GELATIN OF BEAN 11S GLOBULINS BY CA2+-INDEPENDENT TRANSGLUTAMINASE

The cross-linking reaction and gelation of 11S globulins from soybean (glycinin) and broad bean (legumin) by Ca2+-independent transglutaminase were studied. Analyses of the reaction products by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that only acidic subunits of both 11S globulins were polymerized through the formation of intermolecular crosslinkings by transglutaminase. Gel permeation chromatography analyses found that there were no significant differences in the molecular weight distribution profiles of reaction products between glycinin and legumin. These results suggest that the crosslinking reactions of glycinin and legumin by transglutaminase progress in similar ways. On the other hand, theological analyses such as dynamic viscoelastic measurements and compression tests indicated that gelation proceeded more rapidly and the values of hardness of formed gels were higher for glycinin compared with legumin. The water-holding capacity of the gels was significantly higher in the glycinin than in the legumin.