The peptide hydrolase system of Lactobacillus reuteri

Autores
Rollan, Graciela Celestina; Font, Graciela Maria
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Peptide hydrolase system of Lactobacillus reuteri CRL 1098, a lactic acid bacteria of sourdough origin, was investigated. This microorganism has a broad range of peptidases consisting of an active aminopeptidase, X-Prolyl-dipeptidylaminopeptidase, dipeptidase and tripeptidase. Aminopeptidase, iminopeptidase and endopeptidase are most likely located in the cytoplasmic fraction showing no detectable association with the cell membrane, while dipeptidase and tripeptidase are mainly associated with the latter fraction. The peptidases are metalloenzymes activated by Co2+ and inhibited by Cu2+, Hg2+, Cd2+ and by metal-complexing reagents. The aminopeptidase activity inhibited by EDTA can be restored by Mn2+ while that of di- and tripeptidase treated with 1,10-phenantroline can be restored by Zn2+ and Co2+, respectively.
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Materia
Lactic Acid Bacteria
Peptidases
Sourdough
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/38268
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling The peptide hydrolase system of Lactobacillus reuteriRollan, Graciela CelestinaFont, Graciela MariaLactic Acid BacteriaPeptidasesSourdoughhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Peptide hydrolase system of Lactobacillus reuteri CRL 1098, a lactic acid bacteria of sourdough origin, was investigated. This microorganism has a broad range of peptidases consisting of an active aminopeptidase, X-Prolyl-dipeptidylaminopeptidase, dipeptidase and tripeptidase. Aminopeptidase, iminopeptidase and endopeptidase are most likely located in the cytoplasmic fraction showing no detectable association with the cell membrane, while dipeptidase and tripeptidase are mainly associated with the latter fraction. The peptidases are metalloenzymes activated by Co2+ and inhibited by Cu2+, Hg2+, Cd2+ and by metal-complexing reagents. The aminopeptidase activity inhibited by EDTA can be restored by Mn2+ while that of di- and tripeptidase treated with 1,10-phenantroline can be restored by Zn2+ and Co2+, respectively.Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaElsevier Science2001-11info: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/11336/38268Rollan, Graciela Celestina; Font, Graciela Maria; The peptide hydrolase system of Lactobacillus reuteri; Elsevier Science; International Journal of Food Microbiology; 70; 3; 11-2001; 303-3070168-1605CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0168-1605(01)00544-Xinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S016816050100544Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:12:25Zoai:ri.conicet.gov.ar:11336/38268instacron: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:34982025-10-15 15:12:26.005CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The peptide hydrolase system of Lactobacillus reuteri
title The peptide hydrolase system of Lactobacillus reuteri
spellingShingle The peptide hydrolase system of Lactobacillus reuteri
Rollan, Graciela Celestina
Lactic Acid Bacteria
Peptidases
Sourdough
title_short The peptide hydrolase system of Lactobacillus reuteri
title_full The peptide hydrolase system of Lactobacillus reuteri
title_fullStr The peptide hydrolase system of Lactobacillus reuteri
title_full_unstemmed The peptide hydrolase system of Lactobacillus reuteri
title_sort The peptide hydrolase system of Lactobacillus reuteri
dc.creator.none.fl_str_mv Rollan, Graciela Celestina
Font, Graciela Maria
author Rollan, Graciela Celestina
author_facet Rollan, Graciela Celestina
Font, Graciela Maria
author_role author
author2 Font, Graciela Maria
author2_role author
dc.subject.none.fl_str_mv Lactic Acid Bacteria
Peptidases
Sourdough
topic Lactic Acid Bacteria
Peptidases
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 Peptide hydrolase system of Lactobacillus reuteri CRL 1098, a lactic acid bacteria of sourdough origin, was investigated. This microorganism has a broad range of peptidases consisting of an active aminopeptidase, X-Prolyl-dipeptidylaminopeptidase, dipeptidase and tripeptidase. Aminopeptidase, iminopeptidase and endopeptidase are most likely located in the cytoplasmic fraction showing no detectable association with the cell membrane, while dipeptidase and tripeptidase are mainly associated with the latter fraction. The peptidases are metalloenzymes activated by Co2+ and inhibited by Cu2+, Hg2+, Cd2+ and by metal-complexing reagents. The aminopeptidase activity inhibited by EDTA can be restored by Mn2+ while that of di- and tripeptidase treated with 1,10-phenantroline can be restored by Zn2+ and Co2+, respectively.
Fil: Rollan, Graciela Celestina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Font, Graciela Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
description Peptide hydrolase system of Lactobacillus reuteri CRL 1098, a lactic acid bacteria of sourdough origin, was investigated. This microorganism has a broad range of peptidases consisting of an active aminopeptidase, X-Prolyl-dipeptidylaminopeptidase, dipeptidase and tripeptidase. Aminopeptidase, iminopeptidase and endopeptidase are most likely located in the cytoplasmic fraction showing no detectable association with the cell membrane, while dipeptidase and tripeptidase are mainly associated with the latter fraction. The peptidases are metalloenzymes activated by Co2+ and inhibited by Cu2+, Hg2+, Cd2+ and by metal-complexing reagents. The aminopeptidase activity inhibited by EDTA can be restored by Mn2+ while that of di- and tripeptidase treated with 1,10-phenantroline can be restored by Zn2+ and Co2+, respectively.
publishDate 2001
dc.date.none.fl_str_mv 2001-11
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/11336/38268
Rollan, Graciela Celestina; Font, Graciela Maria; The peptide hydrolase system of Lactobacillus reuteri; Elsevier Science; International Journal of Food Microbiology; 70; 3; 11-2001; 303-307
0168-1605
CONICET Digital
CONICET
url http://hdl.handle.net/11336/38268
identifier_str_mv Rollan, Graciela Celestina; Font, Graciela Maria; The peptide hydrolase system of Lactobacillus reuteri; Elsevier Science; International Journal of Food Microbiology; 70; 3; 11-2001; 303-307
0168-1605
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/S0168-1605(01)00544-X
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S016816050100544X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 13.22299

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