Suppression of Surimi Gel Setting by Transglutaminase Inhibitors

Three types of salted meat paste (3% NaCl, 3% NaCl plus 0.66% NH₄Cl or 3% NaCl plus 0.2% EDTA) were prepared from high and second grade surimi, set at 30°C up to 4 br, and subsequently heated at 85°C for 30 min. The gel strength, crosslinking of myosin heavy chain (MHC) and ?-(γ-glutamyl)lysine (?-(γ-Glu)Lys) content were determined. With extended setting time, gel strength, crosslinking of MHC and the content of a crosslinked product, ?-(γ-Glu)Lys, increased markedly in the gel from the high grade surimi. Such changes were suppressed considerably in the presence of NH₄Cl and EDTA and were not observed in the gel prepared from second grade surimi. These results indicated an active participation of intrinsic transglutaminase in the setting process.