Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering
文献类型： 外文期刊
第一作者： Wang, Xiaoyu
作者： Wang, Xiaoyu;Ma, Rui;Liu, Weina;Tu, Tao;Zheng, Fei;You, Shuai;Ge, Jianzhong;Xie, Huifang;Yao, Bin;Luo, Huiying;Wang, Xiaoyu;Xie, Xiangming;Zheng, Fei
作者机构：
期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）
ISSN： 2045-2322
年卷期： 2017 年 7 卷
页码：
收录情况： SCI
摘要： Thermophilic xylanases with high catalytic efficiency are of great interest in the biofuel, food and feed industries. This study identified a GH11 xylanase gene, Tlxyn11B, in Talaromyces leycettanus JCM12802. Recombinant TlXyn11B produced in Pichia pastoris is distinguished by high specific activity (8259 +/- 32 U/mg with beechwood xylan as substrate) and excellent pH stability (from 1.0 to 10.5). The beechwood xylan hydrolysates consisted mainly of xylobiose, xylotriose and xylotetraose, thus TlXyn11B could be used for the production of prebiotic xylooligosaccharide. By using the structure-based rational approach, the N-terminal sequence of TlXyn11B was modified for thermostability improvement. Mutants S3F and S3F/D35V/I/Q/M had elevated T-m values of 60.01 to 67.84 degrees C, with S3F/D35I the greatest. Homology modeling and molecular dynamics (MD) simulation analysis revealed that the substituted F3 and I35 formed a sandwich structure with S45 and T47, which may enhance the overall structure rigidity with lowered RMSD values. This study verifies the efficiency of rational approach in thermostability improvement and provides a xylanase candidate of GH11 with great commercialization potential.
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