A Novel Subfamily of Endo-β-1,4-Glucanases in Glycoside Hydrolase Family 10

Cellulase and xylanase have been widely used in the textile, pulp and paper, animal feed, and food-processing industries. Exploring novel cellulases and xylanases for biocatalysts continues to be a hot issue. Enzymes derived from the polar seas might have novel hydrolysis patterns, substrate specifi...

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Bibliographic Details
Published in:Applied and Environmental Microbiology
Main Authors: Zhao, Fang, Cao, Hai-Yan, Zhao, Long-Sheng, Zhang, Yi, Li, Chun-Yang, Zhang, Yu-Zhong, Li, Ping-Yi, Wang, Peng, Chen, Xiu-Lan
Other Authors: Zhou, Ning-Yi, National Key R&D Program of China, AoShan Talents Cultivation Program Supported by Qingdao National Laboratory for Marine Science and Technology, Taishan Scholars Program of Shandong Province, Young Scholars Program of Shandong University, National Natural Science Foundation of China
Format: Article in Journal/Newspaper
Language:English
Published: American Society for Microbiology 2019
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Online Access:http://dx.doi.org/10.1128/aem.01029-19
https://journals.asm.org/doi/pdf/10.1128/AEM.01029-19
Description
Summary:Cellulase and xylanase have been widely used in the textile, pulp and paper, animal feed, and food-processing industries. Exploring novel cellulases and xylanases for biocatalysts continues to be a hot issue. Enzymes derived from the polar seas might have novel hydrolysis patterns, substrate specificities, or extremophilic properties that have great potential for both fundamental research and industrial applications. Here, we identified a novel cold-adapted and salt-tolerant endo-β-1,4-glucanase, Al CMCase, from an Arctic marine bacterium. It may be useful in certain industrial processes, such as under low temperature or high salinity. Moreover, Al CMCase is a bifunctional representative of glycoside hydrolase (GH) family 10 that preferentially hydrolyzes β-1,4-glucans. With its homologs, it represents a new subfamily in this family. Thus, this study sheds new light on the substrate specificity of GH10.