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Effect of Transglutaminase on Protein Electrophoretic Pattern of Rice, Soybean, and Rice-Soybean Blends

¹Cereal Group, Institute of Agrochemistry and Food Technology (IATA-CSIC), P.O. Box 73, 46100 Burjassot, Valencia, Spain. ²Facultad de Ciencias Agropecuarias, Universidad Nacional de Cordoba, CC 509. 5000, Cordoba, Argentina. ³Corresponding author. Phone: 34 963900022. Fax: 34 963636301. E-mail address: crosell@iata.csic.es

The interactions taking place in composite dough containing rice flour and soybean proteins (5% w/w) in the presence of transglutaminase, an enzyme with cross-linking activity, were studied using different electrophoretic analyses. The interaction between rice proteins and soybean proteins was intensified by the formation of new intermolecular covalent bonds catalyzed by transglutaminase and the indirect formation of disulfide bonds among proteins. The main protein fractions involved in those interactions were both β-conglycinin and glycinin of soybean and the glutelins of the rice flour, although albumins and globulins were also cross-linked. The addition of soybean proteins to rice flour improves the amino acid balance and they also might play an important role on the rice dough properties because soybean proteins interact with rice proteins, yielding protein aggregates of high molecular weight.