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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.11.1.14 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

EC Number Application Comment Organism
1.11.1.14 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

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.14 extracellular
-
 Phanerodontia chrysosporium
-
-

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.14
-
 Phanerodontia chrysosporium

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.14 additional information
-
 4.0 U/ml veratryl alcohol activity, pH 3.5, 30°C Phanerodontia chrysosporium

Storage Stability

EC Number Storage Stability Organism
1.11.1.14 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.14 fuchsine + H2O2
-
 Phanerodontia chrysosporium ?
-
 ?
1.11.1.14 pyrogallol red + H2O2
-
 Phanerodontia chrysosporium ?
-
 ?
1.11.1.14 rhodamine B + H2O2
-
 Phanerodontia chrysosporium ?
-
 ?
1.11.1.14 veratryl alcohol + H2O2 + H+
-
 Phanerodontia chrysosporium veratraldehyde + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.14 lignin peroxidase
-
 Phanerodontia chrysosporium
1.11.1.14 LIP
-
 Phanerodontia chrysosporium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.14 40
-
 immobilized lignin peroxidase, 10°C higher than that of free lignin peroxidase Phanerodontia chrysosporium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.11.1.14 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.14 3.5
-
 similar pH activity profile for the immobilizied and the free enzyme Phanerodontia chrysosporium