Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study.
ACE inhibition
antioxidant activity
hydrolysis
response surface methodology
whey protein concentrate
Journal
Foods (Basel, Switzerland)
ISSN: 2304-8158
Titre abrégé: Foods
Pays: Switzerland
ID NLM: 101670569
Informations de publication
Date de publication:
08 Jan 2020
08 Jan 2020
Historique:
received:
18
09
2019
revised:
07
10
2019
accepted:
09
10
2019
entrez:
16
1
2020
pubmed:
16
1
2020
medline:
16
1
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31936191
pii: foods9010064
doi: 10.3390/foods9010064
pmc: PMC7022510
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Universiti Putra Malaysia
ID : GP-IPS/2018/9643400
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