The culture conditions for maximum secretion of laccase by Loweporus lividus MTCC-1178 have been optimized. The laccase from the culture filtrate of L. lividus MTCC-1178 has been purified to homogeneity. The molecular weight of the purified laccase is 64.8 kDa. The enzymatic characteristics like K (m), pH, and temperature optimum using 2,6-dimethoxyphenol have been determined and found to be 480 mu M, 5.0, and 60 A degrees C, respectively. The K (m) values for other substrates like catechol, m-cresol, pyrogallol, and syringaldazine have also been determined and found to be 230, 210, 320, and 350 mu M, respectively.