Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126

Autores
Niderhaus, Cecilia; Garrido, Mercedes Maria; Insani, Ester Marina; Campos, Eleonora; Wirth, Sonia Alejandra
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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
Fuente
Process biochemistry 67 : 92-98. (April 2018)
Materia
Pichia Pastoris
Bioconversion
Biomass
Bioconversión
Biomasa
Pycnoporus Sanguineus
GH10 Family
Thermostable Endoxylanase
Endoxilanasa Termoestable
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/4450
Acceder
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spelling Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126Niderhaus, CeciliaGarrido, Mercedes MariaInsani, Ester MarinaCampos, EleonoraWirth, Sonia AlejandraPichia PastorisBioconversionBiomassBioconversiónBiomasaPycnoporus SanguineusGH10 FamilyThermostable EndoxylanaseEndoxilanasa TermoestableXylanases 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 BiotecnologíaFil: 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; ArgentinaFil: 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; ArgentinaFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: 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; ArgentinaElsevier2019-02-15T15:04:27Z2019-02-15T15:04:27Z2018-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/4450https://www.sciencedirect.com/science/article/pii/S1359511317316914?via%3Dihub1359-5113https://doi.org/10.1016/j.procbio.2018.01.017Process biochemistry 67 : 92-98. (April 2018)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-10-16T09:29:26Zoai:localhost:20.500.12123/4450instacron: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 09:29:27.195INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv 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
spellingShingle Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126
Niderhaus, Cecilia
Pichia Pastoris
Bioconversion
Biomass
Bioconversión
Biomasa
Pycnoporus Sanguineus
GH10 Family
Thermostable Endoxylanase
Endoxilanasa Termoestable
title_short 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_sort Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126
dc.creator.none.fl_str_mv Niderhaus, Cecilia
Garrido, Mercedes Maria
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author Niderhaus, Cecilia
author_facet Niderhaus, Cecilia
Garrido, Mercedes Maria
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author_role author
author2 Garrido, Mercedes Maria
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author2_role author
author
author
author
dc.subject.none.fl_str_mv Pichia Pastoris
Bioconversion
Biomass
Bioconversión
Biomasa
Pycnoporus Sanguineus
GH10 Family
Thermostable Endoxylanase
Endoxilanasa Termoestable
topic Pichia Pastoris
Bioconversion
Biomass
Bioconversión
Biomasa
Pycnoporus Sanguineus
GH10 Family
Thermostable Endoxylanase
Endoxilanasa Termoestable
dc.description.none.fl_txt_mv 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
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.
publishDate 2018
dc.date.none.fl_str_mv 2018-04
2019-02-15T15:04:27Z
2019-02-15T15:04:27Z
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/20.500.12123/4450
https://www.sciencedirect.com/science/article/pii/S1359511317316914?via%3Dihub
1359-5113
https://doi.org/10.1016/j.procbio.2018.01.017
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
identifier_str_mv 1359-5113
dc.language.none.fl_str_mv eng
language eng
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 Process biochemistry 67 : 92-98. (April 2018)
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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