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Literature summary for 1.4.3.3 extracted from
- Encapsulation of Trigonopsis variabilis D-amino acid oxidase and fast comparison of the operational stabilities of free and immobilized preparations of the enzyme (2008), Biotechnol. Bioeng., 99, 251-260.
General Stability
| General Stability | Organism |
|---|---|
| carrier-free enzyme is entrapped in semipermeable microcapsules produced from the polycation poly(methylene-co-guanidine) in combination with CaCl2 and the polyanions alginate and cellulose sulfate, the effectiveness of the entrapped oxidase for O2-dependent conversion of D-methionine at 25°C is 75-95% of the free enzyme preparation | Trigonopsis variabilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| poly(methylene-co-guanidine) | in the presence of poly(methylene-co-guanidine) (1.8%, w/v) the enzyme activity decreases irreversibly with a half-life time of about 1.75 min at 25°C | Trigonopsis variabilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trigonopsis variabilis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-methionine + 2,6-dichlorophenolindophenol + H2O | - |
Trigonopsis variabilis | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-amino acid oxidase | - |
Trigonopsis variabilis |
| DAO | - |
Trigonopsis variabilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 50 | added FAD does not stabilize DAO at and below 35°C, but it contributes up to 3.6fold extra stability to the enzyme activity at temperatures higher than 35°C, with a half-life of 60 h encapsulated DAO is 720fold more stable than the free enzyme under conditions of bubble aeration at 25°C, the soluble oxidase is stabilized by added FAD only at temperatures of 35°C or greater, at 50°C encapsulated preparations of the oxidase are much more stable than the free enzyme whose half-life is only 40 min | Trigonopsis variabilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | added FAD does not stabilize DAO at and below 35°C, but it contributes up to 3.6fold extra stability to the enzyme activity at temperatures higher than 35°C | Trigonopsis variabilis | |
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