No abstract

Glycated fish protein showed positively biological effects but increased AGEs accumulation in high-fat-diet-fed rats.

The formation of advanced glycation end products (AGEs), regarded as a potentially harmful substance, in the protein glycation course is still under investigation. This study investigated the glycation modification of silver carp myofibrillar protein (MF) with glucose via Maillard-driven chemistry. The resultant conjugates and glycation extent were characterised by chemical indicators, such as Fourier transform infrared spectroscopy, sodium dodecyl sulphate-polyacrylamide gel electrophoresis, colour development, and AGEs level. As the primary responsibility for glycation, the loss of Lysine (Lys) and Arginine (Arg) in MF with longer glycation time (>24 h) was more than 25%. While, the associated AGEs, including Nε-carboxymethyl-lysine (CML), Nε-carboxyethyl-lysine (CEL), and methylglyoxal-derived hydroimidazolone 1 (MG-H1), presented a gradually increasing tendency with glycation time. The kinetic studies indicated that the formation of CML and MG-H1 presented a highly linear correlation with heating time, while the CEL development could be described as an exponential function of glycation time (r ≥ 0.95). Moreover, the correlation analysis among these chemical indicators indicated that colour development was positively correlated with AGEs (r ≥ 0.85), while negatively related to the loss of Lys and Arg (r ≤ −0.89). The findings may help to better control the glycation course of food protein based on the formation of AGEs.