Journal
BIOCHEMISTRY
Volume 54, Issue 23, Pages 3594-3603Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.5b00415
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Funding
- Council of Scientific and Industrial Research, India [37(1603)/13/EMRII, 37(1604)/13/EMRII]
- National Institute of Diabetes and Digestive and Kidney Diseases
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The reversible thermal denaturation of apo a-lactalbumin and lysozyme was monitored via measurement of changes in absorbance and ellipticity in the presence of varying concentrations of seven mono- and oligosaccharides: glucose, galactose, fructose, sucrose, trehalose, raffinose, and stachyose. The temperature dependence of the unfolding curves was quantitatively accounted for by a two-state model, according to which the free energy of unfolding is increased by an amount that is independent of temperature and depends linearly upon the concentration of added saccharide. The increment of added unfolding free energy per mole of added saccharide was found to depend approximately linearly upon the extent of oligomerization of the saccharide. The relative strength of stabilization of different saccharide oligomers could be accounted for by a simplified statistical-thermodynamic model attributing the stabilization effect to volume exclusion deriving from steric repulsion between protein and saccharide molecules.
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