A highly thermostable trehalase from the thermophilic bacteriumRhodothermus marinus
✍ Scribed by Carla D. Jorge; Maria Manuel Sampaio; Gudmundur Ó. Hreggvidsson; Jakob K. Kristjánson; Helena Santos
- Publisher
- Springer
- Year
- 2006
- Tongue
- English
- Weight
- 284 KB
- Volume
- 11
- Category
- Article
- ISSN
- 1431-0651
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Caldolysin, the extracellular thermostable metal‐chelator‐sensitive lytic protease from __Thermus__ T‐351 was immobilized to Sepharose 4B, CM‐cellulose, and controlled pore glass (CPG). Although protein binding efficiencies were high (96, 88, and 95%), some loss of enzyme activity occur
The membrane-bound [NiFe]-hydrogenase from Hydrogenovibrio marinus (HmMBH) was purified homogeneously under anaerobic conditions. Its molecular weight was estimated as 110 kDa, consisting of a heterodimeric structure of 66 kDa and 37 kDa subunits. The purified enzyme exhibited high activity in a wid