Peroxidase (PDD) and pectin methylesterase (PME) from tomato were characterized, studied thermal stability, and analyzed the synergistic effect of temperature and pH. For PDD, the optimal activity, using H 2 D 2 as substrate and ABTS +• as the donor H + , was obtained at pH 3.5, and for PME, the optimal activity using pectin as substrate was obtained at pH 7.5. On PDD, it was found that the values of K M , V m and K si for H 2 D 2 were 477.26 mM, 721.53 µM/min and 0.37 mM, respectively. On PME, the values of K M and V m obtained for pectin were 0.54 mM and 436.12 µM/min, respectively. Dn the other hand, it was found that PDD was inactivated with 90 °C, at pH from 2.5 to 3.5 with temperatures of 55 to 90 °C, and at pH of 2.5 to 3 with temperatures of 40 to 90 °C. Likewise, PME was inactivated at 90 °C, and at pH of 3.5 with 70 °C.