Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Activities of Egg Protein Hydrolysates Produced with Gastrointestinal and Nongastrointestinal Enzymes
Article first published online: 24 JUN 2011
© 2011 Institute of Food Technologists®
Journal of Food Science
Volume 76, Issue 6, pages C801–C807, August 2011
How to Cite
You, S.-J. and Wu, J. (2011), Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Activities of Egg Protein Hydrolysates Produced with Gastrointestinal and Nongastrointestinal Enzymes. Journal of Food Science, 76: C801–C807. doi: 10.1111/j.1750-3841.2011.02228.x
- Issue published online: 5 AUG 2011
- Article first published online: 24 JUN 2011
- MS 20101380 Submitted 12/5/2010, Accepted 4/10/2011.
- ACE-inhibitory activity;
- antioxidant activity;
- egg protein hydrolysates
Abstract: Egg is a well-known rich source of bioactive peptides. In this study, egg protein (egg white and egg yolk proteins) hydrolysates were produced with gastrointestinal enzymes (pepsin and pancreatin) or nongastrointestinal enzymes (thermolysin and alcalase), and fractionated by ultrafiltration and cation exchange chromatography. Angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities, amino acid composition and molecular weight distribution were studied, and the physicochemical properties were related with the bioactivities. Our results showed that egg protein hydrolysates produced with non-GI enzymes (thermolysin and alcalase) showed significantly higher ACE inhibitory activity, whereas similar or even lower antioxidative activities, than those of hydrolysates produced with GI enzymes. ACE-inhibitory activity significantly correlated with the amino acid composition, especially the proportion of positively charged amino acid, whereas antioxidant activities correlated with the proportion of low molecular weight peptides under 500 Da. Understanding the relationship between the bioactivities and physicochemical properties of the hydrolysates/fractions is important to facilitate the development technologies for preparing fractions with improved bioactivities.