Transglutaminase catalyzes the formation of intermolecular and intramolecular ε-(γ-glutamyl)lysyl crosslinks in proteins. The study here examined the substrate effectiveness of soybean 7S and 11S proteins in the intermolecular-crosslinking reaction catalyzed by guinea pig liver transglutaminase.
Both 7S and 11S proteins could act as the substrate for the transglutaminase reaction.The reaction with 11S protein was faster than that of 7S protein. Analyses of the reaction products by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that three main subunit groups of 7S protein and two acidic subunit groups of 11S protein were polymerized through the formation of intermolecular crosslinks by transglutaminase. Interestingly enough, no intermolecular crosslink was formed between the basic subunits of 11S protein. The possible significance of the intermolecular crosslinking catalyzed by transglutaminase is discussed, including the use of this enzyme reaction to improve the properties of food protein.

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