Purification and properties of two xylanases from Aspergillus oryzae

Culture filtrates of Aspergillus foetidus VTT-D-71002, A. oryzae VTT-D-85248, and A. fumigatus VTT-D-82195 contained two proteins harboring xylanase activity and a single β-xylosidase. The two xylanases of A. oryzae were purified to homogeneity by two-stage ion exchange chromatography on DEAE- and CM Sepharose. Both xylanases hydrolyzed soluble 4-O-methylglucuronoxylan with apparently equal efficiency, but xylanase I (pI 7.0) was considerably more effective in the hydrolysis of insoluble, unsubstituted xylan than xylanase II (pI 4.9)