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Unfolding mechanism and stability of immobilized papain

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Abstract

The thermal stability of papain in free solution or immobilized on CPC-silica has been investigated by DSC. At neutralpH, in both conditions, the protein undergoes a thermal transition which corresponds to the sum of two transitions associated with the unfolding of the two domains of the protein. At lowpH, in the case of immobilized papain, only one transition is observed.

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Authors and Affiliations

  1. Istituto di Studi Chimico-Fisici di Macromolecole Sintetiche e Naturali, C.N.R., Via De Marini 6, 16149, Genova

    G. Rialdi

  2. ENICHEM Istituto G. Donegani, Via Fauser 4, 28100, Novara, Italy

    E. Battistel

Authors
  1. G. Rialdi
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  2. E. Battistel
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Rialdi, G., Battistel, E. Unfolding mechanism and stability of immobilized papain. Journal of Thermal Analysis 47, 17–25 (1996). https://doi.org/10.1007/BF01982682

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  • DOI: https://doi.org/10.1007/BF01982682

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