Identification New Angiotansin-1 Converting Enzyme Inhibitory Peptide from Ostrich Egg White Protein Hydrolysate

Abstract

Background: Due to the side effects of anti-hypertension drugs, extracting bioactive peptides from natural sources is of great importance. The mail goal of this study was identifying a peptide for enzyme hydrolytic of ostrich egg white protein hydrolysate (OEWPH) and investigating its inhibitory effects on angiotansin-1 converting enzyme (ACE). Methods: The ostrich egg white protein hydrolysate was prepared using pepsin and pancreatin and then fractionated using evaluated reveres-phase high-performance liquid chromatography (RP-HPLC). Tandem mass analysis of the purified peptide was used to reveal peptide sequence. ACE inhibitory effect and kinetic parameters of the reaction in the presence of the peptide was evaluated. Molecular docking was used to determine the interaction parameters of ACE-peptide comp. Findings: Peptide sequencing of the selected peptide revealed a DAESLSRLLG (MW = 1060/18 Da) and named DG-10. The DG-10 peptide showed a potent inhibitory effect on ACE with the half maximal inhibitory concentration (IC50) value of 0.133 mg/ml. Lineweaver-Burk plot exhibited a non-competitive behavior in the presence of the DG-10 peptide. Molecular interactions and energy binding of the peptide with ACE were investigated via molecular docking. Conclusion: The DG-10 peptide isolated from ostrich egg white protein hydrolysate displayed a potent inhibitory effect on ACE.

Keywords

• Angiotansin-1 converting enzyme (ACE)
• Ostrich egg white protein hydrolysate (OEWPH)
• Peptide