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Literature summary for 3.4.21.4 extracted from
- The properties of covalently immobilized trypsin on soap-free P(MMA-EA-AA) latex particles (2005), Macromol. Biosci., 5, 344-351.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | covalent immobilization of enzyme onto poly(methyl methacrylate)-co-(ethyl acrylate)-co-(acrylic acid) latex particles. Immobilized enzyme shows higher optimal temperature and pH-value than free form. Immobilized enzyme exhibits higher KM-value than free form and better chemical and thermal stability, it maintains 63% of initial activity after reusing ten times | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
commercial preparation | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
vmax-value is 5467 microgramms per min for free enzyme, 793 microgramms per min for immobilized enzyme | Sus scrofa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Sus scrofa | ? | - |
? |  |
| N-alpha-benzoyl-L-Arg ethyl ester + H2O | - |
Sus scrofa | N-alpha-benzoyl-L-Arg + ethanol | - |
? | |
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