Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments

Autores
Gerez, Carla Luciana; Font, Graciela Maria; Rollan, Graciela Celestina
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Gerez, Carla Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
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
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Materia
Α-Gliadin Fragments
Lactic Acid Bacteria
Pediococci
Proteolysis
Sourdough
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:11336/55011
Acceder
id CONICETDig_78a3e1e9d3fc1d1791674818a9d4bbf5
oai_identifier_str oai:ri.conicet.gov.ar:11336/55011
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragmentsGerez, Carla LucianaFont, Graciela MariaRollan, Graciela CelestinaΑ-Gliadin FragmentsLactic Acid BacteriaPediococciProteolysisSourdoughhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Aims: 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.Fil: Gerez, Carla Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: 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; ArgentinaFil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaWiley Blackwell Publishing, Inc2008-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55011Gerez, 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; 427-4320266-82541472-765XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1472-765X.2008.02448.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1472-765X.2008.02448.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:23Zoai:ri.conicet.gov.ar:11336/55011instacron: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 09:45:23.484CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
title Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
spellingShingle Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
Gerez, Carla Luciana
Α-Gliadin Fragments
Lactic Acid Bacteria
Pediococci
Proteolysis
Sourdough
title_short Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
title_full Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
title_fullStr Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
title_full_unstemmed Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
title_sort Functionality of lactic acid bacteria peptidase activities in the hydrolysis of gliadin-like fragments
dc.creator.none.fl_str_mv Gerez, Carla Luciana
Font, Graciela Maria
Rollan, Graciela Celestina
author Gerez, Carla Luciana
author_facet Gerez, Carla Luciana
Font, Graciela Maria
Rollan, Graciela Celestina
author_role author
author2 Font, Graciela Maria
Rollan, Graciela Celestina
author2_role author
author
dc.subject.none.fl_str_mv Α-Gliadin Fragments
Lactic Acid Bacteria
Pediococci
Proteolysis
Sourdough
topic Α-Gliadin Fragments
Lactic Acid Bacteria
Pediococci
Proteolysis
Sourdough
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv 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.
Fil: Gerez, Carla Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
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
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
description 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.
publishDate 2008
dc.date.none.fl_str_mv 2008-11
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/11336/55011
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
0266-8254
1472-765X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55011
identifier_str_mv 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
0266-8254
1472-765X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1472-765X.2008.02448.x
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1472-765X.2008.02448.x
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
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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score 13.13397

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