Homologous expression of the Caldicellulosiruptor bescii CelA reveals that the extracellular protein is glycosylated.

ABSTRACT: Members of the bacterial genus Caldicellulosiruptor are the most thermophilic cellulolytic microbes described with ability to digest lignocellulosic biomass without conventional pretreatment. The cellulolytic ability of different species varies dramatically and correlates with the presence of the multimodular cellulase CelA, which contains both a glycoside hydrolase family 9 endoglucanase and a glycoside hydrolase family 48 exoglucanase known to be synergistic in their activity, connected by three cellulose-binding domains via linker peptides. This architecture exploits the cellulose surface ablation driven by its general cellulase processivity as well as excavates cavities into the surface of the substrate, revealing a novel paradigm for cellulase activity. We recently reported that a del

SUBMITTER: Chung D 

PROVIDER: S-EPMC4370642 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature