Proteomic responses to oxidative damage in meat from ducks exposed to heat stress

Food Chem. 2019 Oct 15:295:129-137. doi: 10.1016/j.foodchem.2019.05.073. Epub 2019 May 8.

Abstract

Heat stress causes oxidative damage and quality reduction in poultry. Here, a tandem mass tag proteomic approach was applied to investigate the proteomic differences in duck meat from birds exposed to heat stress. Altogether 212 differential proteins were identified, including 178 down-regulated and 34 up-regulated proteins, compared to the control. Malondialdehyde and carbonyl content and cooking loss of the chest muscle significantly increased under heat stress. The proteomic analysis indicated that heat stress suppressed mitochondrial functions and respiratory chains, which might be responsible for the higher oxidation level. The results also revealed potential protective proteins involved in the defensive mechanisms against heat stress in duck muscles, such as sarcoplasmic/endoplasmic reticulum calcium ATPases, Mn-superoxide dismutase, heat shock protein family B member 7, methyltransferase like 21C, myosin-binding protein C, and carbonic anhydrase 3. These results provide potential targets for the research and identification of oxidative meat products due to heat stress.

Keywords: Cherry-Valley duck; Heat stress; Oxidation; Proteomics; Tandem mass tag.

MeSH terms

  • Animals
  • Calcium-Transporting ATPases / genetics
  • Calcium-Transporting ATPases / metabolism
  • Cooking
  • Ducks / metabolism
  • HSP27 Heat-Shock Proteins / genetics
  • HSP27 Heat-Shock Proteins / metabolism
  • Male
  • Meat / analysis*
  • Muscle, Skeletal / metabolism
  • Oxidative Stress*
  • Protein Interaction Maps
  • Proteome / analysis*
  • Proteomics / methods*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism

Substances

  • HSP27 Heat-Shock Proteins
  • Proteome
  • Superoxide Dismutase
  • Calcium-Transporting ATPases