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The conformational stability of ovalbumin and lysozyme in the aqueous solutions of various cosolvents

A calorimetric study

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Abstract

A thermodynamic method is reported to monitor the conformational stability of lysozyme and ovalbumin in the presence of various cosolvents. Heats of dilution of the proteins in concentrated aqueous solutions of urea, ethanol or glucose have been determined at 298.15 K by flow microcalorimetry. The pairwise enthalpic interaction coefficients of the proteins in the different solvent media are derived: They allow to gain information about the influence of the cosolvents on the interactions between two interacting hydrated molecules of a protein, hence on its conformational stability. The two proteins behave very differently in the various cosolvents. In glucose, the coefficients for ovalbumin are positive up to 3 mol kg−1 of cosolvent and then negative, while those for lysozyme are negative up to 6 mol kg−1. In urea, coefficients for ovalbumin are positive, while negative for lysozyme up to 7 mol kg1. In ethanol, coefficients for ovalbumin are almost invariant, even at the highest concentrations of cosolvent, underlining that the hydration shell of the protein is such to maintain essentially unaltered the native conformation. For lysozyme, coefficients are negative and almost invariant up to 20 mol kg−1 ethanol: Then, a jump occurs toward much more large and negative values. The observed behaviors are rationalized also on the basis of the results previously obtained for small model molecules in concentrated solutions of urea, ethanol or glucose. The differences between the two proteins are explained in terms of the effects of the cosolvents on hydrophilic and hydrophobic interactions and account for the structural characteristics of each protein. In fact, notwithstanding both are globular proteins, they are differently packed and that could make them to react differently toward the action of a given cosolvent.

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  1. Department of Chemistry, University Federico II of Naples, Complesso Universitario Monte S. Angelo, Via Cintia, 80126, Naples, Italy

    Marcella Niccoli & Giuseppina Castronuovo

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  1. Marcella Niccoli
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  2. Giuseppina Castronuovo
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Correspondence to Marcella Niccoli.

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Niccoli, M., Castronuovo, G. The conformational stability of ovalbumin and lysozyme in the aqueous solutions of various cosolvents. J Therm Anal Calorim 123, 2149–2156 (2016). https://doi.org/10.1007/s10973-015-4921-5

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  • DOI: https://doi.org/10.1007/s10973-015-4921-5

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