Systematic Analysis of Peptide Mapping and Structural and Functional Identification of Protein Hydrolysates Derived from Six Kinds of Livestock/Poultry Meats Based on Peptidomics.

The purpose of this study was to investigate the effects of cooking treatment on the structural properties and potential bioactive peptide release of six meat protein hydrolysates using a cooking-assisted enzymatic hydrolysis model. FTIR showed that cooking reduced the contents of α-helix and β-sheet structures and promoted the formation of β-turn and random helix structures. The enzymatic hydrolysates demonstrated evident antioxidant activity in vitro, both before and after cooking, which was affected by species differences. LC-MS/MS combined with bioinformatics analysis indicated that cooking affected the release of peptides from livestock/poultry meat hydrolysates. A total of 209 heat-stable peptides were identified across six types of meat, of which 60 specific peptides were predicted to exhibit potential inhibitory activity against angiotensin converting enzyme (ACE) inhibitory activity, dipeptidyl peptidase-IV (DPP-IV) inhibitory activity, α-glucosidase inhibition, and antioxidant activity, respectively. This study provides new insights for the efficient preparation of bioactive peptides derived from livestock/poultry meat proteins.