Identification of four new angiotensin I-converting enzyme inhibitory peptides from fermented anchovy sauce

The inhibitory activity of an angiotensin I-converting enzyme (ACE), a key regulatory enzyme of blood pressure from the fermented anchovy sauce, was evaluated, and ACE inhibitory peptides were purified. The ACE activity significantly increased with an increase in salt concentration. In addition, the...

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Published inApplied biological chemistry Vol. 59; no. 1; pp. 25 - 31
Main Authors Kim, Hyun-Jin, Kang, Seong-Gook, Jaiswal, Lily, Li, Jinglei, Choi, Ju-Hee, Moon, Sang-Mi, Cho, Jeong-Yong, Ham, Kyung-Sik
Format Journal Article
LanguageEnglish
Published Seoul The Korean Society for Applied Biological Chemistry 01.02.2016
Springer Nature B.V
한국응용생명화학회
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Summary:The inhibitory activity of an angiotensin I-converting enzyme (ACE), a key regulatory enzyme of blood pressure from the fermented anchovy sauce, was evaluated, and ACE inhibitory peptides were purified. The ACE activity significantly increased with an increase in salt concentration. In addition, the ACE inhibitory activity of the fermented anchovy sauce containing high salt content (25 %) significantly increased with an increase in fermentation time. The maximum activity (96 %) was reached after 15 months of fermentation. Four ACE inhibitors [Pro-Lys (PK), Gly-Cys-Lys (GCK), Asn- His-Pro (NHP), and Asp-Gly-Gly-Pro (DGGP)] in the fermented anchovy sauce were purified through various chromatographic techniques and identified by electrospray ionization tandem mass spectrometer analysis. Four newly identified peptides were synthesized and analyzed for ACE inhibitory activity in order to confirm that the purified peptides were actually ACE inhibitors. The IC 50 values for ACE inhibitory activities of synthesized peptides DGGP, GCK, NHP, and PK were 164, 178, 1172, and 4092 μM, respectively.
Bibliography:G704-000111.2016.59.1.014
ISSN:2468-0834
2468-0842
DOI:10.1007/s13765-015-0129-4