Importance of salt and temperature in myosin polymerization during surimi gelation.

To address the effect of absence of NaCl on myosin heavy chain polymerization during two-step surimi gelation (different setting temperatures/times -5°C/24h and 30°C/30min-followed by heating at 90°C/30min) were considered. In gel samples made without salt (Lot A), no myosin heavy chain (MHC) polymerization was observed, only aggregation, as indicated by the electrophoresis in polyacrylamide/agarose gel profile. Moreover, these gels were characterized by weakly stabilized protein networks as denoted by the dynamic oscillatory measurement and FTIR analysis, resulting in poor quality gels. On the other hand, in gels made with added salt, MHC polymerization occurred, as evidenced by the electrophoresis, and the gelation resulted in a well-stabilized protein network with good physicochemical properties.

Different additives to enhance the gelation of surimi gel with reduced sodium content.

This study tested the effect of adding tetra-sodium pyrophosphate, cystine and lysine as surimi gelation enhancers (Alaska Pollock) in order to reduce the sodium content of gels up to 0.3%. These gels were compared with others that contained 3% NaCl content (the amount typically used for surimi processing). To induce protein gelation, gels were first heated and then set at 5 °C/24 h. Once the physicochemical and rheological properties of the gels were determined, cystine and lysine were found to be the most effective additives improving the characteristics of low NaCl surimi gels. The action of these additives is mainly based on the induction of myofibrillar protein unfolding thus facilitating the formation of the types of bonds needed to establish an appropriate network. It was found that a setting period was needed for gel processing to maximize the effect of the additives.