Recombinant endo-beta-1,4-xylanase from Penicillium canescens

Biochemistry (Mosc). 2003 Dec;68(12):1313-9. doi: 10.1023/b:biry.0000011652.52741.d6.

Abstract

Recombinant endo-beta-1,4-xylanase (Xyl-31rec, 31 kD, pI 8.2-9.3, the tenth family of glycosyl hydrolases) was isolated from the culture liquid of Penicillium canescens (strain with the amplified homologous xylanase gene) by chromatofocusing on Mono P and hydrophobic chromatography on phenyl-Superose. It is shown that the biochemical and kinetic parameters, substrate specificity, stability, and other properties of the recombinant and native enzymes are almost the same. It was found that Xyl-31rec can be used for biobleaching of cellulose, the recombinant P. canescens strains providing a high yield of extracellular Xyl-31rec (up to 800-900 U/ml of culture liquid) and not secreting cellulases.

MeSH terms

  • Absorption
  • Cellulose / metabolism
  • Chromatography
  • Endo-1,4-beta Xylanases / genetics*
  • Endo-1,4-beta Xylanases / isolation & purification
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Penicillium / enzymology*
  • Penicillium / genetics
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism*
  • Substrate Specificity
  • Temperature

Substances

  • Recombinant Proteins
  • Cellulose
  • Endo-1,4-beta Xylanases