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Literature summary for 3.4.21.1 extracted from
- Enhanced heat stability of alpha-chymotrypsin through single-enzyme confinement in Attoliter liposomes (2016), ChemBioChem, 17, 1221-1224 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | P00766 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| pancreas | - |
Bos taurus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-chymotrypsin | - |
Bos taurus |
| alpha-CT | - |
Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
the entrapment of alpha-chymotrypsin within 70-40 nm liposomes formed from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine leads to a remarkable increase in the thermal stability of the enzyme. Heating aqueous suspensions of alpha-chymotrypsin-containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes to 80°C for 30 minutes results in partial enzyme inactivation, whereas the same treatment of aqueous solutions of free enzyme inactivates the enzyme completely. The stabilizing effect of enzyme confinement in the attoliter volumes of the liposomes increases with decreasing numbers of alpha-chymotrypsin molecules per liposome | Bos taurus |
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Release 2023.1 (January 2023)
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