Relationship between pre-rigor temperature of pork longissimus muscle, myofibril-bound calpain activity and protein degradation

Abstract

The effect of pre-rigor temperature incubation on the activity and distribution in sarcoplasmic and myofibrillar fractions of calpains, and meat quality attributes was investigated. Porcine longissimus thoracis muscles were incubated pre-rigor at 14, 22, 30 and 38 °C to 6 h postmortem, followed by another 2 h incubation at 14 °C. Thereafter, muscles were stored at 2 °C for 1 or 4 days. With higher pre-rigor temperature, sarcoplasmic Ca²⁺ concentration, purge loss and myofibril-bound calpain-1 content increased, while shear force declined. Water-holding capacity of isolated myofibrils was lower after pre-rigor incubation at 38 °C. Desmin and troponin T degradation, and myofibril fragmentation was greater upon incubation of isolated myofibrils with added Ca²⁺ in the order 800 μM Ca²⁺ > 40 μM Ca²⁺ > no Ca²⁺, suggesting that calpain-1 and calpain-2 were associated to myofibrils and proteolytically active with sufficient Ca²⁺. Activity of myofibril-bound calpain-1 in muscle incubated pre-rigor at 22 and 30 °C were higher than when incubated at 14 and 38 °C. These results indicate that calpains translocate from the sarcoplasm onto myofibrils with higher pre-rigor temperature to 30 °C and the proteolytic potential of myofibril-associated calpains is thereby increased.

Keywords: Calpain; Particle size; Pre-rigor temperature; Protein degradation; Protein denaturation; Water-holding capacity.