Saccharomyces cerevisiae was obtained from palm wine and used for the extraction of peroxidase. Peroxidase isolated from Saccharomyces cerevisiae was partially purified and characterized. A twelve-day pilot study was carried out which gave the highest activity on day eight. The crude enzyme-specific activity -0.751 U/ mg with 70% ammonium sulfate precipitation of peroxidase was achieved. Peroxidase was partially purified with ammonium sulfate precipitation, following gel filtration on Sephadex G-100. Two peaks connoted as fractions (A & B) on the elution profile of the gel filtration were obtained. The optimum operational conditions for peroxidase -substrate reactions were evaluated. A combined purification fold for both fractions yielded 0.657 with specific activity -0.494 U/ mg. A purification fold of 2.470 with specific activity -1.855 U/mg was obtained for fraction A, while 2.269 fold with specific activity -1.704 U/mg was for fraction B. The optimum pH and temperature were 6.5 and 30 °C for fraction A and 6.0 and 40 °C for fraction B. The peroxidase activity was stable at a pH range of 5.5-7.0 and below 40 °C. The Michaelis-Menten constant (K m ) for o-dianisidine and hydrogen peroxide were 0.2 mM, 0.1111 mM, and 0.0833 mM, 0.1428 mM for fractions A and B. The maximum velocity (V max ) for o-dianisidine and hydrogen peroxide were 10 U/min, 7.1428 U/min, and 8.333 U/min, 9.0909 U/min for fraction A and B. considering these characteristics of peroxidase from Saccharomyces cerevisiae, it helps to understand how yeast cells operate during fermentation.