Contenido production of bioactive peptides from bovine colostrum whey using enzymatic hydrolysis

Bovine colostrum is an essential source of nutritional and immunological factors that are vital for the early development and protection of the newborn. The aim of this study was to evaluate the antioxidant, mineral-binding (iron and calcium), and angiotensin-converting enzyme (ACE) inhibitory properties of the peptides generated through the enzymatic hydrolysis of bovine colostrum whey proteins. Whey proteins were hydrolyzed with pepsin at two pH values (1.3 and 2) in a sequential hydrolysis system with pancreatin at pH 7.5. Three di_erent molecular weight fractions (<10, 10 to 30 and >30 kDa) were obtained by ultrafiltration. The antioxidant and calcium-binding activities increased with the degree of hydrolysis of the proteins and the highest values were obtained in the fractions with less than 10 kDa.. The fractions with molecular weights higher than 30 kDa had the best iron-binding capacity. A high positive correlation (R=0.9669) was obtained between the degree of hydrolysis and the ACE inhibitory activity. These results indicate that the hydrolysis of bovine colostrum whey proteins with pepsin and pancreatin generated peptides with enhanced antioxidant, mineral-binding, and ACE inhibitory capacities.