Abstract
Guinea pig liver transglutaminase is a Ca2+ dependent enzyme which catalyzes the formation of inter- and intramolecular ε-(γ-glutamyl)lysyl cross-links between protein molecules. We have found that solutions of several proteins (αs1-casein, and soybean 11S and 7S globulins) were gelatinized firmly by transglutaminase. The gel formation depended on the protein concentration. In the case of αs1-casein, a reaction mixture containing below 2% was incapable of gelation. However, above 3%, a firm gel was formed by transglutaminase. As to soybean 11S and 7S globulins, reaction mixtures containing below 5% did not form gels, while, above 8%, firm gels were formed. The protein solutions in the presence of EDTA, an inhibitor of transglutaminase, were not gelatinized on treatment with transglutaminase. Thus, transglutaminase and a higher concentration of a substrate protein are indispensable for firm gel formation. It is supposed that the protein gels are formed through covalent bonds with transglutaminase.
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