Abstract
The current study focuses on the experimental evidence to describe the molecular mechanism by which the sugars modulate the thermodynamic stability of hen egg-white lysozyme (Lyz) at pH 2.3. Analysis of thermal and chemical denaturation curves of Lyz under variable concentrations of sugar (trehalose, sucrose, maltose, glucose, ribose, glycerol) at pH 2.3 depicted important results: (i) sugar increases the thermodynamic stability of Lyz, and it typically tracks the order as: trehalose > sucrose > maltose > glucose > ribose > glycerol, and (ii) sugar increases the thermodynamic stability of Lyz via preferential exclusion of sugar at the protein surface, but the repulsive enthalpic interactions of sugar with protein also add to the sugar-mediated increase in thermodynamic stability of the protein. Analysis of the sugar effect on denaturant concentration dependent denaturation free energy of Lyz at pH 2.3 revealed that the sugar counteracts the denaturant (urea, guanidinium chloride (GdnCl)) efficacy to decrease the thermodynamic stability of Lyz. Furthermore, the counteraction efficiency of sugar on denaturant impact to decrease thermodynamic stability of Lyz typically tracks the order as: trehalose > sucrose > maltose > glucose > ribose > glycerol.
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