Partial characterization of xylanase produced by Caldicoprobacter algeriensis, a new thermophilic anaerobic bacterium isolated from an Algerian hot spring

Appl Biochem Biotechnol. 2014 Nov;174(5):1969-81. doi: 10.1007/s12010-014-1153-2. Epub 2014 Aug 27.

Abstract

To date, xylanases have expanded their use in many processing industries, such as pulp, paper, food, and textile. This study aimed the production and partial characterization of a thermostable xylanase from a novel thermophilic anaerobic bacterium Caldicoprobacter algeriensis strain TH7C1(T) isolated from a northeast hot spring in Algeria. The obtained results showed that C. algeriensis xylanase seems not to be correlated with the biomass growth profile whereas the maximum enzyme production (140.0 U/ml) was recorded in stationary phase (18 h). The temperature and pH for optimal activities were 70 °C and 11.0, respectively. The enzyme was found to be stable at 50, 60, 70, and 80 °C, with a half-life of 10, 9, 8, and 4 h, respectively. Influence of metal ions on enzyme activity revealed that Ca(+2) enhances greatly the relative activity to 151.3 %; whereas Hg(2+) inhibited significantly the enzyme. At the best of our knowledge, this is the first report on the production of xylanase by the thermophilic bacterium C. algeriensis. This thermo- and alkaline-tolerant xylanase could be used in pulp bleaching process.

MeSH terms

  • Algeria
  • Clostridium / enzymology*
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / isolation & purification*
  • Enzyme Activation
  • Enzyme Stability
  • Hot Springs / microbiology*
  • Hydrogen-Ion Concentration
  • Substrate Specificity
  • Temperature

Substances

  • Endo-1,4-beta Xylanases