A Comparative Analysis of Protein Stabilizing Potential of Honey and Simulated Honey Sugar Cocktail

Urea and thermal denaturations of bovine serum albumin (BSA) were studied in the absence and the presence of honey or simulated honey sugar cocktail (SHSC) using far-UV CD and ANS fluorescence spectroscopy. Presence of 20% (w/v) honey or SHSC in the incubation mixture shifted the urea transition curve towards higher urea concentrations, being higher in the presence of honey and transformed the two-step, three-state transition into a single-step, two-state transition. A comparison of the far-UV CD and the ANS fluorescence spectra of 4.6 M urea-denatured BSA (U-BSA) in the absence and the presence of 20% (w/v) honey or SHSC suggested greater stabilizing potential of honey than SHSC, as U-BSA maintained native like conformation in the presence of 20% (w/v) honey. Furthermore, thermal transition curves of BSA were also shifted towards higher temperature range in the presence of 20% (w/v) SHSC and honey, showing greater shift in the presence of honey. The far-UV CD spectra of the heat-denatured BSA also showed greater stabilization in the presence of honey. Taken together all these results suggested greater protein stabilizing potential of honey than SHSC against chemical and thermal denaturations of BSA.