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BSA denaturation in the absence and the presence of urea studied by the iso-conversional method and the master plots method

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Abstract

The kinetics of bovine serum albumin (BSA) denaturation in the absence and the presence of urea was studied by the iso-conversional method and the master plots method using differential scanning calorimetry (DSC). The observed denaturation process was irreversible and approximately conformed to the simple order reaction, and the denaturation did not follow rigorously first-order kinetic model or other integral order reaction models. The denaturation temperature (T m), apparent activation energy (E a), approximate order of reaction (n), and pre-exponential factor (A) all distinctly decreased as the 2 mol L−1 urea was added, which indicated that the urea accelerated the denaturation process of BSA and greatly reduced thermal and kinetic stability of BSA. This study also demonstrated that the iso-conversional method, in combination with the master plots method, provides a valuable and useful approach to the study of the kinetic process of protein denaturation.

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Acknowledgements

This study was financially supported by the National Natural Science Foundation of China (Grant Nos. 20373050 and 30600116), the Natural Science Foundation of Hubei, and China Postdoctoral Science Foundation.

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Authors and Affiliations

  1. Changsha Environmental Protection College, ChangSha, 410004, Hunan, China

    Xiaomin Cao

  2. Environmental Monitoring Center of Hunan Province, ChangSha, 410014, Hunan, China

    Yun Tian

  3. College of Chemistry and Molecular Science, Wuhan University, Wuhan, 430072, Hubei, China

    Zhiyong Wang, Yuwen Liu & Cunxin Wang

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  1. Xiaomin Cao
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Correspondence to Xiaomin Cao.

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Cao, X., Tian, Y., Wang, Z. et al. BSA denaturation in the absence and the presence of urea studied by the iso-conversional method and the master plots method. J Therm Anal Calorim 102, 75–81 (2010). https://doi.org/10.1007/s10973-010-0773-1

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