Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | - |
Phanerodontia chrysosporium | |
ethanol | - |
Phanerodontia chrysosporium |
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 | 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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Phanerodontia chrysosporium | - |
- |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 veratryl alcohol + H2O2 | Phanerodontia chrysosporium | - |
2 veratryl aldehyde + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | - |
wild isolate | - |
Purification (Comment) | Organism |
---|---|
native extracellular enzyme 21fold by immobilization on polyurethane foam cubes, ammonium sulfate fractionation, ultrafiltration, and gel filtration | Phanerodontia chrysosporium |
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 | Comment | Organism |
---|---|---|
? | x * 55000, SDS-PAGE | Phanerodontia chrysosporium |
Synonyms | Comment | Organism |
---|---|---|
LIP | - |
Phanerodontia chrysosporium |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
immobilized enzyme, with veratryl alcohol as the substrate | Phanerodontia chrysosporium |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 40 | over 50% of maximal activity within this range, profile overview | Phanerodontia chrysosporium |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
purified enzyme from immobilized Phanerochaete chrysosporium, with veratryl alcohol as the substrate | Phanerodontia chrysosporium |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 10 | activity range, purified enzyme from immobilized Phanerochaete chrysosporium, profile overview | Phanerodontia chrysosporium |
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 | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Phanerodontia chrysosporium |
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 |