Xylan degrading enzyme xylanase was extracted, purified and characterized from Bacillus megaterium SV1. The enzyme was purified to homogeneity by ammonium sulphate precipitation, gel permeation and ion exchange chromatographic techniques. During the series of steps, 28.5fold purification was obtained with 72.7U/mg specific activity of xylanse and the corresponding molecular weight of the enzyme was identified as 24kDa. The optimum conditions for maximal enzyme activity were identified at pH-8.0, temperature 40oC and with 5% of sodium chloride. It is observed that the reactants like calcium chloride, Dithiothreitol, β-mercaptoethanol was found to enhance the activity of enzyme and Mercuric chloride strongly inhibits the enzyme activity. Degradation of Brich wood Xylan was investigated to determine the kinetic parameters Km and Vmax values and was found to be 6.1mg/ml and 280μmol/min/mg respectively. It is also verified that the enzyme Xylanase extracted from Bacillus SV1 was identified as alkalophilic and halotolerant.