Purification and identification of three novel antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) skin

Abstract

Skin protein from a bluefin leatherjacket (Navodon septentrionalis) processing by-product was hydrolyzed by trypsin, flavourzyme, neutrase, papain, alcalase, and pepsin, and protein hydrolysate (BSH) prepared using alcalase showed the highest DPPH, HO, and O2−· scavenging activities among all hydrolysates. Using ultrafiltration and consecutive chromatography, three novel peptides with strong antioxidant properties were purified from BSH, and their sequences were determined as Gly-Ser-Gly-Gly-Leu (GSGGL, BSP-A), Gly-Pro-Gly-Gly-Phe-Ile (GPGGFI, BSP-B), and Phe-Ile-Gly-Pro (FIGP, BSP-C) with molecular weights of 389.41, 546.63, and 432.52Da, respectively. BSP-C exhibited the highest scavenging activities on DPPH (EC50 0.118mg/ml), HO (EC50 0.073mg/ml), and O2−· (EC50 0.311mg/ml) among the three peptides. In addition, BSP-C could effectively inhibit autooxidation in a linoleic acid model system. The antioxidant activities of BSP-A, BSP-B, and BSP-C might be due to the small molecular sizes and the hydrophobic and/or aromatic amino acid residues in their amino acid sequences. The present results suggested that peptides purified from the skin protein hydrolysate of bluefin leatherjacket were excellent antioxidants and could be effectively used as food ingredients and additives, and pharmaceuticals.