There is currently considerable interest on the use of animal, plant, and fungal sources in the production of bioactive peptides, as evidenced by the substantial body of research on the topic. Such sources provide cheap and environmentally friendly aterial as it often includes waste and by-products. Enzymatic hydrolysis is considered an efficient method of obtaining peptides capable of antioxidant activity. Those properties have been proven in terms of radical-scavenging capacity using the DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonic acid)), hydroxyl and superoxide radical methods. Additionally, the reducing power, ferrous ion-chelating (FIC), ferric reducing antioxidant power (FRAP), and the ability of the protein hydrolysates to inhibit lipid peroxidation have also been explored. The results collected in this review clearly indicate that the substrate properties, as well as the conditions under which the hydrolysis reaction is carried out, affect the final antioxidant potential of the obtained peptides. This is mainly due to the structural properties of the obtained compounds such as size or amino acid sequences.