BLGA protein solutions at high ionic strength: Vanishing attractive interactions and frustrated aggregation

作者: R Piazza , S Iacopini , M Galliano

DOI: 10.1209/EPL/I2002-00170-7

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摘要: Aggregation in disperse systems is generally induced or promoted by screening of the electrostatic interactions via addition salts. By combining static and dynamic light scattering results from solutions a simple milk protein, β-lactoglobulin A (BLGA), we show that clustering protein can sometimes be conversely hampered electrolytes. This peculiar behaviour fully correlated with marked non-monotonic trend interparticle as function solution ionic strength. Data obtained conditions where charge has similar absolute value but opposite sign suggest depend on specific surface distribution.

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