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
作者: Zhao, Xin 1 ; Guo, Fangfang 2 ; Ma, Yong 1 ; Wang, Zhihong 1 ; Wu, Hao 1 ; Zhang, Hong 1 ; Gao, Li 1 ; Wen, Tong 1 ;
作者机构: 1.Baotou Teachers Coll, Fac Ecol & Environm, Baotou 014030, Peoples R China
2.Beijing Acad Agr & Forestry Sci, Inst Anim Husb & Vet Med, Beijing Key Lab Prevent & Control Infect Dis Lives, Beijing 100097, Peoples R China
关键词:
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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