Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581...

Autores
Hebert, Elvira Maria; Mamone, Gianfranco; Picariello, Gianluca; Raya, Raul Ricardo; Savoy, Graciela; Ferranti, Pasquale; Addeo, Francesco
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Mamone, Gianfranco. Centro di Spettrometria di Massa Proteomica e Biomolecolare; Italia
Fil: Picariello, Gianluca. Centro di Spettrometria di Massa Proteomica e Biomolecolare; Italia
Fil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Savoy, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Ferranti, Pasquale. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; Italia
Fil: Addeo, Francesco. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; Italia
Materia
Lactobacillus Delbrueckii Subsp. Lactis
Peptide Bioactive
Proteinase
Caseins
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:11336/52215
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/52215
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581Hebert, Elvira MariaMamone, GianfrancoPicariello, GianlucaRaya, Raul RicardoSavoy, GracielaFerranti, PasqualeAddeo, FrancescoLactobacillus Delbrueckii Subsp. LactisPeptide BioactiveProteinaseCaseinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized. Copyright © 2008, American Society for Microbiology. All Rights Reserved.Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Mamone, Gianfranco. Centro di Spettrometria di Massa Proteomica e Biomolecolare; ItaliaFil: Picariello, Gianluca. Centro di Spettrometria di Massa Proteomica e Biomolecolare; ItaliaFil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Savoy, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Ferranti, Pasquale. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; ItaliaFil: Addeo, Francesco. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; ItaliaAmerican Society for Microbiology2008-06info: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/11336/52215Hebert, Elvira Maria; Mamone, Gianfranco; Picariello, Gianluca; Raya, Raul Ricardo; Savoy, Graciela; et al.; Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581; American Society for Microbiology; Applied And Environmental Microbiology; 74; 12; 6-2008; 3682-36890099-22401098-5336CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.00247-08info:eu-repo/semantics/altIdentifier/url/http://aem.asm.org/content/74/12/3682info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:12:51Zoai:ri.conicet.gov.ar:11336/52215instacron: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:34982025-09-10 13:12:51.259CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
title Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
spellingShingle Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
Hebert, Elvira Maria
Lactobacillus Delbrueckii Subsp. Lactis
Peptide Bioactive
Proteinase
Caseins
title_short Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
title_full Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
title_fullStr Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
title_full_unstemmed Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
title_sort Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
dc.creator.none.fl_str_mv Hebert, Elvira Maria
Mamone, Gianfranco
Picariello, Gianluca
Raya, Raul Ricardo
Savoy, Graciela
Ferranti, Pasquale
Addeo, Francesco
author Hebert, Elvira Maria
author_facet Hebert, Elvira Maria
Mamone, Gianfranco
Picariello, Gianluca
Raya, Raul Ricardo
Savoy, Graciela
Ferranti, Pasquale
Addeo, Francesco
author_role author
author2 Mamone, Gianfranco
Picariello, Gianluca
Raya, Raul Ricardo
Savoy, Graciela
Ferranti, Pasquale
Addeo, Francesco
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Lactobacillus Delbrueckii Subsp. Lactis
Peptide Bioactive
Proteinase
Caseins
topic Lactobacillus Delbrueckii Subsp. Lactis
Peptide Bioactive
Proteinase
Caseins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Mamone, Gianfranco. Centro di Spettrometria di Massa Proteomica e Biomolecolare; Italia
Fil: Picariello, Gianluca. Centro di Spettrometria di Massa Proteomica e Biomolecolare; Italia
Fil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Savoy, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Ferranti, Pasquale. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; Italia
Fil: Addeo, Francesco. University of Naples Federico II. Dipartimento di Scienza degli Alimenti; Italia
description The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
publishDate 2008
dc.date.none.fl_str_mv 2008-06
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/11336/52215
Hebert, Elvira Maria; Mamone, Gianfranco; Picariello, Gianluca; Raya, Raul Ricardo; Savoy, Graciela; et al.; Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581; American Society for Microbiology; Applied And Environmental Microbiology; 74; 12; 6-2008; 3682-3689
0099-2240
1098-5336
CONICET Digital
CONICET
url http://hdl.handle.net/11336/52215
identifier_str_mv Hebert, Elvira Maria; Mamone, Gianfranco; Picariello, Gianluca; Raya, Raul Ricardo; Savoy, Graciela; et al.; Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581; American Society for Microbiology; Applied And Environmental Microbiology; 74; 12; 6-2008; 3682-3689
0099-2240
1098-5336
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.00247-08
info:eu-repo/semantics/altIdentifier/url/http://aem.asm.org/content/74/12/3682
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 American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
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 12.993085

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