Interactions of high methoxyl pectin with whey proteins at oil/water interfaces at acid pH

The interactions between whey protein isolate (WPI) and high methoxyl pectin (HMP) at pH 3.5 were investigated in situ using ultrasound (US) and diffusing wave spectroscopy (DWS). HMP was added to 10% oil-in-water emulsions containing 1% WPI. At neutral pH, no protein-pectin interactions were observed as both molecules are negatively charged, while at pH 3.5 bridging flocculation occurred via electrostatic interactions. Four different stages were distinguished during the addition of HMP in WPI-stabilized emulsions at pH 3.5. At a concentration below a critical value, no interactions were observed. At concentrations >0.02% HMP, a change in the l factor indicated a change in the ordering of the emulsion droplets, influenced by long-range interactions. At higher concentrations (in the range between 0.04 and 0.06% HMP), attenuation showed significant changes in the surface of the oil droplets, changes which affected the droplet-droplet interactions. At pectin concentrations >0.05%, attenuation of sound and 1/l* decreased, while velocity of sound and particle size increased, as a result of bridging flocculation. These results demonstrated for the first time that methods such as US and DWS combined permit the observation of the early stages of the interactions between two biopolymers at the interface. This is significant in light of increasing efforts in engineering complex interfacial layers.