Crude green bean (Phaseolus vulgaris L.) peroxidase (GBP) was extracted from fresh pods and partially purified. Following ammonium sulfate fractionation, dialysis, ion-exchange chromatography (DEAE-cellulose), and finally gel filtration, the specific activity obtained was 40.8 U mg⁻¹ corresponding to a purification fold of 32.9 and yield of 49.35%. An enzyme activity assay was optimized and maximal activity was reached in the dark, at pH 7.5 and 25 °C; kinetic studies based on substrate variation showed a Km value of 0.064 mM, with a Vmax of 4.91 U mL⁻¹. Anisidine removal by GBP was studied in batch reactor experiments. At H₂O₂ of 0.2 mM, and at enzyme activity of 3.1 U mL⁻¹, > 95% removal was achieved within 3 h for both p-anisidine (at pH = 4.5) and o-anisidine (at pH = 5.5). Pseudo-first-order kinetics demonstrated speedy degradation within the initial 30 minutes, exhibiting rate constants of 3.93 × 10⁻² min⁻¹ for p-anisidine and 3.54 × 10⁻² min⁻¹ for o-anisidine, with corresponding half-lives of 17.6 and 19.6 minutes. Subsequent to 180 minutes, the rates diminished and the half-lives extended to 26.3 and 36.3 minutes. A 95 Eco-Scale score indicates a highly sustainable procedure utilizing plant-based peroxidase under moderate, a solvent-free for anisidine removal.