TRANSGLUTAMINASE EFFECTS ON LOW-TEMPERATURE GELATION OF FISH-PROTEIN SOLS

Myosin polymerization and formation of epsilon-(gamma-glutamyl)lysine linkages were quantified in Alaska pollock surimi gels which contained no additive (control), or a commercial microbial transglutaminase (MT Gase). As preincubation (''setting'') time at 25 degrees C was increas ed, the gel strength of control and 0.2% MTGase-added samples increase d, with greater increases at higher MTGase levels. SDS-PAGE and HPLC a nalyses showed increasing nondisulfide polymerization and epsilon-(gam ma-glutamyl)lysine dipeptide content, with increasing setting time and /or added MTGase. Content of epsilon-(gamma-glutamyl)lysine dipeptide correlated with gel strength (shear stress) and shear modulus at failu re (G(f)) for these gels. Higher stresses were measured in samples con taining 0.2% MTGase than in controls at corresponding levels of epsilo n-(gamma-glutamyl)lysine dipeptide, indicating that rate of myosin pol ymerization may affect ultimate gel strength.