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HERO ID
992407
Reference Type
Journal Article
Title
Identification and Inhibitory Properties of Multifunctional Peptides from Pea Protein Hydrolysate
Author(s)
Li, H; Aluko, RE
Year
2010
Is Peer Reviewed?
Yes
Journal
Journal of Agricultural and Food Chemistry
ISSN:
0021-8561
EISSN:
1520-5118
Volume
58
Issue
21
Page Numbers
11471-11476
Language
English
PMID
20929253
DOI
10.1021/jf102538g
Abstract
Pea protein isolate was hydrolyzed with alcalase, and the hydrolysate passed through a 1 kDa cutoff ultrafiltration membrane. The permeate was freeze-dried and fractionated on a cationic solid-phase extraction (SPE) column. All fractions were tested for their inhibitory activities against angiotensin-converting enzyme (ACE), renin, and calmodulin-dependent phosphodiesterase 1 (CaMPDE). With the exception of the first eluted fraction, inhibitory properties of the SPE fractions against CaMPDE (but not ACE and renin) were directly related to cationic character (residence time on the column). However, the fraction that eluted with 1% ammonium hydroxide (SPE 1%) had the highest peptide yield and was subsequently fractionated using two consecutive rounds of reversed-phase high-performance liquid chromatography to obtain three peaks with major peptides identified as IR, KF, and EF by ultra performance liquid chromatography-tandem mass spectrometry. The three dipeptides showed weak inhibitory properties toward CaMPDE but strong inhibitions (IC(50) values <25 mM) of ACE and renin. In general, the peptides had higher potency against ACE than against renin. It is indicated from our results that these peptides may be used as potential ingredients to formulate multifunctional food products and nutraceuticals.
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