Influence of pH-Induced Unfolding and Refolding of Egg Albumen on Its Foaming Properties

Abstract

ABSTRACT: The foaming properties of egg albumen, which had been subjected to low and high pH unfolding followed by refolding, were investigated. The foaming capacity of egg albumen, the stability of the foam, or both, could be improved by an unfolding and refolding regime by choosing proper unfolding and refolding pH values. The foaming capacities of egg albumen were greatly improved when the refolding was at pH 6.5, 7.5, or 8.5, whereas the foaming capacities could be either slightly increased or decreased when the refolding was at pH 4.5 or 5.5 compared with the controls. The foam stability was in almost all cases improved by the unfolding and refolding treatments except for a few cases of unfolding at pH 1.5 or 10.5. The foam stability and liquid drainage were improved most when the unfolding was at pH 12.5. Analysis of total and surface sulfhydryl groups, surface hydrophobicity, and protein analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) provided strong evidence that the partial unfolding of egg albumen proteins as well as the interactions among egg albumen proteins through disulfide and/or hydrophobic groups dictated the improvements in foaming properties. The increase in surface hydrophobicity showed better correlation with the improvement of foaming properties than the change of surface sulfhydryl content did.