Crosslinking Between Different Food Proteins by Transglutaminase



Guinea pig liver transglutaminase has been found to catalyze the formation of inter- and intramolecular ε-(γ-glutamyl)lysyl crosslinks in proteins. In this paper we study the formation of polymers between different proteins by reacting them with transglutaminase. Analysis of reaction products between acetylated αs1 -casein and several proteins (αs1 -, k-casein, β-lactoglobulin, soybean 11S and 7S globulin) by sodium dodecyl sulfate polyacrylamide gel electrophoresis and high-performance liquid chromatography indicated that the different proteins were polymerized through the formation of intermolecular crosslinks. This reaction may represent a procedure to improve the properties of food proteins.