An extracellular xylanase was purified to homogeneity from the culture filtrate of ”Xylaria regalis”. The xylanase was purified 10.98 fold, giving a 34.6% yield. The crude enzyme was subjected to a series of the purification procedures, including QAE Sephadex A-25 anion exchange column, hydrophobic interaction phenyl 650M column and Sephadex G-75 gel filtration column chromatography, respectively. The molecular mass of the purified xylanase estimated by SDS-PAGE was approximately 30.8 kDa. The optimal temperature of the enzyme activity was 50℃. The optimal pH of xylanase activity was 5.5 and the enzyme appeared to be stable over the pH range from 5-9. The enzyme activity was inhibited by Cu(superscript 2+), Hg(superscript 2+), EDTA, and β-mercaptoethanol.