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  • Title: Characterization and constitutive expression of a novel endo-1,4-β-D-xylanohydrolase from Aspergillus niger in Pichia pastoris.
    Author: Zheng J, Guo N, Wu L, Tian J, Zhou H.
    Journal: Biotechnol Lett; 2013 Sep; 35(9):1433-40. PubMed ID: 23690032.
    Abstract:
    A putative endo-1,4-β-D-xylanohydrolase gene xyl10 from Aspergillus niger, encoding a 308-residue mature xylanase belonging to glycosyl hydrolase family 10, was constitutively expressed in Pichia pastoris. The recombinant Xyl10 exhibited optimal activity at pH 5.0 and 60 °C with more than 50 % of the maximum activity from 40 to 70 °C. It retained more than 90 % of the original activity after incubation at 60 °C (pH 5.0) for 30 min and more than 74 % after incubation at pH 3.0-13.0 for 2 h (25 °C). The specific activity, K m and V max values for purified Xyl10 were, respectively, 3.2 × 10(3) U mg(-1), 3.6 mg ml(-1) and 5.4 × 10(3) μmol min(-1 )mg(-1) towards beechwood xylan. The enzyme degraded xylan to a series of xylooligosaccharides and xylose. The recombinant enzyme with these properties has the potential for various industrial applications.
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