Laccase enzyme and its role in degradation of pesticide " a mini review
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Laccase activity were found after GLC analysis of culture liquid of mycelium extract Pleurotus djamor (MDU1) grown on malt extract medium with or without inducers. These laccase enzyme (paradiphenol: oxygen oxidoreductase) catalysis the oxidation and polymerization of aromatic compounds in the presence of molecular oxygen. Laccase activity in the malt extract medium had on pH 3 -4 and was stable from pH 3- 10 during 24 hours at room temperature. This enzyme had wide substrates specificity on hydroquinone, methoxy-substituted monophenols and aromatic amines. The laccase activity was found only with compounds having a redox potential lower than 0.5 mV. The highest activity was obtained with methoxy, methyl-substituted p-hydroquinone and aromatic diarnines. Some activity also occurred with the aliphatic compounds 3, 5 - cyclohexadiene-1, 2 -diol.
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