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

• 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
• Subjects: Ecology; Applied Microbiology and Biotechnology; Food Science; Biotechnology; Arctic
• Online Access: http://dx.doi.org/10.1128/aem.01029-19; https://journals.asm.org/doi/pdf/10.1128/AEM.01029-19

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.