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

ABSTRACT: 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 Ca²⁺, Ba²⁺, DTT and β-mercaptoethanol, whereas inhibited by Hg²⁺, Pb²⁺, Ni²⁺ and p-CMB. Purified Xyl-IIb exhibited highest specificity toward birchwood and oat spelts xylan. Kinetics of Xyl-IIb reveal

SUBMITTER: Bagewadi ZK 

PROVIDER: S-EPMC4987633 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature