Abstract
Bacterial laccases have proven to be a potential biocatalyst for various industrial applications due to their remarkable catalytic and stability properties. In this study, a novel thermostable laccase was produced from the bacterium Bacillus licheniformis VNQ by submerged fermentation. The specific activity of crude and purified laccase was found to be 13.17U mg-1 and 83.47U mg-1, respectively. The enzyme possessed a molecular mass of ∼48kDa when characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum temperature and pH for enzyme activity was determined to be 55°C and 5.0, respectively. The enzyme was considered to be thermo-tolerant as it possessed a half-life of 4h at 70°C. The enzyme was utilized for the oxidative biotransformation of in situ synthesized p-quinones to biologically active compounds, 1,4-naphthoquinone and its derivative. The obtained products were characterized using nuclear magnetic resonance (NMR) spectroscopy and gas chromatography-mass spectrometry (GC-MS) analysis. A high yield of naphthoquinones (74.93±1.2%) with 1,4-naphthoquinone (60.61±1.0%), and its derivative 2-hydroxy-1,4-naphthoquinone (14.32±0.2%) was obtained at the optimized reaction conditions.
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