Degradation of sulfonated azo dyes by the purified lignin peroxidase from <Emphasis Type="Italic">Brevibacillus laterosporus</Emphasis> MTCC 2298 |
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Authors: | Sushama S Gomare Jyoti P Jadhav Sanjay P Govindwar |
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Institution: | (1) Department of Biochemistry, Shivaji University, Kolhapur, 416004, India |
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Abstract: | Lignin peroxidase (EC 1.11.1.14) was purified from the Brevibacillus laterosporus MTCC 2298 by ion exchange chromatography. The Km value of the purified lignin peroxidase (using n-propanol as substrate) was 1.6 mM. The MW of purified enzyme determined
with the help of MW-standard markers was approximately 205 kDa. Purity of the enzyme was confirmed by native polyacrylamide
gel electrophoresis (PAGE) and the activity staining using a substrate L-DOPA. Sulfonated azo dyes such as Methyl orange and
Blue-2B were degraded by the purified lignin peroxidase. Degradation of the dyes was confirmed by HPLC, GC-MS, and FTIR spectroscopy.
The mainly elected products of Methyl orange were 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 were 4-(2-hexenoic acid)-2, 5-cyclohexa-diene-one
(m/z = 207; M − 1 = 206) and dehydro-acetic acid derivative (m/z = 223). |
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Keywords: | purification lignin peroxidase degradation sulfonated azo dye PAGE |
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