Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain

Autores
Bustos, Ana Yanina; Font, Graciela Maria; Raya, Raul Ricardo; Taranto, Maria Pia
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Intestinal microbes containing the bile salt hydrolase (BSH) enzyme, releases free BA plus amino acids from conjugated BA. BSH activity triggers cholesterol consumption in liver to synthesize BA de novo leading to consequential cholesterol lowering. Lactobacillus (L.) reuteri CRL 1098 is a probiotic bacterium with a proven hypocholesterolemic effect associated to its ability to hydrolyze BA. In this work we characterized the bile salt hydrolase (bsh) operon of CRL 1098 strain as a single open reading frame of 978 nucleotides that encodes a predicted protein of 325 amino acids, with a calculated mass of 36098.1 Da and a theoretical pI of 4.81. Moreover, deduced BSH protein had high similarity with BSHs of other L. reuteri strain and also exhibited similarity to the Pencillin V amidases of Listeria and Bacillus strains. Five catalytically important amino acids were highly conserved in Lactobacillus, Enterococcus and Bifidobacterium strains while four amino acid motifs around these active sites, were only partially conserved. After the bsh gene product was expressed in the heterologous host Lactococcus lactis NZ9000. The activity was specific towards bile acids but not against alternative substrates. Finally, a significant up-regulation of the bsh gene was observed at pH 5.2 (optimal pH of BSH activity). Our studies suggest that BSHs would have an important but so far unknown role in the physiology and lifestyle of L. reuteri strains. The present work would be useful to unravel the ecological role of the BSH and to deepen their influence in the reduction of blood cholesterol levels
Fil: Bustos, Ana Yanina. 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. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Taranto, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Materia
LACTOBACILLUS REUTERI
BILE SALT HYDROLASE
MOLECULAR CLONING
GENE EXPRESSION
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:11336/58982
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/58982
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic StrainBustos, Ana YaninaFont, Graciela MariaRaya, Raul RicardoTaranto, Maria PiaLACTOBACILLUS REUTERIBILE SALT HYDROLASEMOLECULAR CLONINGGENE EXPRESSIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Intestinal microbes containing the bile salt hydrolase (BSH) enzyme, releases free BA plus amino acids from conjugated BA. BSH activity triggers cholesterol consumption in liver to synthesize BA de novo leading to consequential cholesterol lowering. Lactobacillus (L.) reuteri CRL 1098 is a probiotic bacterium with a proven hypocholesterolemic effect associated to its ability to hydrolyze BA. In this work we characterized the bile salt hydrolase (bsh) operon of CRL 1098 strain as a single open reading frame of 978 nucleotides that encodes a predicted protein of 325 amino acids, with a calculated mass of 36098.1 Da and a theoretical pI of 4.81. Moreover, deduced BSH protein had high similarity with BSHs of other L. reuteri strain and also exhibited similarity to the Pencillin V amidases of Listeria and Bacillus strains. Five catalytically important amino acids were highly conserved in Lactobacillus, Enterococcus and Bifidobacterium strains while four amino acid motifs around these active sites, were only partially conserved. After the bsh gene product was expressed in the heterologous host Lactococcus lactis NZ9000. The activity was specific towards bile acids but not against alternative substrates. Finally, a significant up-regulation of the bsh gene was observed at pH 5.2 (optimal pH of BSH activity). Our studies suggest that BSHs would have an important but so far unknown role in the physiology and lifestyle of L. reuteri strains. The present work would be useful to unravel the ecological role of the BSH and to deepen their influence in the reduction of blood cholesterol levelsFil: Bustos, Ana Yanina. 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; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Taranto, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaSciDoc Publishers2016-05-04info: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/11336/58982Bustos, Ana Yanina; Font, Graciela Maria; Raya, Raul Ricardo; Taranto, Maria Pia; Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain; SciDoc Publishers; International Journal of Genomics, Proteomics, Metabolomics & Bioinformatics; 1; 1; 4-5-2016; 1-82332-27562332-2756CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.19070/2577-4336-160001info:eu-repo/semantics/altIdentifier/url/https://scidoc.org/IJGPMB-2577-4336-01-101.phpinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:42:51Zoai:ri.conicet.gov.ar:11336/58982instacron: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:34982025-09-29 10:42:51.8CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
title Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
spellingShingle Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
Bustos, Ana Yanina
LACTOBACILLUS REUTERI
BILE SALT HYDROLASE
MOLECULAR CLONING
GENE EXPRESSION
title_short Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
title_full Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
title_fullStr Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
title_full_unstemmed Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
title_sort Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain
dc.creator.none.fl_str_mv Bustos, Ana Yanina
Font, Graciela Maria
Raya, Raul Ricardo
Taranto, Maria Pia
author Bustos, Ana Yanina
author_facet Bustos, Ana Yanina
Font, Graciela Maria
Raya, Raul Ricardo
Taranto, Maria Pia
author_role author
author2 Font, Graciela Maria
Raya, Raul Ricardo
Taranto, Maria Pia
author2_role author
author
author
dc.subject.none.fl_str_mv LACTOBACILLUS REUTERI
BILE SALT HYDROLASE
MOLECULAR CLONING
GENE EXPRESSION
topic LACTOBACILLUS REUTERI
BILE SALT HYDROLASE
MOLECULAR CLONING
GENE EXPRESSION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Intestinal microbes containing the bile salt hydrolase (BSH) enzyme, releases free BA plus amino acids from conjugated BA. BSH activity triggers cholesterol consumption in liver to synthesize BA de novo leading to consequential cholesterol lowering. Lactobacillus (L.) reuteri CRL 1098 is a probiotic bacterium with a proven hypocholesterolemic effect associated to its ability to hydrolyze BA. In this work we characterized the bile salt hydrolase (bsh) operon of CRL 1098 strain as a single open reading frame of 978 nucleotides that encodes a predicted protein of 325 amino acids, with a calculated mass of 36098.1 Da and a theoretical pI of 4.81. Moreover, deduced BSH protein had high similarity with BSHs of other L. reuteri strain and also exhibited similarity to the Pencillin V amidases of Listeria and Bacillus strains. Five catalytically important amino acids were highly conserved in Lactobacillus, Enterococcus and Bifidobacterium strains while four amino acid motifs around these active sites, were only partially conserved. After the bsh gene product was expressed in the heterologous host Lactococcus lactis NZ9000. The activity was specific towards bile acids but not against alternative substrates. Finally, a significant up-regulation of the bsh gene was observed at pH 5.2 (optimal pH of BSH activity). Our studies suggest that BSHs would have an important but so far unknown role in the physiology and lifestyle of L. reuteri strains. The present work would be useful to unravel the ecological role of the BSH and to deepen their influence in the reduction of blood cholesterol levels
Fil: Bustos, Ana Yanina. 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. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Raya, Raul Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Taranto, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
description Intestinal microbes containing the bile salt hydrolase (BSH) enzyme, releases free BA plus amino acids from conjugated BA. BSH activity triggers cholesterol consumption in liver to synthesize BA de novo leading to consequential cholesterol lowering. Lactobacillus (L.) reuteri CRL 1098 is a probiotic bacterium with a proven hypocholesterolemic effect associated to its ability to hydrolyze BA. In this work we characterized the bile salt hydrolase (bsh) operon of CRL 1098 strain as a single open reading frame of 978 nucleotides that encodes a predicted protein of 325 amino acids, with a calculated mass of 36098.1 Da and a theoretical pI of 4.81. Moreover, deduced BSH protein had high similarity with BSHs of other L. reuteri strain and also exhibited similarity to the Pencillin V amidases of Listeria and Bacillus strains. Five catalytically important amino acids were highly conserved in Lactobacillus, Enterococcus and Bifidobacterium strains while four amino acid motifs around these active sites, were only partially conserved. After the bsh gene product was expressed in the heterologous host Lactococcus lactis NZ9000. The activity was specific towards bile acids but not against alternative substrates. Finally, a significant up-regulation of the bsh gene was observed at pH 5.2 (optimal pH of BSH activity). Our studies suggest that BSHs would have an important but so far unknown role in the physiology and lifestyle of L. reuteri strains. The present work would be useful to unravel the ecological role of the BSH and to deepen their influence in the reduction of blood cholesterol levels
publishDate 2016
dc.date.none.fl_str_mv 2016-05-04
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/11336/58982
Bustos, Ana Yanina; Font, Graciela Maria; Raya, Raul Ricardo; Taranto, Maria Pia; Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain; SciDoc Publishers; International Journal of Genomics, Proteomics, Metabolomics & Bioinformatics; 1; 1; 4-5-2016; 1-8
2332-2756
2332-2756
CONICET Digital
CONICET
url http://hdl.handle.net/11336/58982
identifier_str_mv Bustos, Ana Yanina; Font, Graciela Maria; Raya, Raul Ricardo; Taranto, Maria Pia; Genetic Characterization and Gene Expression of Bile Salt Hydrolase (bsh ) from Lactobacillus reuteri CRL 1098, a Probiotic Strain; SciDoc Publishers; International Journal of Genomics, Proteomics, Metabolomics & Bioinformatics; 1; 1; 4-5-2016; 1-8
2332-2756
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.19070/2577-4336-160001
info:eu-repo/semantics/altIdentifier/url/https://scidoc.org/IJGPMB-2577-4336-01-101.php
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 SciDoc Publishers
publisher.none.fl_str_mv SciDoc Publishers
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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