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High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations

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成果类型:
期刊论文
作者:
Wang, Yawei;Wang, Jing;Zhang, Zhongqiang;Yang, Jiangke;Turunen, Ossi;...
通讯作者:
Xiong, HR;Turunen, O
作者机构:
[Wang, Yawei; Yang, Jiangke] Wuhan Polytech Univ, Coll Life Sci & Technol, Wuhan 430048, Peoples R China.
[Zhang, Zhongqiang; Xiong, Hairong; Xiong, HR; Wang, Jing] South Cent Univ Nationalities, Coll Life Sci, Wuhan 430074, Peoples R China.
[Turunen, Ossi; Turunen, O] Univ Eastern Finland, Sch Forest Sci, FI-80101 Joensuu, Finland.
通讯机构:
[Xiong, HR ] S
[Turunen, O ] U
South Cent Univ Nationalities, Coll Life Sci, Wuhan 430074, Peoples R China.
Univ Eastern Finland, Sch Forest Sci, FI-80101 Joensuu, Finland.
语种:
英文
关键词:
Thermostability;GH10 xylanase;Mutation;1VBR;Thermotoga maritima
期刊:
Applied Microbiology and Biotechnology
ISSN:
0175-7598
年:
2022
卷:
106
期:
5-6
页码:
2017-2027
基金类别:
This work was financially supported by the project (no. DY135-B2-07) from the China Ocean Mineral Resources R&D Association, Hubei Provincial Technical Innovation Program (no. 2018ABA093).
机构署名:
本校为第一机构
院系归属:
生命科学与技术学院
摘要:
Abstract: A hyperthermostable xylanase XYN10B from Thermotoga maritima (PDB code 1VBR, GenBank accession number KR078269) was subjected to site-directed and error-prone PCR mutagenesis. From the selected five mutants, the two site-directed mutants (F806H and F806V) showed a 3.3–3.5-fold improved enzyme half-life at 100 °C. The mutant XYNA generated by error-prone PCR showed slightly improved stability at 100 °C and a lower Km. In XYNB and XYNC, the additional mutations over XYNA decreased the thermostability and temperature optimum, while el...

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