Article
Molecular and biochemical analyses of CbCel9A/Cel48A, a highly secreted multi-modular cellulase by Caldicellulosiruptor bescii during growth on crystalline cellulose.
PloS one - 1 Jan 2013
Yi Zhuolin, Su Xiaoyun, Revindran Vanessa, Mackie Roderick I, Cann Isaac
Abstract excerpt
During growth on crystalline cellulose, the thermophilic bacterium Caldicellulosiruptor bescii secretes several cellulose-degrading enzymes. Among these enzymes is CelA (CbCel9A/Cel48A), which is reported as the most highly secreted cellulolytic enzyme in this bacterium. CbCel9A/Cel48A is a large multi-modular polypeptide, composed of an N-terminal catalytic glycoside hydrolase family 9 (GH9) module and a...
Topics
- Bacteria
- Cellulase
- Cellulose
- Enzyme Activation
- Gene Expression
- Hydrogen-Ion Concentration
- Hydrolysis
- Kinetics
- Mutation
- Substrate Specificity
- Temperature