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

Abstract

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 mM 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 APPLICATIONSFreshwater 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. bs_bs_banner Journal of Food Biochemistry ISSN 1745-4514 ACE INHIBITORS OF SNAKEHEAD SARCOPLASMIC PROTEIN HYDROLYSATE M. GHASSEM ET AL.

Structural Properties of Phycoerythrin from DulsePalmaria palmata

“…Although the potency of peptide is lower than drug, it does not have side effect (Balti et al 2015). Up to now, many researchers have identified various ACE inhibitory peptides from the enzymatic hydrolysates of food (Amado et al 2014;Ghassem et al 2014;Balti et al 2015;Garc ıa-Moreno et al 2015). Besides, Cheung et al (1980) obtained the interesting results using several synthetic peptides for a substrate of ACE, that is to say, the ACE inhibitory activity of peptide is closely related to the C-terminal dipeptide residues in it.…”

“…Specifically, in case of tryptophan, tyrosine or proline residue is located at the N-terminal side of dipeptide and aromatic amino acid or proline residue is at the C-terminus, its inhibitory potency is the most. Indeed, it has been well known that the peptides are usually composed of hydrophobic and aromatic amino acids (Amado et al 2014;Ghassem et al 2014;Balti et al 2015;Garc ıa-Moreno et al 2015). Therefore, we calculated the contents of hydrophobic and aromatic amino acid residues in dulse PE using the primary structures in this study (Fig.…”

ANGIOTENSIN CONVERTING ENZYME (ACE) INHIBITORY ACTIVITY OF CRUDE AND FRACTIONATED SNAKEHEAD (Channa striata) MEAT EXTRACT

“…Huang, Davidge, and Wu (2013) supported that bioactive compound like protein and peptide had an influential role to lower the blood pressure. Investigations towards the presence of ACE inhibitory bioactive peptide has been conducted by Ghassem, Babji, Said, Mahmoodani, and Arihara (2014) were hydrolyzing sarcoplasmic protein of snakehead fish fillet using alcalase and by Ghassem, Arihara, Babji, Said, and Ibrahim (2011) were hydrolyzing myofibril protein of snakehead fish fillet using thermolysin. Yet, a study of endogenous bioactive protein or peptide with ACE inhibitory activity from snakehead fish fillet is still sparse.…”

The intake assessment of diverse dietary patterns on childhood hypertension: alleviating the blood pressure and lipidemic factors with low-sodium seafood rich in omega-3 fatty acids

“…Seafood is also considered as a good protein source with high digestibility, bioavailability, and efficiency ratio. The presence of essential amino acids (e.g., cystine, lysine, methionine, threonine, and a Multiple linear regression model: R 2 = 82.5%, adjusted R 2 = 79.4% b p-value < 0.05 is significant, ns: non-significant tryptophan) in the structure of angiotensin I-converting enzyme inhibitory peptides may reduce the CH [46]. The consumption of seafood products through high daily intake of dietary potassium is associated with the reduced ratio of sodium (Na) to potassium (K) and blood pressure levels in children [47].…”