Related Experiment Video
Updated: Jun 16, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Angiotensin I converting enzyme inhibitory peptide extracted from freshwater zooplankton
Jung Kwon Lee1, Min-Su Lee, Heum Gi Park
1Faculty of Marine Bioscience and Technology, Gangnueng-Wonju National University, Gangneung, Republic of Korea.
Abstract:
In this study, hydrolysates obtained from the freshwater rotifer Brachionus calyciflonus were investigated for angiotensin I converting enzyme (ACE) inhibitory peptides. Freshwater rotifer protein was hydrolyzed using six separate enzymes in a batch reactor. The peptic hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The highest ACE inhibitory peptide was separated using Sephadex G-25 column chromatography and high-performance liquid chromatography on a C18 column. The 50% inhibitory concentration (IC(50)) value of purified ACE inhibitory peptide was 40.01 microg/mL. ACE inhibitory peptide was identified as being seven amino acid residues of Ala-Gln-Gly-Glu-Arg-His-Arg by N-terminal amino acid sequence analysis. The IC(50) value of purified ACE inhibitory peptide was 47.1 microM, and Lineweaver-Burk plots suggested that the peptide purified from rotifer protein acts as a competitive inhibitor against ACE. The results of this study suggest that peptides derived from freshwater rotifers may be beneficial as antihypertension compounds in functional foods or as pharmaceuticals.
Related Concept Videos
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors
Antihypertensive Drugs: Direct Renin Inhibitors
Antihypertensive Drugs: Angiotensin II Receptor Blockers
Heart Failure Drugs: Inhibitors of Renin-Angiotensin System
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Hormonal Regulation

