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  • Title: An extracellular endo-1,4-beta-xylanase from Aspergillus japonicus: Purification, properties, and characterization of the encoding gene.
    Author: Wakiyama M, Yoshihara K, Hayashi S, Ohta K.
    Journal: J Biosci Bioeng; 2010 Mar; 109(3):227-9. PubMed ID: 20159568.
    Abstract:
    An extracellular endo-1,4-beta-xylanase with specific activity of 566 U/mg was purified from the culture filtrate of a filamentous fungus, Aspergillus japonicus strain MU-2, grown on oat spelt xylan. The purified enzyme showed a single band on SDS-PAGE with an apparent M(r) of 25.1 kDa. Xylanase activity was optimal at pH 5.0 and 60 degrees C. The xylanase gene (xynA) encoded a 42 residue prepropeptide and a 191 residue mature protein. The XynA protein showed the highest sequence identity of 69% to Aspergillus niger XynB (DQ174549), which belongs to the glycoside hydrolase family 11.
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