Finding stable cellulase and xylanase: evaluation of the synergistic effect of pH and temperature

N Biotechnol. 2010 Dec 31;27(6):810-5. doi: 10.1016/j.nbt.2010.10.001. Epub 2010 Oct 19.

Abstract

Ethanol from lignocellulosic biomass has been recognized as one of the most promising alternatives for the production of renewable and sustainable energy. However, one of the major bottlenecks holding back its commercialization is the high costs of the enzymes needed for biomass conversion. In this work, we studied the enzymes produced from a selected strain of Aspergillus niger under solid state fermentation. The cellulase and xylanase enzymatic cocktail was characterized in terms of pH and temperature by using response surface methodology. Thermostability and kinetic parameters were also determined. The statistical analysis of pH and temperature effects on enzymatic activity showed a synergistic interaction of these two variables, thus enabling to find a pH and temperature range in which the enzymes have a higher activity. The results obtained allowed the construction of mathematical models used to predict endoglucanase, β-glucosidase and xylanase activities under different pH and temperature conditions. Optimum temperature values for all three enzymes were found to be in the range between 35°C and 60°C, and the optimum pH range was found between 4 and 5.5. The methodology employed here was very effective in estimating enzyme behavior under different process conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / enzymology*
  • Biofuels
  • Biomass
  • Cellulase / chemistry
  • Cellulase / metabolism*
  • Enzyme Stability*
  • Fermentation
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Hydrogen-Ion Concentration*
  • Temperature*
  • Xylosidases / chemistry
  • Xylosidases / metabolism*
  • beta-Glucosidase / chemistry
  • beta-Glucosidase / metabolism

Substances

  • Biofuels
  • Fungal Proteins
  • Xylosidases
  • beta-Glucosidase
  • Cellulase