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.
Zheng et al. (Wed,) studied this question.