The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose.

The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose.
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多结构域Caldicellulosuptor bescii cela纤维素酶在晶体纤维素的水解时表现出色。

DOI:
10.1038/s41598-017-08985-w
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发表时间:
2017-08-29
期刊:
影响因子:
4.6
通讯作者:
Bomble YJ
Bomble YJ
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Brunecky R;Donohoe BS;Yarbrough JM;Mittal A;Scott BR;Ding H;Taylor Ii LE;Russell JF;Chung D;Westpheling J;Teter SA;Himmel ME;Bomble YJ

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纤维素微纤维的结晶性质是影响生物质可再生性的关键因素之一,生物质可再生性是使纤维素生物燃料成为商业现实所要克服的关键技术和经济障碍。迄今为止,所有已知的真菌酶测试有很大的困难降解高度结晶的纤维素底物。我们已经证明,来自Caldicellulosiruptor besophila的CelA纤维素酶降解高度结晶纤维素以及低结晶度底物,使其成为唯一已知的对高度结晶纤维素起良好作用的纤维素酶。与通常包含用于生物质降解的多个单一催化结构域酶的纤维素分解真菌的分泌体不同,一些细菌系统采用利用多催化结构域纤维素酶的替代策略。此外,CelA在高温下具有极高的热稳定性和高活性,不像商业真菌纤维素酶。此外,我们还确定了对C.含有CelA的纤维素酶混合物似乎与影响真菌纤维素酶的性能障碍显著不同。在这里,我们探讨了CelA在各种预处理底物上的活性和降解机制,以更好地了解生物质的不同散装组分(如木聚糖和木质素)如何影响其性能。
The crystalline nature of cellulose microfibrils is one of the key factors influencing biomass recalcitrance which is a key technical and economic barrier to overcome to make cellulosic biofuels a commercial reality. To date, all known fungal enzymes tested have great difficulty degrading highly crystalline cellulosic substrates. We have demonstrated that the CelA cellulase from Caldicellulosiruptor bescii degrades highly crystalline cellulose as well as low crystallinity substrates making it the only known cellulase to function well on highly crystalline cellulose. Unlike the secretomes of cellulolytic fungi, which typically comprise multiple, single catalytic domain enzymes for biomass degradation, some bacterial systems employ an alternative strategy that utilizes multi-catalytic domain cellulases. Additionally, CelA is extremely thermostable and highly active at elevated temperatures, unlike commercial fungal cellulases. Furthermore we have determined that the factors negatively affecting digestion of lignocellulosic materials by C. bescii enzyme cocktails containing CelA appear to be significantly different from the performance barriers affecting fungal cellulases. Here, we explore the activity and degradation mechanism of CelA on a variety of pretreated substrates to better understand how the different bulk components of biomass, such as xylan and lignin, impact its performance.
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