1. Purification and characterization of angiotensin-1 converting enzyme (ACE)-inhibitory peptide from the jellyfish, Nemopilema nomurai
- Author
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Ho-Sung Moon, Ho-Dong Yoon, Chi-Won Lim, Moon-Hee Lee, So-mi Yeun, Hee-Yeon Park, Na-Young Yoon, Yeon-Kye Kim, and Doo-Seog Lee
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Size-exclusion chromatography ,Peptide ,Angiotensin-converting enzyme ,Carbon-13 NMR ,Applied Microbiology and Biotechnology ,Hydrolysate ,Papain ,chemistry.chemical_compound ,Sephadex ,Genetics ,Proton NMR ,biology.protein ,Agronomy and Crop Science ,Molecular Biology ,Biotechnology - Abstract
The Nemopilema nomurai hydrolysate was produced by the reaction of papain, and an angiotensin-Ι converting enzyme (ACE)-inhibitory peptide was purified by using the molecular cut-offs membrane filter, the gel filtration chromatography with Sephadex LH-20 and the reverse phase chromatographic method using C 18 and C 12 columns. Purification yield of the active peptide was estimated to be 0.2 ± 0.1%, starting from the lyophilized jellyfish. The infrared (IR), proton nuclear magnetic resonance spectroscopy (1H NMR), carbon nuclear magnetic resonance (13C NMR) and mass spectrometry (MS) spectrometer analyses elucidated that the structure of the purified peptide is tyrosine-isoleucine (Tyr-Ile). The inhibitory concentration at 50% (IC50) and Ki values were calculated to be 2.0 ± 0.3 μg/ml and 3.3 ± 0.3 μM, respectively, which acts as a competitive inhibitor to ACE. Keywords : Angiotensin-Ι converting enzyme, Jellyfish, Nemopilema nomurai , Papain hydrolysate, Tyrosine-Isoleucine African Journal of Biotechnology Vol. 12(15), pp. 1888-1893
- Published
- 2013
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