Abstract
This is the first report describing the cloning, expression, and characterization of a putative thermostable, cellulase-free xylanase (XYN) from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum DSM 571. The temperature and pH values for optimal enzyme activity of XYN were found to be 65 °C and pH 6.5, respectively. The XYN activity was apparently enhanced by Co2+, Mn2+, and Tween 60 and significantly inactivated by Al3+, Cu2+, Zn2+, and SDS. The K m and V max values of XYN for the hydrolysis of beechwood xylan were 2.1 mg/ml and 222.1 U/mg, respectively. The k cat values of XYN for beechwood xylan at the optimal temperature and pH values were 481.4 s−1. XYN represents an attractive candidate for use in the large-scale production of xylooligosaccharides (XOs) from forest residues because it is an endo-xylanase capable of degrading xylan.
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This work was financially supported by the State Forestry Administration 948 Program (no. 2014-4-37), the National Natural Science Foundation of China (31370572, 31270612), and the Doctorate Fellowship Foundation of Nanjing Forestry University as well as the Project of Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).
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Xun Li and Hao Shi contributed equally to this work.
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Li, X., Shi, H., Ding, H. et al. Production, Purification, and Characterization of a Cellulase-Free Thermostable Endo-xylanase from Thermoanaerobacterium thermosaccharolyticum DSM 571. Appl Biochem Biotechnol 174, 2392–2402 (2014). https://doi.org/10.1007/s12010-014-1135-4
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DOI: https://doi.org/10.1007/s12010-014-1135-4