Abstract
Examinations were carried out with ovalbumin (OVA) as the protein to clarify the beneficial effects of ascorbic acid on food.
First, in order to elucidate the difference in turbidity of ovalbumin (OVA) dissolved in several kinds of 0.2 M buffer at pH 6, resulting from ascorbic acid (AsA) during incubation at 50°C, the effects of several chelating agents and of two metal ions were investigated. Second, phosphoric acid buffers with an ionic strength of 0.26 to 1.0 were used to examine the influence of increasing ionic strength on OVA turbidity to clarify the mechanism for polymerization of OVA by AsA.
The results obtained from an earlier investigation suggested that one of the causes of the difference in turbidity with various buffers may have been due to metal ion contaminants.
An increase in ionic strength in the phosphoric acid buffer inhibited polymer formation derived from OVA, indicating that both electrostatic and polar bonding occurred in the formation of the polymer.
