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. 2017 Mar 31;15(4):104.
doi: 10.3390/md15040104.

Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology

Shehu Muhammad Auwal  1   2 , Mohammad Zarei  3   4 , Azizah Abdul-Hamid  5 , Nazamid Saari  6
Affiliations

Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology

Shehu Muhammad Auwal et al. Mar Drugs. .

Abstract

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.

Keywords: ACE inhibitory hydrolysates; central composite design; degree of hydrolysis; response surface methodology; stone fish.

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Conflict of interest statement

The authors declare no conflicting interests.

Figures

Figure 1
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 1
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
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 2
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
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
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.
Figure 4
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.
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References

    1. Lee J.K., Jeon J.K., Kim S.K., Byun H.G. Advances in Food and Nutritional Research; Marine Medicinal Foods: Implications and Applications: Animals and Microbes. 1st ed. Volume 65. Elsevier Inc.; Waltham, MA, USA: 2012. Characterization of Bioactive Peptides Obtained from Marine Invertebrates; pp. 47–72. - PubMed
    1. Ariyoshi Y. Angiotensin-converting enzyme-inhibitors derived from food proteins. Trends Food Sci. Technol. 1993;4:139–144. doi: 10.1016/0924-2244(93)90033-7. - DOI
    1. Barbana C., Boye J.I. Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition. Food Chem. 2011;127:94–101. doi: 10.1016/j.foodchem.2010.12.093. - DOI
    1. Wijesekara I., Kim S.K. Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry. Mar. Drugs. 2010;8:1080–1093. doi: 10.3390/md8041080. - DOI - PMC - PubMed
    1. Girgih A.T., Nwachukwu I.D., Hasan F.M., Fagbemi T.N., Malomo S.A., Gill T.A., Aluko R.E. Kinetics of in vitro enzyme inhibition and blood pressure-lowering effects of salmon (Salmo salar) protein hydrolysates in spontaneously hypertensive rats. J. Funct. Foods. 2016;20:43–53. doi: 10.1016/j.jff.2015.10.018. - DOI

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