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The effect of physiological conditions on the surface structure of proteins: Setting the scene for human digestion of emulsions
Institute of Food Research, Norwich Research Park, NR4 7UA, Colney, UK
* e-mail: Julia.Maldonado-Valderrama@bbsrc.ac.uk
Accepted: 19 January 2009
Published online: 8 March 2009
Understanding and manipulating the interfacial mechanisms that control human digestion of food emulsions is a crucial step towards improved control of dietary intake. This article reports initial studies on the effects of the physiological conditions within the stomach on the properties of the film formed by the milk protein ( -lactoglobulin) at the air-water interface. Atomic force microscopy (AFM), surface tension and surface rheology techniques were used to visualize and examine the effect of gastric conditions on the network structure. The effects of changes in temperature, pH and ionic strength on a pre-formed interfacial structure were characterized in order to simulate the actual digestion process. Changes in ionic strength had little effect on the surface properties. In isolation, acidification reduced both the dilatational and the surface shear modulus, mainly due to strong repulsive electrostatic interactions within the surface layer and raising the temperature to body temperature accelerated the rearrangements within the surface layer, resulting in a decrease of the dilatational response and an increase of surface pressure. Together pH and temperature display an unexpected synergism, independent of the ionic strength. Thus, exposure of a pre-formed interfacial -lactoglobulin film to simulated gastric conditions reduced the surface dilatational modulus and surface shear moduli. This is attributed to a weakening of the surface network in which the surface rearrangements of the protein prior to exposure to gastric conditions might play a crucial role.
PACS: 68.35.Ct Interface structure and roughness – / 82.37.Gk STM and AFM manipulations of a single molecule – / 68.03.-g Gas-liquid and vacuum-liquid interfaces –
© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg, 2009