The aim of study was to investigate purification and characterization of xylanase produced by industrially important strain of Aspergillus terreus. The xylanase was purified by one-step hydrophobic interaction chromatography technique 19-fold with 61% yield. Molecular weight and isoelectric point of the enzyme were determined as 19 kDa and pH 9.0, respectively. The enzyme was found to be unglycosylated. Kinetic experiments at 50°C and pH 7.0 resulted in apparent Km and Vmax values of 2.5±0.05 mg xylan/ml and 50.2±0.4 IU/µg protein, respectively. According to its biochemical properties, the enzyme was found to be a member of family-11 xylanase group. Due to its low molecular weight, the enzyme could be advantageous for industrial applications