Physicochemical properties of leftover egg yolk after livetins removal

- Antibody extraction generates large quantities of leftover egg yolk pellet.
- Egg yolk pellet showed inferior emulsion stability but higher viscoelastic moduli than that of egg yolk.
- Increased hydrophobic and hydrogen bonding interactions might be responsible for the changes.

Isolation of immunoglobulin Y (IgY) from egg yolk using water-dilution method generates large quantities of leftover pellet as the co-product. Although egg yolk is well known for its great emulsion property, there is a lack of understanding on how livetins removal would affect the emulsion and rheological properties of the pellet. Therefore, the objective of this study was to determine the effect of soluble protein removal on emulsifying and rheological characteristics of the leftover egg yolk. Egg yolk pellet exhibited distinct structural and physicochemical properties after soluble protein removal. Emulsions prepared from pellet were more vulnerable to coalescence instability than that of egg yolk, although both had a similar oil droplet size. Egg yolk displayed a Newtonian behaviour, compared to a shear-thinning behaviour of pellet. Pellet showed a higher apparent viscosity as well as higher viscoelastic moduli than those of egg yolk, probably due to increased hydrogen bond and hydrophobic interactions in the pellet. Therefore, the changes on the emulsion stability and the rheological properties of egg yolk after soluble proteins removal should be considered in food formulation and processing. Further study is needed to improve the emulsion property of pellet for uses in the food industry.