Fisheries and Aquatic Sciences

한국수산과학회 (The Korean Society of Fisheries and Aquatic Science)
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Characterization of antioxidative peptide purified from black eelpout (Lycodes diapterus) hydrolysate

  • Lee, Jung Kwon (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Byun, Hee-Guk (Department of Marine Biotechnology, Gangneung-Wonju National University)
  • 투고 : 2019.06.24
  • 심사 : 2019.09.13
  • 발행 : 2019.10.31
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초록

The functional peptides from protein hydrolysates of various fishery sources have been identified such as antioxidant activity. The main intention of this study was purification and characterization of antioxidative peptide from black eelpout muscle. The antioxidative peptides were purified from black eelpout (Lycodes diapterus) muscle using different proteases. Antioxidant activity of black eelpout hydrolysates was evaluated using DPPH radical scavenging activity. Among six hydrolysates, the pepsin hydrolysate had the highest antioxidant activity compared to the other hydrolysates. Therefore, it was further purified and a peptide with seven amino acid residues of DLVKVEA (784 Da) was identified by amino acid sequence analysis. The EC50 value for scavenging DPPH radicals by purified peptide was 688.77 μM. Additionally, the purified peptide exhibited protective effect against DNA damage induces by oxidation in mouse macrophages (RAW 264.7 cells). The results of this study suggest that black eelpout muscle protein hydrolysate could potentially contribute to development of bioactive peptides in basic research.

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피인용 문헌

  1. Purification and characterization of antioxidant peptides from hairtail surimi hydrolysates and their effects on beef color stability vol.86, pp.7, 2019, https://doi.org/10.1111/1750-3841.15804