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Protein aggregation mechanism in UHT milk: supramolecular evidences

Rutigliano, M., Rusco, G., Picariello, G., Bulgari, O., Spadaccino, G., Gagliardi, R., Di Luccia, A., Addeo, F., la Gatta, B.
European food research & technology 2020 v.246 no.5 pp. 1081-1094
UHT milk, ambient temperature, food research, mass spectrometry, protein aggregates, sediments, storage temperature
The protein aggregation mechanism in UHT milk samples stored at ambient temperature for 1, 3 and 5 months was assessed in this study. Three phases of the UHT milks were studied: supernatants, dispersed phase and sediments. The supernatants showed a great variability, suggesting the presence of a dynamic arrangement within the protein system of UHT milk, which moves towards the formation of the sediment. The application of 2D-electrophoresis (AU-PAGEᴺᴿ-SDS-PAGEᴿ) and mass spectrometry analyses were carried out to study the main heat-induced supramolecular protein aggregates. These aggregates were found mainly in the supernatant and their composition changed along the storage, as a consequence of the medium chemical changes, which are temperature- and pH-depended, whereas the composition of the dispersed phase and sediment denoted a hierarchical mechanism of assembling.