Effect of glycation on protein structure, amino acid composition and digestibility of silver carp mince

Summary This study was to investigate the effects of glycation on the quality of silver carp mince (SCM) proteins. The browning index (BI), sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE), Fourier transform infrared spectroscopy (FTIR), total amino acid composition, chemical score, protein digestibility and reductive power of digested products were determined. The correlation between the degree of glycation, protein structure and protein nutritional quality was analysed. The results showed that the BI value of SCM‐G increased with the increase in heating time. Myosin heavy chain (MHC), myosin light chain (MLC), tropomyosin and actin were the main protein reactants for glycation. Glycation led to the expansion of the secondary structure of SCM proteins. Glycation reduced lysine and cysteine content but did not change the first limiting amino acid (Val) in SCM. The essential amino acid content of glycated SCM remained consistent with the amino acid nutritional requirements for children and above recommended by FAO/WHO. In addition, glycation did not change protein digestibility but significantly increased the reducing power of digested products with increasing degree of glycation. These results provided a theoretical basis for the application of glycation in food processing industry and the development of aquatic products with high nutritional value.