大豆タンパク質とトリメチルアンモニウム4級アミン基を含む表面活性剤との相互作用(I) : コングリシニンの核磁気共鳴による研究

概要

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The interactions between conglycinin and surfactants at pH 7.6 have been studied by nuclear magnetic resonance technique. When a surfactant binds to a protein and the molecular motion of all the alkyl groups of the surfactant is restricted, this effect being greater for the CH_3 in trimethylammonium residue than for the terminal CH_3 group. The head group, trimethylammonium residue is in a more polar environment than the other CH_2 groups and terminal CH_3 group. Hence although hydrophobic bonding may account for a significant portion of the binding free energy, electrostatic forces are also important and may determine the site of the interaction. The interactions may cause physical properties of soybean protein to change on heating followed by freezing.