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Literature summary for 4.3.1.24 extracted from
- Stabilization of phenylalanine ammonia lyase from Rhodotorula glutinis by encapsulation in polyethyleneimine-mediated biomimetic silica (2015), Appl. Biochem. Biotechnol., 176, 999-1011 .
General Stability
| General Stability | Organism |
|---|---|
| encapsulated enzyme shows high operational stability of 7 reaction cycles | Rhodotorula glutinis |
| stability (thermal stability, pH-stability, stability of the enzyme against denaturants and storage stability) is improved by encapsulation | Rhodotorula glutinis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
L-phenylalanine | the Km-value of encapsulated enzyme in biomimetic silica is higher than that of the soluble enzyme due to lower total surface area and increased mass transfer resistance | Rhodotorula glutinis |  |
| 0.56 | - |
L-phenylalanine | pH 8.8, 30°C, soluble enzyme | Rhodotorula glutinis | |
| 1.04 | - |
L-phenylalanine | pH 8.8, 30°C, encapsulated enzyme | Rhodotorula glutinis | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| Ethanol | 20%, the soluble enzyme shows approximately 75%, the encapsulated enzyme retains 83% of its original activity | Rhodotorula glutinis |
| SDS | in the presence of 2% SDS, the soluble enzyme shows approximately 10%, the encapsulated enzyme retains 47% of its original activity | Rhodotorula glutinis |
| urea | 6 M, the soluble enzyme shows 17%, the encapsulated enzyme retains 25% of its original activity | Rhodotorula glutinis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodotorula glutinis | - |
- |
- |
| Rhodotorula glutinis CICC 32917 | - |
- |
- |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 25°C, Tris-HCl buffer solution (pH 8.8), residual activities of soluble and encapsulated enzymes after 20 days are 10% and 46% | Rhodotorula glutinis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine | - |
Rhodotorula glutinis | trans-cinnamate + NH3 | - |
? | |
| L-phenylalanine | - |
Rhodotorula glutinis CICC 32917 | trans-cinnamate + NH3 | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Rhodotorula glutinis |
| 50 | - |
pH-optimum of encapsulated enzyme | Rhodotorula glutinis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 70 | 30°C: about 55% of maximal activity (immobilized enzyme), about 35% of maximal activity (soluble enzyme), 70°C: about 55% of maximal activity (immobilized enzyme), about 10% of maximal activity (soluble enzyme) | Rhodotorula glutinis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal stability of the enzyme is improved by encapsulation | Rhodotorula glutinis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.7 | - |
assay at | Rhodotorula glutinis |
| 8.8 | - |
encapsulated enzyme, soluble enzyme | Rhodotorula glutinis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | pH 6.0: about 60% of maximal activity (immobilized enzyme), about 40% of maximal activity (soluble enzyme), pH 10.0: about 90% of maximal activity (immobilized enzyme), about 80% of maximal activity (soluble enzyme) | Rhodotorula glutinis |
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