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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/37402
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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 Técnicas2025-09-29T09:38:40Zoai: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:34982025-09-29 09:38:41.127CONICET 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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1844613222796099584 |
score |
13.070432 |