Abstract
CelA is the most abundant enzyme secreted by Caldicellulosiruptor bescii and has been shown to outperform mixtures of commercially available exo- and endoglucanases in vitro. CelA 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. Here, repeated aspartate residues were introduced into the N-terminal ends of CelA GH9 and GH48 domains to improve secretion efficiency and/or catalytic efficiency of CelA. Among several constructs, the highest activity on carboxymethylcellulose (CMC), 0.81 ± 0.03 mg/mL was observed for the C. bescii strain containing CelA with 5-aspartate tag at the N-terminal end of GH9 domain—an 82% increase over wild type CelA. In addition, expression of CelA with N-terminal repeated aspartate residues in C. bescii results in a dramatic increase in its ability to grow on Avicel. Biotechnol. Bioeng. 2017;114: 945–950.
Original language | American English |
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Pages (from-to) | 945-950 |
Number of pages | 6 |
Journal | Biotechnology and Bioengineering |
Volume | 114 |
Issue number | 5 |
DOIs | |
State | Published - 2017 |
Bibliographical note
Publisher Copyright:© 2016 Wiley Periodicals, Inc.
NREL Publication Number
- NREL/JA-2700-67747
Keywords
- biomass deconstruction
- Caldicellulosiruptior
- CelA
- repeated aspartate residues