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Improvement of the catalytic characteristics of a salt-tolerant GH10 xylanase from Streptomyce rochei L10904
- Li, Qin, Sun, Baoguo, Li, Xiuting, Xiong, Ke, Xu, Youqiang, Yang, Ran, Hou, Jie, Teng, Chao
- International journal of biological macromolecules 2018 v.107 pp. 1447-1455
- carbohydrate binding, catalytic activity, corn cobs, mutants, salt tolerance, sodium chloride, thermal stability, xylan, xylanases, xylose
- A GH10 xylanase Srxyn10 from Streptomyce rochei L10904, and its truncated derivative, Srxyn10M, were investigated. Both displayed great salt-tolerant ability, retaining more than 95% and 91% activity after incubation at 37°C for 1h in 3.0M and 5.0M NaCl, respectively. They exhibited a special hydrolytic property of forming xylobiose as the major product and produced fewer xylose compounds when combined with a reported xylanase while digesting corncob xylans. The mutant, Srxyn10M, was constructed from Srxyn10 by deleting the C-terminal carbohydrate-binding module. It possessed a 3.26-fold higher specific activity on beechwood xylan than Srxyn10. Moreover, Srxyn10M showed greater substrate affinity and catalytic efficiency than Srxyn10 when beechwood xylan, birchwood xylan, and oat-spelt xylan were used as substrates. The thermostability was also greatly improved. Therefore, the application potential was markedly enhanced by the improvement of these properties.