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Literature summary for 1.11.1.14 extracted from

  • Gomare, S.; Jadhav, J.; Govindwar, S.
    Degradation of sulfonated azo dyes by the purified lignin peroxidase from Brevibacillus laterosporus MTCC 2298 (2008), Biotechnol. Bioprocess Eng., 13, 136-143.
No PubMed abstract available
Search for more literature for 1.11.1.14

Application

Application Comment Organism
environmental protection lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes Brevibacillus laterosporus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6
-
 n-Propanol 27°C, pH 1.0 Brevibacillus laterosporus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
205000
-
 SDS-PAGE Brevibacillus laterosporus

Organism

Organism UniProt Comment Textmining
Brevibacillus laterosporus
-
 MTCC 2298
-

Purification (Commentary)

Purification (Comment) Organism
ion exchange chromatography, 4°C Brevibacillus laterosporus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
n-propanol + H2O2
-
 Brevibacillus laterosporus propionaldehyde + H2O
-
 ?

Synonyms

Synonyms Comment Organism
lignin peroxidase
-
 Brevibacillus laterosporus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Brevibacillus laterosporus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
1
-
-
 Brevibacillus laterosporus

pH Range

pH Minimum pH Maximum Comment Organism
1 5
-
 Brevibacillus laterosporus