Identification and Characterization of Novel ACE Inhibitory and Antioxidant Peptides from Sardina pilchardus Hydrolysate.

ABSTRACT: Sardina pilchardus is a valuable source of bioactive peptides with potential applications in functional foods. In this study, we investigated the angiotensin-converting enzyme (ACE) inhibitory activity of Sardina pilchardus protein hydrolysate (SPH) produced using dispase and alkaline protease. Our results showed that the low molecular mass fractions (<3 kDa) obtained through ultrafiltration exhibited more effective ACE inhibition, as indicated by screening with ACE inhibitory activity. We further identified the low molecular mass fractions (<3 kDa) using an LC-MS/MS rapid screening strategy. A total of 37 peptides with potential ACE inhibitory activity were identified based on high biological activity scores, non-toxicity, good solubility, and novelty. Molecular docking was used to

SUBMITTER: Shao M 

PROVIDER: S-EPMC10252845 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature