LAUSR

Abstract Smooth-hound viscera proteins were enzymatically hydrolyzed, using Esperase ® , and the resulting hydrolysate was fractionated by ultrafiltration through four membranes with decreasing molecular weight (MW) cut-offs. Five fractions were obtained, FI (>50 kDa), FII (5–50 kDa), FIII (3–5 kDa), FIV (1–3 kDa) and FV ( 50 of 101.61 and 92.75 μg/ml. Moreover, they showed interesting blood pressure-lowering results in hypertensive rats after 4 h of oral administration (200 mg/kg body weight). Both fractions were then fractionated by RP-HPLC and eluted peptides were analyzed by nanoLC–MS/MS. The molecular docking study of IAGPPGSAGPAG, VVPFEGAV, PLPKRE, and PTVPKRPSPT showed that peptides were able to bind ACE through a complex of hydrophobic, hydrogen bonds, van der Waals and electrostatic interactions, as well as to interact with the three residues coordinating with Zn 2+ . Hence, this study provides a useful bioprocess for the use of smooth-hound byproducts as a natural source of hypotensive agents.