One-step purification and characterization of a low molecular weight xylanase from Aspergillus terreus NRRL 1960

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 oC and pH 7.0 resulted in apparent K m and V max 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.