A new xylanase from a Trichoderma harzianum strain

J Ind Microbiol Biotechnol. 1999 Jul;23(1):682-5. doi: 10.1038/sj.jim.2900682.

Abstract

A new xylanase (XYL2) was purified from solid-state cultures of Trichoderma harzianum strain C by ultrafiltration and gel filtration. SDS-PAGE of the xylanase showed an apparent homogeneity and molecular weight of 18 kDa. It had the highest activity at pH 5.0 and 45 degrees C and was stable at 50 degrees C and pH 5.0 up to 4 h xylanase. XYL2 had a low Km with insoluble oat spelt xylan as substrate. Compared to the amino acid composition of xylanases from Trichoderma spp, xylanase XYL2 presented a high content of glutamate/glutamine, phenylalanine and cysteine, and a low content of serine. Xylanase XYL2 improved the delignification and selectivity of unbleached hardwood kraft pulp.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Weight
  • Trichoderma / enzymology*
  • Ultrafiltration
  • Wood
  • Xylan Endo-1,3-beta-Xylosidase
  • Xylosidases / chemistry
  • Xylosidases / isolation & purification*
  • Xylosidases / metabolism

Substances

  • Amino Acids
  • Xylosidases
  • Xylan Endo-1,3-beta-Xylosidase