Abstract
The objective of this study was to purify and characterize the β-secretase inhibitor from enzymatic hydrolysates of skate skin, for the development of a novel antidementia agent that may be utilized in the drug or functional food industries. β-secretase inhibitory peptide was purified from various enzymatic hydrolysates of skate skin. Among six enzymatic hydrolysates, the Neutrase hydrolysate showed the highest β-secretase inhibitory activity. Consecutive purification of the skate skin hydrolysate using Sephadex G-25 column chromatography and octadecylsilane C18 reversed phase HPLC techniques was used to isolate a potent β-secretase inhibitory peptide composed of 12 amino acids, Gln–Gly–Try–Arg–Pro–Leu–Arg–Gly–Pro–Glu–Phe–Leu (MW: 1,391 Da). The purified peptide had strong β-secretase inhibitory activity, with IC50 value of 24.26 μM, and displayed a non-competitive mode of inhibition. Among the synthesized β-secretase inhibitory peptides, the tetrapeptide Pro–Glu–Phe–Leu had the highest β-secretase inhibitory activity. The result of this study suggests that the β-secretase inhibitory peptide derived from skate skin could be potential candidates to develop nutraceuticals and pharmaceuticals.
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Acknowledgments
This research was financially supported by the Ministry of Education, Science Technology (MEST), Gangwon Province, Gangneung City, Gangneung Science Industry Foundation (GSIF) as the R&D Project for Gangneung science park promoting program.
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This article does not contain any studies with human or animal subjects.
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Lee, J.K., Li-Chan, E.C.Y. & Byun, HG. Characterization of β-secretase inhibitory peptide purified from skate skin protein hydrolysate. Eur Food Res Technol 240, 129–136 (2015). https://doi.org/10.1007/s00217-014-2314-9
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DOI: https://doi.org/10.1007/s00217-014-2314-9