The GH10 and GH48 dual-functional catalytic domains from a multimodular glycoside hydrolase synergize in hydrolyzing both cellulose and xylan

文献类型： 外文期刊

第一作者： Chu, Yindi

作者： Chu, Yindi;Hao, Zhenzhen;Wang, Kaikai;Tu, Tao;Huang, Huoqing;Wang, Yuan;Bai, Ying Guo;Wang, Yaru;Luo, Huiying;Yao, Bin;Su, Xiaoyun;Chu, Yindi

作者机构：

关键词： Caldicellulosiruptor bescii; Cellulase; Xylanase; Synergy; GH10; GH48; Multimodular; Bifunctional; Biofuel

期刊名称：BIOTECHNOLOGY FOR BIOFUELS （ 影响因子：6.04； 五年影响因子：6.485 ）

ISSN：

年卷期： 2019 年 12 卷 1 期

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收录情况： SCI

摘要： Background: Regarding plant cell wall polysaccharides degradation, multimodular glycoside hydrolases (GHs) with two catalytic domains separated by one or multiple carbohydrate-binding domains are rare in nature. This special mode of domain organization endows the Caldicellulosiruptor bescii CelA (GH9-CBM3c-CBM3b-CBM3b-GH48) remarkably high efficiency in hydrolyzing cellulose. CbXyn10C/Cel48B from the same bacterium is also such an enzyme which has, however, evolved to target both xylan and cellulose. Intriguingly, the GH10 endoxylanase and GH48 cellobiohydrolase domains are both dual functional, raising the question if they can act synergistically in hydrolyzing cellulose and xylan, the two major components of plant cell wall. Results: In this study, we discovered that CbXyn10C and CbCel48B, which stood for the N- and C-terminal catalytic domains, respectively, cooperatively released much more cellobiose and cellotriose from cellulose. In addition, they displayed intramolecular synergy but only at the early stage of xylan hydrolysis by generating higher amounts of xylo-oligosaccharides including xylotriose, xylotetraose, and xylobiose. When complex lignocellulose corn straw was used as the substrate, the synergy was found only for cellulose but not xylan hydrolysis. Conclusion: This is the first report to reveal the synergy between a GH10 and a GH48 domain. The synergy discovered in this study is helpful for understanding how C. bescii captures energy from these recalcitrant plant cell wall polysaccharides. The insight also sheds light on designing robust and multi-functional enzymes for plant cell wall polysaccharides degradation.

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