Abstract
To establish a foam separation technique using proteins as a foaming reagent, it is important to know the foaming characteristics of various protein solutions and to demonstrate the effective application of these proteins. In this study, the effects of pH and coexistent substances on the foam formation of various proteins were examined.The results are as follows.(1) The foaming capacity of globular proteins such as casein, hemoglobin, soy protein, and albumin was enhanced in both strong acid and alkaline solutions. In contrast, gelatin, which is a fibrous protein, had only a slight dependency on pH.(2) The foam formation of proteins varied with the differences of cations in the solution. The enhanced potential were Na+=K+>Mg2+>Sr2+>>Ca2+ in order. Anions had no effect on foaming capacity.(3) The foaming capacity of casein was elevated with the addition of LAS (sodium linear-dosecylbenzenesulfonate). In contrast, the capacity of casein was lowered by the presence of SDS (sodium dodecyl suophate).(4) Globular proteins showed denaturation, dissociation and association with pH and coexistent substances, and these change affected foam formation.It is possible to generate the optimum amount of proteinaceous foam by taking advantage of each protein's unique characteristics.
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