Effect of roasting temperature on lipid and protein oxidation and amino acid residue side chain modification of beef patties
Chao Xia, Pingping Wen, Yaming Yuan, Xiaofan Yu, Yijing Chen, Huiqing Xu, Guiyou Cui, Jun Wang
Abstract
< 0.001). SDS-PAGE showed that the band of myosin heavy chain (MHC, 220 kDa) was significantly degraded, while the band of actin (42 kDa) was still clearly visible. The analysis of UPLC-MS/MS results found that the aromatic amino acid residues in all samples were oxidized to a certain extent, especially tryptophan. Other oxidative modifications, including α-amiooadipic acid (AAA), hydroxyethyl lysine (CEL) and malondialdehyde (MDA), were only present in roasted samples and not in raw meat. The results suggested that lipid oxidation and protein oxidation were closely related to colour parameters. The oxidation of proteins and lipids was aggravated at higher temperature. Amino acid side chains were also modified at high temperature, and this change was particularly evident in aromatic amino acids. These results provided new insights for the oxidation of proteins and lipids of beef and the modification level of amino acid residues under high temperature conditions, which will help us to improve the cooking quality of meat foods.