Author(s):

Sachchidanand, Ajay Kumar Singh, Yashab Kumar, Harison Masih and Kunal Singh

Abstract: Laccase is a copper containing polyphenol oxidase that acts on a wide range of substrate. A laccase producing fungi (Trichoderma spp.) was isolated and subjected to purification, characterization and dye decolorization study. Laccase activity was highest when operated at the following condition, Bengal gram used as a solid state substrate, 7 days incubation, 25 °C temperature, and pH-6 and inoculum size 2%. Guaiacol and sodium acetate buffer were used to assay laccase production. The enzyme was partially purified by ammonium sulphate precipitation and dialysis method. The purified enzyme was obtained with a specific activity of 89.959 IU/mg protein and a final yield of 70.26%. The optimal pH and temperature of the laccase was recorded to be 5 and 45 °C respectively. The values of kinetic parameters K_m and V_max for purified laccase were noted at 0.055 and 37.037 respectively, for guaiacol as substrate. The enzyme activity of crude enzyme and partially purified enzyme was observed to be 18.181 IU/ml and 44.710 IU/ml respectively. 63.866% of decolorization was observed at 48 h with Congo red and 19.009% with Rhodamine B by laccase enzyme produced by Trichoderma spp. is able to decolorize Congo red dye and Rhodamine B and can be used in controlling environmental pollution.

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