Angiotensin I–Converting Enzyme Inhibitory Peptides from Snakehead Fish Sarcoplasmic Protein Hydrolysate

In this study, the angiotensin I‐converting enzyme (ACE) inhibitory peptides were isolated from snakehead fish sarcoplasmic protein hydrolysates. Enzymatic hydrolysis of sarcoplasmic protein was performed using various commercial enzymes. The alcalase hydrolysate with the highest ACE inhibition acti...

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Bibliographic Details
Published in:Journal of food biochemistry 2014-04, Vol.38 (2), p.140-149
Main Authors: Ghassem, Masomeh, Babji, Abdul Salam, Said, Mamot, Mahmoodani, Fatemeh, Arihara, Keizo
Format: Article
Language:English
Subjects:
antihypertensive effect
cytotoxicity
enzymatic hydrolysis
Freshwater
freshwater fish
gels
humans
hydrolysates
hydrolysis
inhibitory concentration 50
ionization
liquid chromatography
mass spectrometry
peptides
protein hydrolysates
subtilisin
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Summary:In this study, the angiotensin I‐converting enzyme (ACE) inhibitory peptides were isolated from snakehead fish sarcoplasmic protein hydrolysates. Enzymatic hydrolysis of sarcoplasmic protein was performed using various commercial enzymes. The alcalase hydrolysate with the highest ACE inhibition activity was purified with gel chromatography and reversed phased high‐performance liquid chromatography. The purified fractions were then subjected to electrospray ionization quadrupole‐micro‐time‐of‐flight mass spectrometry for amino acid characterization. Two novel ACE inhibitory peptides LYPPP and YSMYPP with IC₅₀ values of 1.3 and 2.8 μM were identified, respectively. The pattern of ACE inhibition, resistance to hydrolysis by gastrointestinal proteases and cytotoxic potencies of isolated peptides were described. The results showed no cytotoxicity of peptides on human embryonic fibroblast cell line (MRC‐5) and human hepatocarcinoma cell line (HepG2). PRACTICAL APPLICATIONS: Freshwater fish muscle proteins and their hydrolysates offer huge potential as novel sources of natural bioactive peptides with angiotensin I‐converting enzyme (ACE) inhibitory activity. The present study revealed the identification of two strong ACE inhibitory peptides obtained from alcalase hydrolysis of snakehead fish sarcoplasmic protein. However, further studies are required to determine the in vivo antihypertensive activity of the purified potent ACE inhibitory peptides.
ISSN:0145-8884
1745-4514
DOI:10.1111/jfbc.12031