Ovotransferrin: Structure, bioactivities, and preparation
2012
Wu, Jianping | Acero-Lopez, Alexandra
Ovotransferrin, accounting for about 12–13% of total egg white proteins, is synthesized by the avian transferrin gene in the oviduct. It is made of a monomeric glycoprotein consisting of 686 amino acid residues. As a member of transferrin family, ovotransferrin folds into two globular lobes, each containing an iron-binding site located within the interdomain cleft of each lobe. In addition to providing antimicrobial activity, it also functions to transport iron to the developing embryo. The antimicrobial property of ovotransferrin is thought to be due to its ability to sequester the iron necessary for the growth of microorganisms, rendering then iron deprived. Recent evidence further suggests that its role as an essential component of the egg's antimicrobial defense system is very likely iron independent. This antimicrobial property implies its applications as an infant formula ingredient, a food additive, and an antimicrobial agent for improving animal health. A wide range of bioactivities such as antifungal, antiviral, anticancer, antioxidative, antihypertensive, and immunomodulatory activities have been reported recently for ovotransferrin or its derived peptides. In this review, the structure, bioactivity, and preparation of ovotransferrin are presented, and its potential as a nutraceutical and functional food ingredient is described.
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