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ORIGINAL ARTICLE
Antioxidant and Renin-Angiotensin System Inhibitory Properties of Cashew Nut and Fluted-Pumpkin Protein Hydrolysates
1
Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg R3T 2N2, Canada
2
Department of Food Science and Technology, Federal University of Technology, Akure, Nigeria
3
Department of Food Science and Technology, Federal University of Agriculture, Makurdi, Nigeria
4
Department of Food Science and Technology, Mountain Top University, Prayer City, Lagos, Nigeria
Submission date: 2020-01-14
Final revision date: 2020-05-07
Acceptance date: 2020-05-14
Online publication date: 2020-06-19
Publication date: 2020-06-19
Corresponding author
Sunday A. Malomo
Food Science and Technology, Federal University of Technology, Akure, Ilesha-Benin Expressway, PMB 704, Akure, Nigeria
Food Science and Technology, Federal University of Technology, Akure, Ilesha-Benin Expressway, PMB 704, Akure, Nigeria
Pol. J. Food Nutr. Sci. 2020;70(3):275-289
KEYWORDS
TOPICS
Functional foodsAmino acids/Minerals AvailabilityNutraceuticalsNutsBioactive peptidesChemical and enzymatic modificationIsolation
ABSTRACT
Antioxidant and renin-angiotensin system (RAS)-inhibitory protein hydrolysates derived from the enzymatic hydrolysis of cashew nut (CNP) and fluted pumpkin (FPP) proteins were investigated. The CNP and FPP hydrolysates (CNPH and FPPH) from pepsin or Alcalase treatments were subjected to membrane ultrafiltration using different MWCOs to obtain <1, 1–3, 3–5, 5–10 and >10 kDa peptide fractions. Hydrolysis of protein isolates at similar enzyme levels allowed obtaining peptic hydrolysates with a lower degree of hydrolysis (46.7-48.0%) when compared to the Alcalase-produced hydrolysates (47.7-50.3%). Amino acid composition revealed that CNPH had 28% hydrophobic residues when compared to higher contents (32-35%) in the 3-10 kDa peptide fractions. In contrast, aromatic residues increased from 8% in the FPPH to 9-13% in the peptide fractions. The in vitro •OH and DPPH• scavenging activities were significantly (p<0.05) enhanced by ultrafiltration but potency was inversely related to peptide size. The ferric-reducing power was the highest for the <1 kDa CNPH (2.47) when compared to 1.33 for CNPH and other peptide fractions. Metal chelation ability was significantly (p<0.05) enhanced by ultrafiltration only for the CNPH with 21% compared to ~96% for the peptide fractions. ACE inhibition was significantly (p<0.05) lower for the Alcalase CNPH and peptide fractions (~87%) compared to ~92% of pepsin-CNPH. However, renin inhibition was significantly (p<0.05) increased by ultrafiltration from 45.7 and 62.1% to ~82.4 and 96.5% for FPPH and CNPH, respectively. We conclude that the strong antioxidant properties coupled with RAS inhibition make CNPH and FPPH as well as their low molecular weight peptides potential ingredients to formulate health-promoting foods.
FUNDING
We acknowledge support of the Natural Sciences and Engineering Council of Canada (NSERC), funding reference number RGPIN 2018-06019. Cette recherche a été financée par le Conseil de recherches en sciences naturelles et en génie du Canada (CRSNG), numéro de référence RGPIN 2018-06019.
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