Thermal denaturation and functional properties of egg proteins in the presence of hydrocolloid gums

The aim of this study was to investigate the thermal stability, foaming and emulsifying properties of egg white and egg yolk constituents (egg yolk plasma and egg yolk granule) in the presence of hydrocolloid gums. Differential scanning calorimetry was used to examine the thermal stability of proteins. Heat denaturation of proteins were not influenced from the presence of anionic pectin and i-carrageenan and neutral guar gum. The residual denaturation enthalpy was observed to decrease as a result of protein aggregation. Thermal treatment have been observed to be detrimental to foaming capacity of egg white, while foam stability was improved. The foam stability was enhanced in the presence of pectin which may provide a strong viscoelastic film together with protein. Emulsifying activity and stability and of egg yolk granule and plasma were reduced after heat treatment. The presence of guar gum improved the emulsifying properties, while both pectin and guar gum reduced the rate and extend of creaming of egg yolk protein - stabilized proteins after heat treatment. (c) 2006 Elsevier Ltd. All rights reserved.