Influence of high pressure on bovine serum albumin and its complex with dextran sulfate

被引:56
作者
Galazka, VB
Ledward, DA
Sumner, IG
Dickinson, E
机构
[1] BBSRC, FOOD RES INST, READING RG6 2EF, BERKS, ENGLAND
[2] UNIV LEEDS, PROCTER DEPT FOOD SCI, LEEDS LS2 9JT, W YORKSHIRE, ENGLAND
关键词
protein-polysaccharide interaction; high-pressure processing; surface hydrophobicity; protein aggregation; differential scanning calorimetry; size exclusion chromatography;
D O I
10.1021/jf9700642
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
High-pressure processing of bovine serum albumin (BSA) solutions (0.1-1 wt % protein, pH ?) has shown decreasing protein surface hydrophobicity 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 total 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 treatment conditions. Size exclusion chromatography indicates extensive pressure-induced protein unfolding and aggregation during BSA treatment at 400 MPa. Complexation with polysaccharide at low ionic strength protects the globular protein against pressure-induced aggregation. The loss of the protective effect of DS on addition of electrolyte (0.1 M NaCl) is consistent with the predominantly electrostatic character of the protein-polysaccharide interaction.
引用
收藏
页码:3465 / 3471
页数:7
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