Article
Probing the stability of the modular family 10 xylanase from Rhodothermus marinus.
Extremophiles : life under extreme conditions - 1 Dec 2003
Abou-Hachem Maher, Olsson Fredrik, Nordberg Karlsson Eva
Abstract excerpt
The thermophilic bacterium Rhodothermus marinus produces a modular xylanase (Xyn10A) consisting of two N-terminal carbohydrate-binding modules (CBMs), followed by a domain of unknown function, and a catalytic module flanked by a fifth domain. Both Xyn10A CBMs bind calcium ions, and this study explores the effect of these ions on the stability of the full-length enzyme. Xyn10A and truncated forms thereof were...
Topics
- Amino Acid Sequence
- Binding Sites
- Calcium
- Calorimetry, Differential Scanning
- Differential Thermal Analysis
- Enzyme Stability
- Molecular Sequence Data
- Mutation
- Oligonucleotides
- Protein Binding
- Rhodothermus
- Substrate Specificity
- Thermodynamics
- Xylosidases