Insight into the Thermophilic Mechanism of a Glycoside Hydrolase Family 5 beta-Mannanase

文献类型： 外文期刊

第一作者： Liu, Weina

作者： Liu, Weina;Tu, Tao;Gu, Yuan;Wang, Yuan;Zheng, Fei;Zheng, Jie;Wang, Yaru;Su, Xiaoyun;Yao, Bin;Luo, Huiying

作者机构：

关键词： glycoside hydrolase family 5 (GHS); beta-mannanase; thermostability; site-directed mutagenesis; molecular dynamics (MD) simulation

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2019 年 67 卷 1 期

页码：

收录情况： SCI

摘要： To study the molecular basis for thermophilic beta-mannanase of glycoside hydrolase family 5, two beta-mannanases, TlManSA and PMan5A, from Talaromyces leycettanus JCM12802 and Penicillium sp. WN1 were used as models. The four residues, His112 and Phe113, located near the antiparallel beta-sheet at the barrel bottom and Leu375 and Ala408 from loop 7 and loop 8 of PMan5A, were inferred to be key thermostability contributors through module substitution, truncation, and site-directed mutagenesis. The effects of these four residues on the thermal properties followed the order H112Y > A408P > L375H > F113Y and were strongly synergetic. These results were interpreted structurally using molecular dynamics (MD) simulations, which showed that improved hydrophobic interactions in the inner wall of the beta-barrel and the rigidity of loop 8 were caused by the outside domain of the barrel bottom and proline, respectively. The TIM barrel bottom and four specific residues responsible for the thermostability of GHS beta-mannanases were elucidated.

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