Many food protein hydrolysates have been shown to have antioxidant activities, and recent research focuses on low molecular peptides produced during hydrolysis of food protein. Korean rice wine contains about 60-70% of protein at dry base and originates from raw materials. It has been suggested that the protein is transformed into low molecular weight peptides, and have antioxidant activity during fermentation. The objectives of this study were to evaluate the antioxidant activity of the pre-purified and purified peptides found in Korean rice wine and to identify the responsible peptides. The wine extract of Samhaeju, a traditional Korean rice wine made by low temperature fermentation, was evaporated at $35^{circ}C$. The two methods employed in the evaluation of antioxidant activity were the DPPH radical scavenging method and the beta-carotene bleaching test. The pre-purified samples showed 808 AAC (Antioxidant Activity Coefficient) and 56.5% AOA (Antioxidant Activity), which were higher than $alpha$-tocopherol (572 AAC and 78% AOA). The rice wine extract was separated by reversed-phase HPLC. The protective effect of the four most antioxidant active fractions were tested for t-butyl hydroperoxide induced oxidation of healthy human erythrocytes and the byproduct was determined by malondialdehyde formation. Fraction No.5 showed 35% lower MDA concentration as compared to the control. The peptides were further purified using consecutive chromatographic methods and 4 antioxidant peptides were isolated. The amino acid sequences of the peptides were identified as Ile-His-His, Val- Val-His(Asn), Leu-Val-Pro, and Leu(Val)-Lys-Arg-Pro. The AAC value of the synthetic form of the identified peptides was the highest for Ile-His-His.