ORIGINAL ARTICLE
In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties
 
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1
Department of Food and Human Nutritional Sciences, University of Manitoba, R3T 2N2 Winnipeg, Canada
2
Department of Food Science & Technology, Obafemi Awolowo University, 220002 Ile-Ife, Nigeria
3
Department of Soil and Land Resources Management, Faculty of Agriculture, Obafemi Awolowo University, 220002 Ile-Ife, Nigeria
4
Department of Agronomy, Faculty of Agriculture, Obafemi Awolowo University, 220002 Ile-Ife, Nigeria
CORRESPONDING AUTHOR
Akinsola Albert Famuwagun   

Food Science and Technology, Obafemi Awolowo University, 2200055, Ile-Ife, Nigeria
Submission date: 2020-08-25
Final revision date: 2020-11-10
Acceptance date: 2020-11-12
Online publication date: 2020-12-09
Publication date: 2020-12-09
 
Pol. J. Food Nutr. Sci. 2020;70(4):429–443
 
KEYWORDS
TOPICS
ABSTRACT
Hydrolysates were produced using Alcalase (AH), chymotrypsin (CH), pepsin (PH), and trypsin (TH), and also fluted pumpkin leaf protein isolate (FLI) as a substrate. AH had the lowest degree of hydrolysis (16.37%) but exhibited overall superior antioxidant and enzyme inhibitory properties. Therefore, it was fractionated by membrane ultrafiltration to give <1, 1-3, 3-5, 5-10, and >10 kDa peptide fractions. Gel permeation chromatography showed that the molecular weight of the FLI was 19.77 kDa and that of the hydrolysates was below 7.5 kDa. The hydrolysate peptides had a high content of hydrophobic amino acids but low levels of sulfur-containing amino acids, when compared to protein of FLI. Peptide sequence analysis showed that the hydrolysates consisted of dipeptides, tripeptides, and tetrapeptides with molecular weights below 500 Da. The hydrolysates were also stronger inhibitors of linoleic acid oxidation, α-amylase, α-glucosidase, and angiotensin converting enzyme (ACE) than FLI. Among the fractions, the <1 and 1-3 kDa were the most effective free radical scavengers and metal chelators in addition to their strong inhibitory activities against α-amylase, α-glucosidase, and ACE. We conclude that the AH and low molecular weight peptide fraction (<3 kDa) could find applications in formulating foods with various bioactive properties.
FUNDING
This research was supported by the International Development Research Centre and Global Affairs Canada through the Canadian International Food Security Research Fund, Project 107983 on synergizing indigenous vegetables and fertilizer micro-dosing innovations among West African farmers.
 
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