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Literature summary for 1.11.1.13 extracted from

  • Zhang, H.; Zhang, X.; Geng, A.
    Expression of a novel manganese peroxidase from Cerrena unicolor BBP6 in Pichia pastoris and its application in dye decolorization and PAH degradation (2020), Biochem. Eng. J., 153, 107402 .
No PubMed abstract available

Application

Application Comment Organism
environmental protection as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation Cerrena unicolor
additional information the recombinant isotzyme MnP3 from Cerrena unicolor strain BBP6, rMnP3-BBP6, has promising biotechnological application potential in textile industries and polycyclic aromatic hydrocarbon bioremediation Cerrena unicolor

Cloned(Commentary)

Cloned (Comment) Organism
gene mnp3, recombinant expression of isozyme MnP3 as soluble extracellular protein in Pichia pastoris using alpha-factor as the signal peptide the recombinant enzyme has a MnP activity of 154.5 U/l Cerrena unicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular manganese peroxidase (MnP) is an extracellular glycosylated heme protein Cerrena unicolor
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ two Ca2+ per subunit Cerrena unicolor
Fe2+ in the heme b group Cerrena unicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2 Cerrena unicolor
-
2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2 Cerrena unicolor BBP6
-
2 Mn(III) + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Cerrena unicolor A0A7D5FUQ6
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-
Cerrena unicolor BBP6 A0A7D5FUQ6
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein manganese peroxidase (MnP) is an extracellular glycosylated heme protein Cerrena unicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2
-
Cerrena unicolor 2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2
-
Cerrena unicolor BBP6 2 Mn(III) + 2 H2O
-
?
brilliant blue R + H2O2 dye decolorization Cerrena unicolor ?
-
?
bromophenol blue + H2O2 dye decolorization Cerrena unicolor ?
-
?
bromophenol blue + H2O2 dye decolorization Cerrena unicolor BBP6 ?
-
?
crystal violet + H2O2 dye decolorization Cerrena unicolor ?
-
?
crystal violet + H2O2 dye decolorization Cerrena unicolor BBP6 ?
-
?
fluorene + H2O2 denim bleaching PAH degradation, product analysis by HPLC Cerrena unicolor 9H-fluorene-3,4-diol
-
?
methyl orange + H2O2 dye decolorization Cerrena unicolor ?
-
?
additional information isozyme MnP3 shows a broad substrate specificity Cerrena unicolor ?
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additional information isozyme MnP3 shows a broad substrate specificity Cerrena unicolor BBP6 ?
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phenanthrene + 2 H+ + 2 H2O2 denim bleaching PAH degradation, product analysis by HPLC Cerrena unicolor phenanthrene-9,10-dione + 2 H2O
-
?
Remazol Brilliant Blue R + H2O2 dye decolorization Cerrena unicolor ?
-
?
Remazol Brilliant Blue R + H2O2 dye decolorization Cerrena unicolor BBP6 ?
-
?

Synonyms

Synonyms Comment Organism
MnP3
-
Cerrena unicolor
rMnP3-BBP6
-
Cerrena unicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Cerrena unicolor

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 70 activity range, profile overview Cerrena unicolor

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 55 over 80% of maximal activity remains, recombinant enzyme, temperature stability profile, overview Cerrena unicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.7
-
-
Cerrena unicolor

pH Range

pH Minimum pH Maximum Comment Organism
3.5 6 activity range, profile overview Cerrena unicolor

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 4.7 over 50% of maximal activity remains, recombinant enzyme, pH stability profile, overview Cerrena unicolor

Cofactor

Cofactor Comment Organism Structure
heme b manganese peroxidase (MnP) is an extracellular glycosylated heme protein, it harbors one heme b (iron(II)-protoporphyrin IX) group per subunit Cerrena unicolor

General Information

General Information Comment Organism
physiological function manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides Cerrena unicolor