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KMID : 1161420100130020357
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Journal of Medicinal Food
2010 Volume.13 No. 2 p.357 ~ p.363
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Angiotensin I Converting Enzyme Inhibitory Peptide Extracted from Freshwater Zooplankton
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Lee Jung-Kwon
Lee Min-Su
Park Heum-Gi
Kim Se-Kwon
Byun Hee-Guk
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Abstract
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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 (IC50) value of purified ACE inhibitory peptide was 40.01?μg/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 IC50 value of purified ACE inhibitory peptide was 47.1?μM, 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.
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KEYWORD
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angiotensin I converting enzyme, freshwater rotifer, hydrolysates, peptide, zooplankton
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