The influence of cosolvent composition on the thermal denaturation and gelation of bovine serum albumin (BSA) has been studied. Cosolvent composition was varied by changing the ratio of glycerol to sucrose in 40 wt% cosolvent solutions containing BSA. Differential scanning calorimetry measurements on 0.5 wt% BSA solutions showed that the thermal denaturation temperature of the protein increased with increasing sucrose content. Temperature scanning dynamic shear rheology and turbidity measurements on 4 wt% BSA solutions showed that the gelation temperature and final gel strength increased with increasing sucrose concentration. These observations were attributed to the fact that sucrose was more effective than glycerol at increasing the thermal stability and attraction between globular BSA molecules through a steric exclusion effect. The molecular origin of these effects is the tendency for the system to minimize the contact area of the protein molecules with the surrounding cosolvent solution.
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