Abstract
In this research, the effect of sorbitol on the structure, thermal stability and activity of native carboxypeptidase A from bovine pancreas was investigated using ultraviolet–visible (UV–Vis) spectroscopy, spectroflorimertry, circular dichroism (CD) and kinetic techniques, molecular docking and simulation. The results of the measurement of fluorescence at two temperatures (308 and 318 K) showed that sorbitol quenched the intrinsic fluorescence of carboxypeptidase A with the static mode. Further, based on the calculation of some thermodynamic parameters including Gibbs free-energy, enthalpy and entropy changes, the binding process of sorbitol to carboxypeptidase A was spontaneous and the main force in stabilizing the complex consisted of the van der Waals and hydrogen interactions. The molecular docking results were also the same as those obtained for quenching fluorescence. Further, the CD spectra and fluorescence results revealed that sorbitol influenced the carboxypeptidase A structure. The thermal stability studies of the carboxypeptidase A–sorbitol complex also showed that the transition temperature (Tm) of carboxypeptidase A was increased with the raising concentration of sorbitol. In addition, the results of kinetic studies showed that sorbitol increased the Vmax and kcat/Km values, so it could increase the activity and stability of carboxypeptidase A.
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