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

LÓPEZ, EMILSE CAMILA; EBERHARDT, AGUSTINA; MARINO, FERNANDA; MAMMARELLA, ENRIQUE J.; SIHUFE, GUILLERMO A.; MANZO, RICARDO M.

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 afterbovine whey enzymatic hydrolysis using food-grade Alcalase®. The aim of this reportwas to characterize relevant physicochemical properties of the bioactivepeptides and further evaluate their influence with degree of hydrolysis (DH%)through the employment of separative techniques. Results have shown that lowmolecular weight (LMW) peptides containing voluminous cationic and aromaticamino acid residues should be responsible forAHA whereas those related to AOA are associated to LMW peptides with anionicand both non-polar aliphatic and aromatics amino acid residues within their sequence.It was also seen that both bioactivities are highly correlated between eachother. Furthermore, an extensive DH% negatively influenced inradical-scavenging AOA but affected positively ACE-inhibition through theincrease of the number of bioactive fractions. Therefore, the use of Alcalase® for achieving bioactivefractions with antioxidant and antihypertensive activities is suitable formanufacturing special functional food formulations.