Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions

Chibuike C. Udenigwe, Yin Shiou Lin, Wen C. Hou, Rotimi E. Aluko

Research output: Contribution to journalArticle

117 Citations (Scopus)

Abstract

Enzymatic hydrolysates from flaxseed protein were investigated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. Pepsin, ficin, trypsin, papain, thermolysin, pancreatin and Alcalase were used to hydrolyze flaxseed proteins followed by fractionation using ultrafiltration to isolate low-molecular-weight peptides, and separation of the Alcalase hydrolysate into cationic peptide fractions. Using N-(3-[2-furyl]acryloyl)-phenylalanylglycylglycine as substrate, the protein hydrolysates showed a concentration-dependent ACE inhibition (IC50, 0.0275-0.151 mg/ml) with thermolysin hydrolysate and Alcalase cationic peptide fraction I (FI) showing the most potent activity. Flaxseed peptide fractions also showed no or moderate inhibitory activities against human recombinant renin (IC50, 1.22-2.81 mg/ml). Kinetics studies showed that the thermolysin hydrolysate and FI exhibited mixed-type pattern of ACE inhibition whereas cationic peptide fraction II inhibited renin in uncompetitive fashion. These results show that the protein components of flaxseed meal possess peptide amino acid sequences that can be exploited as potential food sources of anti-hypertensive agents.

Original languageEnglish
Pages (from-to)199-207
Number of pages9
JournalJournal of Functional Foods
Volume1
Issue number2
DOIs
Publication statusPublished - Apr 2009

Fingerprint

Protein Hydrolysates
Flax
renin
protein hydrolysates
peptidyl-dipeptidase A
linseed
Peptidyl-Dipeptidase A
Renin
peptides
Thermolysin
Subtilisins
hydrolysates
kinetics
Peptides
subtilisin
enzyme inhibition
Inhibitory Concentration 50
inhibitory concentration 50
Ficain
ficain

Keywords

  • Angiotensin converting enzyme
  • Bioactive peptides
  • Enzyme inhibition kinetics
  • Flaxseed
  • IC
  • Protein hydrolysates
  • Renin

ASJC Scopus subject areas

  • Food Science
  • Medicine (miscellaneous)
  • Nutrition and Dietetics

Cite this

Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions. / Udenigwe, Chibuike C.; Lin, Yin Shiou; Hou, Wen C.; Aluko, Rotimi E.

In: Journal of Functional Foods, Vol. 1, No. 2, 04.2009, p. 199-207.

Research output: Contribution to journalArticle

@article{5a02af9ab01a42e4837adb48f5f1f6cc,
title = "Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions",
abstract = "Enzymatic hydrolysates from flaxseed protein were investigated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. Pepsin, ficin, trypsin, papain, thermolysin, pancreatin and Alcalase were used to hydrolyze flaxseed proteins followed by fractionation using ultrafiltration to isolate low-molecular-weight peptides, and separation of the Alcalase hydrolysate into cationic peptide fractions. Using N-(3-[2-furyl]acryloyl)-phenylalanylglycylglycine as substrate, the protein hydrolysates showed a concentration-dependent ACE inhibition (IC50, 0.0275-0.151 mg/ml) with thermolysin hydrolysate and Alcalase cationic peptide fraction I (FI) showing the most potent activity. Flaxseed peptide fractions also showed no or moderate inhibitory activities against human recombinant renin (IC50, 1.22-2.81 mg/ml). Kinetics studies showed that the thermolysin hydrolysate and FI exhibited mixed-type pattern of ACE inhibition whereas cationic peptide fraction II inhibited renin in uncompetitive fashion. These results show that the protein components of flaxseed meal possess peptide amino acid sequences that can be exploited as potential food sources of anti-hypertensive agents.",
keywords = "Angiotensin converting enzyme, Bioactive peptides, Enzyme inhibition kinetics, Flaxseed, IC, Protein hydrolysates, Renin",
author = "Udenigwe, {Chibuike C.} and Lin, {Yin Shiou} and Hou, {Wen C.} and Aluko, {Rotimi E.}",
year = "2009",
month = "4",
doi = "10.1016/j.jff.2009.01.009",
language = "English",
volume = "1",
pages = "199--207",
journal = "Journal of Functional Foods",
issn = "1756-4646",
publisher = "Elsevier Ltd",
number = "2",

}

TY - JOUR

T1 - Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions

AU - Udenigwe, Chibuike C.

AU - Lin, Yin Shiou

AU - Hou, Wen C.

AU - Aluko, Rotimi E.

PY - 2009/4

Y1 - 2009/4

N2 - Enzymatic hydrolysates from flaxseed protein were investigated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. Pepsin, ficin, trypsin, papain, thermolysin, pancreatin and Alcalase were used to hydrolyze flaxseed proteins followed by fractionation using ultrafiltration to isolate low-molecular-weight peptides, and separation of the Alcalase hydrolysate into cationic peptide fractions. Using N-(3-[2-furyl]acryloyl)-phenylalanylglycylglycine as substrate, the protein hydrolysates showed a concentration-dependent ACE inhibition (IC50, 0.0275-0.151 mg/ml) with thermolysin hydrolysate and Alcalase cationic peptide fraction I (FI) showing the most potent activity. Flaxseed peptide fractions also showed no or moderate inhibitory activities against human recombinant renin (IC50, 1.22-2.81 mg/ml). Kinetics studies showed that the thermolysin hydrolysate and FI exhibited mixed-type pattern of ACE inhibition whereas cationic peptide fraction II inhibited renin in uncompetitive fashion. These results show that the protein components of flaxseed meal possess peptide amino acid sequences that can be exploited as potential food sources of anti-hypertensive agents.

AB - Enzymatic hydrolysates from flaxseed protein were investigated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. Pepsin, ficin, trypsin, papain, thermolysin, pancreatin and Alcalase were used to hydrolyze flaxseed proteins followed by fractionation using ultrafiltration to isolate low-molecular-weight peptides, and separation of the Alcalase hydrolysate into cationic peptide fractions. Using N-(3-[2-furyl]acryloyl)-phenylalanylglycylglycine as substrate, the protein hydrolysates showed a concentration-dependent ACE inhibition (IC50, 0.0275-0.151 mg/ml) with thermolysin hydrolysate and Alcalase cationic peptide fraction I (FI) showing the most potent activity. Flaxseed peptide fractions also showed no or moderate inhibitory activities against human recombinant renin (IC50, 1.22-2.81 mg/ml). Kinetics studies showed that the thermolysin hydrolysate and FI exhibited mixed-type pattern of ACE inhibition whereas cationic peptide fraction II inhibited renin in uncompetitive fashion. These results show that the protein components of flaxseed meal possess peptide amino acid sequences that can be exploited as potential food sources of anti-hypertensive agents.

KW - Angiotensin converting enzyme

KW - Bioactive peptides

KW - Enzyme inhibition kinetics

KW - Flaxseed

KW - IC

KW - Protein hydrolysates

KW - Renin

UR - http://www.scopus.com/inward/record.url?scp=64549083283&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=64549083283&partnerID=8YFLogxK

U2 - 10.1016/j.jff.2009.01.009

DO - 10.1016/j.jff.2009.01.009

M3 - Article

VL - 1

SP - 199

EP - 207

JO - Journal of Functional Foods

JF - Journal of Functional Foods

SN - 1756-4646

IS - 2

ER -