4.7 Review

Meta-proteomics for the discovery of protein biomarkers of beef tenderness: An overview of integrated studies

Journal

FOOD RESEARCH INTERNATIONAL
Volume 127, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.foodres.2019.108739

Keywords

Integromics; Mass spectrometry; Proteomics; Meat; Cattle; Biological mechanisms

Funding

  1. Marie Sklodowska-Curie Career-FIT [MF20180029]
  2. Marie Sklodowska-Curie [713654]
  3. Meat Technology Ireland (MTI) a co-funded industry/Enterprise Ireland project [TC 2016 002]
  4. Pole Aquitain Agro-Alimentation et Nutrition (France)
  5. INRA (National Institute of Agronomical Research)
  6. INAO (National Institute of Origin and Quality)
  7. FNADT Massif Central (France)
  8. DATAR Massif Central (France)
  9. ANR GenAnimal
  10. APIS-GENE
  11. SICA Rouge des Pres
  12. Region Pays de la Loire (France)
  13. Marie Curie Actions (MSCA) [713654] Funding Source: Marie Curie Actions (MSCA)

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This meta-proteomics review focused on proteins identified as candidate biomarkers of beef tenderness by comparing extreme groups of tenderness using two-dimensional electrophoresis (2-DE) associated with mass spectrometry (MS). We reviewed in this integromics study the results of 12 experiments that identified protein biomarkers from two muscles, Longissimus thoracis (LT) and Semitendinosus (ST), of different types of cattle: young bulls, steers or cows from beef breeds (Charolais, Limousin, Blond d'Aquitaine), hardy breed (Salers) or mixed breed (PDO Maine-Anjou). Comparative proteomics of groups differing in their tenderness evaluated by instrumental Wamer-Bratzler shear force (WBSF) or by sensory analysis using trained panelists, revealed 61 proteins differentially abundant (P < 0.05) between tender and tough groups. A higher number of discriminative proteins was observed for LT (50 proteins) compared to ST muscle (28 proteins). The Gene Ontology annotations showed that the proteins of structure and contraction, protection against oxidative stress and apoptosis, energy metabolism, 70 family HSPs and proteasome subunits are more involved in LT tenderness than in ST. Amongst the list of candidate biomarkers of tenderness some proteins such as HSPB1 are common between the two muscles whatever the evaluation method of tenderness, but some relationships with tenderness for other proteins (MYH1, TNNT3, HSPB6) were inversed. Muscle specificities were revealed in this meta-proteomics. For example, Parvalbumin (PVALB) appeared as a robust biomarker in ST muscle whatever the evaluation method of tenderness. HSPA1B seems to be a robust candidate for LT tenderness (with WBSF) regardless the animal type. Some gender specificities were further identified including similarities between cows and steers (MSRA and HSPA9) in contrast to bulls. The comparison of the 12 proteomic studies revealed strong dissimilarities to identify generic biomarkers of beef tenderness. This integrative analysis allowed better understanding of the biological processes involved in beef tenderness in two muscles and their variations according to the main factors underlying this quality. It allowed also proposing for the first time a comprehensive list of candidate biomarkers to be evaluated deeply to validate their relationships with tenderness on a large number of cattle and breeds.

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