Formation of N(ε)-Carboxymethyl-Lysine and N(ε)-Carboxyethyl-Lysine in Heated Fish Myofibrillar Proteins with Glucose: Relationship with Its Protein Structural Characterization.

The formation of advanced glycation end products (AGEs), including N(ε)-carboxymethyl-lysine (CML) and N(ε)-carboxyethyl-lysine (CEL), in a fish myofibrillar protein and glucose (MPG) model system at 80 °C and 98 °C for up to 45 min of heating were investigated. The characterization of protein structures, including their particle size, ζ-potential, total sulfhydryl (T-SH), surface hydrophobicity (H(0)), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR), were also analyzed. It was found that the covalent binding of glucose and myofibrillar protein at 98 °C promoted protein aggregation when compared with the fish myofibrillar protein (MP) heated alone, and this aggregation was associated with the formation of disulfide bonds between myofibrillar proteins. Furthermore, the rapid increase of CEL level with the initial heating at 98 °C was related to the unfolding of fish myofibrillar protein caused by thermal treatment. Finally, correlation analysis indicated that the formation of CEL and CML had a significantly negative correlation with T-SH content (r = -0.68 and r = -0.86, p ≤ 0.011) and particle size (r = -0.87 and r = -0.67, p ≤ 0.012), but was weakly correlated with α-Helix, β-Sheet and H(0) (r(2) ≤ 0.28, p > 0.05) during thermal treatment. Overall, these findings provide new insights into the formation of AGEs in fish products based on changes of protein structure.