Optimization of the enzymatic hydrolysis conditions of waste from shortfin scad (Decapterus Macrosoma) for the production of angiotensin I-converting enzyme (ACE) inhibitory peptide using response surface methodology
This study aims to optimize enzymatic hydrolysis process for producing angiotensin I-converting enzyme (ACE) inhibitory peptides from protein hydrolysate of shortfin scad (Decapterus Macrosoma) waste (SWH). The enzymatic hydrolysis conditions, namely the temperature (40, 50, 60°C), time (B: 60, 120,...
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Published in | International food research journal Vol. 24; no. 4; p. 1735 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Selangor
Universiti Putra Malaysia, Faculty of Food Science & Technology
01.08.2017
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Subjects | |
Online Access | Get full text |
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Summary: | This study aims to optimize enzymatic hydrolysis process for producing angiotensin I-converting enzyme (ACE) inhibitory peptides from protein hydrolysate of shortfin scad (Decapterus Macrosoma) waste (SWH). The enzymatic hydrolysis conditions, namely the temperature (40, 50, 60°C), time (B: 60, 120, 180 min), pH (C: 7, 8, 9) and enzyme substrate concentrations (D: 1, 2, 3%) on yield, degree of hydrolysis (DH) and ACE-inhibitory activity were analysed. Responses were optimized using the response surface methodology (RSM) by employing four factors, 3-levels and the Central Composite Design (CCD). The optimized conditions were further validated to indicate the validity of the prediction model. The optimal conditions obtained for the hydrolysis conditions were at temperature of 50°C, time of 60 min, pH of 9 and enzyme to substrate concentration of 2.92%. The experimental result for yield was lower than the predicted value, as generated by RSM. However, the degree of hydrolysis of SWH was higher than the predicted value. The ACE inhibitory activity of SWH was 79.34%, and showed lower than the predicted value. Therefore, the optimized conditions of SWH served as good conditions for the production of bioactive peptide with high ACE inhibitory activity. |
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ISSN: | 1985-4668 2231-7546 |