Abstract
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.
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