uri
http://hdl.handle.net/11336/57250
dc.description.abstract
The whey protein β-lactoglobulin (BLG) is highly allergenic. Lactic acid bacteria can degrade milk proteins. The capacity of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 to hydrolyse the major BLG epitopes (V41-K60; Y102-R124; L149-I162) and decrease their recognition by IgE of allergic patients was evaluated. The intensity of BLG degradation was analysed by Tricine SDS-PAGE and RP-HPLC. Peptides released were identified by LC-MS/MS and the hydrolysates were tested for their capacity to inhibit IgE binding by ELISA test. L. delbrueckii subsp. bulgaricus CRL 656 degraded BLG (35%, 8 h). The sequence analysis of the released peptides indicated that this strain degraded three main BLG epitopes. BLG-positive sera (3-5 year old children) were used for testing IgE binding inhibition of BLG hydrolysates from the Lactobacillus strain. The hydrolysates were less immuno-reactive (32%) than the heated BLG. L. delbrueckii subsp. bulgaricus CRL 656 could be used for developing hypoallergenic dairy products.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Β-Lactoglobulin
dc.subject
Allergy
dc.subject
Lactic Acid Bacteria
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Lactobacillus
dc.subject.classification
Alimentos y Bebidas
dc.subject.classification
Otras Ingenierías y Tecnologías
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-04-05T18:42:25Z
dc.journal.volume
127
dc.journal.number
2
dc.journal.pagination
487-492
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Pescuma, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
dc.description.fil
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
dc.description.fil
Fil: Rabesona, Hanitra. Institut National de la Recherche Agronomique; Francia
dc.description.fil
Fil: Drouet, Martine. Unité Allergologie Générale et Pneumologie; Francia
dc.description.fil
Fil: Choiset, Yvan. Institut National de la Recherche Agronomique; Francia
dc.description.fil
Fil: Haertlé, Thomas. Institut National de la Recherche Agronomique; Francia
dc.description.fil
Fil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
dc.description.fil
Fil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
dc.description.fil
Fil: Chobert, Jean-Marc. Institut National de la Recherche Agronomique; Francia
dc.journal.title
Food Chemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.foodchem.2011.01.029
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0308814611000914
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