Addition of tert-butylhydroquinone or a mixture of butylated hydroxyanisole and tert-butylhydroquinone (200 ppm on a lipid basis) during SPI processing gave increased protein solibility over that of the con&l (55%. 56% and 34%. resuectivelv). These increased solubilities correspond to 32% and 18% decrease in oxidation of free sulthydryls and 20% and 12% reduction in protein oxidation, as determined by protein carbonyl content. Increased protein solubilities, due to added antioxidants, were accompanied by higher total protein surface hydrophobicity, as determined by the sodium dodecyl sulfate (SDS) binding method, and soluble protein hydrophobic&y, as determined by the fluorescence probe S-anilino-1-naphthalene sulfonate (ANS).
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