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Mar Drugs
2017 Mar 31;154:. doi: 10.3390/md15040104.
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Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology.
Muhammad Auwal S
,
Zarei M
,
Abdul-Hamid A
,
Saari N
.
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The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values. This study aimed to establish the conditions for its optimum hydrolysis with bromelain to generate angiotensin I-converting enzyme (ACE)-inhibitory hydrolysates. Response surface methodology (RSM) based on a central composite design was used to model and optimize the degree of hydrolysis (DH) and ACE-inhibitory activity. Process conditions including pH (4-7), temperature (40-70 °C), enzyme/substrate (E/S) ratio (0.5%-2%) and time (30-360 min) were used. A pH of 7.0, temperature of 40 °C, E/S ratio of 2% and time of 240 min were determined using a response surface model as the optimum levels to obtain the maximum ACE-inhibitory activity of 84.26% at 44.59% degree of hydrolysis. Hence, RSM can serve as an effective approach in the design of experiments to improve the antihypertensive effect of stone fish hydrolysates, which can thus be used as a value-added ingredient for various applications in the functional foods industries.
Figure 1. Response surface plots for the effects of independent factors on degree of hydrolysis: (a) pH and E/S ratio; (b) temperature and time (c) enzyme/substrate (E/S) ratio and time.
Figure 2. Response surface plots for the effects of the independent factors on angiotensin I-converting enzyme (ACE)-inhibitory activity: (a) pH and temperature; (b) pH and E/S ratio; (c) temperature and E/S ratio (d) temperature and time.
Figure 3. Response optimization for the hydrolysis parameters, predicted responses, and their level of desirability. Y1 = degree of hydrolysis (DH, %), Y2 = ACE-inhibitory activity (%), D = Composite desirability for YI and Y2 responses, d1 = individual desirability of Y1, d2 = individual desirability of Y2. Optimum selected conditions of pH, temperature, enzyme/substrate ratio and time are shown in red whereas the maximum predicted responses of Y1 and Y2 are shown in blue.
Figure 4. Functional properties of stone fish hydrolysates prepared using bromelain as influenced by pH; (a) Solubility profile (b) Foaming capacity and (c) Foam stability. Each value represents a mean of triplicate determinations.
Balti,
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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,
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Bordbar,
The improvement of the endogenous antioxidant property of stone fish (Actinopyga lecanora) tissue using enzymatic proteolysis.
2013,
Pubmed
,
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Cattaneo,
Anti-inflammatory and antioxidant activities, functional properties and mutagenicity studies of protein and protein hydrolysate obtained from Prosopis alba seed flour.
2014,
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Cumby,
Antioxidant activity and water-holding capacity of canola protein hydrolysates.
2008,
Pubmed
Ghanbari,
Actinopyga lecanora hydrolysates as natural antibacterial agents.
2012,
Pubmed
,
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Ghanbari,
Angiotensin-I Converting Enzyme (ACE) Inhibitory and Anti-Oxidant Activities of Sea Cucumber (Actinopyga lecanora) Hydrolysates.
2015,
Pubmed
,
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Haque,
Influence of milk peptides in determining the functionality of milk proteins: a review.
1993,
Pubmed
Iwaniak,
Food-Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction.
2014,
Pubmed
Jimsheena,
Colorimetric, high-throughput assay for screening Angiotensin I-converting enzyme inhibitors.
2009,
Pubmed
Lee,
Characterization of bioactive peptides obtained from marine invertebrates.
2012,
Pubmed
Li,
Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Razor Clam Sinonovacula constricta.
2016,
Pubmed
Lu,
Angiotensin-I-converting enzyme-inhibitory peptides in commercial Wisconsin Cheddar cheeses of different ages.
2016,
Pubmed
Wijesekara,
Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry.
2010,
Pubmed