The role of molecular size in antioxidant activity of peptide fractions from Pacific hake (Merluccius productus) hydrolysates.

The antioxidative properties of Pacific hake hydrolysates and their peptidic fractions varying in molecular size were assessed. Hydrolysates produced by different proteases (Alcalase, bromelain, Flavourzyme, Protamex, Protease A"Amano"2, Protease N"Amano"K, Protin SD NY10, Umamizyme-K, Validase BNP-L, Validase FPexo) generally possessed good metal ion chelating (33-73% at 3mg/ml), DPPH radical scavenging (18-30% at 1mg/ml), ferric ion reducing power (abs700nm 0.36-0.86 at 3 mg/ml) and ABTS radical scavenging (47-85% at 0.067 mg/ml) activity, as well as a good capability to suppress lipid peroxidation in a linoleic acid model system. Peptide size (<1.4 kDa) was important for ABTS radical scavenging activity, whereas specific peptide composition (which depended on the particular protease used) was the governing factor for effective lipid peroxidation. Validase BNP-L was the most promising enzyme for producing Pacific hake hydrolysates with good antioxidative activity in various assays and similar effectiveness as the synthetic antioxidant BHT to inhibit lipid peroxidation.