Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork

Abstract

The objective of this study was to determine the extent to which early postmortem (PM) pH decline influences proteolysis of the intermediate filament protein desmin, the costameric proteins vinculin and talin and autolysis of μ-calpain in the longissimus muscle (LM) of pigs from two genetic lines. Based on the LM 3 h pH (H = 3 h pH of LM > 6.0; L = 3 h pH of LM pH < 5.7) PM, 10 carcasses per line and pH group were selected. The average 3 h pH within pH group was 6.23 (H) and 5.44 (L). The LM samples were collected 24, 48, 72, and 120 h PM and percent drip loss was measured after 1, 2, and 4 d of storage. Samples collected at 24, 48, 72, and 120 h PM were used to monitor desmin, vinculin, and talin degradation and samples collected at 24 h PM were used to determine the extent of μ-calpain autolysis by immunoblotting. Higher ( P < 0.01) pH values at 45 min, 6 h, and 24 h PM and lower ( P < 0.01) drip losses after 1, 2, and 4 d of storage were recorded in the H-compared to the L-group. Abundance of the 76 kDa μ-calpain autolysis product was greater ( P < 0.01), proteolysis of talin at all measured time points and proteolysis of desmin after 24 and 48 h PM was greater ( P ⩽ 0.03) in the H-group than in the L-group. The current findings indicate activation rate of μ-calpain may be associated with proteolysis of desmin and talin and could play a role in the development of drip loss. The rate of early PM pH decline can partly explain the variation of desmin and talin degradation by affecting the activation of μ-calpain.