A new hydrolysis method for producing peptides from porcine hemoglobin has been developed. Current processes are based on the use of expensive enzymes or high hydrostatic pressures. In the present study, a cheap and effective process has been assayed to produce peptides from purified porcine hemoglobin. A solution of purified hemoglobin is heated at different temperatures and pressurized at 4 MPa while a stream of nitrogen is injected into the reactor. A total of 82% of initial hemoglobin was transformed into peptides presenting an average size of 3.2 kDa. Some preferential hydrolyzed bonds have been detected. The peptide size distribution was evaluated at different times and temperatures. It has been demonstrated that this technique produces large amounts of peptides possessing good antioxidant properties. Furthermore, functional properties are conserved, and a desirable decrease in color (80%) is achieved.