Production, Purification, and Characterization of a Cellulase-Free Thermostable Endo-xylanase from Thermoanaerobacterium thermosaccharolyticum DSM 571.

Li, Xun; Shi, Hao; Ding, Huaihai; Zhang, Yu; Wang, Fei

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 Co, Mn, and Tween 60 and significantly inactivated by Al, Cu, Zn, and SDS. The K and V values of XYN for the hydrolysis of beechwood xylan were 2.1 mg/ml and 222.1 U/mg, respectively. The k values of XYN for beechwood xylan at the optimal temperature and pH values were 481.4 s. 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.

THERMOPHILIC bacteria; HEAT stability in proteins; XYLANASES; DEPOLYMERIZATION; HYDROLYSIS

Applied Biochemistry & Biotechnology, 2014, Vol 174, Issue 7, p2392

0273-2289

Academic Journal

10.1007/s12010-014-1135-4