Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-β-Xylanase from Caldicellulosiruptor owensensis

Author:

Liu Xin1,Liu Tengfei2,Zhang Yuebin3,Xin Fengjiao1,Mi Shuofu4,Wen Boting1,Gu Tianyi1,Shi Xinyuan2,Wang Fengzhong1,Sun Lichao1ORCID

Affiliation:

1. Laboratory of Biomanufacturing and Food Engineering, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R. China

2. School of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing 100102, P.R. China

3. State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Rd, Dalian 116023, P.R. China

4. National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, P.R. China

Funder

Ministry of Science and Technology of the People's Republic of China

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

General Agricultural and Biological Sciences,General Chemistry

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1. Xylanase-Producing Microbes and Their Real-World Application;International Journal of Chemical Engineering;2023-11-01

2. Investigating the effect of substrate binding on the catalytic activity of xylanase;Applied Microbiology and Biotechnology;2023-09-16

3. Marine enzymes: Classification and application in various industries;International Journal of Biological Macromolecules;2023-03

4. Thermostable Enzymes and Their Applications;Thermophilic Anaerobes;2023

5. Current status of hyperthermophilic enzyme production;Developments and Applications of Enzymes from Thermophilic Microorganisms;2023

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