This study compared the effectiveness of alkaline protease, neutral protease, trypsin, and papain in hydrolyzing oyster proteins and evaluated the antioxidant activities of the resulting hydrolysates. Alkaline protease achieved the highest degree of hydrolysis (30.96%) and the highest proportion of peptides ≤1 kDa (64.23%). Papain showed the lowest hydrolysis degree (18.29%). After separation by Sephadex G-15 gel filtration chromatography, the resulting low-molecular-weight peptide fractions (≤1 kDa) from each hydrolysate exhibited higher in vitro antioxidant activity than the higher-molecular-weight fractions (>1 kDa). Notably, trypsin and papain-derived low-molecular-weight fractions (OPP-T2 and OPP-P2) demonstrated stronger DPPH radical scavenging and inhibition of linoleic acid autoxidation than those from alkaline and neutral proteases. Cell experiments revealed that all low-molecular-weight fractions effectively alleviated H2O2-induced oxidative damage in LO2 cells. OPP-T2 and OPP-P2 exhibited significantly stronger protection of cell membrane integrity and enhancement of superoxide dismutase (SOD) activity than OPP-A2 and OPP-N2 (p < 0.05). OPP-T2 also showed the most pronounced increase in glutathione peroxidase (GSH-Px) activity (p < 0.05). These findings demonstrate that protease selection critically influences hydrolysis efficiency and antioxidant activity, with molecular weight being a key determinant of peptide antioxidant capacity. This work provides a reference for the development and application of oyster peptides.
Huang et al. (Mon,) studied this question.