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dc.contributor.author
Gerez, Carla Luciana
dc.contributor.author
Font, Graciela Maria
dc.contributor.author
Rollan, Graciela Celestina
dc.date.available
2018-08-10T20:48:22Z
dc.date.issued
2008-11
dc.identifier.citation
Gerez, Carla Luciana; Font, Graciela Maria; Rollan, Graciela Celestina; Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments; Wiley Blackwell Publishing, Inc; Letters in Applied Microbiology; 47; 5; 11-2008; 427-432
dc.identifier.issn
0266-8254
dc.identifier.uri
http://hdl.handle.net/11336/55011
dc.description.abstract
Aims: To evaluate the role of the peptidase activities from sourdough lactic acid bacteria (LAB) in the degradation of α-gliadin fragments. Methods and Results: Different proline-containing substrates were hydrolysed by LAB indicating pro-specific peptidase activities. Lactobacillus plantarum CRL 775 and Pediococcus pentosaceus CRL 792 displayed the highest tri- and di-peptidase activities, respectively. Lactobacillus plantarum strains hydrolysed more than 60%α-gliadin fragments corresponding to the 31-43 and 62-75 amino acids in the protein after 2 h. None of the LAB strains alone could hydrolyse 57-89 α-gliadin peptide; however, the combination of L. plantarum CRL 775 and P. pentosaceus CRL 792 led to hydrolysis (57%) of this peptide in 8 h. Conclusions: The capacity of LAB strains to degrade α-gliadin fragments was not correlated to individual peptidase activities. Several strains separately degraded the 31-43 and 62-75 α-gliadin fragments, while the 57-89 peptide degradation was associated with the combination of peptidase profiles from pooled LAB strains. This is the first report on the peptide hydrolase system of sourdough pediococci and its ability to reduce α-gliadin fragments. Significance and Impact of the Study: This study contributes to a better knowledge of sourdough LAB proteolytic system and its role in the degradation of proline-rich α-gliadin peptides involved in celiac disease. © 2008 The Authors.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Α-Gliadin Fragments
dc.subject
Lactic Acid Bacteria
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Pediococci
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Proteolysis
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Sourdough
dc.subject.classification
Alimentos y Bebidas
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Otras Ingenierías y Tecnologías
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-07-11T15:23:43Z
dc.identifier.eissn
1472-765X
dc.journal.volume
47
dc.journal.number
5
dc.journal.pagination
427-432
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Gerez, Carla Luciana. 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: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
dc.journal.title
Letters in Applied Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/j.1472-765X.2008.02448.x
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1472-765X.2008.02448.x
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