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Int J Mol Sci
2015 Dec 04;1612:28870-85. doi: 10.3390/ijms161226140.
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Angiotensin-I Converting Enzyme (ACE) Inhibitory and Anti-Oxidant Activities of Sea Cucumber (Actinopyga lecanora) Hydrolysates.
Ghanbari R
,
Zarei M
,
Ebrahimpour A
,
Abdul-Hamid A
,
Ismail A
,
Saari N
.
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In recent years, food protein-derived hydrolysates have received considerable attention because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive and anti-oxidative activities are receiving special attention as both activities can play significant roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities of Actinopyga lecanora (A. lecanora) hydrolysates, which had been prepared by alcalase, papain, bromelain, flavourzyme, pepsin, and trypsin under their optimum conditions. The alcalase hydrolysate showed the highest ACE inhibitory activity (69.8%) after 8 h of hydrolysis while the highest anti-oxidative activities measured by 2,2-diphenyl 1-1-picrylhydrazyl radical scavenging (DPPH) (56.00%) and ferrous ion-chelating (FIC) (59.00%) methods were exhibited after 24 h and 8 h of hydrolysis, respectively. The ACE-inhibitory and anti-oxidative activities displayed dose-dependent trends, and increased with increasing protein hydrolysate concentrations. Moreover, strong positive correlations between angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities were also observed. This study indicates that A. lecanora hydrolysate can be exploited as a source of functional food owing to its anti-oxidant as well as anti-hypertension functions.
Figure 1. ACE inhibitory activities (%) of A. lecanora hydrolysates as affected by hydrolysis time using enzymatic digestion during 24 h. Sample concentration for this assay was 10.0 mg dry weight/mL. Results represent the mean ± SD of three replications.
Figure 2. ACE inhibitory activities (%) of A. lecanora hydrolysates at different concentrations between 0.0 and 10.0 mg of dry weight/mL. Results represent the means ± SD of three replications.
Figure 3. Effect of hydrolysis time on the DPPH radical scavenging activities (%) of different A. lecanora hydrolysates generated from enzymatic digestion for 24 h. Sample concentration for this assay was 1.0 mg/mL. Results represent the means ± SD of three replications.
Figure 4. Changes in DPPH radical scavenging activities (%) of A. lecanora hydrolysates as a function of concentrations between 0.0 and 1.0 mg dry weight/mL. Each value is the mean ± SD of three replications.
Figure 5. Effect of hydrolysis time on the ferrous ion chelating activity (FIC) (%) of A. lecanora hydrolysates generated from enzymatic digestion for 24 h. Sample concentration for this assay was 1.0 mg dry weight/mL. Each value is the mean ± SD of three replications.
Figure 6. Changes in ferrous ion chelating activities (%) of A lecanora/hydrolysates at concentration between 0.0 and 1.0 mg dry weight/mL Each value is the mean ± SD of three replications.
Figure 7. Correlation between bioactivities (%) of A. lecanora alcalase hydrolysates. (a) ACE inhibition versus DPPH radical scavenging activity; (b) ACE inhibition versus metal ion chelating activity. R2 values indicated the best-fit linearity functions. Bars represent standard deviations from triplicate determinations.
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