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Protein aggregation mechanism in UHT milk: supramolecular evidences

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Abstract

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.

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Rutigliano, M., Rusco, G., Picariello, G. et al. Protein aggregation mechanism in UHT milk: supramolecular evidences. Eur Food Res Technol 246, 1081–1094 (2020). https://doi.org/10.1007/s00217-020-03474-3

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  • DOI: https://doi.org/10.1007/s00217-020-03474-3

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