Egg proteins: fractionation, bioactive peptides and allergenicity

Abstract

Eggs are an important source of macro and micronutrients within the diet, comprised of proteins, lipids, vitamins, and minerals. They are constituted by a shell, the white (containing 110 g kg^-1 proteins: ovalbumin, ovotransferrin, ovomucoid, lysozyme and ovomucin), and the yolk (containing 150-170 g kg^-1 proteins: lipovitellins, phosvitin, livetins, and low-density lipoproteins). Owing to their nutritional value and biological characteristics, both the egg white and yolk proteins are extensively fractionated using different techniques (e.g., liquid chromatography, ultrafiltration, electrophoresis, and chemical precipitation), in which liquid chromatography is the most commonly used technique to obtain individual proteins with high protein recovery and purity to develop novel food products. However, concerns over allergenic responses induced by certain egg proteins (e.g., ovomucoid, ovalbumin, ovotransferrin, lysozyme, α-livetin, and lipoprotein YGP42) limit their widespread use. As such, processing technologies (e.g., thermal processing, enzymatic hydrolysis, and high-pressure treatment) are investigated to reduce the allergenicity by conformational changes. In addition, biological activities (e.g., antioxidant, antimicrobial, antihypertensive, and anticancer activities) associated with egg peptides have received more attention, in which enzyme hydrolysis is demonstrated as a promising way to break polypeptides sequences and produce bioactive peptides to provide nutritional and therapeutic benefits for human health. © 2018 Society of Chemical Industry.

Keywords: allergenicity; bioactive peptides; egg proteins; fractionation.