Acta Biologica Hungarica
Volume/Issue:
Volume 63: Issue 3
Thermodynamic and kinetic processes during the unfolding of BSA in the presence of the mycotoxin patulin
Authors: Eszter Horváth 1 , Nikoletta Kálmán 1 , M. Pesti 1 , K. Iwata 2 , and S. Kunsági-Máté
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  • 1 University of Pécs Department of General and Environmental Microbiology, Faculty of Sciences H-7624 Pécs Ifjúság u. 6 Hungary
  • 2 Gakushuin University Department of Chemistry, Faculty of Science 1-5-1 Mejiro, Toshima-ku Tokyo 171-8588 Japan
  • 3 University of Pécs Department of General and Physical Chemistry, Faculty of Sciences H-7624 Pécs Ifjúság u. 6 Hungary
  • 4 János Szentágothai Research Center H-7624 Pécs Ifjúság u. 34 Hungary
DOI:
https://doi.org/10.1556/abiol.63.2012.3.9
Page Count:
389–398
Publication Date:
01 Sep 2012
Online Publication Date:
10 Sep 2012
Article Category:
Research Article
Restricted access

The effects of the mycotoxin patulin on the thermodynamics and kinetics of the transition of bovine serum albumin (BSA) in aqueous solution were studied by Differential Scanning Calorimetry and Photoluminescence methods. Results show that in the presence of patulin, the free enthalpy change during the transition of BSA was decreased by an average of ∼ 46 kJ/mol, the free energy change was decreased by ∼ 4 kJ/mol, and the activation energy fell from ∼ 1546 to ∼ 840 kJ/mol. These results indicate that the bioactivity of patulin is based on the kinetic rather than on the thermodynamic properties of the transition. This is the first evidence of the direct interaction of patulin with the free thiol-containing BSA, a process which could contribute to the adverse cyto- and genotoxic effects induced by patulin.

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Cover Acta Biologica Hungarica
Acta Biologica Hungarica
Print ISSN:
0236-5383
Online ISSN:
1588-256X
Keywords:
Patulin; BSA unfolding; transition thermodynamics and kinetics; free enthalpy; activation energy

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