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• W2944500516 abstract "Polysorbates are widely used in food and cosmetic products and pharmaceuticals for emulsion stabilization, preventing surface absorption and as stabilizers against protein aggregation. But their impacts on the secondary structure and conformational stabilization of bovine casein, a typical intrinsically disordered protein (IDP), have not been fully addressed so far, which is crucial to evaluate the performance of polysorbates as stabilizer for food products containing bovine casein. Here, we assessed the effects of polysorbate 20 (PS-20) and polysorbate 80 (PS-80) on the secondary structure and conformation of bovine casein micelles by fluorescence and circular dichroism spectra, dynamic light scattering (DLS), small angle x-ray scattering (SAXS) and transition electron microscopy (TEM). In addition, three-dimensional structure of bovine β-casein, a major component of bovine casein, was predicted using homology modelling with the aid of PSIPRED server to outline the potential binding sites of bovine casein for polysorbates. We found that PS-20 presented a higher binding affinity (Ka = 3.76 × 106 M−1) and stoichiometry (n = 0.89) to bovine casein than that of PS-80 (Ka = 1.45 × 106 M−1, n = 0.45). The α-helical and β-sheet conformation of bovine casein was increased upon binding with PS-20 whereas binding of PS-80 had little impact on secondary structural elements of this milk protein. Moreover, bovine casein micelles were dissociated by PS-20, which co-assembled into micellar-like particles with a rather spherical shape and homogenous size distribution ranging from 20 to 50 nm in diameter. The lauric acid chains may bind with disordered regions connected by colloidal calcium phosphate (CCP) as the core, and the sorbitan groups may associate with N-terminal outwards as the shell providing hydrophilicity to stabilize the polysorbates-casein complex. On the contrary, PS-80 led to formation of sponge-like aggregates with the radius ranging from 200 to 500 nm as indicated by the data of DLS, SAXS and TME. We assume that the stearic hindrance originating from oleic group and the kink due to the cis-double bond in the sidechain of PS-80 contribute to the aggregation of bovine casein induced by PS-80. Furthermore, a tentative binding mechanism of polysorbates with bovine casein micelles and model of complexes were proposed to illustrate the polysorbates-induced structural change and conformational stabilization of bovine casein micelles. Thus, we argue that the difference in binding of polysorbates to bovine casein may influence the functional properties (emulsification, foaming ability, etc) of milk protein. Taken together, we suggest that PS-20 may be preferred option as potential protein stabilizer for dairy products, and careful consideration should be given when selecting PS-80 as stabilizer for bovine casein, a typical IDP." @default.
• W2944500516 created "2019-05-16" @default.
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• W2944500516 date "2019-11-01" @default.
• W2944500516 modified "2023-10-14" @default.
• W2944500516 title "How much can we trust polysorbates as food protein stabilizers - The case of bovine casein" @default.
• W2944500516 cites W1584551345 @default.
• W2944500516 cites W1598477851 @default.
• W2944500516 cites W1927136751 @default.
• W2944500516 cites W1930279317 @default.
• W2944500516 cites W1964433740 @default.
• W2944500516 cites W1973744073 @default.
• W2944500516 cites W1975596071 @default.
• W2944500516 cites W1977444364 @default.
• W2944500516 cites W1981907317 @default.
• W2944500516 cites W1982126789 @default.
• W2944500516 cites W1983057339 @default.
• W2944500516 cites W1983709263 @default.
• W2944500516 cites W1985446400 @default.
• W2944500516 cites W1986117705 @default.
• W2944500516 cites W1991485241 @default.
• W2944500516 cites W1993374679 @default.
• W2944500516 cites W1995586409 @default.
• W2944500516 cites W1999401096 @default.
• W2944500516 cites W2004377868 @default.
• W2944500516 cites W2005112107 @default.
• W2944500516 cites W2006474646 @default.
• W2944500516 cites W2020556156 @default.
• W2944500516 cites W2037385269 @default.
• W2944500516 cites W2038239888 @default.
• W2944500516 cites W2040132500 @default.
• W2944500516 cites W2040184556 @default.
• W2944500516 cites W2046670381 @default.
• W2944500516 cites W2048691768 @default.
• W2944500516 cites W2051131010 @default.
• W2944500516 cites W2053674858 @default.
• W2944500516 cites W2064886412 @default.
• W2944500516 cites W2068201004 @default.
• W2944500516 cites W2071306814 @default.
• W2944500516 cites W2073059515 @default.
• W2944500516 cites W2075329646 @default.
• W2944500516 cites W2075359431 @default.
• W2944500516 cites W2075849880 @default.
• W2944500516 cites W2077175042 @default.
• W2944500516 cites W2083094311 @default.
• W2944500516 cites W2090685806 @default.
• W2944500516 cites W2091728388 @default.
• W2944500516 cites W2114698004 @default.
• W2944500516 cites W2116034627 @default.
• W2944500516 cites W2117782820 @default.
• W2944500516 cites W2118894252 @default.
• W2944500516 cites W2120675400 @default.
• W2944500516 cites W2122159871 @default.
• W2944500516 cites W2123382940 @default.
• W2944500516 cites W2123663818 @default.
• W2944500516 cites W2133992781 @default.
• W2944500516 cites W2138376010 @default.
• W2944500516 cites W2148710218 @default.
• W2944500516 cites W2153187042 @default.
• W2944500516 cites W2156343873 @default.
• W2944500516 cites W2160127456 @default.
• W2944500516 cites W2162980545 @default.
• W2944500516 cites W2163097259 @default.
• W2944500516 cites W2199336171 @default.
• W2944500516 cites W2272891930 @default.
• W2944500516 cites W2298471346 @default.
• W2944500516 cites W2321189783 @default.
• W2944500516 cites W237049291 @default.
• W2944500516 cites W2484882412 @default.
• W2944500516 cites W2489181495 @default.
• W2944500516 cites W2492728286 @default.
• W2944500516 cites W2515074928 @default.
• W2944500516 cites W2622584234 @default.
• W2944500516 cites W2707646777 @default.
• W2944500516 cites W2739999456 @default.
• W2944500516 cites W2746604201 @default.
• W2944500516 cites W2768295294 @default.
• W2944500516 cites W2773786937 @default.
• W2944500516 cites W2784152273 @default.
• W2944500516 cites W2790042864 @default.
• W2944500516 cites W2792955528 @default.
• W2944500516 cites W2810498648 @default.
• W2944500516 cites W2907384381 @default.
• W2944500516 doi "https://doi.org/10.1016/j.foodhyd.2019.05.013" @default.
• W2944500516 hasPublicationYear "2019" @default.
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