EC Number | Application | Comment | Organism |
---|---|---|---|
1.11.1.14 | environmental protection | lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes | Brevibacillus laterosporus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.11.1.14 | 1.6 | - |
n-Propanol | 27°C, pH 1.0 | Brevibacillus laterosporus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.11.1.14 | 205000 | - |
SDS-PAGE | Brevibacillus laterosporus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.14 | Brevibacillus laterosporus | - |
MTCC 2298 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.1.14 | ion exchange chromatography, 4°C | Brevibacillus laterosporus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.14 | additional information | Sulfonated azo dyes such as Methyl orange and Blue-2B are degraded by the purified lignin peroxidase. Degradation of the dyes is confirmed by HPLC, GC-MS, and FTIR spectroscopy. The mainly elected products of Methyl orange are 4-substituted hexanoic acid (m/z = 207), 4-cyclohexenone lactone cation (m/z = 191), and 4-isopropanal-2, 5-cyclohexa-dienone (m/z = 149) and for Blue-2B are 4-(2-hexenoic acid)-2, 5-cyclohexa-diene-one (m/z = 207) and dehydro-acetic acid derivative (m/z = 223), proposed pathway of degradation | Brevibacillus laterosporus | ? | - |
? | |
1.11.1.14 | n-propanol + H2O2 | - |
Brevibacillus laterosporus | propionaldehyde + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.1.14 | lignin peroxidase | - |
Brevibacillus laterosporus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.14 | 40 | - |
- |
Brevibacillus laterosporus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.14 | 10 | 90 | lignin peroxidase is active in a broad range of temperature where higher temperature of about 90°C affects not the enzymatic configuration (thermal denaturation) | Brevibacillus laterosporus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.14 | 1 | - |
- |
Brevibacillus laterosporus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.14 | 1 | 5 | - |
Brevibacillus laterosporus |