We have studied the kinetics of decolorization of aqueous solutions of the dye Indigo Carmine and its biocatalytic degradation by the enzyme horseradish peroxidase (HRP). Experiments were carried out with a dye concentration of 2.5 x 10(-5) mol L-1 over a temperature range of 25-60 degrees C and decolorization was monitored spectrophotometrically at 610 nm. Furthermore, the concentration of H2O2 (30%, 3%, 0.3%, 0.03% and 0.003%), essential for enzyme activation, the pH (4, 5, 6, 7, and 8) and the amount of enzyme (1, 2, and 3 mg) were varied. In the kinetic studies, it was observed that the decolorization curves followed first-order kinetics, which were used to determine the rate constants which ranged from 10(-2) to 10(-3) min(-1), proving this to be a fast process, with color disappearance between 30 and 60 min. Acid conditions pH (4, 5, and 6), temperatures between 40 degrees C and 60 degrees C and hydrogen peroxide concentration between 0.3% and 0.003% with 2 mg of HRP enzyme, favored decolorization. The kinetic parameters [ activation energy (E-a), activation enthalpy (Delta H-#), activation Gibbs energy (Delta G(#)), and activation entropy (Delta S-#)] were determined using the Arrhenius and Eyring equations. The results obtained for the best experimental conditions were as follows: E-a = 15.6 kJ moL(-1), Delta H-# 18.2 kJ moL(-1), Delta G(#) = 7.3 kJ moL(-1), and Delta S-# = 0.036 kJ moL(-1) K-1, with an efficiency of 99% of decolorization. Studies showed that HRP combined with H2O2 is effective in the decolorization and degradation of the Indigo Carmine dye.