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Degradation of myosin heavy chain and its potential as a source of natural bioactive peptides in dry-cured ham

Mora, L., M, Gallego, F, Toldrá
Food bioscience 2019 v.30 pp. 100416
actin, bioactive compounds, cathepsins, cured meats, flavor, meat, muscles, myofibrillar proteins, myosin heavy chains, myosin light chains, peptides, proteolysis, tandem mass spectrometry, texture, troponin T
Myofibrillar proteins are extensively degraded by muscle endo- and exopeptidases during the ageing of meat and the processing of meat products. One of the most studied products is dry-cured ham. This degradation implies changes in the product in terms of texture (mainly due to calpains and cathepsins endopeptidases) and flavour (due to the action of exopeptidases) and defines its final quality. During the last decade, naturally generated peptides from the myofibrillar proteins titin, myosin light chain, troponin T, LIM domain-binding protein 3, and actin have been identified using peptidomic approaches, also showing the potential to act as bioactives in the human body when ingested. In this study, tandem mass spectrometry has been used for the identification of the peptides generated during the proteolysis of myosin heavy chain protein after 9 months of Spanish dry-cured ham processing. The size, sequence, and properties of some of the peptides showed their potential to act as bioactives.