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

Autores
Niderhaus, Cecilia; Garrido, Mercedes María; 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.
Fil: Niderhaus, Cecilia. Universidad de Buenos Aires; Argentina
Fil: Garrido, Mercedes María. Universidad de Buenos Aires; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Materia
BIOMASS BIOCONVERSION–GH10 FAMILY
PICHIA PASTORIS
THERMOSTABLE ENDOXYLANASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/85178
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126Niderhaus, CeciliaGarrido, Mercedes MaríaInsani, Ester MarinaCampos, EleonoraWirth, Sonia AlejandraBIOMASS BIOCONVERSION–GH10 FAMILYPICHIA PASTORISTHERMOSTABLE ENDOXYLANASEhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2https://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Xylanases 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.Fil: Niderhaus, Cecilia. Universidad de Buenos Aires; ArgentinaFil: Garrido, Mercedes María. Universidad de Buenos Aires; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaFil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaFil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaElsevier2018-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/85178Niderhaus, Cecilia; Garrido, Mercedes María; Insani, Ester Marina; Campos, Eleonora; Wirth, Sonia Alejandra; Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126; Elsevier; Process Biochemistry; 67; 4-2018; 92-981359-5113CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1359511317316914info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2018.01.017info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:03:54Zoai:ri.conicet.gov.ar:11336/85178instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:03:54.298CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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
BIOMASS BIOCONVERSION–GH10 FAMILY
PICHIA PASTORIS
THERMOSTABLE ENDOXYLANASE
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 María
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author Niderhaus, Cecilia
author_facet Niderhaus, Cecilia
Garrido, Mercedes María
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author_role author
author2 Garrido, Mercedes María
Insani, Ester Marina
Campos, Eleonora
Wirth, Sonia Alejandra
author2_role author
author
author
author
dc.subject.none.fl_str_mv BIOMASS BIOCONVERSION–GH10 FAMILY
PICHIA PASTORIS
THERMOSTABLE ENDOXYLANASE
topic BIOMASS BIOCONVERSION–GH10 FAMILY
PICHIA PASTORIS
THERMOSTABLE ENDOXYLANASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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.
Fil: Niderhaus, Cecilia. Universidad de Buenos Aires; Argentina
Fil: Garrido, Mercedes María. Universidad de Buenos Aires; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; 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
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/11336/85178
Niderhaus, Cecilia; Garrido, Mercedes María; Insani, Ester Marina; Campos, Eleonora; Wirth, Sonia Alejandra; Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126; Elsevier; Process Biochemistry; 67; 4-2018; 92-98
1359-5113
CONICET Digital
CONICET
url http://hdl.handle.net/11336/85178
identifier_str_mv Niderhaus, Cecilia; Garrido, Mercedes María; Insani, Ester Marina; Campos, Eleonora; Wirth, Sonia Alejandra; Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126; Elsevier; Process Biochemistry; 67; 4-2018; 92-98
1359-5113
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1359511317316914
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2018.01.017
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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