Vb. Galazka et al., INFLUENCE OF HIGH-PRESSURE ON BOVINE SERUM-ALBUMIN AND ITS COMPLEX WITH DEXTRAN SULFATE, Journal of agricultural and food chemistry, 45(9), 1997, pp. 3465-3471
High-pressure processing of bovine serum albumin (BSA) solutions (0.1-
1 wt % protein, pH ?) has shown decreasing protein surface hydrophobic
ity with increasing pressure, which is further reduced in the presence
of dextran sulfate (DS) (BSA:DS weight ratio of 2:1 and 4:1). The tot
al calorimetric enthalpy Delta H for pure BSA is substantially reduced
after treatment at 600 MPa, and both the endothermic peak temperature
and the value of Delta H for BSA + DS is reduced under the same treat
ment conditions. Size exclusion chromatography indicates extensive pre
ssure-induced protein unfolding and aggregation during BSA treatment a
t 400 MPa. Complexation with polysaccharide at low ionic strength prot
ects the globular protein against pressure-induced aggregation. The lo
ss of the protective effect of DS on addition of electrolyte (0.1 M Na
Cl) is consistent with the predominantly electrostatic character of th
e protein-polysaccharide interaction.