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Literature summary for 4.1.1.7 extracted from
- Practical application of different enzymes immobilized on sepabeads (2008), Bioprocess Biosyst. Eng., 31, 163-171.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | Production of immobilized enzyme on Sepabeads EC-EA by C-C coupling | Pseudomonas putida |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| Production as hexahistidine fusion protein by fermentation of Escherichia coli cells as host strain. | Pseudomonas putida |
General Stability
| General Stability | Organism |
|---|---|
| The freeze-drying of immobilized Sepabeads EC-EA/BFD leads to an inactivation of the enzyme. | Pseudomonas putida |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | essential for the activity | Pseudomonas putida |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 240000 | - |
- |
Pseudomonas putida |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by Ni-NTA column purification. | Pseudomonas putida |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | - |
Pseudomonas putida | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
After 24 h of catalytic activity the immobilized biocatalyst Sepabeads EC-EA/BFD showed a remaining activity of 5% of its initial value. | Pseudomonas putida |
| additional information | - |
specific activity of around 62 U/g dry carrier. The activity is determined for the reaction of acetaldehyde (500 mM) and benzaldehyde (50 mM) at pH 8.0 | Pseudomonas putida |
| additional information | - |
Stability of Sepabeads EC-EA/BFD is determined by repetitive batch experiments while carrying out the synthesis of 2-hydroxy-1-phenylpropanone. The reaction of benzaldehyde and acetaldehyde is carried out at 30°C and after each batch is washed. The decrease of the initial reaction rate is followed for six batches. The newly prepared biocatalyst (enzyme loading 320 mg/g) shows an initial reaction rate of 130 U/g carrier with respect to the C-C-coupling reaction, whereby the rate decreases down to 10% (13 U/g) in the sixth batch. | Pseudomonas putida |
| 11 | - |
activity of free BFD | Pseudomonas putida |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| benzoylformate decarboxylase | - |
Pseudomonas putida |
| BFD | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
at pH 8.0 | Pseudomonas putida |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | At temperatures above 70°C and lower than 20°C the activity decreases below 10 U/g carrier. | Pseudomonas putida |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | - |
Pseudomonas putida | |
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