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논문검색

Purification and Characterization of AngiotensinⅠconverting Enzyme Inhibitory Peptides from the Rotifer, Brachionus calyciflorus.

초록

영어

The functional peptides from protein hydrolysates of various fishery sources have been identified such as antioxidative activity, angiotensinⅠconverting enzyme (ACE) inhibitor activity and antibiotic activity. The peptides regulating blood pressure are known to be potent inhibitors of ACE1). Freshwater rotifers are commonly used as live feed for freshwater fish. Larval fish generally have a high demand for dietary protein due to their high growth rates, and extensive
catabolism of amino acids for the production of metabolic energy2). In this study, the hydrolysates obtained from the rotifer, Brachionus clayciflonus was investigated for ACE inhibitory peptides. The rotifer protein was hydrolyzed using Alcalase, α-chymotrypsin, Neutrase, pepsin, papain, and trypsin in a batch reactor. The peptic hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The peptic hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The IC50 value of peptic
hydrolysate for ACE inhibitory activity was 0.52 mg/ml. We attempted to isolate ACE inhibitory peptides from pepsin prepared rotifer hydrolysate using gel filtration on a Sephadex G-25 column and high performance liquid chromatography on an ODS column. Further study is planned to analyze the amino acid sequence of peptides purified from the peptic hydrolysates of the
rotifer.

저자정보

  • Chan Jun Jeon Faculty of Marine Bioscience and Technology, Kangnung National University
  • Hee-Jung Kim Faculty of Marine Bioscience and Technology, Kangnung National University
  • Jung Kwon Lee Faculty of Marine Bioscience and Technology, Kangnung National University
  • Hee-Guk Byun Faculty of Marine Bioscience and Technology, Kangnung National University

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