Winged bean seeds is a rich source of proteins with amino acid composition comparable to soybean. In this study, winged bean seed was proteolyzed using papain enzyme under optimum pH and temperature conditions. The crude proteolysate was determined for in vitro ACE inhibitory and antioxidative activities. The ACE inhibitory, DPPH• radical scavenging and metal ion chelating activities were found to be 87.2%, 65.0% and 65.7% respectively. The proteolysate was further characterized using a two-step purification, which consisted of reverse phase-high performance liquid chromatography (RP-HPLC) and isoelectric focusing. Fractions showing ACE inhibitory activity between 50.1 and 87.2% with reasonable peptide content were subjected to peptide sequencing. Three multifunctional bioactive peptides were successfully identified, namely YPNQKV, FDIRA and VSARDLVG. The physical and biochemical properties of the peptides were compared.