Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli

Autores
Rollan, Graciela Celestina; De Angelis, M.; Gobbetti, M.; Font, Graciela Maria
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aims: To characterize the peptide hydrolase system of Lactobacillus plantarum CRL 759 and CRL 778 and evaluate their proteolytic activity in reducing gliadin-like fractions. Methods and Results: The intracellular peptide hydrolase system of Lact. plantarum CRL 759 and CRL 778 involves amino-, di- (DP), tri- (TP) and endopeptidase activities. These peptidases are metalloenzymes inhibited by EDTA and 1,10-phenanthroline and stimulated by Co2+. DP and TP activities of Lact. plantarum CRL 759 and CRL 778, respectively, were completely inhibited by Cu2+. Lactobacillus plantarum CRL 778 showed the highest proteolytic activity and amino acids release in fermented dough. The synthetic 31-43 a-gliadin fragment was hydrolysed to 36% and 73% by Lact. plantarum CRL 778 and CRL 759 respectively. Conclusions: Lactobacillus plantarum CRL 759 and CRL 778 have an active proteolytic system, which is responsible for the high amino acid release during sourdough fermentation and the hydrolysis of the 31-43 α-gliadin-like fragment. Significance and Impact of the Study: This work provides new information of use when obtaining sourdough starters for bread making. Moreover, knowledge regarding lactobacilli capable of reducing the level of gliadin-like fractions, a toxic peptide for coeliac patients, has a beneficial health impact.
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: De Angelis, M.. Istituto Scienze delle Produzioni Alimentari; Italia
Fil: Gobbetti, M.. Università degli Studi di Bari; Italia
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; Argentina
Materia
Gliadin
Lactobacillus
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:11336/55384
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/55384
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilliRollan, Graciela CelestinaDe Angelis, M.Gobbetti, M.Font, Graciela MariaGliadinLactobacillusProteolysisSourdoughhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Aims: To characterize the peptide hydrolase system of Lactobacillus plantarum CRL 759 and CRL 778 and evaluate their proteolytic activity in reducing gliadin-like fractions. Methods and Results: The intracellular peptide hydrolase system of Lact. plantarum CRL 759 and CRL 778 involves amino-, di- (DP), tri- (TP) and endopeptidase activities. These peptidases are metalloenzymes inhibited by EDTA and 1,10-phenanthroline and stimulated by Co2+. DP and TP activities of Lact. plantarum CRL 759 and CRL 778, respectively, were completely inhibited by Cu2+. Lactobacillus plantarum CRL 778 showed the highest proteolytic activity and amino acids release in fermented dough. The synthetic 31-43 a-gliadin fragment was hydrolysed to 36% and 73% by Lact. plantarum CRL 778 and CRL 759 respectively. Conclusions: Lactobacillus plantarum CRL 759 and CRL 778 have an active proteolytic system, which is responsible for the high amino acid release during sourdough fermentation and the hydrolysis of the 31-43 α-gliadin-like fragment. Significance and Impact of the Study: This work provides new information of use when obtaining sourdough starters for bread making. Moreover, knowledge regarding lactobacilli capable of reducing the level of gliadin-like fractions, a toxic peptide for coeliac patients, has a beneficial health impact.Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: De Angelis, M.. Istituto Scienze delle Produzioni Alimentari; ItaliaFil: Gobbetti, M.. Università degli Studi di Bari; ItaliaFil: 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; ArgentinaWiley Blackwell Publishing, Inc2005-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55384Rollan, Graciela Celestina; De Angelis, M.; Gobbetti, M.; Font, Graciela Maria; Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 99; 6; 12-2005; 1495-15021364-5072CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2672.2005.02730.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1365-2672.2005.02730.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 Técnicas2025-09-03T10:07:34Zoai:ri.conicet.gov.ar:11336/55384instacron: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 10:07:35.167CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
title Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
spellingShingle Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
Rollan, Graciela Celestina
Gliadin
Lactobacillus
Proteolysis
Sourdough
title_short Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
title_full Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
title_fullStr Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
title_full_unstemmed Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
title_sort Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli
dc.creator.none.fl_str_mv Rollan, Graciela Celestina
De Angelis, M.
Gobbetti, M.
Font, Graciela Maria
author Rollan, Graciela Celestina
author_facet Rollan, Graciela Celestina
De Angelis, M.
Gobbetti, M.
Font, Graciela Maria
author_role author
author2 De Angelis, M.
Gobbetti, M.
Font, Graciela Maria
author2_role author
author
author
dc.subject.none.fl_str_mv Gliadin
Lactobacillus
Proteolysis
Sourdough
topic Gliadin
Lactobacillus
Proteolysis
Sourdough
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Aims: To characterize the peptide hydrolase system of Lactobacillus plantarum CRL 759 and CRL 778 and evaluate their proteolytic activity in reducing gliadin-like fractions. Methods and Results: The intracellular peptide hydrolase system of Lact. plantarum CRL 759 and CRL 778 involves amino-, di- (DP), tri- (TP) and endopeptidase activities. These peptidases are metalloenzymes inhibited by EDTA and 1,10-phenanthroline and stimulated by Co2+. DP and TP activities of Lact. plantarum CRL 759 and CRL 778, respectively, were completely inhibited by Cu2+. Lactobacillus plantarum CRL 778 showed the highest proteolytic activity and amino acids release in fermented dough. The synthetic 31-43 a-gliadin fragment was hydrolysed to 36% and 73% by Lact. plantarum CRL 778 and CRL 759 respectively. Conclusions: Lactobacillus plantarum CRL 759 and CRL 778 have an active proteolytic system, which is responsible for the high amino acid release during sourdough fermentation and the hydrolysis of the 31-43 α-gliadin-like fragment. Significance and Impact of the Study: This work provides new information of use when obtaining sourdough starters for bread making. Moreover, knowledge regarding lactobacilli capable of reducing the level of gliadin-like fractions, a toxic peptide for coeliac patients, has a beneficial health impact.
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: De Angelis, M.. Istituto Scienze delle Produzioni Alimentari; Italia
Fil: Gobbetti, M.. Università degli Studi di Bari; Italia
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; Argentina
description Aims: To characterize the peptide hydrolase system of Lactobacillus plantarum CRL 759 and CRL 778 and evaluate their proteolytic activity in reducing gliadin-like fractions. Methods and Results: The intracellular peptide hydrolase system of Lact. plantarum CRL 759 and CRL 778 involves amino-, di- (DP), tri- (TP) and endopeptidase activities. These peptidases are metalloenzymes inhibited by EDTA and 1,10-phenanthroline and stimulated by Co2+. DP and TP activities of Lact. plantarum CRL 759 and CRL 778, respectively, were completely inhibited by Cu2+. Lactobacillus plantarum CRL 778 showed the highest proteolytic activity and amino acids release in fermented dough. The synthetic 31-43 a-gliadin fragment was hydrolysed to 36% and 73% by Lact. plantarum CRL 778 and CRL 759 respectively. Conclusions: Lactobacillus plantarum CRL 759 and CRL 778 have an active proteolytic system, which is responsible for the high amino acid release during sourdough fermentation and the hydrolysis of the 31-43 α-gliadin-like fragment. Significance and Impact of the Study: This work provides new information of use when obtaining sourdough starters for bread making. Moreover, knowledge regarding lactobacilli capable of reducing the level of gliadin-like fractions, a toxic peptide for coeliac patients, has a beneficial health impact.
publishDate 2005
dc.date.none.fl_str_mv 2005-12
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/11336/55384
Rollan, Graciela Celestina; De Angelis, M.; Gobbetti, M.; Font, Graciela Maria; Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 99; 6; 12-2005; 1495-1502
1364-5072
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55384
identifier_str_mv Rollan, Graciela Celestina; De Angelis, M.; Gobbetti, M.; Font, Graciela Maria; Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 99; 6; 12-2005; 1495-1502
1364-5072
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.1365-2672.2005.02730.x
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1365-2672.2005.02730.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
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
_version_ 1842270007867736064
score 12.885934

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