Antioxidant, angiotensin-converting enzyme inhibitory activity and other functional properties of egg white proteins and their derived peptides – A review
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The Department of Animal Science originally concerned itself with teaching the selection, breeding, feeding and care of livestock. Today it continues this study of the symbiotic relationship between animals and humans, with practical focuses on agribusiness, science, and animal management.
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The Department of Animal Husbandry was established in 1898. The name of the department was changed to the Department of Animal Science in 1962. The Department of Poultry Science was merged into the department in 1971.
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- Department of Animal Husbandry (1898–1962)
- College of Agricultural and Life Sciences (parent college)
- Department of Poultry Science (merged with, 1971)
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Abstract
Egg white contains many functionally important proteins: ovalbumin (54%), ovotransferrin (12%), ovomucoid (11%), ovoglobulin (G2 and G3, 8%), ovomucin (3.5%), and lysozyme (3.5%) are major proteins, while ovoinhibitors, ovomacroglobulin, ovoglycoprotein, ovoflavoprotein, thiamine-binding proteins, and avidin are minor proteins present in egg white. These proteins, as well as the peptides derived from the proteins, have been recognized for their functional importance as antioxidant, antimicrobial, metal-chelating, anti-viral, anti-tumour, and angiotensin-converting enzyme (ACE)-inhibitory activities. Among the functional properties of the peptides, antioxidant and antimicrobial activities are important characteristics for food processing while other properties such as ACE-inhibitory activity of the peptides can have important health-related functionalities. Bioactive peptides can be produced from egg white proteins by enzyme hydrolysis, chemical treatments, or thermal treatments at different pH conditions. The effective functional peptides produced from egg white proteins are usually smaller than 2 kDa in molecular size. However, these peptides are known for their beneficial activities in vitro only, and little work has been done to prove their beneficial effects in vivo. Therefore, further studies are needed to see if the bioactive peptides derived from egg white proteins are helpful for humans in the future.
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This article is published as Abeyrathne, E. D. N. S., X. Huang, and D. U. Ahn. "Antioxidant, angiotensin-converting enzyme inhibitory activity and other functional properties of egg white proteins and their derived peptides–A review." Poultry science 97, no. 4 (2018): 1462-1468. doi:10.3382/ps/pex399.