The characterization and determination of kinetic parameters of bromelain extracted from curaua (Ananas erectifolius) white and purple varieties were studied. Optimal pH and temperature conditions for proteolytic activity were determined by azocasein method. The enzyme has shown optimum activity at pH 6.0 for white and 6.0 and 7.0 for purple curaua, and at 40 °C and 60 °C for white curaua and at 40°C for the purple curaua. The lowest result of Km and the highest result of Vmax/Km were found for purple curaua,but the two varieties showed affinity by the substrate, with Km value of 185.18 µmol·L-1min, Vmax of 158.73µmol·L-1 and activation energy of 13,903 for white curaua and Km of 192.0 µmol·L-1min, Vmax of 188.68µmol·L-1 and activation energy of 14,941 cal/mol for purple curaua. This enzyme showed lower activation energy (26,000~28,000 cal/mol) than those of other coexisting proteinases.