Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches

Autores
Ortiz, María Eugenia; Bleckwedel, Juliana; Fadda, Silvina G.; Picariello, Gianluca; Hebert, Elvira Maria; Raya, Raul Ricardo; Mozzi, Fernanda Beatriz
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Several plants, fungi, algae, and certain bacteria produce mannitol, a polyol derived from fructose. Mannitol has multiple industrial applications in the food, pharmaceutical, and medical industries, being mainly used as a non-metabolizable sweetener in foods. Many heterofermentative lactic acid bacteria synthesize mannitol when an alternative electron acceptor such as fructose is present in the medium. In previous work, we reported the ability of Lactobacillus reuteri CRL 1101 to efficiently produce mannitol from sugarcane molasses as carbon source at constant pH of 5.0; the activity of the enzyme mannitol 2-dehydrogenase (MDH) responsible for the fructose conversion into mannitol being highest during the log cell growth phase. Here, a detailed assessment of the MDH activity and relative expression of the mdh gene during the growth of L. reuteri CRL 1101 in the presence of fructose is presented. It was observed that MDH was markedly induced by the presence of fructose. A direct correlation between the maximum MDH enzyme activity and a high level of mdh transcript expression during the log-phase of cells grown in a fructose-containing chemically defined medium was detected. Furthermore, two proteomic approaches (2DE and shotgun proteomics) applied in this study confirmed the inducible expression of MDH in L. reuteri. A global study of the effect of fructose on activity, mdh gene, and protein expressions of MDH in L. reuteri is thus for the first time presented. This work represents a deep insight into the polyol formation by a Lactobacillus strain with biotechnological potential in the nutraceutics and pharmaceutical areas.
Fil: Ortiz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Bleckwedel, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Fadda, Silvina G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Picariello, Gianluca. Istituto Di Scienze Dell'alimentazione; Italia
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Raya, Raul Ricardo. University of Toronto; Canadá. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Materia
lactic acid bacteria
manitol dehydrogenase
fermentation
proteomics
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:11336/37402
Acceder
id CONICETDig_e3e23d317d2e695a30218db445177049
oai_identifier_str oai:ri.conicet.gov.ar:11336/37402
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approachesOrtiz, María EugeniaBleckwedel, JulianaFadda, Silvina G.Picariello, GianlucaHebert, Elvira MariaRaya, Raul RicardoMozzi, Fernanda Beatrizlactic acid bacteriamanitol dehydrogenasefermentationproteomicshttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Several plants, fungi, algae, and certain bacteria produce mannitol, a polyol derived from fructose. Mannitol has multiple industrial applications in the food, pharmaceutical, and medical industries, being mainly used as a non-metabolizable sweetener in foods. Many heterofermentative lactic acid bacteria synthesize mannitol when an alternative electron acceptor such as fructose is present in the medium. In previous work, we reported the ability of Lactobacillus reuteri CRL 1101 to efficiently produce mannitol from sugarcane molasses as carbon source at constant pH of 5.0; the activity of the enzyme mannitol 2-dehydrogenase (MDH) responsible for the fructose conversion into mannitol being highest during the log cell growth phase. Here, a detailed assessment of the MDH activity and relative expression of the mdh gene during the growth of L. reuteri CRL 1101 in the presence of fructose is presented. It was observed that MDH was markedly induced by the presence of fructose. A direct correlation between the maximum MDH enzyme activity and a high level of mdh transcript expression during the log-phase of cells grown in a fructose-containing chemically defined medium was detected. Furthermore, two proteomic approaches (2DE and shotgun proteomics) applied in this study confirmed the inducible expression of MDH in L. reuteri. A global study of the effect of fructose on activity, mdh gene, and protein expressions of MDH in L. reuteri is thus for the first time presented. This work represents a deep insight into the polyol formation by a Lactobacillus strain with biotechnological potential in the nutraceutics and pharmaceutical areas.Fil: Ortiz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Bleckwedel, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Fadda, Silvina G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Picariello, Gianluca. Istituto Di Scienze Dell'alimentazione; ItaliaFil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Raya, Raul Ricardo. University of Toronto; Canadá. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaFil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; ArgentinaPublic Library of Science2017-01info: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/11336/37402Ortiz, María Eugenia; Bleckwedel, Juliana; Fadda, Silvina G.; Picariello, Gianluca; Hebert, Elvira Maria; et al.; Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches; Public Library of Science; Plos One; 12; 1; 1-2017; 1-211932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0169441info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0169441info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:27:52Zoai:ri.conicet.gov.ar:11336/37402instacron: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 14:27:53.173CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
title Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
spellingShingle Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
Ortiz, María Eugenia
lactic acid bacteria
manitol dehydrogenase
fermentation
proteomics
title_short Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
title_full Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
title_fullStr Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
title_full_unstemmed Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
title_sort Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches
dc.creator.none.fl_str_mv Ortiz, María Eugenia
Bleckwedel, Juliana
Fadda, Silvina G.
Picariello, Gianluca
Hebert, Elvira Maria
Raya, Raul Ricardo
Mozzi, Fernanda Beatriz
author Ortiz, María Eugenia
author_facet Ortiz, María Eugenia
Bleckwedel, Juliana
Fadda, Silvina G.
Picariello, Gianluca
Hebert, Elvira Maria
Raya, Raul Ricardo
Mozzi, Fernanda Beatriz
author_role author
author2 Bleckwedel, Juliana
Fadda, Silvina G.
Picariello, Gianluca
Hebert, Elvira Maria
Raya, Raul Ricardo
Mozzi, Fernanda Beatriz
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv lactic acid bacteria
manitol dehydrogenase
fermentation
proteomics
topic lactic acid bacteria
manitol dehydrogenase
fermentation
proteomics
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Several plants, fungi, algae, and certain bacteria produce mannitol, a polyol derived from fructose. Mannitol has multiple industrial applications in the food, pharmaceutical, and medical industries, being mainly used as a non-metabolizable sweetener in foods. Many heterofermentative lactic acid bacteria synthesize mannitol when an alternative electron acceptor such as fructose is present in the medium. In previous work, we reported the ability of Lactobacillus reuteri CRL 1101 to efficiently produce mannitol from sugarcane molasses as carbon source at constant pH of 5.0; the activity of the enzyme mannitol 2-dehydrogenase (MDH) responsible for the fructose conversion into mannitol being highest during the log cell growth phase. Here, a detailed assessment of the MDH activity and relative expression of the mdh gene during the growth of L. reuteri CRL 1101 in the presence of fructose is presented. It was observed that MDH was markedly induced by the presence of fructose. A direct correlation between the maximum MDH enzyme activity and a high level of mdh transcript expression during the log-phase of cells grown in a fructose-containing chemically defined medium was detected. Furthermore, two proteomic approaches (2DE and shotgun proteomics) applied in this study confirmed the inducible expression of MDH in L. reuteri. A global study of the effect of fructose on activity, mdh gene, and protein expressions of MDH in L. reuteri is thus for the first time presented. This work represents a deep insight into the polyol formation by a Lactobacillus strain with biotechnological potential in the nutraceutics and pharmaceutical areas.
Fil: Ortiz, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Bleckwedel, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Fadda, Silvina G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Picariello, Gianluca. Istituto Di Scienze Dell'alimentazione; Italia
Fil: Hebert, Elvira Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Raya, Raul Ricardo. University of Toronto; Canadá. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
Fil: Mozzi, Fernanda Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina
description Several plants, fungi, algae, and certain bacteria produce mannitol, a polyol derived from fructose. Mannitol has multiple industrial applications in the food, pharmaceutical, and medical industries, being mainly used as a non-metabolizable sweetener in foods. Many heterofermentative lactic acid bacteria synthesize mannitol when an alternative electron acceptor such as fructose is present in the medium. In previous work, we reported the ability of Lactobacillus reuteri CRL 1101 to efficiently produce mannitol from sugarcane molasses as carbon source at constant pH of 5.0; the activity of the enzyme mannitol 2-dehydrogenase (MDH) responsible for the fructose conversion into mannitol being highest during the log cell growth phase. Here, a detailed assessment of the MDH activity and relative expression of the mdh gene during the growth of L. reuteri CRL 1101 in the presence of fructose is presented. It was observed that MDH was markedly induced by the presence of fructose. A direct correlation between the maximum MDH enzyme activity and a high level of mdh transcript expression during the log-phase of cells grown in a fructose-containing chemically defined medium was detected. Furthermore, two proteomic approaches (2DE and shotgun proteomics) applied in this study confirmed the inducible expression of MDH in L. reuteri. A global study of the effect of fructose on activity, mdh gene, and protein expressions of MDH in L. reuteri is thus for the first time presented. This work represents a deep insight into the polyol formation by a Lactobacillus strain with biotechnological potential in the nutraceutics and pharmaceutical areas.
publishDate 2017
dc.date.none.fl_str_mv 2017-01
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/11336/37402
Ortiz, María Eugenia; Bleckwedel, Juliana; Fadda, Silvina G.; Picariello, Gianluca; Hebert, Elvira Maria; et al.; Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches; Public Library of Science; Plos One; 12; 1; 1-2017; 1-21
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37402
identifier_str_mv Ortiz, María Eugenia; Bleckwedel, Juliana; Fadda, Silvina G.; Picariello, Gianluca; Hebert, Elvira Maria; et al.; Global analysis of mannitol 2-dehydrogenase in lactobacillus reuteri crl 1101 during mannitol production through enzymatic, genetic and proteomic approaches; Public Library of Science; Plos One; 12; 1; 1-2017; 1-21
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0169441
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0169441
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 Public Library of Science
publisher.none.fl_str_mv Public Library of 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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