Physicochemical characterisation of ACE-inhibitory and antioxidant peptides from Alcalase® whey protein hydrolysates using fractionation strategies

Abstract

Antioxidant activity (AOA) and ACE-inhibitory activity (AHA) were obtained by enzymatic hydrolysis of bovine whey using food-grade Alcalase®. The aim of this report was to characterise relevant physicochemical properties of the bioactive peptides and evaluate them with respect to the degree of hydrolysis (DH) using separation techniques. The results suggest that low molecular weight peptides containing high concentrations of cationic and aromatic amino acid residues were responsible for AHA, whereas those related to AOA would possess anionic and both nonpolar aliphatic and aromatic amino acid residues within their sequence. Furthermore, an extensive DH negatively influenced radical scavenging AOA but positively affected angiotensin-converting enzyme (ACE) inhibition.