Neprilysin (NEP) and Angiotensin Converting Enzyme-I (ACE-I) inhibitory dipeptides from chicken carcass hydrolysates

Abstract

Chicken carcasses constitute a meat co-product rich in proteins but with low economical value. In this sense, the use of enzymatic hydrolysis for the production of bioactive peptides gives an extra economical and functional value to this product. The aim of this study was to identify di- and tripeptides obtained from the hydrolysis of chicken carcass using two different endoproteases, Alcalase 4.0 L and Protamex, at different times of incubation. Hydrolysate A1 (Alcalase-1h) showed the highest neprilysin and ACE-I inhibitory activity with inhibition rates of 91.45 and 86.41% at 10 mg/mL, respectively. The hydrolysate was fractionated with RP-HPLC, and fractions 2–3, and 11–14 showed the highest neprilysin inhibition values. In these fractions, a total of 11576 peptide sequences were identified by liquid chromatography and mass spectrometry in tandem (LC-MS/MS). The dipeptide VV showed the highest neprilysin inhibitory activity with an inhibition rate of 75.24% at 1 mmol/mL, whereas dipeptides RP, AR and GP were responsible for 87.66, 66.37 and 66.18% ACE-inhibitory activity at 1 mmol/mL, respectively. This study confirms the potential of peptides obtained from the hydrolysis of chicken carcasses be used as neprilysin and ACE inhibitors and, therefore, for the prevention and control of cardiovascular diseases.