Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates

Rong He, Adeola Alashi, Sunday A. Malomo, Abraham T. Girgih, Dongfang Chao, Xingrong Ju, Rotimi E. Aluko

Research output: Contribution to journalArticle

75 Citations (Scopus)
23 Downloads (Pure)

Abstract

In this study, rapeseed protein isolate (RPI) was digested with various proteases to produce rapeseed protein hydrolysates (RPHs), which were then separated into different peptide fractions (<1, 1'3, 3'5, and 5'10 kDa) by membrane ultrafiltration. Membrane fractionation showed that peptides with sizes <3 kDa had significantly (p < 0.05) reduced surface hydrophobicity when compared to the RPHs and peptide fractions with sizes >3 kDa. In contrast, the <3 kDa peptides showed significantly (p < 0.05) higher oxygen radical scavenging ability when compared to the >3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5'10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (~24 mm Hg) while Proteinase K RPH was the least effective (~5 mm Hg) after 8 h. However, the PP RPH had the most prolonged effect with BP reduction of ~20 mm Hg after 24 h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.
Original languageEnglish
Pages (from-to)153-159
Number of pages7
JournalFood Chemistry
Volume141
Issue number1
DOIs
Publication statusPublished - Nov 2013

Fingerprint

rapeseed protein
Protein Hydrolysates
Brassica rapa
antihypertensive agents
protein hydrolysates
Scavenging
Antihypertensive Agents
Free Radicals
Subtilisins
Pancreatin
subtilisin
Pepsin A
Blood pressure
pancreatin
Peptides
peptides
Thermolysin
pepsin
Endopeptidase K
blood pressure

Cite this

He, R., Alashi, A., Malomo, S. A., Girgih, A. T., Chao, D., Ju, X., & Aluko, R. E. (2013). Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates. Food Chemistry, 141(1), 153-159. https://doi.org/10.1016/j.foodchem.2013.02.087
He, Rong ; Alashi, Adeola ; Malomo, Sunday A. ; Girgih, Abraham T. ; Chao, Dongfang ; Ju, Xingrong ; Aluko, Rotimi E. / Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates. In: Food Chemistry. 2013 ; Vol. 141, No. 1. pp. 153-159.
@article{7b260d31900d47e4b423b5cf54935251,
title = "Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates",
abstract = "In this study, rapeseed protein isolate (RPI) was digested with various proteases to produce rapeseed protein hydrolysates (RPHs), which were then separated into different peptide fractions (<1, 1'3, 3'5, and 5'10 kDa) by membrane ultrafiltration. Membrane fractionation showed that peptides with sizes <3 kDa had significantly (p < 0.05) reduced surface hydrophobicity when compared to the RPHs and peptide fractions with sizes >3 kDa. In contrast, the <3 kDa peptides showed significantly (p < 0.05) higher oxygen radical scavenging ability when compared to the >3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5'10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (~24 mm Hg) while Proteinase K RPH was the least effective (~5 mm Hg) after 8 h. However, the PP RPH had the most prolonged effect with BP reduction of ~20 mm Hg after 24 h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.",
keywords = "Open access version available, Angiotensin converting enzyme, Antihypertensive properties, Membrane ultrafiltration, Oxygen radical absorbance capacity, Protein hydrolysate, Rapeseed protein isolate, Renin, Spontaneously hypertensive rat",
author = "Rong He and Adeola Alashi and Malomo, {Sunday A.} and Girgih, {Abraham T.} and Dongfang Chao and Xingrong Ju and Aluko, {Rotimi E.}",
note = "Imported on 12 Apr 2017 - DigiTool details were: month (773h) = November, 2013; Journal title (773t) = Food Chemistry. ISSNs: 0308-8146;",
year = "2013",
month = "11",
doi = "10.1016/j.foodchem.2013.02.087",
language = "English",
volume = "141",
pages = "153--159",
journal = "Journal of Micronutrient Analysis",
issn = "0308-8146",
publisher = "Elsevier BV",
number = "1",

}

He, R, Alashi, A, Malomo, SA, Girgih, AT, Chao, D, Ju, X & Aluko, RE 2013, 'Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates', Food Chemistry, vol. 141, no. 1, pp. 153-159. https://doi.org/10.1016/j.foodchem.2013.02.087

Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates. / He, Rong; Alashi, Adeola; Malomo, Sunday A.; Girgih, Abraham T.; Chao, Dongfang; Ju, Xingrong; Aluko, Rotimi E.

In: Food Chemistry, Vol. 141, No. 1, 11.2013, p. 153-159.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates

AU - He, Rong

AU - Alashi, Adeola

AU - Malomo, Sunday A.

AU - Girgih, Abraham T.

AU - Chao, Dongfang

AU - Ju, Xingrong

AU - Aluko, Rotimi E.

N1 - Imported on 12 Apr 2017 - DigiTool details were: month (773h) = November, 2013; Journal title (773t) = Food Chemistry. ISSNs: 0308-8146;

PY - 2013/11

Y1 - 2013/11

N2 - In this study, rapeseed protein isolate (RPI) was digested with various proteases to produce rapeseed protein hydrolysates (RPHs), which were then separated into different peptide fractions (<1, 1'3, 3'5, and 5'10 kDa) by membrane ultrafiltration. Membrane fractionation showed that peptides with sizes <3 kDa had significantly (p < 0.05) reduced surface hydrophobicity when compared to the RPHs and peptide fractions with sizes >3 kDa. In contrast, the <3 kDa peptides showed significantly (p < 0.05) higher oxygen radical scavenging ability when compared to the >3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5'10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (~24 mm Hg) while Proteinase K RPH was the least effective (~5 mm Hg) after 8 h. However, the PP RPH had the most prolonged effect with BP reduction of ~20 mm Hg after 24 h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.

AB - In this study, rapeseed protein isolate (RPI) was digested with various proteases to produce rapeseed protein hydrolysates (RPHs), which were then separated into different peptide fractions (<1, 1'3, 3'5, and 5'10 kDa) by membrane ultrafiltration. Membrane fractionation showed that peptides with sizes <3 kDa had significantly (p < 0.05) reduced surface hydrophobicity when compared to the RPHs and peptide fractions with sizes >3 kDa. In contrast, the <3 kDa peptides showed significantly (p < 0.05) higher oxygen radical scavenging ability when compared to the >3 kDa peptides and RPHs. In vitro inhibition of angiotensin I-converting enzyme (ACE) was significantly (p < 0.05) higher for the Thermolysin, Proteinase K and Alcalase RPHs when compared to the pepsin + pancreatin (PP) and Flavourzyme RPHs. The Alcalase RPH had significantly (p < 0.05) higher renin inhibition among the RPHs, while with the exception of Thermolysin, the 5'10 kDa peptide fraction had the least renin-inhibitory ability when compared to the <5 kDa peptide fractions. Oral administration (100 mg/kg body weight) of the RPHs and RPI to spontaneously hypertensive rats (SHR) showed the Alcalase RPH to be the most effective in blood pressure (BP) reduction (~24 mm Hg) while Proteinase K RPH was the least effective (~5 mm Hg) after 8 h. However, the PP RPH had the most prolonged effect with BP reduction of ~20 mm Hg after 24 h of oral administration. We conclude that the strong BP-lowering ability of Alcalase and PP RPHs could be due to high resistance of the peptides to structural degradation coupled with high absorption rate within the gastrointestinal tract.

KW - Open access version available

KW - Angiotensin converting enzyme

KW - Antihypertensive properties

KW - Membrane ultrafiltration

KW - Oxygen radical absorbance capacity

KW - Protein hydrolysate

KW - Rapeseed protein isolate

KW - Renin

KW - Spontaneously hypertensive rat

U2 - 10.1016/j.foodchem.2013.02.087

DO - 10.1016/j.foodchem.2013.02.087

M3 - Article

C2 - 23768341

VL - 141

SP - 153

EP - 159

JO - Journal of Micronutrient Analysis

JF - Journal of Micronutrient Analysis

SN - 0308-8146

IS - 1

ER -