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CC BY 4.0 · Journal of Health and Allied Sciences NU 2024; 14(S 01): S26-S34
DOI: 10.1055/s-0044-1782643
Original Article

Modification of Bioactive Properties in Food Protein Hydrolysates by Alcalase and Trypsin

Nishithkumar Jogi
1   Nitte (Deemed to be University), Department of Food Safety and Nutrition, Nitte University Center for Science and Research, Mangaluru. Karnataka, India
,
Anjaly Mathew
1   Nitte (Deemed to be University), Department of Food Safety and Nutrition, Nitte University Center for Science and Research, Mangaluru. Karnataka, India
,
Bangera Sheshappa Mamatha 
1   Nitte (Deemed to be University), Department of Food Safety and Nutrition, Nitte University Center for Science and Research, Mangaluru. Karnataka, India
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Abstract

Background Protein hydrolysates are the fragments of proteins that form during the hydrolysis with promised bioactive properties. Enzymatic hydrolysis produces bioactive peptides with specific amino acid profile. Among all the properties, angiotensin-I converting enzyme (ACE-I) inhibitory activity of the protein hydrolysates attained maximum attention to combat life-threatening disease like hypertension.

Methodology In the present study 10 protein-rich food sources (> 20% protein content on dry basis) were used to prepare protein hydrolysates using alcalase and trypsin to investigate the effect of enzymes on ACE-I inhibitory and antioxidant activity.

Results Among all the sources, the highest degree of hydrolysis was observed in sardine (62.89%) followed by soybean (61.24%) when hydrolyzed by alcalase. Kidney pea exhibited highest ACE-I inhibitory activity with IC50 value of 0.517 and 0.521 when hydrolyzed using both trypsin and alcalase, respectively. All the sources selected showed nonsignificant changes in ACE-I inhibitory activity between alcalase and trypsin (p < 0.05) except Bengal gram and chicken. Antioxidant activity was higher in alcalase hydrolyzed egg yolk (43.08%).

Conclusion Among the sources, all animal proteins hydrolyzed using alcalase exhibited significantly higher (p < 0.05) antioxidant activity than trypsin. However, protein hydrolysates prepared from sardine using alcalase would yield bioactive peptides with higher ACE-I inhibitory and antioxidant activity. Therefore, use of alcalase as a substitution for trypsin would be economical for large-scale production. Henceforth, food protein hydrolyzed by alcalase can be used as a functional ingredient for the development of functional or nutraceutical foods to combat lifestyle diseases.

Keywords

protein hydrolysates - ACE-I inhibitory activity - proteolytic enzymes - food proteins


Publication History

Article published online:
23 May 2024

© 2024. The Author(s). This is an open access article published by Thieme under the terms of the Creative Commons Attribution License, permitting unrestricted use, distribution, and reproduction so long as the original work is properly cited. (https://creativecommons.org/licenses/by/4.0/)

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