Suppression of surimi gel setting by transglutaminase inhibitors
1995
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 degrees up to 4 hr, and subsequently heated at 85 degrees C for 30 min. The gel strength, crosslinking of myosin heavy chain (MHC) and epsilon-(gamma-glutamyl)lysine (epsilon-(gammay-Glu)Lys) content were determined. With extended setting time, gel strength, crosslinking of MHC and the content of a crosslinked product, epsilon-(gamma-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.
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