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Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application

Xylanases decrease the xylan content in pretreated biomass releasing it from hemicellulose, thus improving the accessibility of cellulose for cellulases. In this work, an endo-β-1,4-xylanase from Aspergillus fumigatus var. niveus (AFUMN-GH10) was successfully expressed. The structural analysis and b...

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Autores principales: Velasco, Josman, Oliva, Bianca, Mulinari, Evandro José, Quintero, Leidy Patricia, da Silva Lima, Awana, Gonçalves, Aline Larissa, Gonçalves, Thiago Augusto, Damasio, André, Squina, Fabio Marcio, Ferreira Milagres, Adriane Maria, Abdella, Asmaa, Wilkins, Mark R., Segato, Fernando
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881608/
https://www.ncbi.nlm.nih.gov/pubmed/31799141
http://dx.doi.org/10.1016/j.btre.2019.e00382
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author Velasco, Josman
Oliva, Bianca
Mulinari, Evandro José
Quintero, Leidy Patricia
da Silva Lima, Awana
Gonçalves, Aline Larissa
Gonçalves, Thiago Augusto
Damasio, André
Squina, Fabio Marcio
Ferreira Milagres, Adriane Maria
Abdella, Asmaa
Wilkins, Mark R.
Segato, Fernando
author_facet Velasco, Josman
Oliva, Bianca
Mulinari, Evandro José
Quintero, Leidy Patricia
da Silva Lima, Awana
Gonçalves, Aline Larissa
Gonçalves, Thiago Augusto
Damasio, André
Squina, Fabio Marcio
Ferreira Milagres, Adriane Maria
Abdella, Asmaa
Wilkins, Mark R.
Segato, Fernando
author_sort Velasco, Josman
collection PubMed
description Xylanases decrease the xylan content in pretreated biomass releasing it from hemicellulose, thus improving the accessibility of cellulose for cellulases. In this work, an endo-β-1,4-xylanase from Aspergillus fumigatus var. niveus (AFUMN-GH10) was successfully expressed. The structural analysis and biochemical characterization showed this AFUMN-GH10 does not contain a carbohydrate-binding module. The enzyme retained its activity in a pH range from 4.5 to 7.0, with an optimal temperature at 60 °C. AFUMN-GH10 showed the highest activity in beechwood xylan. The mode of action of AFUMN-GH10 was investigated by hydrolysis of APTS-labeled xylohexaose, which resulted in xylotriose and xylobiose as the main products. AFUMN-GH10 released 27% of residual xylan from hydrothermally-pretreated corn stover and 14% of residual xylan from hydrothermally-pretreated sugarcane bagasse. The results showed that environmentally friendly pretreatment followed by enzymatic hydrolysis with AFUMN-GH10 in low concentration is a suitable method to remove part of residual and recalcitrant hemicellulose from biomass.
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spelling pubmed-68816082019-12-03 Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application Velasco, Josman Oliva, Bianca Mulinari, Evandro José Quintero, Leidy Patricia da Silva Lima, Awana Gonçalves, Aline Larissa Gonçalves, Thiago Augusto Damasio, André Squina, Fabio Marcio Ferreira Milagres, Adriane Maria Abdella, Asmaa Wilkins, Mark R. Segato, Fernando Biotechnol Rep (Amst) Research Article Xylanases decrease the xylan content in pretreated biomass releasing it from hemicellulose, thus improving the accessibility of cellulose for cellulases. In this work, an endo-β-1,4-xylanase from Aspergillus fumigatus var. niveus (AFUMN-GH10) was successfully expressed. The structural analysis and biochemical characterization showed this AFUMN-GH10 does not contain a carbohydrate-binding module. The enzyme retained its activity in a pH range from 4.5 to 7.0, with an optimal temperature at 60 °C. AFUMN-GH10 showed the highest activity in beechwood xylan. The mode of action of AFUMN-GH10 was investigated by hydrolysis of APTS-labeled xylohexaose, which resulted in xylotriose and xylobiose as the main products. AFUMN-GH10 released 27% of residual xylan from hydrothermally-pretreated corn stover and 14% of residual xylan from hydrothermally-pretreated sugarcane bagasse. The results showed that environmentally friendly pretreatment followed by enzymatic hydrolysis with AFUMN-GH10 in low concentration is a suitable method to remove part of residual and recalcitrant hemicellulose from biomass. Elsevier 2019-10-30 /pmc/articles/PMC6881608/ /pubmed/31799141 http://dx.doi.org/10.1016/j.btre.2019.e00382 Text en © 2019 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Velasco, Josman
Oliva, Bianca
Mulinari, Evandro José
Quintero, Leidy Patricia
da Silva Lima, Awana
Gonçalves, Aline Larissa
Gonçalves, Thiago Augusto
Damasio, André
Squina, Fabio Marcio
Ferreira Milagres, Adriane Maria
Abdella, Asmaa
Wilkins, Mark R.
Segato, Fernando
Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title_full Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title_fullStr Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title_full_unstemmed Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title_short Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
title_sort heterologous expression and functional characterization of a gh10 endoxylanase from aspergillus fumigatus var. niveus with potential biotechnological application
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881608/
https://www.ncbi.nlm.nih.gov/pubmed/31799141
http://dx.doi.org/10.1016/j.btre.2019.e00382
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