Mining of camel rumen metagenome to identify novel alkali-thermostable xylanase capable of enhancing the recalcitrant lignocellulosic biomass conversion

Bioresour Technol. 2019 Jun:281:343-350. doi: 10.1016/j.biortech.2019.02.059. Epub 2019 Feb 12.

Abstract

The aim of this study was to isolate and characterize novel alkali-thermostable xylanase genes from the mixed genome DNA of camel rumen metagenome. In this study, a five-stage computational screening procedure was utilized to find the primary candidate enzyme with superior properties from the camel rumen metagenome. This enzyme was subjected to cloning, purification, and structural and functional characterization. It showed high thermal stability, high activity in a broad range of pH (6-11) and temperature (30-90 °C) and effectivity in recalcitrant lignocellulosic biomass degradation. Our results demonstrated the power of in silico analysis to discover novel alkali-thermostable xylanases, effective for the bioconversion of lignocellulosic biomass.

Keywords: Alkaline thermostable xylanase; Camel rumen; Metagenome; Recalcitrant compounds.

MeSH terms

  • Alkalies
  • Animals
  • Biomass*
  • Camelus
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Lignin / metabolism*
  • Metagenome*
  • Rumen / metabolism
  • Temperature

Substances

  • Alkalies
  • lignocellulose
  • Lignin
  • Endo-1,4-beta Xylanases