A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction
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 bioc...
| Autores principales: | , , , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier
2020
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| Materias: | |
| Acceso en línea: | 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 |
| _version_ | 1855035711907954688 |
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| author | Ontañon, Ornella Mailen Ghio, Silvina Marrero Diaz De Villegas, Rubén Garrido, Mercedes Maria Talia, Paola Mónica Fehér, Csaba Campos, Eleonora |
| author_browse | Campos, Eleonora Fehér, Csaba Garrido, Mercedes Maria Ghio, Silvina Marrero Diaz De Villegas, Rubén Ontañon, Ornella Mailen Talia, Paola Mónica |
| author_facet | Ontañon, Ornella Mailen Ghio, Silvina Marrero Diaz De Villegas, Rubén Garrido, Mercedes Maria Talia, Paola Mónica Fehér, Csaba Campos, Eleonora |
| author_sort | Ontañon, Ornella Mailen |
| collection | INTA Digital |
| 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA6637 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2020 |
| publishDateRange | 2020 |
| publishDateSort | 2020 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | INTA66372021-11-15T15:54:34Z A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction Ontañon, Ornella Mailen Ghio, Silvina Marrero Diaz De Villegas, Rubén Garrido, Mercedes Maria Talia, Paola Mónica Fehér, Csaba Campos, Eleonora Glycosides Glucans Bran Glicosidos Enterobacter Glucanos Salvado 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 2020-01-08T16:58:19Z 2020-01-08T16:58:19Z 2019-11 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng info:eu-repograntAgreement/INTA/PNAIyAV/1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía. info:eu-repo/semantics/restrictedAccess application/pdf Elsevier Food Chemistry 298: 124999 (Noviembre 2019) |
| spellingShingle | Glycosides Glucans Bran Glicosidos Enterobacter Glucanos Salvado Ontañon, Ornella Mailen Ghio, Silvina Marrero Diaz De Villegas, Rubén Garrido, Mercedes Maria Talia, Paola Mónica Fehér, Csaba Campos, Eleonora 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 |
| 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_short | A thermostable GH8 endoglucanase of Enterobacter sp. R1 is suitable for β- glucan deconstruction |
| title_sort | thermostable gh8 endoglucanase of enterobacter sp r1 is suitable for β glucan deconstruction |
| topic | Glycosides Glucans Bran Glicosidos Enterobacter Glucanos Salvado |
| 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 |
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