Minimal addition of transglutaminase on the preparation and characteristics of tilapia (Oreochromis mossambicus) surimi

Transglutaminase (TGase) of microbial origin catalyzes the transamide reaction with a glutamine residue in proteins, which correlates with the surimi setting (suwari) process and plays a vital role in manufacturing fish surimi products. This study investigates the effect of TGase-assisted agglutination at different incubation temperatures (20, 30, 40, and 50 & DEG;C) in setting the stage to characterize its microstructural influence on agglutination strength and tilapia surimi. Results showed that the preparation of combined heat and TGase treatments significantly increased the hardness, elasticity, gel strength, and water-holding capacity of tilapia surimi gels (P < 0.05). G & PRIME; and G & DPRIME; values were increased, whereas Tan & delta; was decreased, with significant differences among conditions (P < 0.05). In addition, SDS-polyacrylamide gel electrophoresis showed that myosin heavy chain (MHC) was cross-linked into aggregated macromolecules by TGase. In general, the good performance of tilapia surimi was obtained by heating with minimum addition TGase (0.147 U/g surimi) at 40-50 & DEG;C for 1 h. Hence, this study could provide a theoretical basis for developing surimi products with good structure, quality, and high nutritional value.