ABSTRACT
Transglutaminase (TG) catalyzes acyl-transfer reactions, introducing covalent cross-links between L-lysine and L-glutamine residues. As a result, peptides are connected and the structure of a stabilized protein network is formed, thereby improving protein strength. In this study, wheat flour was incubated with TG for different time intervals (0, 30, 60, 120, and 240 min) and the extent of polymer formation and proteins involved were investigated by SE-HPLC, SDS-PAGE, and RP-HPLC. Results indicated that the amount of polymers formed increased with incubation time. TG induced the cross-linking of HMW glutenin subunits more so than of other proteins in wheat.
