Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase.

The effects of curdlan in combination with microbial transglutaminase on the gelling properties of hairtail muscle protein were investigated. When curdlan of 4g/100g paste was combined with transglutaminase at a concentration of 0.4units/g meat paste, the gel strength, water holding capacity and the whiteness of the heated gel were improved. Textural profiles, such as hardness, springiness, cohesiveness, guminess and chewiness, reached their peaks as well. The increased band intensity of cross-linked proteins, accompanied by weakened myosin heavy chain, was observed from the SDS-PAGE pattern, indicating that curdlan might activate the formation of more ε-(γ-glutamyl) lysine cross-links induced by transglutaminase, especially at the level of 0.4units/g paste, leading to a denser gel matrix.