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

Fatima Abdelhameed Hussein,Shehu Muhammad Auwal,Nazamid Saari,Mohammad Zarei,Azizah Abdul Hamid,Wan Zunairah Wan Ibadullah,Shyan Yea Chay

doi:10.3390/foods9010064

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.

Highlights

Hypertension is considered a key risk factor in cardiovascular-related diseases including stroke, peripheral and coronary heart diseases
This study represents a pioneer work on the optimization of whey protein concentrate hydrolysis studytorepresents a pioneer with work dual on the optimization of inhibition whey protein concentrate usingThis
The optimized hydrolysis parameters were determined as follow: Temperature = 58.2and antioxidant activities)

Summary

Introduction

Hypertension is considered a key risk factor in cardiovascular-related diseases including stroke, peripheral and coronary heart diseases. Angiotensin-I converting enzyme (ACE) has been identified as the key enzyme which increases blood pressure in human body. It cleaves the inactive decapeptide, angiotensin-I, to an octapeptide, angiotensin-II, which acts as a potent vasoconstrictor, Foods 2020, 9, 64; doi:10.3390/foods9010064 www.mdpi.com/journal/foods. The dual action of ACE results in a rise in the blood pressure. Inhibition of ACE by reducing angiotensin II generation and increasing bradykinin generation is necessary to control high blood pressure. The increasing health awareness drives consumers to look for natural alternatives that are safer with minimal side effects compared to synthetic blood pressure-controlling drugs. Positive results have been garnered with the discovery of bioactive peptides derived from various food proteins

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Conclusion