Endo-1,4-beta-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZ alpha A and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 degrees C on beechwood xylan. Under these conditions, the K-m, V-max and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 mu mol min(-1) mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K+, Na+, Li2+, Cd2+, and Co2+. However, in the presence of EDTA, Hg2+ and Fe3+, xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail. (c) 2013 Elsevier Inc. All rights reserved.