Interfacial properties of heat-treated ovalbumin

The interfacial properties (kinetics of adsorption at the air/water interface, rheology of the interfacial layer) of ovalbumin molecules, unheated or previously heat-denatured in solution (10 g L−1, pH 7, NaCl 50 mM) under controlled conditions (up to 40 min at 80 °C), were investigated. Heat treatments induced the formation of covalent aggregates which surface exhibits a higher hydrophobicity and an increased exposition of sulfhydryl groups when compared to native ovalbumin (unheated). Although they have a larger hydrodynamic size, aggregates adsorb as fast as native ovalbumin at the air/water interface. However, aggregates are able to established rapid contacts in the interfacial layer as shown by the fast increase of both surface pressure and shear elastic constant. In contrast, native ovalbumin needs longer time to developed intermolecular contacts and exhibits lower foam stability even if the shear elastic constant on aging reached higher value than for ovalbumin aggregates.

Compared to native ovalbumin, heat-denatured/aggregated ovalbumin molecules exhibit a more open structure (higher hydrophobicity, exposed free sulfhydryl) favoring rapid contacts at the air/water interface that prevent premature foam destabilization mechanisms.Figure optionsDownload as PowerPoint slide