Application of recombinant chum salmon cystatin to Alaska pollack (Theragra chalcogramma) surimi to prevent gel weakening

Recombinant chum salmon cystatin (RC) expressed in Saccharomyces cerevisiae was purified by His-select nickel affinity chromatography. The specific inhibitory activities of RC against papain and cathepsin L were 7.45 and 10.24 U/mg, respectively. RC was stable over pH 5.0 to 7.0 and at temperature below 65 degrees C. RC was used to prevent the gel weakening of Alaska pollock surimi. RC at 100 mu g/g showed the highest inhibitory activity against the autolysis of surimi based on the analysis of TCA-soluble peptides. As the concentration of RC increased, both the breaking force and deformation of modori gel greatly increased (P < 0.05). The addition of RC resulted in less expressible drip, which coincided with the increase of whiteness. More myosin heavy chain (MHC) was retained as the addition of RC increased. Therefore, RC could prevent the degradation of proteins in Alaska pollock surimi and was better than egg white (EW). Thus, RC could be applied to Alaska pollock surimi to prevent gel weakening and RC at 100 mu g/g was the optimal concentration.