Lipid-Induced Oxidative Modifications Decrease the Bioactivities of Collagen Hydrolysates from Fish Skin: The Underlying Mechanism Based on the Proteomic Strategy.

Collagen peptides exhibit various bioactivities, including antioxidation and ACE inhibition. However, the bioactivities of collagen peptides decrease gradually due to oxidation deterioration during storage, and this degradation of bioactive peptides is rarely studied. In this study, the oxidative levels and the bioactivities of collagen peptides were investigated during an oxidative-induced storage accelerated by lipids. The results suggested that the oxidation of collagen peptides was divided into three stages. At the early stage, the carbonyl content of collagen peptides increased rapidly (from 2.32 to 3.72 μmol/g peptide), showing a close correlation with their bioactivities (for antioxidation, r = -0.947; for ACE inhibition, r = -0.911). The oxidation level in the middle stage continued but was stable, and the bioactivities decreased. At the later stage, the Schiff base and dityrosine content increased significantly and showed a strong correlation with the bioactivities (antioxidation, r = -0.820, -0.801; ACE inhibition, r = -0.779, -0.865). The amino acid and proteomic analyses showed that Met, Lys, and Arg were susceptible to oxidation and revealed their oxidative modification types. This study provided an insight into the dynamic oxidative modifications of collagen peptides, which were shown to correlate well with the change in bioactivities.