Laccase production by a monokaryotic strain of Pycnoporus cinnabarinus derived from a dikaryotic strain

Monokaryotic Pycnoporus cinnabarinus strains were obtained from the dikaryo tic strain I-938. One of these, designated MK18, consistently produced high laccase activity. In cultures of MK18 and I-938 where ferulic acid was add ed as laccase inducer, laccase activity was enhanced about 2.5-fold reachin g 3400 U/l for the MK18 strain. Laccase was purified to homogeneity and und er the selected growth conditions, only one isoform of the enzyme was produ ced. The N-terminal sequence was similar to the amino terminal sequence of laccase II from Trametes versicolor. The enzyme was stable at 60 degrees C for more than 1 h.