Abstract: The screening and identification of specific peptides is the key to species identification using mass spectrometry because of the difference in the peptide composition between different species. In this study, the stability of the peptides derived from the enzymatic hydrolysis of bovine myoglobin was explored during thermal processing. Factors with a great influence on the stability of the peptides were selected from the processing methods and the chemical factors involved in these methods. The identification rate of myoglobin and the response values to its peptides were comparatively studied at different levels of each factor, and the tolerance of each peptide was analyzed to each factor. The results showed that heating modes, additives, auxiliary materials, and metal ions affected the stability of the peptides. Among these factors, three heating modes (boiling, frying, and high pressure processing), and the addition of sodium chloride or Mg2+ had a greater impact on the stability of the peptides, while heating temperature, heating time, additives, capsaicin, K+, and Ca2+ had less impact on it. Peptide 2# derived from bovine myoglobin and peptide 13# derived from myosin-2 showed high response values and the strongest stability during thermal processing. In addition, peptide 13# has more significant advantages for authenticity identification of meat products. The mechanism for controlling the stability of peptides derived from bovine myoglobin during thermal processing will provide a theoretical basis for selecting stable target peptides for meat authenticity identification.

Key words: bovine myoglobin; processing methods; processing factors; peptide stability; authenticity identification