This work was supported by a grant from the Korean Ministry of Health and Welfare.
Isolation of an Angiotensin Converting Enzyme Inhibitory Peptide from Irradiated Bovine Blood Plasma Protein Hydrolysates
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 68, Issue 8, pages 2469–2472, October 2003
How to Cite
Lee, S.H. and Song, K.B. (2003), Isolation of an Angiotensin Converting Enzyme Inhibitory Peptide from Irradiated Bovine Blood Plasma Protein Hydrolysates. Journal of Food Science, 68: 2469–2472. doi: 10.1111/j.1365-2621.2003.tb07047.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- MS 20030330 Submitted 6/14/03, Revised 7/8/03, Accepted 8/22/03.
- ACE inhibitor;
- blood plasma protein;
ABSTRACT: An angiotensin converting enzyme (ACE) inhibitory peptide was isolated and purified from the hydrolysates of the irradiated bovine blood plasma protein. Blood plasma protein was irradiated at 10 kGy to eliminate microbial contamination and was enzymatically hydrolyzed using several commercial proteases: Alcalase, Esperase, and Flavourzyne. An ACE inhibitory peptide was isolated using membrane filtration, gel permeation chromatography, normal phase and reverse phase high-performance liquid chromatography. The purified ACE inhibitory peptide was identified to be a tripeptide, His-Pro-Tyr, having IC50 value of 1.68 μM.