Different concentrations of γ-polyglutamic acid and transglutaminase were added to chicken myofibr- illar protein, in order to study the effects of γ-polyglutamic acid combined with transglutaminase on the myofibril- lar protein heat-induced gelatin properties, the changes of hardness, springiness, water holding capacity, whiteness and the chemical force in the gelatin were measured. The results showed that the γ-polyglutamic acid and transg- lutaminase had obvious effect on the gelatin properties of chicken myofibrillar protein. However, the improvement of gelatin properties was more obvious after the γ-polyglutamic acid and transglutaminase compounds were used, and when the concentration of transglutaminase was 0.5%, the concentration of γ-polyglutamic acid was 0.6‰, gelatin hardness, springiness, water holding capacity reached the maximum; when the concentration of transgluta- minase was 0.7%, the concentration of γ-polyglutamic acid was 1.2‰, gelatin whiteness value reached the minimum. The chemical force analysis showed that after the γ-polyglutamic acid and transglutaminase treatment, hydrophobic interaction and non-disulfide covalent bond were major factor in maintaining the stability of the three-dimensional structure of the gelatin, ionic bonds, hydrogen bonds and disulphide bonds were the secondary factors. SDS-PAGE studies indicated that transglutaminase could catalyze the cross-linking reaction between γ-polyglutamic-protein and protein-protein to form macromolecular substances.