Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering.
Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering.
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通过合理的蛋白质工程改进 Talaromyces leycettanus 木聚糖酶的热稳定性
DOI:
10.1038/s41598-017-12659-y
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发表时间:
2017-11-10
影响因子:
4.6
通讯作者:
Luo H
中科院分区:
文献类型:
--
作者:
Wang X;Ma R;Xie X;Liu W;Tu T;Zheng F;You S;Ge J;Xie H;Yao B;Luo H
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 Tm values of 60.01 to 67.84 °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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DOI:
10.1016/j.ijbiomac.2016.03.003
发表时间:
2016-06-01
影响因子:
8.2
作者:
Alponti, Juliana Sanchez;Maldonado, Raquel Fonseca;Ward, Richard J.
通讯作者:
Ward, Richard J.
影响因子:
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作者:
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通讯作者:
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影响因子:
5
作者:
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通讯作者:
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影响因子:
2.9
作者:
Luo, Huiying;Li, Jiang;Yao, Bin
通讯作者:
Yao, Bin
影响因子:
4.4
作者:
de Lima Damasio, Andre R.;Silva, Tony M.;Polizeli, Maria de Lourdes T. M.
通讯作者:
Polizeli, Maria de Lourdes T. M.