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Literature summary for 1.11.1.14 extracted from

  • Qiu, H.; Li, Y.; Ji, G.; Zhou, G.; Huang, X.; Qu, Y.; Gao, P.
    Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase (2009), Biores. Technol., 100, 3837-3842.
    View publication on PubMed

Activating Compound

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

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

Inhibitors Comment Organism Structure
H2O2 the inhibitory concentration of H2O2 might be different for different dyes Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Phanerodontia chrysosporium
-
-

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
F.F. Lombard ME446 (ATCC 34541)
-

Purification (Commentary)

Purification (Comment) Organism
-
Phanerodontia chrysosporium

Specific Activity [micromol/min/mg]

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

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 and Products (Substrate)

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

Synonyms Comment Organism
lignin peroxidase
-
Phanerodontia chrysosporium
LIP
-
Phanerodontia chrysosporium

Temperature Optimum [°C]

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 [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5
-
similar pH activity profile for the immobilizied and the free enzyme Phanerodontia chrysosporium