Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
Josman Velasco, Bianca Oliva, Evandro José Mulinari, Leidy Patricia Quintero, Awana da Silva Lima, Aline Larissa Gonçalves, Thiago Augusto Gonçalves, André Damasio, Fabio Marcio Squina, Adriane Maria Ferreira Milagres, Asmaa Abdella, Mark R. Wilkins, Fernando Segato
ARTIGO
Inglês
Agradecimentos: This work was financially supported by São Paulo Research Foundation (FAPESP), grants #2014/18714-2, #2014/06923-6, #2017/00525-0, #2017/22669-0, and by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), grants 443916/2014-4, 304816/2017, 404654/2018-5 and...
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Agradecimentos: This work was financially supported by São Paulo Research Foundation (FAPESP), grants #2014/18714-2, #2014/06923-6, #2017/00525-0, #2017/22669-0, and by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), grants 443916/2014-4, 304816/2017, 404654/2018-5 and 302627/2018-9. This study was also financed in part by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - Brazil (CAPES) - Finance Code 001. The Egyptian Cultural Educational Bureau, the University of Nebraska Agricultural Research Division/FAPESP SPRINT program, the Nebraska Corn Checkoff Presidential Chair Endowment and São Carlos Institute of Physics
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Abstract: 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-ß-1,4-xylanase from Aspergillus fumigatus var. niveus (AFUMN-GH10) was successfully expressed. The structural...
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Abstract: 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-ß-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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FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESP
2014/18714-2; 2014/06923-6; 2017/00525-0; 2017/22669-0
CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQ
443916/2014-4; 304816/2017; 404654/2018-5; 302627/2018-9
COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPES
001
Aberto
Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
Josman Velasco, Bianca Oliva, Evandro José Mulinari, Leidy Patricia Quintero, Awana da Silva Lima, Aline Larissa Gonçalves, Thiago Augusto Gonçalves, André Damasio, Fabio Marcio Squina, Adriane Maria Ferreira Milagres, Asmaa Abdella, Mark R. Wilkins, Fernando Segato
Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
Josman Velasco, Bianca Oliva, Evandro José Mulinari, Leidy Patricia Quintero, Awana da Silva Lima, Aline Larissa Gonçalves, Thiago Augusto Gonçalves, André Damasio, Fabio Marcio Squina, Adriane Maria Ferreira Milagres, Asmaa Abdella, Mark R. Wilkins, Fernando Segato
Fontes
Biotechnology reports (Fonte avulsa) |