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An extracellular thermostable xylanase (Xyl-IIb) produced by  Penicillium citrinum  isolate HZN13 was purified to homogeneity using DEAE-Sepharose, Sephadex G-100 and Bio-Gel P-60 chromatography with specific activity of 6272.7 U/mg and 19.6-fold purification. The purification revealed the occurrence of multiple forms of xylanases (Xyl-I, Xyl-IIa, Xyl-IIb and Xyl-III). The molecular mass of highly purified Xyl-IIb was ~31 kDa with SDS-PAGE. The enzyme was cellulase-free, thermostable (55–75 °C) and acidophilic (3.5–5.0). It was activated by Ca 2+ , Ba 2+ , DTT and β-mercaptoethanol, whereas inhibited by Hg 2+ , Pb 2+ , Ni 2+  and  p -CMB. Purified Xyl-IIb exhibited highest specificity toward birchwood and oat spelts xylan. Kinetics of Xyl-IIb revealed a  K   m  of 10 mg/ml and 16.7 mg/ml and  V   max  of 9523g and 15,873 U/mg with birchwood and oat spelts xylan, respectively, indicating high affinity toward birchwood xylan. The xylanase (Xyl-IIb) belongs to glycosyl hydrolase (GH) family 10 based on conserved regions. Xylanase-encoding gene ( xynB ) consists of 1501 bp with an open reading frame of 264 bp which was predicted to encode a protein having 87 amino acids and shared homology with endo-1,4-beta-xylanase ( xynB ) gene from  Penicillium citrinum . Cloned  xynB  gene was expressed in  E. coli  BL21 (DE3) with xylanase activity (80 U/mg) and confirmed to be GH-10 Xyl-IIa based on molecular mass (~40 kDa). These properties of xylanase make it promising for their applications in biofuel industries.   Electronic supplementary material  The online version of this article (doi:10.1007/s13205-016-0489-4) contains supplementary material, which is available to authorized users.

Purification, characterization, gene cloning and expression of GH-10 xylanase (Penicillium citrinum isolate HZN13)