Journal
BIORESOURCE TECHNOLOGY
Volume 100, Issue 21, Pages 5255-5259Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2009.05.057
Keywords
Angiotensin I converting enzyme; Marine rotifer; Peptide; Alcalase; Hydrolysates
Funding
- Marine Bioprocess Research Center of the Marine Biotechnology Program
- Ministry of Land, Transport and Maritime, Republic of Korea
- Korea Institute of Marine Science & Technology Promotion (KIMST) [B10400107A280000100] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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, alpha-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 mu M, 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. (C) 2009 Elsevier Ltd. All rights reserved
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