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Literature summary for 4.2.1.84 extracted from
- A novel molecular chaperone GroEL2 from Rhodococcus ruber and its fusion chimera with nitrile hydratase for co-enhanced activity and stability (2018), Chem. Eng. Sci., 192, 235-243 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| chaperone GroEL2 is co-expressed with nitrile hydratase (NHase) in Escherichia coli in three ways: (a) monocistronic expression with one T7 promoter, (b) bicistronic expression with double T7 promoters, and (c) fusion expression with one T7 promoter driving the NHase-GroEL2 chimera. The NHase-GroEL2 chimera is the most successful expression strategy. Maximal nitrile hydratase activity is enhanced by 63.6% compared with the single NHase control | Rhodococcus ruber |
General Stability
| General Stability | Organism |
|---|---|
| residual activity levels after heat shock and acrylamide immersion increase by 2.9fold and 1.1fold, respectively in nitrile hydratase-chaperone GroEL2 chimera compared with the single nitrile hydratase control | Rhodococcus ruber |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus ruber | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
residual activity levels after heat shock and acrylamide immersion increase by 2.9fold and 1.1fold, respectively in nitrile hydratase-chaperone GroEL2 chimera compared with the single nitrile hydratase control | Rhodococcus ruber |
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Release 2023.1 (January 2023)
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