Gelation Properties of Egg White Proteins: A Review

ABSTRACT

Egg white proteins (EWPs) are valuable ingredients in the food industry due to their unique functional properties, including gelling, foaming, and emulsifying. The gelation properties of EWPs are particularly important, as they serve as the foundation for many food applications. The denaturation and aggregation of EWPs lead to the formation of a dense three-dimensional gel network structure, which is influenced by both intrinsic and extrinsic factors. EWPs’ gels can be formed through physical and chemical methods, with heating being the most common approach. Researchers have recently explored novel processes to modify the gelation properties of EWPs, which have shown promising results. Importantly, EWPs are crucial components of various food formulations, including surimi and other meat- and plant-based food products. Previous studies have focused on the basic gelation properties of EWPs, but the effect of advanced technologies and intrinsic and extrinsic factors on their gelation potential have not been systematically reviewed. Hence, this review paper provides a systematic overview of the research around the gelation properties of EWPs and their application, serving as a guide for researchers and industry professionals to explore the versatility and value of EWPs as substantial food ingredients.

KEYWORDS:

• Egg white proteins
• gelation properties
• heating
• novel process
• isoelectric point
• egg-based food products

Disclosure statement

No potential conflict of interest was reported by the author(s).