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Proteomic methods and approaches to the detection of tissue-specific and tissue-generating proteins and peptides – which form corrective properties – in studied meat samples and specially developed meat products were successfully tried out in 2016–2017. The methods allow one to confirm protein and peptide authenticity and also detect bio-markers of proteolytic changes in meat after slaughter. The following proteomic techniques were used in the present research: two-dimensional O’Farrell electrophoresis with isoelectrofocusing in ampholin and immobilin pH gradients, the detection of proteins on two-dimensional electrophoregrams by staining with Coomassie R-250 and silver nitrate, and mass spectrometric identification of proteins by means of MALDI-TOF and MS/MS methods. Contractile actomyosin complex proteins, such as myosin light chains and tropomyosins, were the most informative among proteins of species specificity. It is also necessary to mention that earlier experiments allowed us to choose enzymes which play a part in carbohydrate metabolism (glyceraldehyde 3-phosphate dehydrogenase and β-enolase) as markers. In addition to the listed proteins, myoglobins, actins, and several other proteins in horse meat have showed high species specificity and have been detected well. A system of species specificity (authenticity) of meat raw materials was suggested. The system allows the presence of pork, beef, horse, and camel meat to be detected in both raw and heat-treated products if the content is 5% and more. The data has been obtained by means of bioinformatics, a highly useful tool for formulating an algorithm to identify the protein markers for the Atlas “Proteomic profiles of farm animals meat proteins”. “Proteomic profiles of farm animals muscle proteins”.
, horse meat
, camel meat
, muscle proteins
, peptide fingerprint
, MALDI-TOF mass spectrometry
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