“…In this regard, it has been observed that the presence of hydrophobic residues such as Trp, Tyr, Pro, or Phe at the C-terminal end, as well as aliphatic amino acids such as Gly, Val, Leu, and Ile at the N-terminal position, leads to higher ACE inhibitions [ 130 , 131 , 132 ]. Specifically, ACEi peptides have been identified in hydrolysates from feet, blood corpuscle, legs with claws, bone, viscera, or a mixture of combs and wattles, showing IC 50 values lower than 100 µM in many cases [ 22 , 85 , 97 , 98 , 133 ]. The protein source of these peptides depends on the used byproduct.…”