The hydrolysis of egg-white protein precipitate (EWPP) with trypsin, chymotrypsin, and elastase was studied. The peptides obtained were determined for their antioxidative properties. Chymotrypsin caused the most extensive degradation of EWPP. The degrees of hydrolysis (DHs) of the one-hour hydrolysates were 77.6%, 55.8%, and 43.3% for chymotrypsin, trypsin, and elastase, respectively. Only small peptides with molecular weights of 5-10 kDa (74.2%) and <3 kDa (25.6%) were found in the one-hour hydrolysate with chymotrypsin, whereas products with higher molecular weights (78 kDa, 37 kDa, 34 kDa, and 78 kDa, respectively) as well as the small peptides were produced with elastase and trypsin. In the ensuing hours the rate of hydrolysis slowed and the DHs of the final hydrolysates were 95.8%, 95.3%, and 79.9% for trypsin, chymotrypsin, and elastase. The RP-HPLC profiles of the final hydrolysates showed differences in the hydrophobicity of the generated peptides. All hydrolysates exhibited weak scavenging activity of DPPH free radicals.