Tyrosinase was purified from Solanum melongena by ammonium sulfate precipitation, Sephadex G-150 and DEAF-Sephacel column chromatography. The molecular weight of the purified tyrosinase was approximately 88,600 daltons with 805 amino acid residues. The amino acid composition showed the characteristic high contents of glycine, glutamic acid and serine residues. The enzyme had high substrate specificity towards (+)-catechin. The K_m value for L-DOPA was 20.8 mM. L-ascorbic acid, β-mercaptoethanol, sodium diethyldithiocabamate, KCN and NaN₃ had strong inhibitory effects on enzyme activity. Sodium diethyfdithiocabamate was a competitive inhibitor of the enzyme with a K_i value of 5.2 × 10^(-2) mM. The optimum pH of the enzyme was 9.0 and the optimum temperature was 65㎖ with L-DOPA as a substrate. In addition, the activity was enhanced by addition of Ca^(2+) or Cu^(2+), but decreased in the presence of Fe^(2+), Fe^(3+) and Zn^(2+) ions.