RESUMO
Oxidation of phenolic compounds is an urgent need in textile industry, biological refinements, pulp and paper production. In present study, a laccase was purified from symbiotic bacterium of Bacillus sp. CF96 existing in termite digestive system. The extracellular laccase was purified via amnion sulfate precipitation, membrane dialysis, and ion exchange chromatography. The results showed that the Bacillus CF96 laccase possesses a molecular mass of 63 kDa, an optimal pH and temperature of 8.0 and 60 °C. Results showed that Zn2+, Mn2+ and Fe2+ were considered as the activator ions, while SDS was the main inhibitor. Using syringaldazine (SGZ) as substrate, the half-life of laccase at optimal temperature was 148 min; Km and Vmax were 0.737 µM and 100.5 U/mg. In addition, the enzyme showed a high effect on indigo dye with 90% bleaching capacity compared to control. In conclusion, the laccase has potential applications in industries under the provided optimal conditions.
