数字农科院2.0

Anaerobic Fungal Carbohydrate-Binding Modules Exhibit Preference for Fusion to Hemicellulases and Enhance Their Enzymatic Hydrolysis

文献类型： 外文期刊

作者： Shi, Qicheng;Wang, Dongyang;Duan, Chen;Li, Yuqi;Tu, Tao;Zhu, Weiyun;Cann, Isaac;Cheng, Yanfen

作者机构：

关键词： anaerobic fungi;carbohydrate-binding module;carbohydrate active enzyme gene cluster;fusion preference;hemicellulose degradation

期刊名称： JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

ISSN： 0021-8561

年卷期： 2026 年

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： As auxiliary components of the carbohydrate active enzymes (CAZymes), carbohydrate-binding modules (CBMs) influence the enzymatic hydrolysis of substrates. To investigate the role of anaerobic fungal CBMs in lignocellulose degradation, an architectural analysis of bacterial and fungal CBM-containing protein sequences was completed. Results indicated that 67.9% of the fungal CBMs were incorporated into the plant-biomass-degrading enzymes and 51.1% of the anaerobic fungal CBMs were biased to be fused with the hemicellulose-degrading enzymes. Based on the transcriptomic data of anaerobic fungus Pecoramyces ruminantium F1, three upregulated CBM-fused hemicellulose-degrading enzyme gene clusters were identified. Results suggested that the fused CBMs retained the enzymatic function of the associated CAZymes. Importantly, the CBM1 domains of acetyl xylan esterase (AxeA16138) and alpha-L-arabinofuranosidase (AraA02173) possessed a crucial role to promote the xylanase-mediated hydrolysis of hemicellulose. These results demonstrated that anaerobic fungal CBMs harbor substantial potential to enhance hemicellulose degradation.

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