A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction

Autores
Ontañon, Ornella Mailen; Ghio, Silvina; Marrero Diaz De Villegas, Rubén; Garrido, Mercedes Maria; Talia, Paola Mónica; Fehér, Csaba; Campos, Eleonora
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glycoside hydrolase family 8 (GH8) includes endoglucanases, lichenases, chitosanases and xylanases, which are essential for polysaccharides breakdown. In this work, we studied a thermally stable GH8 from the cellulose synthase complex of Enterobacter sp. R1, for deconstruction of β-glucans. The biochemical characterization of the recombinant GH8ErCel showed high specificity towards barley β-glucan and lichenan and lower activity on carboxymethylcellulose and swollen cellulose, yielding different length oligosaccharides. By molecular modeling, six conserved subsites for glucose binding and some possible determinants for its lack of xylanase and chitosanase activity were identified. GH8ErCel was active at a broad range of pH and temperature and presented remarkable stability at 60 °C. Additionally, it hydrolyzed β-glucan from oat and wheat brans mainly to tri- and tetraoligosaccharides. Therefore, GH8ErCel may be a good candidate for enzymatic deconstruction of β-glucans at high temperature in food and feed industries, including the production of prebiotics and functional foods.
Instituto de Biotecnología
Fil: Ontañon, Ornella Mailén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marrero Diaz de Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fehér, Csaba. Budapest University of Technology and Economics. Faculty of Chemical Technology and Biotechnology. Department of Applied Biotechnology and Food Science. Biorefinery Research Group; Hungría
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fuente
Food Chemistry 298: 124999 (Noviembre 2019)
Materia
Glycosides
Glucans
Bran
Glicosidos
Enterobacter
Glucanos
Salvado
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/6637
Acceder
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network_acronym_str INTADig
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spelling A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstructionOntañon, Ornella MailenGhio, SilvinaMarrero Diaz De Villegas, RubénGarrido, Mercedes MariaTalia, Paola MónicaFehér, CsabaCampos, EleonoraGlycosidesGlucansBranGlicosidosEnterobacterGlucanosSalvadoGlycoside hydrolase family 8 (GH8) includes endoglucanases, lichenases, chitosanases and xylanases, which are essential for polysaccharides breakdown. In this work, we studied a thermally stable GH8 from the cellulose synthase complex of Enterobacter sp. R1, for deconstruction of β-glucans. The biochemical characterization of the recombinant GH8ErCel showed high specificity towards barley β-glucan and lichenan and lower activity on carboxymethylcellulose and swollen cellulose, yielding different length oligosaccharides. By molecular modeling, six conserved subsites for glucose binding and some possible determinants for its lack of xylanase and chitosanase activity were identified. GH8ErCel was active at a broad range of pH and temperature and presented remarkable stability at 60 °C. Additionally, it hydrolyzed β-glucan from oat and wheat brans mainly to tri- and tetraoligosaccharides. Therefore, GH8ErCel may be a good candidate for enzymatic deconstruction of β-glucans at high temperature in food and feed industries, including the production of prebiotics and functional foods.Instituto de BiotecnologíaFil: Ontañon, Ornella Mailén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marrero Diaz de Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fehér, Csaba. Budapest University of Technology and Economics. Faculty of Chemical Technology and Biotechnology. Department of Applied Biotechnology and Food Science. Biorefinery Research Group; HungríaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2020-01-08T16:58:19Z2020-01-08T16:58:19Z2019-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/6637https://www.sciencedirect.com/science/article/pii/S030881461931101X0308-8146https://doi.org/10.1016/j.foodchem.2019.124999Food Chemistry 298: 124999 (Noviembre 2019)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repograntAgreement/INTA/PNAIyAV/1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía.info:eu-repo/semantics/restrictedAccess2025-10-16T09:29:44Zoai:localhost:20.500.12123/6637instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-16 09:29:44.321INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
title A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
spellingShingle A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
Ontañon, Ornella Mailen
Glycosides
Glucans
Bran
Glicosidos
Enterobacter
Glucanos
Salvado
title_short A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
title_full A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
title_fullStr A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
title_full_unstemmed A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
title_sort A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
dc.creator.none.fl_str_mv Ontañon, Ornella Mailen
Ghio, Silvina
Marrero Diaz De Villegas, Rubén
Garrido, Mercedes Maria
Talia, Paola Mónica
Fehér, Csaba
Campos, Eleonora
author Ontañon, Ornella Mailen
author_facet Ontañon, Ornella Mailen
Ghio, Silvina
Marrero Diaz De Villegas, Rubén
Garrido, Mercedes Maria
Talia, Paola Mónica
Fehér, Csaba
Campos, Eleonora
author_role author
author2 Ghio, Silvina
Marrero Diaz De Villegas, Rubén
Garrido, Mercedes Maria
Talia, Paola Mónica
Fehér, Csaba
Campos, Eleonora
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Glycosides
Glucans
Bran
Glicosidos
Enterobacter
Glucanos
Salvado
topic Glycosides
Glucans
Bran
Glicosidos
Enterobacter
Glucanos
Salvado
dc.description.none.fl_txt_mv Glycoside hydrolase family 8 (GH8) includes endoglucanases, lichenases, chitosanases and xylanases, which are essential for polysaccharides breakdown. In this work, we studied a thermally stable GH8 from the cellulose synthase complex of Enterobacter sp. R1, for deconstruction of β-glucans. The biochemical characterization of the recombinant GH8ErCel showed high specificity towards barley β-glucan and lichenan and lower activity on carboxymethylcellulose and swollen cellulose, yielding different length oligosaccharides. By molecular modeling, six conserved subsites for glucose binding and some possible determinants for its lack of xylanase and chitosanase activity were identified. GH8ErCel was active at a broad range of pH and temperature and presented remarkable stability at 60 °C. Additionally, it hydrolyzed β-glucan from oat and wheat brans mainly to tri- and tetraoligosaccharides. Therefore, GH8ErCel may be a good candidate for enzymatic deconstruction of β-glucans at high temperature in food and feed industries, including the production of prebiotics and functional foods.
Instituto de Biotecnología
Fil: Ontañon, Ornella Mailén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marrero Diaz de Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fehér, Csaba. Budapest University of Technology and Economics. Faculty of Chemical Technology and Biotechnology. Department of Applied Biotechnology and Food Science. Biorefinery Research Group; Hungría
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Glycoside hydrolase family 8 (GH8) includes endoglucanases, lichenases, chitosanases and xylanases, which are essential for polysaccharides breakdown. In this work, we studied a thermally stable GH8 from the cellulose synthase complex of Enterobacter sp. R1, for deconstruction of β-glucans. The biochemical characterization of the recombinant GH8ErCel showed high specificity towards barley β-glucan and lichenan and lower activity on carboxymethylcellulose and swollen cellulose, yielding different length oligosaccharides. By molecular modeling, six conserved subsites for glucose binding and some possible determinants for its lack of xylanase and chitosanase activity were identified. GH8ErCel was active at a broad range of pH and temperature and presented remarkable stability at 60 °C. Additionally, it hydrolyzed β-glucan from oat and wheat brans mainly to tri- and tetraoligosaccharides. Therefore, GH8ErCel may be a good candidate for enzymatic deconstruction of β-glucans at high temperature in food and feed industries, including the production of prebiotics and functional foods.
publishDate 2019
dc.date.none.fl_str_mv 2019-11
2020-01-08T16:58:19Z
2020-01-08T16:58:19Z
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/20.500.12123/6637
https://www.sciencedirect.com/science/article/pii/S030881461931101X
0308-8146
https://doi.org/10.1016/j.foodchem.2019.124999
url http://hdl.handle.net/20.500.12123/6637
https://www.sciencedirect.com/science/article/pii/S030881461931101X
https://doi.org/10.1016/j.foodchem.2019.124999
identifier_str_mv 0308-8146
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repograntAgreement/INTA/PNAIyAV/1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía.
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Food Chemistry 298: 124999 (Noviembre 2019)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.712165

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