The current study describes the purify and characterize xylanase from Trichoderma virens. Xylanase (Xy1a) was purified to homogeneity 47.6-fold via sephacryl S-200. The molecular mass of Xy1a estimated by gel filtration was once 20 kDa with 24.7% recovery. Purity was proven by means of SDS-PAGE and a single band was observed. The highest activity of the Xy1a was observed at pH 5.5 and at temperature 50°C. The Xy1a enzyme was very stable up to 50°C. The purified xy1a showed higher affinity for Birchwood xylan with Km and Vmax of 5.83 mg/ml and 0.575µmol min-1 mg-1, respectively. Metallic cations, such as Ca2+ and Ni2+ were found to enhance the enzymatic activity of the purified Xy1a, while Cu2+, Co2+, Pb2+and Zn2+ ions were found to be partially inhibitory. Metallic cations, such as Hg2+ and Cd2+ were found to be strongly inhibited the enzyme. Based on the results, it could be confirmed that the purified enzyme has potential role in some application such as the food, feed, pharmaceutical and paper industries.
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