Separation and identification of ACE inhibitory peptides from lizard fish proteins hydrolysates by metal affinity-immobilized magnetic liposome.

Abstract Purification of peptides responsible for angiotensin I-converting enzyme (ACE) inhibitory activity from highly complex protein hydrolysates is difficult. Affinity chromatography is a powerful method for purification of peptides. In this study, a metal affinity-immobilized magnetic liposome (MA-IML) was prepared using lipid, N-hexadecyl iminodiacetic acid (HIDA) and magnetic nanoparticles made of FeCl3·6H2O and FeCl2·4H2O as main materials. MA-IML was used to adsorb ACE inhibitory peptides from lizard fish proteins hydrolysates. The optimal pH of adsorption solution was 8.5. The peptide sample adsorbed by MA-IML was separated by reverse phase-high performance liquid chromatography (RP-HPLC). Upon amino acid sequence analysis and verification, an ACE inhibitory peptide with IC50 value of 108 μM was identified to be VYP. Molecular docking results indicated that VYP bound to ACE via multiple binding sites. The present study demonstrated that MA-IML might be a useful tool for separating ACE inhibitory peptides from proteins hydrolysates.