A xylanase from the Bacillus sp. strain DSNC 101, isolated from soil, was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography followed by gel filtration chromatography. The enzyme cleaved xylan, but not carboxymethyl cellulose, Avicel, soluble starch, and pNPX. The main product of oat spelts xylan hydrolysates was xylobiose. The xylanase had a molecular weight of 25 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and pH for the xylanase activity were $50^{circ}C$ and 6.0, respectively. $K_{m};and;V_{max}$ of the enzyme for oat spelts xylan were 12.5 mg of xylan/ml and 869.5 unit/mg of protein, respectively. Xylanase was completely inhibited by Hg, Cu, and N-bromosuccinimide, but was stimulated by Ca, Co, and Mg.