The solubility of wheat gluten was greatly improved at pH 4 or lower where
it showed good emulsifying activity. This might be due to its high surface
activity in the acidic pH range and the formation of a stable protein film
surrounding the oil droplets. Among the major gluten proteins, gliadins sho
wed higher surface activity than glutenins, The content of glutenins in the
adsorbed protein film was higher than that of gliadins, and glutenins are
likely to have been adsorbed more tightly than gliadins. These results sugg
est that gluten proteins exhibit complex behavior, such as adsorption/desor
ption/displacement/rearrangement during the adsorption process in a gluten-
stabilized emulsion.