Abstract
Laccase is an extracellular enzyme that is widely used in the decolonization of textile dyes in waste water. The aim of our study was to isolate, purify, characterize and immobilize the laccase enzyme produced by Trametes versicolor HBB 7328. Purified laccase enzyme was immobilized in polyacrylamide gel to explore its ability in decolonization of textile dyes. Laccase purification process was carried out by fractionation using ammonium sulphate (80%) followed by DEAE Sepharose column (30 × 3 cm) chromatography method. Recovery and fold purification in this step were 27.35 and 16.23%. Purified laccase (named as LAC1) revealed its optimum activity at pH 5.0 and 35 °C temperature, and displayed remarkable stability in the range of 30-40 °C and in the pH range (pH 3.0-7.0). The single bands on SDS-PAGE represent the purity of LAC1 with molecular weight of 60 kDa. Both free and immobilized laccase assessed for their ability to decolorize textile dyes. Free laccase decolorized Methyl red to 72.705%, Reactive orange to 57.851%, Reactive blue to 37.231%, Bromophenol blue to 24.412% however Immobilized laccase decolorized Methyl red to 89.823%, Reactive orange to 63.151%, Reactive blue to 59.548%, Bromophenol blue to 49.421% respectively. This study proposes the role of laccase from Trametes versicolor HBB 7328 in decolonization of textile dyes.