Enzymatic Characterization of a Rumen Microorganism-Derived Multifunctional Glycoside Hydrolase and Its GH26 Domain with Mannanase Activity

文献类型： 外文期刊

第一作者： Zhao, Xin

作者： Zhao, Xin;Ma, Yong;Wang, Zhihong;Wu, Hao;Zhang, Hong;Gao, Li;Wen, Tong;Guo, Fangfang

作者机构：

关键词： Segatella bryantii; endo-beta-1,4-glucanase; endo-beta-1,4-mannanase; multifunctional enzyme

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）

ISSN： 0021-8561

年卷期： 2025 年 73 卷 22 期

页码：

收录情况： SCI

摘要： In this study, a novel multifunctional glycoside hydrolase (GH) with two distinct domains homologous to the GH family 5 (GH5) and family 26 (GH26) was isolated from the rumen microorganism Segatella bryantii. The heterologous expression product of this enzyme exhibited both endo-beta-1,4-glucanase and endo-beta-1,4-mannanase activities. Intriguingly, segmental expression studies indicated that the GH26 domain alone contributed to the beta-mannanase activity, and its specific activity reached 2060 U/mg under optimal conditions (30 degrees C, pH 5.5). Furthermore, site-directed mutagenesis confirmed that the glutamic acid residues at positions 165 and 276 were indispensable for the catalytic activity of the GH26 domain. Collectively, a novel multifunctional GH from a symbiotic microorganism of ruminants was identified. Preliminary enzymatic characterizations of its GH26 family domain, which has independent beta-mannanase activities, were determined.

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