Evaluation of the ACE-Inhibitory Activity of Egg-White Proteins Degraded with Pepsin
 
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Publication date: 2013-06-30
 
Pol. J. Food Nutr. Sci. 2013;63(2):103–108
 
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ABSTRACT
Increasing the potency of antihypertensive food-derived peptides is a critical and important step in the development of natural drugs for cardiovascular diseases prevention. We have proposed the egg-white protein precipitate (EWPP) obtained as a byproduct of cystatin and lysozyme isolation as a potential source of ACE-inhibitory peptides derived by pepsin digestion. The results indicated that hydrolysis of EWPP with pepsin produced the ACE inhibitory activity. During 3-h hydrolysis (DH: 38.3%), the IC50 value of EWPP hydrolysate was significantly increased and finally reached IC50=643.1 μg/mL. This hydrolysate was further fractionated by RP-HPLC. The peptide fraction exhibiting the highest ACE inhibitory activity was rechromatographed. Three peptide subfractions exhibiting ACE-inhibitory activities of 69.0, 25.0, and 37.6 μg/mL were further characterised. In each of them, mixtures of peptides with different molecular masses were observed.
 
CITATIONS (3):
1.
Bioactive peptides from egg: a review
Z. Bhat, Sunil Kumar, Hina Bhat
Nutrition & Food Science
 
2.
Bioactive peptides of animal origin: a review
Z. Bhat, Sunil Kumar, Hina Bhat
Journal of Food Science and Technology
 
3.
Recently Isolated Food-derived Antihypertensive hydrolysates and Peptides: A Review
Arshdeep Kaur, Kehinde Adesegun, Poorva Sharma, Deepansh Sharma, Sawinder Kaur
Food Chemistry
 
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ISSN:1230-0322