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논문검색

Purification and Characterization of an Antioxidative Peptide Obtained from Rotifer Protein by Enzymatic Hydrolysis

초록

영어

The rotifer, Brachionus rotundiformis is most commonly used as live feed for fish larvae cultures at early stages. Larval fish generally have a high demand for dietary protein due to their rapid growth rates and extensive catabolism of amino acids for the production of metabolic energy1). The rotifer has been studied as a food source for marine fish because of its size and rich nutrients, which make it a good source for large quantity cultivation2). In order to identify the antioxidative peptide in the hydrolysate of the rotifer, which is hydrolyzed by Alcalase, Neutrase, -chymotrypsin, α papain, pepsin, and trypsin in a batch reactor, the antioxidative activities of hydrolysates were evaluated using direct free radical scavenging activity. Among the six hydrolysates, peptic hydrolysate, had the highest antioxidative activity compared
to the other hydrolysates. The peptide showing strong antioxidative activity was isolated from the hydrolysate using consecutive chromatographic methods including Sephadex G-25 Gel-chromatography and high-performance liquid chromatography on an ODS column. The antioxidative peptide was purified and the molecular weight measured. Further studies are planned to measure the cytotoxic effect on MRC-5 and ECV304 cell lines.

저자정보

  • Ji-Ho Yun Faculty of Marine Bioscience and Technology, Kangnung National University
  • Ji-Suk Oh Faculty of Marine Bioscience and Technology, Kangnung National University
  • Su-Hee Hong Faculty of Marine Bioscience and Technology, Kangnung National University
  • Se-Kwon Kim Department of Chemistry, Pukyong National University
  • Hee-Guk Byun Faculty of Marine Bioscience and Technology, Kangnung National University

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