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• W2078956670 abstract "Intermolecular disulfide bond formation in pure β-lactoglobulin (β-Lg) B and in its 1:1 mixture with α-lactalbumin (α-La), heated at 85 °C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry. Disulfide bonding between β-Lg monomers was more extensive than reported in the literature for a temperature of 68.5 °C, including formation of trimers connected by two of the three adjacent cysteines, C106/C119/C121. The participation of the different thiol groups in disulfide bonds appeared to depend on their location in the native structure, with surface-located cysteines more involved than internally located ones. This also applied to α-La−β-Lg interactions, where the predominant participants were the surface-located αC111, αC120, αC61, and αC6. The least active participant was αC28, suggesting that it becomes sterically inaccessible during unfolding of the protein. High ionic strength apparently promoted disulfide bonding. The order of cysteine participation at the high ionic strength was similar to that at low ionic strength, with fewer native-location bonds observed and a lower activity of some groups, such as β-C106/C119/C121 and αC61. Keywords: Whey proteins; α-lactalbumin; β-lactoglobulin; heat-induced aggregation; disulfide bonds; cysteine; thiol; mass spectrometry" @default.
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• W2078956670 date "2003-12-01" @default.
• W2078956670 modified "2023-10-16" @default.
• W2078956670 title "Steric Effects Governing Disulfide Bond Interchange during Thermal Aggregation in Solutions of β-Lactoglobulin B and α-Lactalbumin" @default.
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• W2078956670 doi "https://doi.org/10.1021/jf034582q" @default.
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