Identification and Characterization of Novel ACE Inhibitory and Antioxidant Peptides from

Area of Science:

• Marine Biotechnology
• Food Science
• Biochemistry

Background:

• Sardina pilchardus is a rich source of bioactive peptides.
• Angiotensin-converting enzyme (ACE) inhibitors are crucial for managing hypertension.
• Functional foods offer health benefits beyond basic nutrition.

Purpose of the Study:

• To investigate the ACE inhibitory and antioxidant activities of Sardina pilchardus protein hydrolysate (SPH).
• To identify novel ACE inhibitory peptides from SPH using advanced screening techniques.
• To explore the potential of these peptides for functional food applications.

Main Methods:

• Production of SPH using dispase and alkaline protease.
• Ultrafiltration to isolate low molecular mass fractions (<3 kDa).
• LC-MS/MS for peptide identification and molecular docking for activity prediction.
• In vitro synthesis and validation of identified peptides for ACE inhibition and antioxidant activity.

Main Results:

• Low molecular mass fractions (<3 kDa) of SPH showed significant ACE inhibitory activity.
• 37 potential ACE inhibitory peptides were identified, with 11 showing high docking scores.
• Six synthesized peptides (FIGR, FILR, FQRL, FRAL, KFL, KLF) demonstrated in vitro ACE inhibitory and antioxidant activities.
• These peptides competitively inhibited ACE by binding to its active pockets and possess antioxidant properties.

Conclusions:

• Sardina pilchardus is a promising source for natural ACE inhibitors and antioxidants.
• LC-MS/MS combined with molecular docking is an effective strategy for discovering bioactive peptides.
• Identified peptides hold potential for the development of novel functional foods for cardiovascular health.