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Stability of bovine serum albumin at different pH

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Summary

The effect of pH on the thermal denaturation of BSA containing fatty acids was studied by use of differential scanning calorimetry (DSC). Thermal scanning of BSA aqueous solutions gave various types of DSC curves depending on the protein concentration and on the pH. The broad bimodal endothermic transition was suggested to be connected with loose protein structure in contradistinction to single peak for compact molecule structure. The propensity toward precipitation at pH conditions ranging from 3.8 to 5 was observed. A scan-rate independent and partly reversible behavior of the thermal heating of BSA was found. Deconvolution of DSC traces in non-two-state model with assumption of two- or three-component transition allowed to study the effect of pH on different parts of BSA molecule.

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Authors and Affiliations

  1. University of Silesia, A. Chełkowski’ Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland

    Anna Michnik

  2. University of Silesia, A. Chełkowski’ Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland

    Katarzyna Michalik

  3. University of Silesia, A. Chełkowski’ Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland

    Zofia Drzazga

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  1. Anna Michnik
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  2. Katarzyna Michalik
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  3. Zofia Drzazga
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Michnik, A., Michalik, K. & Drzazga, Z. Stability of bovine serum albumin at different pH. J Therm Anal Calorim 80, 399–406 (2005). https://doi.org/10.1007/s10973-005-0667-9

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  • DOI: https://doi.org/10.1007/s10973-005-0667-9

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