Abstract
The effects of NaCl, dextran sulfate (DS), and initial protein concentration on thermal stability of β-lactoglobulin ( β-LG) and α-lactalbumin ( α-LA) at pH 6.8 were investigated. NaCl was the biggest factor in accelerating protein aggregation as shown by an increase in turbidity, molecular size, and a decrease in protein solubility. DS at low concentration showed a protective effect against aggregation. Evidence suggested some degree of interaction between β-LG and DS. At higher concentration, phase separation between biopolymers favored aggregation, which resulted in an increase in turbidity and a reduction in protein solubility.
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