Molecular Association State of Bovine Serum Albumin and Its Effect on Emulsifying Activity(Food & Nutrition)

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概要

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• 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 -SO^-_4 had different effects on the intermolecular association of BSA. Aggregates (A) of BSA comprising A_1, A_2, A_3, A_4, A_5, A_6 and A_7 were detected in the control and the anion (100 mM) containing emulsions. The extent of association of BSA was in the order; control > -SO^-_4 > -TCA-. The EA also showed the same order whereas the viscosity of emulsions showed the reverse order. High energy input per unit volume (> 684 10^6 J・m^<-3>) caused molecular dissociation and a concomitant decrease in EA. Apparently, a certain degree of association is required for EA of BSA.

• 社団法人日本農芸化学会の論文
• 1988-05-23

著者

• Haque Z

  Cornell Univ. Ny Usa

• Haque Z

  Institute Of Food Science Cornell University

• HAQUE Zahurul

  Institute of Food Science, Cornell University

• KINSELLA E.

  Institute of Food Science, Cornell University

• Kinsella E.

  Institute Of Food Science Cornell University

• Haque Zahurul

  Institute Of Food Science Cornell University

関連論文

• Molecular Association State of Bovine Serum Albumin and Its Effect on Emulsifying Activity(Food & Nutrition)
• One-Step Lipophilization of Proteins Using Fatty Acyl Anhydride
• Interaction between κ-Casein and β-Lactoglobulin: Effect of Calcium
• Heat-induced Changes in the Hydrophobicity of Kappacasein and β-Lactoglobulin
• Interactions between κ-Casein and β-Lactoglobulin: Effects of Anions on Covalent Stabilization of the Complex

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