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 US 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. © 1984, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.

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Motoki, M., Nio, N., & Takinami, K. (1984). Functional Properties of Food Proteins Polymerized by Transglutaminase. Agricultural and Biological Chemistry, 48(5), 1257–1261. https://doi.org/10.1271/bbb1961.48.1257

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