Physicochemical and Functional Properties of Hen Ovalbumin Dephosphorylated by Acid Phosphatase(Food & Nutrition)

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Hen egg ovalbumin is a mixture of three kinds of proteins, A_1, A_2, and A_3 with two, one, and no phosphoryl residues, respectively. These three proteins were obtained by acid phosphatase treatment and then chromatography on a DEAE cellulofine AH column. The isoelectric points of A_1, A_2, and A_3 were found by isoelectric focusing to be pH 4.75, 4.89, and 4.94, respectively. The denaturation temperature of each protein was examined by differential scanning calorimetry at its own isoelectric point and at pH 4.65. At both pHs, A_3 had alower denaturation temperature than A_2 or A_1. The surface tension of an A_3 solution reached a constant more quickly than A_1 or A_2 after formation of a new surface of the solution. These results indicate that the completely dephosphorylated ovalbumin A_3 is more susceptible to heat and surface denaturation than phosphorylated avalbumin is. The difference in the heat aggregation patterns of A_1, A_2, and A_3 solutions at different pH or salt concentrations showed that the electrostatic-repulsive force is important in helping to prevent the random aggregation of denatured ovalbumin.
社団法人日本農芸化学会の論文
1988-04-23