Title
Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application
Author
Josman Velasco, Bianca Oliva, Evandro José Mulinari, Leidy Patricia Quintero, Awanada Silva Lima, Aline Larissa Gonçalves, Thiago Augusto Gonçalves, André Damasio, Fabio Marcio Squina, Adriane Maria Ferreira Milagres, Asmaa Abdella, Mark R. Wilkins, Fernando Segato
Year
2019
Journal
Biotechnology Reports
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-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.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Protein folding, Thermal stability, Biochemistry