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Protein denaturation kinetic processes of a simple and a complex reaction mechanism analyzed by an iso-conversional method

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Abstract

The protein denaturation kinetic processes of a simple and a complex reaction mechanism represented by bovine serum albumin and hen egg-white lysozyme were analyzed by an iso-conversional method using differential scanning calorimetry. After differential scanning calorimetry using the iso-conversional method, the results were found to pose distinct contrasts between the two proteins. Bovine serum albumin showed an increasing peak temperature of the transition as the scan rate and protein concentration increased, whereas hen egg-white lysozyme exhibited almost constant peak temperature. The differential scanning calorimetry transition of bovine serum albumin was calorimetrically irreversible, while one part of hen egg-white lysozyme denaturation process was irreversible during which aggregation occurred and the other part was reversible. The iso-conversional method indicated that the value of bovine serum albumin apparent activation energy hardly varied with the degree of conversion, which showed that the denaturation kinetic process should conform to single reaction model. Using the master plots method, the most possible kinetic model for bovine serum albumin denaturation might be described by F n kinetic model. On the contrary, the hen egg-white lysozyme value of apparent activation energy decreased with the increase of degree of conversion. It was not a process involving the two standard reversible states, and can be described by the simple Lumry–Eyring model. The iso-conversional method provides new opportunities in exploring a simple and a complex reaction mechanism 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 the 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, Yunwen Liu & Cunxin Wang

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  1. Xiaomin Cao
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  2. Yun Tian
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Correspondence to Yun Tian.

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Cao, X., Tian, Y., Wang, Z. et al. Protein denaturation kinetic processes of a simple and a complex reaction mechanism analyzed by an iso-conversional method. J Therm Anal Calorim 117, 1489–1495 (2014). https://doi.org/10.1007/s10973-014-3872-6

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  • DOI: https://doi.org/10.1007/s10973-014-3872-6

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