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...

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Detalles Bibliográficos
Publicado: 2018
Materias:
Biomass Bioconversion–GH10 Family
Pichia pastoris
Thermostable endoxylanase
Agricultural wastes
Agriculture
Bioconversion
Cellulose
Cellulosic ethanol
Enzyme activity
Lignin
Saccharification
Sugars
Yeast
Biomass bioconversions
Glycoside hydrolase family 10
Heterologous expression
Heterologous production
Lignocellulose bioconversions
Pichia Pastoris
White-rot basidiomycetes
Biomass
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v67_n_p92_Niderhaus
http://hdl.handle.net/20.500.12110/paper_13595113_v67_n_p92_Niderhaus
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_13595113_v67_n_p92_Niderhaus
record_format dspace
spelling paper:paper_13595113_v67_n_p92_Niderhaus2023-06-08T16:11:23Z Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126 Biomass Bioconversion–GH10 Family Pichia pastoris Thermostable endoxylanase Agricultural wastes Agriculture Bioconversion Cellulose Cellulosic ethanol Enzyme activity Lignin Saccharification Sugars Yeast Biomass bioconversions Glycoside hydrolase family 10 Heterologous expression Heterologous production Lignocellulose bioconversions Pichia Pastoris Thermostable endoxylanase White-rot basidiomycetes Biomass 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. © 2018 Elsevier Ltd 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v67_n_p92_Niderhaus http://hdl.handle.net/20.500.12110/paper_13595113_v67_n_p92_Niderhaus
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Biomass Bioconversion–GH10 Family
Pichia pastoris
Thermostable endoxylanase
Agricultural wastes
Agriculture
Bioconversion
Cellulose
Cellulosic ethanol
Enzyme activity
Lignin
Saccharification
Sugars
Yeast
Biomass bioconversions
Glycoside hydrolase family 10
Heterologous expression
Heterologous production
Lignocellulose bioconversions
Pichia Pastoris
Thermostable endoxylanase
White-rot basidiomycetes
Biomass
spellingShingle Biomass Bioconversion–GH10 Family
Pichia pastoris
Thermostable endoxylanase
Agricultural wastes
Agriculture
Bioconversion
Cellulose
Cellulosic ethanol
Enzyme activity
Lignin
Saccharification
Sugars
Yeast
Biomass bioconversions
Glycoside hydrolase family 10
Heterologous expression
Heterologous production
Lignocellulose bioconversions
Pichia Pastoris
Thermostable endoxylanase
White-rot basidiomycetes
Biomass
Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126
topic_facet Biomass Bioconversion–GH10 Family
Pichia pastoris
Thermostable endoxylanase
Agricultural wastes
Agriculture
Bioconversion
Cellulose
Cellulosic ethanol
Enzyme activity
Lignin
Saccharification
Sugars
Yeast
Biomass bioconversions
Glycoside hydrolase family 10
Heterologous expression
Heterologous production
Lignocellulose bioconversions
Pichia Pastoris
Thermostable endoxylanase
White-rot basidiomycetes
Biomass
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. © 2018 Elsevier Ltd
title 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_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
publishDate 2018
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13595113_v67_n_p92_Niderhaus
http://hdl.handle.net/20.500.12110/paper_13595113_v67_n_p92_Niderhaus
_version_ 1768545477596282880

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