Biotechnology Reports (Dec 2019)

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

Journal volume & issue
Vol. 24

Abstract

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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. Keywords: Endoxylanase, Filamentous fungi, Corn stover, Sugarcane bagasse, Xylooligosaccharides