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 × 103 U mg−1, 3.6 mg ml−1 and 5.4 × 103 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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This work was financially supported by Genencor Innovation Grant.
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Jia Zheng and Ning Guo contributed equally to this work.
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Zheng, J., Guo, N., Wu, L. et al. Characterization and constitutive expression of a novel endo-1,4-β-d-xylanohydrolase from Aspergillus niger in Pichia pastoris . Biotechnol Lett 35, 1433–1440 (2013). https://doi.org/10.1007/s10529-013-1220-8
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DOI: https://doi.org/10.1007/s10529-013-1220-8