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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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The objective of this study was to purify and characterize the β-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. β-secretase inhibitory peptide was purified from various enzymatic hydrolysates of blackfin flounder muscle. Among six enzymatic hydrolysates, the Alcalase hydrolysate revealed highest β-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 β-secretase inhibitory peptide composed of 5 amino acids, Leu–Thr–Gln–Asp–Trp (MW: 526.7 Da). The IC<SUB>50</SUB> value of purified β-secretase inhibitory peptide was 126.93 μM. 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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Abstract
Introduction
Materials and Methods
Results and Discussion
Conclusion
References
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UCI(KEPA) : I410-ECN-0101-2018-472-003099688