Production and Partial Characterization of an Alkaline Xylanase from a Novel Fungus Cladosporium oxysporum

Biomed Res Int. 2016:2016:4575024. doi: 10.1155/2016/4575024. Epub 2016 Apr 26.

Abstract

A new fungus Cladosporium oxysporum GQ-3 producing extracellular xylanase was isolated from decaying agricultural waste and identified based on the morphology and comparison of internal transcribed spacer (ITS) rDNA gene sequence. C. oxysporum produced maximum xylanase activity of 55.92 U/mL with wheat bran as a substrate and NH4Cl as a nitrogen source. Mg(2+) improved C. oxysporum xylanase production. Partially purified xylanase exhibited maximum activity at 50°C and pH 8.0, respectively, and showed the stable activity after 2-h treatment in pH 7.0-8.5 or below 55°C. Mg(2+) enhanced the xylanase activity by 2% while Cu(2+) had the highest inhibition ratio of 57.9%. Furthermore, C. oxysporum xylanase was resistant to most of tested neutral and alkaline proteases. Our findings indicated that Cladosporium oxysporum GQ-3 was a novel xylanase producer, which could be used in the textile processes or paper/feed industries.

MeSH terms

  • Bacterial Proteins / chemistry
  • Cladosporium / enzymology*
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / isolation & purification*
  • Endo-1,4-beta Xylanases / metabolism
  • Endopeptidases / chemistry
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Temperature
  • Triticum / chemistry

Substances

  • Bacterial Proteins
  • Endo-1,4-beta Xylanases
  • Endopeptidases
  • alkaline protease