To produce bioactive peptides from collagen was hydrolyzed from Striped Catfish (Pangasius pangasius) using protease (papain enzyme) and the peptides were evaluated for antioxidant activity. The degree of hydrolysis (DH), DPPH radical-scavenging activity, and reducing power of the peptides were investigated. Papain enzyme was further used to produce collagen peptides with different time of hydrolysis. Within 160 min of hydrolysis, the maximum cleavage of peptide bonds from fish skin and fish bone occurred were found with DH 4.57% and 1.75%, respectively. Collagen peptide from fish skin and fish bone exhibited the highest antioxidant activity after 160 min incubation. DPPH radical scavenging activity of collagen hydrolysate from fish bone was higher (71.55%) than that of these hydrolysed collagen from fish skin (63.06%). However reducing power activity of the collagen peptide hydrolysed from fish skin (0.817) was higher than that of the collagen peptide hydrolysed from fish bone (0.788). Therefore, papain enzyme could be used to produce the collagen peptides possessing antioxidative activities.