Effect of reducing agents on physicochemical properties and gel-forming ability of surimi produced from frozen fish

Effects of different reducing agents (cysteine, ascorbic acid and sodium bisulfite) at various levels on physicochemical properties of protein, transglutaminase activity and gel properties of surimi produced from frozen croaker, lizardfish, threadfin bream and bigeye snapper were studied. Addition of cysteine resulted in the highest increase in the breaking force and the deformation of surimi gels, compared with other reducing agents. The optimum levels of cysteine were 0.05, 0.1, 0.05 and 0.1% (w/w) for surimi from frozen croaker, lizardfish, threadfin bream and bigeye snapper, respectively. Surimi from frozen croaker with cysteine added showed a similar breaking force and deformation to that produced from fresh fish. With addition of cysteine, an increase in sulfhydryl content with a concomitant decrease in disulfide bond content was generally observed. Ca²⁺ ATPase activity also increased, indicating the renaturation of the myosin molecule. T_max of peak 1 (myosin peak) of all surimi sols in the presence of cysteine was shifted to higher temperature. The increased transglutaminase activity was observed with addition of cysteine. Therefore, reducing agents, especially cysteine, recovered the denatured muscle proteins and activated the transglutaminase in the muscle, leading to the increased gel-forming ability of surimi produced from frozen fish.