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

LÓPEZ EC; EBERHARDT A; MARINO F; MAMMARELLA EJ; SIHUFE GA; MANZO RM

INTERNATIONAL JOURNAL OF DAIRY TECHNOLOGY

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 2022 vol. 75 p. 538 - 552

1364-727X

Antioxidant (AOA) and ACE-inhibition (AHA) activities were obtained by bovine wheyenzymatic hydrolysis using food-grade Alcalase®. The aim of this report was tocharacterize relevant physicochemical properties of the bioactive peptides and evaluatethem with respect to degree of hydrolysis (DH%) using separation techniques. Theresults suggest that low molecular weight (LMW) peptides containing voluminouscationic and aromatic amino acid residues would be responsible for AHA, whereas thoserelated to AOA would possess anionic and both non-polar aliphatic and aromatic aminoacid residues within their sequence. Furthermore, an extensive DH% negativelyinfluenced radical-scavenging AOA but positively affected ACE-inhibition.