In surimi the cryoprtecatnts have been shown to preserve the structural stability of myofibrillar proteins and reduce the exposure of buried hydrophopic residues on the proteins surface, thus slowing down the kinetics of aggregation of proteins (Herrera and Mackie 2004). Among the factors that were found to decrease myofibrillar protein solubility, the interaction of lipid oxidized products with proteins was found to be important (Shobana and Naidu 2000). This process involves the interaction of oxidized lipids with the cystine—SH group, the NH3 group of lysine, and N—terminus group of aspartic acid, tyrosine, methionine, and arginine (Kussi et al. 1975, cited by Siddaiah et al. 2001).