Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126
Xylanases are key enzymes for agricultural biomass saccharification for the production of cellulosic ethanol. Success in enzymatic lignocellulose bioconversion is restricted by enzyme production costs, activity and stability under harsh reaction conditions, and their performance when interacting int...
| Autores principales: | , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
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Elsevier
2019
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/4450 https://www.sciencedirect.com/science/article/pii/S1359511317316914?via%3Dihub https://doi.org/10.1016/j.procbio.2018.01.017 |
| _version_ | 1855035325569564672 |
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| author | Niderhaus, Cecilia Garrido, Mercedes Maria Insani, Ester Marina Campos, Eleonora Wirth, Sonia Alejandra |
| author_browse | Campos, Eleonora Garrido, Mercedes Maria Insani, Ester Marina Niderhaus, Cecilia Wirth, Sonia Alejandra |
| author_facet | Niderhaus, Cecilia Garrido, Mercedes Maria Insani, Ester Marina Campos, Eleonora Wirth, Sonia Alejandra |
| author_sort | Niderhaus, Cecilia |
| collection | INTA Digital |
| description | Xylanases are key enzymes for agricultural biomass saccharification for the production of cellulosic ethanol. Success in enzymatic lignocellulose bioconversion is restricted by enzyme production costs, activity and stability under harsh reaction conditions, and their performance when interacting into cellulolytic cocktails. In this work, we present the heterologous expression and enzymatic characterization of a novel endo-β-1,4 xylanase of glycoside hydrolase family 10 (GH10ps) from the white-rot basidiomycete Pycnoporus sanguineus BAFC 2126. Recombinant expression of GH10ps in Pichia pastoris showed that it is a robust enzyme active at a wide range of pHs and temperatures, and with a half-life of 3 h at 70 °C and a stability higher than 48 h at 60 °C. Recombinant GH10ps was also capable of releasing xylooligosaccharides and xylose from pretreated agricultural waste biomass and also complemented commercial cellulases in lignocellulose bioconversion to fermentable sugars. |
| format | info:ar-repo/semantics/artículo |
| id | INTA4450 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2019 |
| publishDateRange | 2019 |
| publishDateSort | 2019 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | INTA44502019-02-15T15:08:49Z Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 Niderhaus, Cecilia Garrido, Mercedes Maria Insani, Ester Marina Campos, Eleonora Wirth, Sonia Alejandra Pichia Pastoris Bioconversion Biomass Bioconversión Biomasa Pycnoporus Sanguineus GH10 Family Thermostable Endoxylanase Endoxilanasa Termoestable Xylanases are key enzymes for agricultural biomass saccharification for the production of cellulosic ethanol. Success in enzymatic lignocellulose bioconversion is restricted by enzyme production costs, activity and stability under harsh reaction conditions, and their performance when interacting into cellulolytic cocktails. In this work, we present the heterologous expression and enzymatic characterization of a novel endo-β-1,4 xylanase of glycoside hydrolase family 10 (GH10ps) from the white-rot basidiomycete Pycnoporus sanguineus BAFC 2126. Recombinant expression of GH10ps in Pichia pastoris showed that it is a robust enzyme active at a wide range of pHs and temperatures, and with a half-life of 3 h at 70 °C and a stability higher than 48 h at 60 °C. Recombinant GH10ps was also capable of releasing xylooligosaccharides and xylose from pretreated agricultural waste biomass and also complemented commercial cellulases in lignocellulose bioconversion to fermentable sugars. Instituto de Biotecnología Fil: Niderhaus, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina 2019-02-15T15:04:27Z 2019-02-15T15:04:27Z 2018-04 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/4450 https://www.sciencedirect.com/science/article/pii/S1359511317316914?via%3Dihub 1359-5113 https://doi.org/10.1016/j.procbio.2018.01.017 eng info:eu-repo/semantics/restrictedAccess application/pdf Elsevier Process biochemistry 67 : 92-98. (April 2018) |
| spellingShingle | Pichia Pastoris Bioconversion Biomass Bioconversión Biomasa Pycnoporus Sanguineus GH10 Family Thermostable Endoxylanase Endoxilanasa Termoestable Niderhaus, Cecilia Garrido, Mercedes Maria Insani, Ester Marina Campos, Eleonora Wirth, Sonia Alejandra Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title | Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title_full | Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title_fullStr | Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title_full_unstemmed | Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title_short | Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 |
| title_sort | heterologous production and characterization of a thermostable gh10 family endo xylanase from pycnoporus sanguineus bafc 2126 |
| topic | Pichia Pastoris Bioconversion Biomass Bioconversión Biomasa Pycnoporus Sanguineus GH10 Family Thermostable Endoxylanase Endoxilanasa Termoestable |
| url | http://hdl.handle.net/20.500.12123/4450 https://www.sciencedirect.com/science/article/pii/S1359511317316914?via%3Dihub https://doi.org/10.1016/j.procbio.2018.01.017 |
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