Film forming and foaming behavior of food proteins

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Abstract
The current state of understanding of protein structure as it relates to its function in foaming has proven to be of sufficient accuracy to predict the effects of particular modifications in soy proteins. Comparative whipping studies performed on egg white, casein, Bovine serum albumin and soy protein showed important differences both in the development and subsequent stability of foams produced from these proteins. Our understanding of the structures of soy proteins and the alterations induced by reductive modification and heating implied that similar modifications would have dramatic impact on the foaming properties specifically of the 11S protein. The foaming ability and stability of the 11S protein were enhanced dramatically by cleavage of intersubunit disulfide bridging. Computerized lamellar measurement techniques developed in this laboratory indicated that these modifications enhanced the ability of the protein to foam rapidly and then to stabilize surface films at the rate typically encountered in the whipping of foams.