Functional Properties of Food Proteins Polymerized by Transglutaminase

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Abstract
The following properties of food proteins polymerized by guinea pig liver transglutaminase were investigated: (1) solubility, (2) emulsifying activity and emulsion stability, and (3) unfrozen water content by pulsed NMR. Several food proteins (αsl- and k-caseins, and soybean 7S and 11S globulins) were polymerized by this enzyme. Solubility and emulsifying activity of polymerized αsl-casein were higher than those of the native protein in the range of pH 4~6. Unfrozen water contents of polymerized soybean globulins were much higher than those of the native proteins. These results suggest that transglutaminase treatment may be used for the production of new food protein material with higher hydration ability.