Tyr-Pro-Lys, an angiotensin I-converting enzyme inhibitory peptide derived from broccoli (Brassica oleracea Italica)

Published on Jan 1, 2006in Food Chemistry7.514
· DOI :10.1016/J.FOODCHEM.2005.06.050
Ju-Eun Lee1
Estimated H-index: 1
 (Hanyang University), In Young Bae25
Estimated H-index: 25
 (Hanyang University)+ 1 AuthorsCha Bum Yang1
Estimated H-index: 1
 (Hanyang University)
Sources
Abstract
Abstract To investigate the naturally occurring angiotensin I-converting enzyme (ACE) inhibitor, broccoli ( Brassica oleracea Italica ) extracts were used for its isolation and identification. After treatment with 50% acetone for membrane breakdown, ethyl acetate, n -butanol, and water were used for the preparation of broccoli extracts. The water-soluble extract from broccoli had 76.9% ACE inhibitory activity, while those of other organic solvent extracts showed lower ACE inhibitory activities. An ACE inhibitory peptide was isolated using column chromatographic methods including: Amberlite XAD-4, Sephadex LH-20, and high performance liquid chromatography. The purified ACE inhibitory peptide was identified to be a tripeptide, Tyr-Pro-Lys, having an IC 50 value of 10.5 μg protein/ml.
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Tests were conducted to evaluate the inhibitory effects of collagen peptides in the hydrolysate of sea bream scales on the activity of angiotensin I converting enzyme (ACE, EC3.4.15.1). The scales were hydrolyzed using an alkaline protease treatment by which 92% of the peptides were degraded to form hydrolysate. The 50% inhibitory concentration of the peptides was as high as 0.57 mg ml−1. In addition, using spontaneously hypertensive rats, oral administration of 300 mg of the peptides (kg of bod...
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Mar 16, 2004·Journal of Agricultural and Food Chemistry5.28
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