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Abstract
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 [ver mas...]
dc.contributor.authorOntañon, Ornella Mailen
dc.contributor.authorGhio, Silvina
dc.contributor.authorMarrero Diaz De Villegas, Rubén
dc.contributor.authorGarrido, Mercedes Maria
dc.contributor.authorTalia, Paola Mónica
dc.contributor.authorFehér, Csaba
dc.contributor.authorCampos, Eleonora
dc.date.accessioned2020-01-08T16:58:19Z
dc.date.available2020-01-08T16:58:19Z
dc.date.issued2019-11
dc.identifier.issn0308-8146
dc.identifier.otherhttps://doi.org/10.1016/j.foodchem.2019.124999
dc.identifier.urihttp://hdl.handle.net/20.500.12123/6637
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S030881461931101X
dc.description.abstractGlycoside 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.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherElsevieres_AR
dc.relationinfo:eu-repograntAgreement/INTA/PNAIyAV/1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía.es_AR
dc.rightsinfo:eu-repo/semantics/restrictedAccesses_AR
dc.sourceFood Chemistry 298: 124999 (Noviembre 2019)es_AR
dc.subjectGlycosideseng
dc.subjectGlicosidoses_AR
dc.subjectEnterobacteres_AR
dc.subjectGlucanseng
dc.subjectGlucanoses_AR
dc.subjectBraneng
dc.subjectSalvadoes_AR
dc.titleA thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstructiones_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Biotecnologíaes_AR
dc.description.filFil: Ontañon, Ornella Mailén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Marrero Diaz de Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Fehér, Csaba. Budapest University of Technology and Economics. Faculty of Chemical Technology and Biotechnology. Department of Applied Biotechnology and Food Science. Biorefinery Research Group; Hungríaes_AR
dc.description.filFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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