Antioxidant activity of hydrolysates and peptide fractions derived from porcine hemoglobin.

Porcine hemoglobin hydrolysate (PHH) was prepared with 6 different proteases (flavourzyme, papain, A.S.1398, alcalase, pepsin and trypsin). There was no correlation between extent of hydrolysis and antioxidant activity (p > 0.05). The peptic hydrolysate prepared at 60 min possessed the strongest antioxidant potential (67.0 ± 1.84%) among different hydrolysates, which was fractionated into 4 major types by ultrafiltration membranes with different molecular weight cut-off (MWCO), PHH-I (Mw > 10 kDa), PHH-II (Mw = 5-10 kDa), PHH-III (Mw = 3-5 kDa) and PHH-IV (Mw < 3 kDa). PHH-IV possessed higher inhibitory effects of lipid peroxidation and scavenging effects on superoxide radical compared with larger MW fractions. Four fractions possessed the scavenging effects on 1, 1-diphenyl-2-picrylhy-drazyl (DPPH) and hydroxyl radicals in the order PHH-IV > PHH-I > PHH-III > PHH-II. MW of the 2 major peptide fractions from PHH-IV was located at 2476 Da (F1) and 1042 Da (F2), respectively. PHH-IV could be utilized to develop physiologically functional foods or therapy drugs.