Highly stable laccase from repeated-batch culture of Funalia trogii ATCC 200800


APPLIED BIOCHEMISTRY AND MICROBIOLOGY, vol.50, no.1, pp.55-61, 2014 (SCI-Expanded) identifier identifier identifier


The effect of temperature, pH, different inhibitors and additives on activity and stability of crude laccase obtained from repeated-batch culture of white rot fungus Funalia trogii ATCC 200800 was studied. The crude enzyme showed high activity at 55-90A degrees C, which was maximal at 80-95A degrees C. It was highly stable within the temperature intervals 20-50A degrees C. The half life of the enzyme was about 2 h and 5 min at 60A degrees C and 70A degrees C, respectively. pH optimum of fungal laccase activity was revealed at pH 2.5. The enzyme from F. trogii ATCC 200800 was very stable between pH values of 3.0-9.0. NaN3 and KCN were detected as the most effective potent enzyme inhibitors among different compounds tested. The fungal enzyme was highly resistant to the various metal ions, inorganic salts, and organic solvents except propanol, at least for 5 min. Because of its high stability and efficient decolorization activity, the use of the crude F. trogii ATCC 200800 laccase instead of pure enzyme form may be a considerably cheaper solution for biotechnological applications.