Molecular Association State of Bovine Serum Albumin and Its Effect on Emulsifying Activity

抄録

Oil-in-water (4:6) emulsions stabilized with bovine serum albumin (BSA) (0.225 HIM), at pH 7, were used to study the effects of molecular association on the viscosity of emulsions and emulsifying activity (EA). Anions -TCA^- and -SO₄^- 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.