Journal of Marine Bioscience and Biotechnology (한국해양바이오학회지)

The Korean Society for Marine Biotechnology (한국해양바이오학회)
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Characterization of β-Secretase Inhibitory Peptide Purified from Blackfin flounder (Glyptocephalus stelleri) Protein Hydrolysate

  • Lee, Jung Kwon (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Kim, Sung Rae (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Byun, Hee-Guk (Department of Marine Biotechnology, Gangneung-Wonju National University)
  • Received : 2018.01.12
  • Accepted : 2018.02.06
  • Published : 2018.06.30
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Abstract

The objective of this study was to purify and characterize the ${\beta}-secretase$ inhibitor from enzymatic hydrolysates of blackfin flounder muscle, for development of a novel anti-dementia agent that may be used in the drug or functional food industries. ${\beta}-secretase$ inhibitory peptide was purified from various enzymatic hydrolysates of blackfin flounder muscle. Among six enzymatic hydrolysates, the Alcalase hydrolysate revealed highest ${\beta}-secretase$ inhibitory activity. Consecutive purification of the blackfin flounder muscle hydrolysate using Sephadex G-25 column chromatography and octadecylsilane C18 reversed phase HPLC techniques were used to isolate a potent ${\beta}-secretase$ inhibitory peptide composed of 5 amino acids, Leu-Thr-Gln-Asp-Trp (MW: 526.7 Da). The $IC_{50}$ value of purified ${\beta}-secretase$ inhibitory peptide was $126.93{\mu}M$. Results of this study suggest that peptides derived from blackfin flounder muscle may be beneficial as anti-dementia compounds in functional foods or as pharmaceuticals.

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