THERMODYNAMIC AND KINETIC PROCESSES DURING THE UNFOLDING OF BSA IN THE PRESENCE OF THE MYCOTOXIN PATULIN

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 similar to 46 kJ/mol, the free energy change was decreased by similar to 4 kJ/mol, and the activation energy fell from similar to 1546 to similar 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.