Pigeon pea penta- and hexapeptides with antioxidant properties also inhibit renin and angiotensin-I-converting enzyme activities
Corresponding Author
Aderonke I. Olagunju
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Correspondence
Aderonke I. Olagunju, Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Email: [email protected]
Search for more papers by this authorAdeola M. Alashi
Research & Development, Custom Agricultural Intelligence Inc., Regina, Saskatchewan, Canada
Search for more papers by this authorOlufunmilayo S. Omoba
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Search for more papers by this authorVictor N. Enujiugha
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Search for more papers by this authorRotimi E. Aluko
Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba, Canada
Search for more papers by this authorCorresponding Author
Aderonke I. Olagunju
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Correspondence
Aderonke I. Olagunju, Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Email: [email protected]
Search for more papers by this authorAdeola M. Alashi
Research & Development, Custom Agricultural Intelligence Inc., Regina, Saskatchewan, Canada
Search for more papers by this authorOlufunmilayo S. Omoba
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Search for more papers by this authorVictor N. Enujiugha
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
Search for more papers by this authorRotimi E. Aluko
Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba, Canada
Search for more papers by this author[corrections added on 29 October, 2022 after first online publication: 4th author's name was corrected]
Abstract
Pigeon pea protein was sequentially digested with pepsin followed by pancreatin and the hydrolysate separated into 18 fractions using reversed-phase high-performance liquid chromatography. Fractions were analyzed for in vitro antioxidant properties (radical scavenging, metal chelation, and ferric iron reducing ability) in addition to inhibition of renin and angiotensin-converting enzyme (ACE). The most active fractions were analyzed by mass spectroscopy followed by identification of 10 peptide sequences (7 pentapeptides and 3 hexapeptides). All the peptides showed a wide range of multifunctional activity by scavenging hydroxyl (31.9–66.8%) and superoxide (25.6–100.0%) radicals in addition to ACE inhibition (7.4–100%) with significant (p < .05) differences between the peptides. AGVTVS, TKDIG, TSRLG, GRIST, and SGEKI were the most active; however, AGVTVS had the highest hydrophobic residue and exhibited the strongest activity against ACE, renin as well as superoxide and hydroxyl radicals.
Practical applications
There is an increasing attraction of researchers to food peptides especially from legume proteins. Enzymatic digestion as well as high performance liquid chromatography (HPLC) purification has become an important process used to separate peptides with significant biological activities and health-promoting effects. There is useful information regarding the bioactive and functional (in vitro antioxidant, antidiabetic, in vitro/in vivo antihypertensive) properties of hydrolyzed and ultra-filtered pigeon pea fractions but scant research output still exists for purified peptides from pigeon pea establishing their therapeutic potential. The present study aimed to separate peptide fractions from pigeon pea hydrolysate and identify available amino acid sequences from the parent protein. Therefore, peptide sequences generated from the most bioactive fractions showed prospects for the expanded industrial utilization of pigeon pea. Further promoting its application as functional ingredient or additive for alleviating angiotensin-converting enzyme-related diseases.
CONFLICT OF INTEREST
The authors declare that they have is no conflict of interest.
Open Research
DATA AVAILABILITY STATEMENT
The data that support the findings of this study are available from the corresponding author upon reasonable request.
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