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Literature summary for 1.10.3.2 extracted from

  • Sarika, C.; Rekha, K.; Narasimha Murthy, B.
    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 .
    View publication on PubMed
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Application

Application Comment Organism
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
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

General Stability Organism
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

Organism UniProt Comment Textmining
Trametes versicolor
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-dimethoxyphenol + O2
-
 Trametes versicolor ?
-
 ?

Synonyms

Synonyms Comment Organism
p-diphenol:dioxygenoxidoreductase
-
 Trametes versicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 immobilized enzyme, substrate: 2,6-dimethoxyphenol Trametes versicolor

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 immobilized enzyme, substrate: 2,6-dimethoxyphenol Trametes versicolor

pH Range

pH Minimum pH Maximum Comment Organism
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