Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species
Conway, J. M., Pierce, W. S., Le, J. H., Harper, G. W., Wright, J. H., Tucker, A. L., … Kelly, R. M. (2016, January 27). Journal of Biological Chemistry, Vol. 291, pp. 6732–6747.
author keywords: biofuel; cell surface; cell surface enzyme; enzyme; glycoside hydrolase; plant cell wall; Caldicellulosiruptor; S-layer; lignocellulose
MeSH headings : Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Cloning, Molecular; Clostridiales / chemistry; Clostridiales / classification; Clostridiales / enzymology; Escherichia coli / genetics; Escherichia coli / metabolism; Gene Expression; Genome, Bacterial; Glucans / metabolism; Glycoside Hydrolases / chemistry; Glycoside Hydrolases / genetics; Glycoside Hydrolases / metabolism; Kinetics; Mutation; Phylogeny; Polysaccharides / metabolism; Protein Binding; Protein Engineering; Protein Structure, Tertiary; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Substrate Specificity; Wood / metabolism; Xylans / metabolism
topics (OpenAlex): Enzyme Production and Characterization; Biofuel production and bioconversion; Studies on Chitinases and Chitosanases
TL;DR:
The results here provide new insights into the architecture and role of SLHdomain GHs and demonstrate that hemicellulose degradation can be enhanced through non-native SLH domain GHs engineered into the genomes of Caldicelluosiruptor species.
(via
Semantic Scholar)
UN Sustainable Development Goal Categories
15. Life on Land
(OpenAlex)
Sources: Web Of Science, NC State University Libraries