Abstract:

Fresh water fish surimi products processing is one of the main directions of fisheries processing industry in China. Gelation is the most important factor that affects the quality of surimi products. So making the mechanism of gel formation clear is of great significance. In the present study, chemical methods were used to determine the changes in ion, disulfide and hydrogen bonds and hydrophobic interactions during the formation of grass carp (Ctenopharyngodon idellus) surimi gels and the technique used to analyze protein conformation changes was laser-Ramman spectroscopy. Furthermore, the effects of chemical forces and protein conformation on the formation of surimi gels were elucidated. The results illustrated that during surimi gel formation, ion bonds and hydrogen bonds decreased significantly. However, hydrophobic interactions, disulfide bonds and non-disulfinde covalent bonds increased markedly. The α-helix of protein conformation was change into turn and random coil structures in part. Based on these results, it can be concluded that hydrophobic interactions, disulfide bonds and non-disulfide covalent bonds are the main chemical forces affecting the formation of surimi gels from frozen grass carp and that α-helix and random coil structures are the main protein conformations keeping the structure of frozen grass carp surimi gels stable.

Key words: surimi gel, chemical force, protein conformation, mechanism