Changes in glycated myofibrillar proteins conformation on the formation of N?-carboxymethyllysine under gradient thermal conditions

N epsilon-carboxymethyllysine (CML), a frequently used marker of advanced glycation end products (AGEs) in food, was generated in food processing easily and caused changes in myofibrillar proteins (MPs) characterization. The relevance between glycosylated MPs structure alternation and CML formation under thermal conditions have been reported. However, the correlation mechanism was not clear yet. In this work, the influence of gradient heating (50 degrees C, 60 degrees C, 70 degrees C, 80 degrees C, and 90 degrees C) on the different degrees of glycated MPs, which determined the correlation with CML formation in protein structural changes of MPs. In the rising stage of the CML level, gly-cation accelerated the fibrillation and aggregation behavior of MPs during heating and increased surface hy-drophobicity and particle size. The protein cross-linking affected the protein modification caused by heating and glycation. This work highlights the substantial influences of glycosylation and thermal treatments on MPs, which transformed the MPs structural characteristics and CML level.