Interactions between κ-Casein and β-Lactoglobulin: Effects of Anions on Covalent Stabilization of the Complex

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概要

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• Structure breaking anions, triehloroacetate (-TCA-) and thiocyanate (-SCN-), significantly increased the interaction between <κ>K</κ>-casein (K-C) and β-actoglobulin (B-Lg) to give the covalently stabilized K-C/B-Lg tetrameric (A4) complex, whereas "structure making" anions, chloride (-Cl-) and especially sulfate (-SO4-), reduced it. The reactivity of K-C with B-Lg in the presence of these anions followed the order, -TCA->-SCN->-Cl->-SO4- (100 mM). The percentile distribution of the covalent bonded K-C/B-Lg A4 complex after 720 s of heating at 70°C in -TCA- (100 HIM) was one order greater than it was in -SO4-. During storage of the heated K-C/B-Lg mixture, the B-Lg A3/K-C interaction in -TCA- was rapid and uneffected by the holding temperature, whereas in -SO4-, the reaction rate was inversely related to the temperature, being apparently controlled by the relative concentration of monomeric K-C.

• 社団法人 日本農芸化学会の論文

著者

• Kinsella John

  Institute Of Food Science Cornell University

• Haque Zahurul

  Institute Of Food Science Cornell University

• KRISTJANSSON Magnus

  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)
• Evidence of a Urea-induced Sulfhydryl Oxidation Reaction in Proteins(Food & Nutrition)
• 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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