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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/58982
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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 Técnicas2025-09-03T10:10:26Zoai: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:34982025-09-03 10:10:27.226CONICET 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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13.13397 |