ABSTRACT
A protein isolate, with a 74.4% (w/w) protein content, was recovered from a simulated potato processing plant waste effluent by complexation with carboxymethylcellulose. The protein solubility of the isolate was satisfactory, it decreased in the presence of NaCl, but was not markedly affected by heat treatment. The isolate exhibited remarkable foaming and foam stabilizing properties, compared with lyophilized egg white, which are attributed to the very high surface activity of the potato protein molecules, which following adsorption at a/w interfaces, result in a much higher surface pressure development compared with egg albumen. A significant part of the foaming ability and the high surface activity of the isolate should be connected with the presence in the isolate of a small fraction of proteins with a relatively low molecular weight. The sulfhydryl groups of these proteins, following adsorption at the a/w interface, during the process of foam formation and denaturation are oxidized leading to the possible formation of intermolecular disulfide linkages.
