Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Abstract The aim of the present study was to assess biochemical and molecular structural characteristics a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in termite gut microbiome by shotgun metagenomic approach. This endoxylanase candidate amplified, cloned, heterologously expressed Escherichia coli purified. recombinant enzyme active at broad range temperatures (37–60 ºC) pH values (4–10), with optimal activity 50 ºC 9. Moreover, its remained more than 80% maximum °C for 8 h. In addition, Xyl10B found be stable presence salt several ions chemical reagents frequently used industry. These make this an interesting pulp paper bleaching industries, since process requires enzymes without cellulase resistant high alkaline (thermo-alkaliphilic enzymes). products xylan hydrolysis (short xylooligosaccharides, xylose xylobiose) could suitable application as prebiotics production bioethanol. Graphical