title: Modification of functional properties of egg-white proteins.
abstract: Egg-white proteins are extensively utilised as food ingredients due to their unique functional properties. Several attempts have been made in order to improve the functional properties of egg-white proteins and to identify the optimal formulations for unique food products. Experimental data proves that controlled denaturation of egg-white proteins can have a beneficial impact on various functional applications in the food industry such as emulsifying ability, heat stability, and gelation. This review describes the effect of heat-induced denaturation on protein structure and functionality. Studies on the impact of Maillard reaction, which aim to elucidate the structure-function relationship of egg-white proteins, are presented. A novel approach which could be the basis for the development of new methods aiming to improve the functional properties of egg-white proteins is also discussed.
authors.affiliation: School of Life Sciences, Heriot-Watt University, Edinburgh EH14 4AS, Scotland. L.Campbell@hw.ac.uk
authors.forename: Lydia
authors.initials: L
authors.lastname: Campbell
authors.forename: Vassilios
authors.initials: V
authors.lastname: Raikos
authors.forename: Stephen R
authors.initials: SR
authors.lastname: Euston
mesh_terms: D004527:Egg Proteins / Q000737:chemistry* / Q000502:physiology*; D005782:Gels; D006358:Hot Temperature; D015416:Maillard Reaction; D017510:Protein Folding; D012995:Solubility; D013329:Structure-Activity Relationship
chemical_list: D004527:Egg Proteins; D005782:Gels