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Literature summary extracted from
- Immobilized laccase-based biosensor for the detection of disubstituted methyl and methoxy phenols - application of Box-Behnken design with response surface methodology for modeling and optimization of performance parameters (2016), Artif. Cells Nanomed. Biotechnol., 44, 1741-1752 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.10.3.2 | analysis | sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent | Trametes versicolor |
| 1.10.3.2 | environmental protection | sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent | Trametes versicolor |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.10.3.2 | co-cross-linking method is superior to the other methods of immobilization in terms of operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent | Trametes versicolor |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.10.3.2 | Trametes versicolor | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.10.3.2 | 2,6-dimethoxyphenol + O2 | - |
Trametes versicolor | ? | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.10.3.2 | p-diphenol:dioxygenoxidoreductase | - |
Trametes versicolor |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.10.3.2 | 45 | - |
immobilized enzyme, substrate: 2,6-dimethoxyphenol | Trametes versicolor |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.10.3.2 | 35 | 60 | 35°C: about 60% of maximal activity, 60°C: about 60% of maximal activity, immobilized enzyme, substrate: 2,6-dimethoxyphenol | Trametes versicolor |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.10.3.2 | 6.8 | - |
immobilized enzyme, substrate: 2,6-dimethoxyphenol | Trametes versicolor |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.10.3.2 | 6 | 7.5 | pH 6.0: about 55% of maximal activity, pH 7.5: about 55% of maximal activity, immobilized enzyme, substrate: 2,6-dimethoxyphenol | Trametes versicolor |
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