Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study

Abstract

Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functional values due to the high content of branched-chain amino acid. This study was designed to establish the optimum conditions for Alcalase-hydrolysis of WPC to produce protein hydrolysates with dual biofunctionalities of angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities via response surface methodology (RSM). The results showed that the optimum conditions were achieved at temperature = 58.2 °C, E/S ratio = 2.5%, pH = 7.5 and hydrolysis time = 361.8 min in order to obtain the maximum DH (89.2%), ACE-inhibition (98.4%), DPPH• radical scavenging activity (50.1%) and ferrous ion chelation (73.1%). The well-fitted experimental data to predicted data further validates the regression model adequacy. Current study demonstrates the potential of WPC to generate bifunctional hydrolysates with ACE inhibition and antioxidant activity. This finding fosters the use of WPC hydrolysate as a novel, natural ingredient for the development of functional food products.

Hydrolysates from ultrafiltrated double‐cream cheese whey: Enzymatic hydrolysis, antioxidant, and ACE‐inhibitory activities and peptide characterization

“…There were no statistically significant differences in ACE-inhibitory activity between the ALC (87.93 ± 3.57%), CHY (92.10 ± 2.64%), and FLA (82.08 ± 6.06%) hydrolysates. As the results obtained in this work, previous studies have obtained whey protein hydrolysates with antioxidant and ACE-inhibitory properties (Corrêa et al, 2014;Hussein et al, 2020;Martín-del-Campo et al, 2019;O'Keeffe et al, 2017). As antioxidant activity, ACEinhibitory capacity depends on enzyme specificity that can affect the composition of each hydrolysates in terms of peptide and their amino acid composition.…”

“…A longer time of hydrolysis and higher E:S ratio could cause the degradation chelating peptides previously TA B L E 6 Experimental and predicted values for response variables using optimal conditions for enzymatic hydrolysis of WPC with alcalase (ALC), chymotrypsin (CHY), and flavourzyme (FLA) produced. Hussein et al (2020) reported a negative relation of the E:S ratio on iron-chelating activity. By contrast, chelating ability increased as hydrolysis progressed until a maximum value and then decreased with longer times of hydrolysis.…”

“…Increasing E:S ratio and a long time of hydrolysis could cause greater degradation and impact on the functionality of peptides produced. Researches have been previously performed to establish the optimum hydrolysis conditions for the production of biologically active hydrolysates with a maximum activity (Athira et al, 2015;Ballatore et al, 2020;Hussein et al, 2020;Martín-del-Campo et al, 2019).…”

“…Whey protein hydrolysates can exert antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities due to the release of bioactive peptides after hydrolytic process (Corrêa et al, 2014;Hussein et al, 2020;Martín-del-Campo et al, 2019;O'Keeffe et al, 2017). Antioxidant peptides can reduce oxidative stress by donating of hydrogens or electrons to radical species or by chelating of metal ions that promote reactions for generation of radicals (Power et al, 2013;Sarmadi & Ismail, 2010).…”

CHEESE and WHEY: The Outcome of Milk Curdling

“…Hussein et al [ 11 ] investigated the hydrolysis of WPC by alcalase by means of response surface methodology. The aim of the study was to determine the appropriate conditions for the production of protein hydrolysates with dual biofunctionalities, that is, angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities.…”