Hydrolysis Mechanism of Multimodular Endoglucanases with Distinctive Domain Composition in the Saccharification of Cellulosic Substrates

文献类型： 外文期刊

第一作者： Zheng, Fei

作者： Zheng, Fei;Yang, Junzhao;Sun, Qingyang;Zhang, Xinrui;Li, Ruilin;He, Xiangwei;Zhao, Guozhu;Zheng, Fei;Yang, Junzhao;Sun, Qingyang;Zhang, Xinrui;Li, Ruilin;He, Xiangwei;Zhao, Guozhu;Luo, Huiying

作者机构：

期刊名称：BIOMACROMOLECULES （ 影响因子：5.4； 五年影响因子：5.8 ）

ISSN： 1525-7797

年卷期： 2024 年 25 卷 9 期

页码：

收录情况： SCI

摘要： Two multimodular endoglucanases in glycoside hydrolase family 5, ReCel5 and ElCel5, share 73% identity and exhibit similar modular structures: family 1 carbohydrate-binding module (CBM1); catalytic domain; CBMX2; module of unknown function. However, they differed in their biochemical properties and catalytic performance. ReCel5 showed optimal activity at pH 4.0 and 70 degrees C, maintaining stability at 70 degrees C (>80% activity). Conversely, ElCel5 is optimal at pH 3.0 and 50 degrees C (>50% activity at 50 degrees C). ElCel5 excels in degrading CMC-Na (256 U/mg vs 53 U/mg of ReCel5). Five domain-truncated (TM1-TM5) and four domain-replaced (RM1-RM4) mutants of ReCel5 with the counterparts of ElCel5 were constructed, and their enzymatic properties were compared with those of the wild type. Only RM1, with ElCel5-CBM1, displayed enhanced thermostability and activity. The hydrolysis of pretreated corn stover was reduced in most TM and RM mutants. Molecular dynamics simulations revealed interdomain interactions within the multimodular endoglucanase, potentially affecting its structural stability and complex biological catalytic processes.

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