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.