A new method was established to estimate the foaming properties of proteins from the conductivity of foams using a simple apparatus that consisted of a glass column with the conductivity cell. A close correlation was observed between the initial conductivity of foams and the foam volumes of heat-denatured ovalbumins or 11 native proteins, suggesting that the initial conductivity of foams can be used as a measure of foaming power. In addition, a close correlation was obtained between the foam stability determined from changes in the conductivity and foam volume with time of heat-denatured ovalbumins or 11 native proteins, suggesting that foam stability also can be estimated from changes in the conductivity of foams. The advantages of the conductivity measurements are to determine the foaming properties more simply and accurately than the currently used methods.

The soy protein-galactomannan conjugate prepared by the Maillard reaction removed the allergenicity of the 34 kDa protein which is frequently recognized by the IgE antibody in the sera of soybean-sensitive patients as a major allergen. Monitoring of polyclonal antibody titers by an indirect enzyme-linked immunosorbent assay and immunoblotting of rabbit sera, monoclonal antibody, and human allergic sera showed that soy protein-galactomannan conjugation was more effective in reducing the allergenicity of the soy protein than transglutaminase treatments and/or chymotrypsin. The soy protein-galactomannan conjugate was highly soluble at all pHs, while untreated soy protein was sparingly soluble at pH 4-6. Heat stability and emulsifying properties were greatly improved by conjugation with galactomannan.

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