• Fisheries and Aquatic Sciences
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• v.19 no.2
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• pp.11.1-11.7
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• 2016

In this study, purified peptides from shrimp waste hydrolysates (SWHs) were examined for their inhibitory effects against ${\beta}$-secretase. During consecutive purification using a Sephadex G-25 column chromatography and high performance liquid chromatography on a C18 column, a potent ${\beta}$-secretase inhibitory peptide Asp-Val-Leu-Phe-His (629 Da) was isolated and identified from SWH24 by Q-TOF MS/MS and the $IC_{50}$ value was determined to be $92.70{\mu}M$. The ${\beta}$-secretase inhibition patterns of the purified peptides were found to be competitive. Among synthesized ${\beta}$-secretase inhibitory peptides, Leu-Phe-His had higher ${\beta}$-secretase inhibitory activity than the others. The result of this study suggests that the ${\beta}$-secretase inhibitory peptide derived from SWH24 could be potential candidates to develop nutraceuticals and pharmaceuticals.