Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey protein in vitro gastrointestinal digests

Vermeirssen, Vanessa, Van Camp, John and Verstraete, Willy (2005) Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey protein in vitro gastrointestinal digests. Journal of the Science of Food and Agriculture, 85 3: 399-405. doi:10.1002/jsfa.1926


Author Vermeirssen, Vanessa
Van Camp, John
Verstraete, Willy
Title Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey protein in vitro gastrointestinal digests
Formatted title
Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey protein in vitro gastrointestinal digests
Journal name Journal of the Science of Food and Agriculture   Check publisher's open access policy
ISSN 1097-0010
0022-5142
Publication date 2005-02-01
Year available 2004
Sub-type Article (original research)
DOI 10.1002/jsfa.1926
Open Access Status Not Open Access
Volume 85
Issue 3
Start page 399
End page 405
Total pages 7
Place of publication West Sussex, England
Publisher John Wiley & Sons
Language eng
Subject 110801 Medical Bacteriology
Formatted abstract
In vitro gastrointestinal digestion of pea and whey protein produced high angiotensin I converting enzyme (ACE) inhibitory activity with IC50 values of 0.070 and 0.041 mg protein ml-1 respectively. Ultrafiltration/centrifugation using a membrane with a molecular weight cut-off of 3000 Da decreased the IC50 value to 0.055 mg protein ml-1 for pea permeate and 0.014 mg protein ml-1 for whey permeate. Further fractionation by reverse phase HPLC gave IC50 values as low as 0.016 mg protein ml-1 for pea and 0.003 mg protein ml-1 for whey. Consequently, these purification steps enriched the ACE inhibitory activity of the pea digest more than four times and that of the whey digest more than 13 times. HPLC profiles after digestion and ultrafiltration indicate that high ACE inhibitory activity is due to short and more hydrophobic peptides. The results also suggest that potent ACE inhibitory peptides were present alongside low active peptides in whey hydrolysate, while all peptides had more or less the same ACE inhibitory activity in pea hydrolysate. In addition, the hydrolysates and enriched fractions will resist in vivo gastrointestinal digestion after oral administration. Hence these ACE inhibitory peptides, as part of functional foods, can play significant roles in the prevention and treatment of hypertension.
Keyword Angiotensin I converting enzyme inhibitory peptides
Pea protein
Whey protein
Ultrafiltration
High-performance liquid chromatography
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Advanced Water Management Centre Publications
 
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Created: Mon, 16 Feb 2009, 22:52:31 EST by Joanne Mellor on behalf of Advanced Water Management Centre