Fractionation and Emulsifying Properties of Plasma Proteins(Food & Nutrition)

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Plasma proteins were separated into five fractions by ion-exchange chromatography, and then the emulsifying properties and heat denaturation of the fractions were investigated. Serum albumin-rich and γ-globulin-rich fractions were obtained, respectively. A solution of each fraction (1% w/v, pH 7.0) was heated at 80℃ for 30 min. The gel filtration patterns indicated that high molecular weight polymers arose upon heat treatment in all fractions. The emulsifying activity index (EAI) of all fractions, except those containing γ^globulin, increased on heat treatment. A solution of γ-globulin formed a gel and it lost its emulsifying activity. It was shown that γ-globulin plays a predominant role in the decrease in emulsifying activity of plasma proteins at neutral pH during heat treatment and that the removal of γ-globulin from the plasma proteins effectively prevents the decrease in emulsifying activity under these conditions.
社団法人日本農芸化学会の論文
1988-11-23