A new xylanase from Penicillium griseofulvum

Meded Rijksuniv Gent Fak Landbouwkd Toegep Biol Wet. 2001;66(3a):261-6.

Abstract

A new xylanase (pgxynA) from Penicillium griseofulvum A160 has been isolated and characterised using a screening method based on the ability to digest a complex substrate. The enzyme belongs to the hydrolase family 11 or G and shows an optimum pH of 5.0 and an optimum temperature of 50 degrees C. The xylanase breaks down the xylan to very small oligosaccharides. The corresponding gene (PGXYNA) was cloned and expressed in Aspergillus oryzae. A second xylanase gene with 66% identity to PGXYNA has also been isolated from P. griseofulvum A160. The recombinant pgxynA xylanase has been tested in some industrial applications. In bread making, hard rolls volume increased significantly using this enzyme. In wheat flour processing, the enzyme improved the separation of gluten from starch. In poultry, the addition of the A160 xylanase to a wheat-based diet led to an higher body weight as well as to a better feed conversion ratio.

MeSH terms

  • Amino Acid Sequence
  • Consensus Sequence
  • Endo-1,4-beta Xylanases / chemistry
  • Endo-1,4-beta Xylanases / genetics
  • Endo-1,4-beta Xylanases / isolation & purification
  • Endo-1,4-beta Xylanases / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Penicillium / enzymology*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Triticum / metabolism

Substances

  • Endo-1,4-beta Xylanases