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sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured BlTreA, probably due to the fact that these sugars favor the formation of tertiary architectures. Sorbitol is more effective than any of the other two sugars
sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured enzyme. Far-UV CD measurements demonstrate the ability of sugar osmolytes to shift the secondary structure of guanidine hydrochloride-denatured enzyme towards near-native conformations. ANS fluorescence intensity measurements reveal a reduction of exposed hydrophobic surfaces upon the treatment of denatured enzyme with sugar osmolytes