“…From a structure activity point of view of ACE inhibitors, studies have demonstrated that the ACE inhibitory activity of a peptide depends on the presence of specific residues at N and C-termini [8]. The presence of hydrophobic residues, particularly leucine, valine, isoleucine, and glycine, at the N-terminus of a peptide, produced higher ACE inhibitory activity, while aromatic amino acids, such as phenylalanine, proline, tryptophan, and tyrosine, are preferred at the C-terminus [55]. Additionally, the presence of positively charged residues, specifically arginine and lysine, near the C-terminus were also considered to be essential for the ACE inhibitory potential of peptides [56].…”