Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | in order to obtain a high and sustainable activity of lignin peroxidase, H2O2 is supplied through a co-immobilized glucose oxidase (GOD)-catalyzed oxidation reaction | Phanerodontia chrysosporium |
Application | Comment | Organism |
---|---|---|
environmental protection | a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization | Phanerodontia chrysosporium |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
H2O2 | the inhibitory concentration of H2O2 might be different for different dyes | Phanerodontia chrysosporium |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Phanerodontia chrysosporium | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | - |
F.F. Lombard ME446 (ATCC 34541) | - |
Purification (Comment) | Organism |
---|---|
- |
Phanerodontia chrysosporium |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
4.0 U/ml veratryl alcohol activity, pH 3.5, 30°C | Phanerodontia chrysosporium |
Storage Stability | Organism |
---|---|
at 4°C the activity of the immobilized lignin peroxidase decreases slowly. After 1 month, about 95% activity is still retained, free lignin peroxidase loses about 30% of its initial activity, indicating that the storage stability of lignin peroxidase considerably increases after the immobilization on nanoporous gold | Phanerodontia chrysosporium |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
fuchsine + H2O2 | - |
Phanerodontia chrysosporium | ? | - |
? | |
pyrogallol red + H2O2 | - |
Phanerodontia chrysosporium | ? | - |
? | |
rhodamine B + H2O2 | - |
Phanerodontia chrysosporium | ? | - |
? | |
veratryl alcohol + H2O2 + H+ | - |
Phanerodontia chrysosporium | veratraldehyde + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
lignin peroxidase | - |
Phanerodontia chrysosporium |
LIP | - |
Phanerodontia chrysosporium |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
immobilized lignin peroxidase, 10°C higher than that of free lignin peroxidase | Phanerodontia chrysosporium |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
after 2 h incubation at 45°C, 55% of the initial activity of the immobilized lignin peroxidase (on nanoporous gold) is still retained while the free lignin peroxidase is completely deactivated, pH 3.5 citrate buffer | Phanerodontia chrysosporium |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3.5 | - |
similar pH activity profile for the immobilizied and the free enzyme | Phanerodontia chrysosporium |