Abstract
Guanidine hydrochloride (GdnHCl) and thermal denaturation studies on lysozyme were made in the absence and the presence of a simulated honey sugar cocktail (SHSC). GdnHCl denaturation curve was shifted towards higher denaturant concentration along with an increase in value in the presence of SHSC, when studied by MRE222 nm and tryptophan fluorescence measurements. Far- and near-UV CD as well as ANS fluorescence spectra of the partially-denatured lysozyme indicated greater retention of the folded structure in the presence of SHSC. The thermal transition curve showed a shift towards the higher temperature range along with an increase in the melting temperature in the presence of SHSC, when studied by MRE222 nm and DSC measurements. Taken together, all these results suggested SHSC-induced chemical and thermal stabilization of lysozyme.
Published Version
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