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Reactivation of GdnHCl-denatured BlTreA in the presence of various concentrations of sugar osmolytes. Reactivation was initiated by diluting the unfolded enzyme into the standard buffer (50 mM Hepes-NaOH buffer, pH 8.0) in the absence (control) and presence of various concentrations of sugars, including sorbitol (a), sucrose (b), and trehalose (c). TreA activity was measured at the indicated times and the enzymatic activity of native enzyme was taken as 100%.
