Purification and biochemical characterization of an endoxylanase from<i>Aspergillus versicolor</i>

Abstract

An endoxylanase (p-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pl of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a K,, of 6.5 mg ml-' and a V ,nax of 1440 U (mg protein)-'.