In the literature, several processes have been described to obtain peroxidases. The purpose of this work was to obtain peroxidase from Copaifera langsdorffii leaves and characterize it partially using a factorial design of experiments and univaried tests, to confirm the results obtained by the factorial design of experiments. Peroxidase activity was measured using the guaiacol: hydrogen peroxide system. The isolated peroxidase presented 81.6% of horseradish peroxidase activity and was easy to obtain from leaves of an abundant tree distributed all over the country. Semi-purified peroxidase (COP) was precipitated with acetone 65% (v.v-1) of the crude extract, obtaining the acetone powder. The COP optimum reaction pH values were between 5.0-7.0 and the temperatures between 5 and 45 °C, with a maximum activity at pH 6.0 and 35 °C. The enzyme was stable in temperatures below 50 °C and pH from 4.5 to 9.0 for up to 24 hours. The peroxidase was inactivated after 4 hours at 80 °C and after 3 minutes at 96 °C. This enzyme can possibly be used as a diagnostic reagent, biosensor and for other analytical methods in several fields of Sciences.
copaiba; enzyme; vegetal extract
