The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-08985-w.pdf
Reference43 articles.
1. Zverlov, V. et al. Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile ‘Anaerocellum thermophilum’ with separate glycosyl hydrolase family 9 and 48 catalytic domains. Microbiology, 144 (1998).
2. Young, J. et al. Deletion of Caldicellulosiruptor bescii CelA reveals its crucial role in the deconstruction of lignocellulosic biomass. Biotechnology for Biofuels 7(1), 1–8 (2014).
3. Brunecky, R. et al. Revealing nature’s cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA. Science, 342 2013.
4. Bischof, R. H., Ramoni, J. & Seiboth, B. Cellulases and beyond: the first 70 years of the enzyme producer Trichoderma reesei. Microbial Cell Factories 15(1), 106 (2016).
5. Kari, J. et al. Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity. Journal of Biological Chemistry, (2014).
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