Abstract
Tryptic WPHs with considerable residual whey protein content intact were developed from two sheep/goat WPCs (65% and 80% protein) without pH control. Pasteurization was used to avoid denaturation. Changes in non-protein nitrogen (DH_TCASN), free amino groups (DH_TNBS), and major whey proteins were used to investigate the degree and extent of hydrolysis. Antihypertensive potential (ACE-IA), radical scavenging (DPPH-RSA), and iron chelation (Fe-CA) were assessed. No statistically significant changes in pH (5.84−6.29) were observed during hydrolysis and storage. At the start of hydrolysis, DH_TCASN was ≅11% for both substrates whereas DH_TNBS was >10% and >5% for WP65 and WP80, respectively. After one-hour hydrolysis, DH_TCASN was ≅17% for both substrates and DH_TNBS was ≅15% and ≅11% for WP65 and WP80, respectively. The β-lactoglobulin, α-lactalbumin, and caseinomacropeptide of WP65 were hydrolyzed by 14 ± 1.3%, 73.9 ± 2.6% and 37 ± 2.6%. The respective values for WP80 were 14.9 ± 1.7%, 79.9 ± 1%, and 32.7 ± 4.8%. ACE-IA of the hydrolysates of both substrates was much higher (>80%) than that of controls (<10%). Hydrolysis, substrate type, and storage did not affect the DPPH-RSA (45−54%). Fe-CA of the WP65 and WP80 hydrolysates were ≅40% and ≅20%, respectively; a similar outcome was found in the respective controls. Refrigerated storage for 17 h did not affect the degree of hydrolysis and biofunctional activities.