Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis |
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Authors: | Jung Kwon Lee Suhee Hong Joong-Kyun Jeon Se-Kwon Kim Hee-Guk Byun |
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Affiliation: | 1. Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University, 120 Gangneung Daehakro, Gangneung 210-720, Republic of Korea;2. Department of Chemistry, Pukyong National University, Busan 608-737, Republic of Korea |
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Abstract: | Angiotensin I converting enzyme (ACE) inhibitory peptide was isolated from the marine rotifer, Brachionus rotundiformis. ACE inhibitory peptides were separated from rotifer hydrolysate prepared by Alcalase, α-chymotrypsin, Neutrase, papain, and trypsin. The Alcalase hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The IC50 value of Alcalase hydrolysate for ACE inhibitory activity was 0.63 mg/ml. We attempted to isolate ACE inhibitory peptides from Alcalase prepared rotifer hydrolysate using gel filtration on a Sephadex G-25 column and high performance liquid chromatography on an ODS column. The IC50 value of purified ACE inhibitory peptide was 9.64 μM, and Lineweaver–Burk plots suggest that the peptide purified from rotifer protein acts as a competitive inhibitor against ACE. Amino acid sequence of the peptide was identified as Asp-Asp-Thr-Gly-His-Asp-Phe-Glu-Asp-Thr-Gly-Glu-Ala-Met, with a molecular weight 1538 Da. The results of this study suggest that peptides derived from rotifers may be beneficial as anti-hypertension compounds in functional foods resource. |
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Keywords: | Angiotensin I converting enzyme Marine rotifer Peptide Alcalase Hydrolysates |
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