The effect of hydrotropic agents on the heat coagulation of bovine serum albumin.
The effect of two hydrotrophic solubilizers on the heat coagulation of bovine serum albumin (BSA) has been investigated. Photon correlation spectroscopy indicated possible unfolding of BSA molecules in solutions of sodium benzoate and sodium salicylate at 25 degrees C. The effect of these hydrotropes on the heat coagulation of BSA was concentration-dependent. Relatively low concentrations stabilized the protein structure as indicated by the increase in the transition temperature(Tm) and induced gelation at temperatures and BSA concentrations lower than those required in the absence of hydrotropes. Higher concentrations of the hydrotropes considerably reduced Tm and inhibited gelation of BSA, the effect of sodium salicylate being more pronounced, as was the lower aggregation rate of BSA. The behaviour of these hydrotropes as protein denaturants differs from that of neutral electrolytes but is similar to that of concentrated solutions of urea.
Saleh
A M
AM
Department of Pharmaceutics, Faculty of Pharmacy, University of Alexandria, Egypt.
Florence
A T
AT
Whateley
T L
TL
el-Khordagui
L K
LK
D001565:Benzoates / Q000032:analysis; D019817:Benzoic Acid; D003460:Crystallization; D005612:Freeze Drying; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D012710:Serum Albumin, Bovine / Q000032:analysis*; D012980:Sodium Salicylate / Q000032:analysis
D001565:Benzoates; D012710:Serum Albumin, Bovine; D019817:Benzoic Acid; D012980:Sodium Salicylate