A 3% suspension of heat-stabilized defatted rice bran was treated with papain, followed by inactivating the enzyme by heat, and centrifuged. The supernatant was subjected to ultrafiltration, and fractions with various molecular sizes, F1 (>30 kDa), F2 (10-30 kDa), F3 (5-10 kDa), F4 (3-5 kDa), and F5 (3 kDa<), were freeze-dried, and evaluated for antimutagenicity by Ames test using Salmonella typhimurium TA 100 against phenazine methosulfate. The F3 fraction containing highest antimutagenicity from ultrafiltration was separated into 6 fractions by DEAE-Sephadex A-25 ion-exchange column chromatography (F3-1-F3-6). Each fractions having protein contents were pooled, dialyzed, freeze dried, and evaluated for antimutagenicity. Among the six fractions, the F3-1, F3-2, and F3-6 fractions showed antimutagenicity, which were 80.2, 53.4, and 58.6% at concentration of $100;{mu}g/plate$, respectively. These F3-1, F3-2, and F3-6 fractions were subjected to Sephadex G-50 gel filtration column chromatography for further purification. Among the purified fractions, the F3-1-1, F3-2-2, and F3-6-1 fractions showed antimutagenicity of 84.5, 58.6, and 69.8% at concentration of $100;{mu}g/plate$, respectively. It is thought that these peptides can find application for nutraceutical and pharmaceutical products.