Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability
作者： Bongkosh Vardhanabhuti , Umut Yucel , John N. Coupland , E. Allen Foegeding
DOI: 10.1016/J.FOODHYD.2008.09.006
关键词: Denaturation (biochemistry) 、 Biopolymer 、 Thermal stability 、 Chromatography 、 Chemistry 、 Turbidity 、 Whey protein 、 Electrophoresis 、 Beta-lactoglobulin 、 Size-exclusion chromatography
摘要: Abstract The effect of interactions between β-lactoglobulin (β-LG) and dextran sulfate (DS) on thermal stability at near neutral pH was investigated. Samples containing 6% w/w β-LG DS ( M w = 5–500 kDa) different biopolymer weight ratios, (5.6–6.2), NaCl concentrations (0–30 mM) were heated 85 °C for 15 min. Turbidity results showed that the presence appropriate ratio significantly lowered turbidity β-LG. Solutions DS:β-LG ratios 0.02 or less improved heat as indicated by decreased turbidity. Analysis unheated mixture size exclusion chromatography coupled with multi-angle laser light scattering (SEC–MALLS) an interaction DS. aggregates increased decreased. β-LG–DS had a greater negative charge seen from electrophoretic mobility measurement. Addition 30 mM inhibited complex formation reducing β-LG, suggesting electrostatic in nature. Other than property, amount native appeared to be major factor determining how altered heat-induced aggregation. denaturation temperature indicating did not improve stabilizing its state but rather altering provide information will facilitate application whey proteins polysaccharides functional ingredients foods beverages.
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