As a highly phosphorylated protein, phosvitin shows a powerful antioxidant and metal-binding activity. However, its extraordinary resistance to protease activities limits the possibility of using phosvitin as a source for the production of functional peptides. The objectives of this study were to test the possibilities of using alkaline or acid hydrolysis to produce small peptides from phosvitin and to investigate the functional properties of the resulting peptides. Phosvitin was dissolved in various concentrations of NaOH (0.025N-0.3N) or HCl (0.05N–6N) and incubated in a shaker water bath (37◦C for NaOH and 60◦CforHCl) for 1-6 h. After incubation, the degree of hydrolysis, and the functional properties of the hydrolysateswere determined.Phosvitin showed higherresistanceto acid hydrolysis than alkaline hydrolysis.Incubation of phosvitinin 0.075 N NaOHsolution at 37◦Cfor 1h and 2N HCl at 60◦Cfor 6 h partially hydrolyzedphosvitin, but 0.1 N NaOH at 37◦C for 3 h or 3N HCl at 60◦Cfor 6 h incubation was needed forthe complete hydrolysis of phosvitin. Increasing degree of hydrolysis inphosvitin either by HCl or NaOH negatively affected their antioxidant and Fe-chelating capacities.Cu+2-chelating activity, however, increased significantly by hydrolyzingphosvitinwith 0.1N NaOH or2N HCl. The alkalinehydrolysates(0.05 N and 0.1NNaOH)and acid hydrolysates(2 N HCl) significantly increased the solubility of Ca+2 in sodium phosphate buffer (pH 6.8) compared to the control.