Characterization, surface properties and biological activities of protein hydrolysates obtained from hake (Merluccius merluccius) heads

Abstract

The present study reports the surface and antioxidant properties, as well as the angiotensin-I converting enzyme (ACE) inhibitory activity of protein hydrolysates (HHPHs) from European hake (Merluccius merluccius) heads and obtained with Savinase®. Hake heads protein hydrolysates contained high protein content between 84.75 and 87.92% and a high percentage of essential amino acids. They have a high nutritional value and could be used as supplement in poorly balanced dietary proteins. All protein hydrolysates possessed interesting surface properties, which were governed by their concentrations Hake heads protein hydrolysates displayed a high ACE inhibitory activity. The IC50 values recorded for the ACE inhibitory activity of all HHPHs varied between 0.24 and 1.4 mg/mL. Therefore, HHPHs can be used as a promising source of functional peptides with good surface and biological properties.