Abstract
Oil-in-water (4:6) emulsions stabilized with bovine serum albumin (BSA) (0.225 mM), at pH 7, were used to study the effects of molecular association on the viscosity of emulsions and emulsifying activity (EA). Anions -TCA– and -S04 had different effects on the intermolecular association of BSA. Aggregates (A) of BSA comprising A1, A2, A3, A4, A5, A6 and A7 were detected in the control and the anion (100 mM) containing emulsions. The extent of association of BSA was in the order; control >-SO4>-TCA–. The EA also showed the same order whereas the viscosity of emulsions showed the reverse order. High energy input per unit volume (>684 106 J.m-3) caused molecular dissociation and a concomitant decrease in EA. Apparently, a certain degree of association is required for EA of BSA.
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