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During heat treatment, the soluble milk proteins get denatured and then aggregate together or at the surface of casein micelles to form mixed aggregates. These supramolecular aggregates possess potentially useful functional properties for replacing certain food additives, but these properties are sensitive to supramolecular structure and the presence of soluble proteins. We thus developed an innovative method for characterizing the mixed milk protein aggregates. Working up from a separation system based on asymmetrical flow field-flow fractionation coupled with multiangle laser light-scattering and refractive index detectors (A4F-MALLS-DRI), we developed appropriate methods for separating different populations within heated solutions of milk proteins. This technique, when applied on a complex mixture, can separate protein aggregates over a very broad size range (5 nm–1µm), determine the size and apparent molar mass of the component structures, and quantify each population. Although developed for milk proteins, this novel technique should be extended to plant proteins, which are often aggregated, and lead to a better understanding of their functional properties.

Participants

These results were obtained as part of a doctoral thesis sponsored with funding from the Pays de la Loire regional council: the ‘PROFIL’ project, led in collaboration with UMR STLO and dairy industry partners in the public-interest research association BBA.

Publication

T. Loiseleux, A. Rolland-Sabate, C. Garnie, T. Croguennec, S. Guilois a, M. Anton, A. Riaublanc Determination of hydro-colloidal characteristics of milk protein aggregates using Asymmetrical Flow Field-Flow Fractionation coupled with Multiangle Laser Light Scattering and Differential Refractometer (AF4-MALLS-DRi). Food Hydrocolloids 74 (2018) 197-206, https://doi.org/10.1016/j.foodhyd.2017.08.012