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Forghani B
,
Ebrahimpour A
,
Bakar J
,
Abdul Hamid A
,
Hassan Z
,
Saari N
.
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Stichopus horrens flesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) of Stichopus horrens hydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC(50) value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC(50) value of 2.24 mg/mL), trypsin hydrolysate (IC(50) value of 2.28 mg/mL), papain hydrolysate (IC(50) value of 2.48 mg/mL), bromelain hydrolysate (IC(50) value of 4.21 mg/mL), and protamex hydrolysate (IC(50) value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC(50) values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.
Figure 1. Effect of hydrolysis time on the degree of hydrolysis of S. horrens hydrolysates using different enzymes. Results are reported as mean ± SD. Error bar denotes standard deviation.
Figure 2. ACE inhibitory activity (IC50 mg/mL) of S. horrens hydrolysates as affected by proteolysis time. Error bar denotes standard deviation.
Figure 3. Relationship between DH and IC50 value of S. horrens hydrolysed by alcalase and flavourzyme.
Figure 4. SDS-PAGE of S. horrens hydrolysates at 30, 60, 120, 180, 240, and 300 min performed using 15% resolving gel. Each well consists of 3.36 μg protein. The lane indicated as PM was the protein molecular marker.
Balti,
Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.
2010, Pubmed
Balti,
Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.
2010,
Pubmed
Balti,
Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products.
2010,
Pubmed
Cheung,
Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.
1980,
Pubmed
Cheung,
Inhibition of homogeneous angiotensin-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops jararaca.
1973,
Pubmed
Cushman,
Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung.
1971,
Pubmed
He,
High throughput and rapid screening of marine protein hydrolysates enriched in peptides with angiotensin-I-converting enzyme inhibitory activity by capillary electrophoresis.
2007,
Pubmed
Herregods,
Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides.
2011,
Pubmed
Kristinsson,
Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases.
2000,
Pubmed
Laemmli,
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
1970,
Pubmed
Lee,
Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis.
2009,
Pubmed
Lu,
Isolation of an antihypertensive peptide from alcalase digest of Spirulina platensis.
2010,
Pubmed
Murray,
Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.
2007,
Pubmed
Ondetti,
Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents.
1977,
Pubmed
Raia,
Angiotensin-converting enzyme inhibitors: a comparative review.
1990,
Pubmed
Rao,
Molecular and biotechnological aspects of microbial proteases.
1998,
Pubmed
Rozan,
Free amino acids present in commercially available seedlings sold for human consumption. A potential hazard for consumers.
2000,
Pubmed
Vercruysse,
ACE inhibitory activity in enzymatic hydrolysates of insect protein.
2005,
Pubmed
Wang,
Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats.
2008,
Pubmed
Yang,
Inhibition of proliferation of PC3 cells by the branched-chain fatty acid, 12-methyltetradecanoic acid, is associated with inhibition of 5-lipoxygenase.
2003,
Pubmed
,
Echinobase
Yokoyama,
Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.
1992,
Pubmed
Yuan,
Two new holostan-type triterpene glycosides from the sea cucumber Bohadschia marmorata JAEGER.
2008,
Pubmed
,
Echinobase
Zhao,
A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate.
2009,
Pubmed
,
Echinobase
