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Literature summary for 1.11.1.14 extracted from

  • Vandana, T.; Kumar, S.; Swaraj, S.; Manpal, S.
    Purification, characterization, and biodelignification potential of lignin peroxidase from immobilized Phanerochaete chrysosporium (2019), BioResources, 14, 5380-5399 .
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
EDTA
-
Phanerodontia chrysosporium
ethanol
-
Phanerodontia chrysosporium

Protein Variants

Protein Variants Comment Organism
additional information enzyme LiP obtained from a wild isolate of Phanerochaete chrysosporium immobilized on polyurethane foam cubes is purified 21fold using ammonium sulfate precipitation and size exclusion chromatography. The enzyme with a molecular mass of 55 kDa exhibited a considerably higher pH tolerance and thermostability compared with the native enzyme. It shows a strong affinity for the substrate veratryl alcohol and has kinetic constant values of 142.86 micromol and 0.065 mM. inhibited the activity, while ethanol, EDTA, Cu2+, Mn+, Na+, and Fe2+ exhibited induction. Purified LiP completely decolorizes (100%) bromophenyl blue, bromothymol blue, and bromocresol green. The 96% and 72% degradation obtained with phenol and Congo red is also higher compared to crude LiP. Treatment with LiP shows reduction in acid detergent lignin (ADL) as compared to untreated straws, with a maximum of 2.87 units obtained in jowar followed by 2.66 units in paddy straw. The digestibility of all straws increased, the response varying from a maximum of 21.27 units in proso millet to a minimum of 12.32 units obtained in little millet. The enzyme from immobilized organism exhibits an enhanced pH stability compared with the native enzyme obtained in the submerged cultures. It retains over 75% of activity at pH 6.5 for over 15 min Phanerodontia chrysosporium

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol
-
Phanerodontia chrysosporium
Ag+
-
Phanerodontia chrysosporium
cysteine
-
Phanerodontia chrysosporium
Hg2+
-
Phanerodontia chrysosporium
Silver nitrate
-
Phanerodontia chrysosporium
Sodium azide
-
Phanerodontia chrysosporium
Zn2+
-
Phanerodontia chrysosporium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michalis-Menten kinetics Phanerodontia chrysosporium
0.056
-
veratryl alcohol pH 5.5, 30°C, purified enzyme from immobilized Phanerochaete chrysosporium Phanerodontia chrysosporium
0.07
-
veratryl alcohol pH 5.5, 30°C, purified enzyme from free Phanerochaete chrysosporium Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Phanerodontia chrysosporium
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ activates Phanerodontia chrysosporium
Fe2+ activates Phanerodontia chrysosporium
Mn2+ activates Phanerodontia chrysosporium
additional information Mg2+ and Ca2+ fail to have any effect on the LiP activity Phanerodontia chrysosporium
Na+ activates Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 veratryl alcohol + H2O2 Phanerodontia chrysosporium
-
2 veratryl aldehyde + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
wild isolate
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme 21fold by immobilization on polyurethane foam cubes, ammonium sulfate fractionation, ultrafiltration, and gel filtration Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 veratryl alcohol + H2O2
-
Phanerodontia chrysosporium 2 veratryl aldehyde + 2 H2O
-
?
catechol + H2O2
-
Phanerodontia chrysosporium ? + 2 H2O
-
?
dimethoxyphenol + H2O2
-
Phanerodontia chrysosporium ? + 2 H2O
-
?
guaiacol + H2O2
-
Phanerodontia chrysosporium ? + 2 H2O
-
?
additional information lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates. It has the distinction of being able to oxidize methoxylated aromatic rings without a free phenolic group, which generates cation radicals that can react further by a variety of pathways, including ring opening, demethylation, and phenol dimerization. In contrast with laccases, LiP does not require mediators to degrade high redox-potential compounds, but it needs H2O2 to initiate catalysis. Substrate specificity, no or poor activity with ferulic acid, vanillic acid, diaminobenzidine, and HoBT. Purified LiP obtained from immobilized Phanerochaete chrysosporium completely decolorizes bromophenyl blue, bromothymol blue, and bromocresol green, purified enzyme from immobilized Phanerochaete chrysosporium shows increased dye decolorization efficiency compared to the enzyme from non-immobilized Phanerochaete chrysosporium Phanerodontia chrysosporium ?
-
-
syringaldehyde + H2O2
-
Phanerodontia chrysosporium ? + 2 H2O
-
?

Subunits

Subunits Comment Organism
? x * 55000, SDS-PAGE Phanerodontia chrysosporium

Synonyms

Synonyms Comment Organism
LIP
-
Phanerodontia chrysosporium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
immobilized enzyme, with veratryl alcohol as the substrate Phanerodontia chrysosporium

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 40 over 50% of maximal activity within this range, profile overview Phanerodontia chrysosporium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 80 the purified enzyme exhibits a higher thermostability and retains over 50% of the activity, even after 120 min of incubation at both 60°C and 65°C. Loss of 25% of the activitiy after 120 min at 70°C. 25% activity is maintained after 100 min at both 75°C and 80°C and activity is completely lost after 120 min Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
purified enzyme from immobilized Phanerochaete chrysosporium, with veratryl alcohol as the substrate Phanerodontia chrysosporium

pH Range

pH Minimum pH Maximum Comment Organism
3 10 activity range, purified enzyme from immobilized Phanerochaete chrysosporium, profile overview Phanerodontia chrysosporium

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5
-
immobilized enzyme, retains over 75% of activity at pH 6.5 for over 15 min Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme
-
Phanerodontia chrysosporium

General Information

General Information Comment Organism
physiological function extracellular enzymes of white-rot fungi play an important role in the deconstruction of lignin in lignocellulosic biomass. Lignin peroxidase plays a role in biodegradation of plant cell wall lignin. LiP may also play a major role in the bio-delignification of lignocellulose in crop residues. Lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates Phanerodontia chrysosporium