Modifying the Functional Properties of Egg Proteins Using Novel Processing Techniques: A Review.

Abstract

Egg proteins can be used in a wide range of food products, owing to their excellent foaming, emulsifying, and gelling properties. Another important functional property is the susceptibility of egg proteins to enzymatic hydrolysis, as protein digestion is closely related to its nutritional value. These functional properties of egg proteins are likely to be changed during food processing. Conventional thermal processing can easily induce protein denaturation and aggregation and consequently reduce the functionality of egg proteins due to the presence of heat-labile proteins. Accordingly, there is interest from the food industry in seeking novel nonthermal or low-thermal techniques that sustain protein functionality. To understand how novel processing techniques, including high hydrostatic pressure, pulsed electric fields, ionizing radiation, ultraviolet light, pulsed light, ultrasound, ozone, and high pressure homogenization, affect protein functionality, this review introduces the mechanisms involved in protein structure modification and describes the structure-functionality relationships. Novel techniques differ in their mechanisms of protein structure modification and some have been shown to improve protein functionality for particular treatment conditions and product forms. Although there is considerable industrial potential for the use of novel techniques, further studies are required to make them a practical reality, as the processing of egg proteins often involves other influencing factors, such as different pH and the presence of other food additives (for example, salts, sugar, and polysaccharides).