To add value, cereal grains such as sorghum are often malted. To date, not many studies have been performed to assess how such malting affects the activities of purified peroxidases from sorghum. Therefore, peroxidases were purified from malted versions of improved sorghum varieties SK5912 and KSV8. The purification was performed using (NH4)2SO4 precipitation and ion exchange chromatography and properties were compared. Whereas malted SK5912 peroxidase (MSSP) had its Soret peak at 403 nm, that of KSV8 (MKSP) peaked at 402 nm. Their extinction coefficients were also slightly different (ε 403 = 128 mm−1 cm−1 for MSSP and ε 402 = 130 mm−1 cm−1 for MKSP); while their mass spectrometry determined molecular weights were the same, 35.325 kDa. Electron spin resonance (EPR) spectra of both enzymes show high spin ferric heme signals (g = 6.00, 4.98 and 2.00) similar to those found in other peroxidases. The optimum pH for the activity of both peroxidases with guaiacol was pH 5, while their optimum temperature was 40 °C. Steady state kinetics, reduction potential, binding constant, metal affinities etc., differed among the peroxidases. Malting greatly increased the activities of the peroxidases beyond those from unmalted grains and that perhaps explains why calcium and other metals affected their activities only moderately.