Effect of rigor temperature and frozen storage on functional properties of hot-boned manufacturing beef

Within 45 min post-mortem, 10mm thick strips of semitendinosus muscle from both unstimulated and high voltage stimulated heifer sides were held at 0, 5, 10, 25 and 35 °C for 24 hr, during which they entered rigor. Half the samples were frozen and stored at -20 °C for one month. The pH, sarcomere length, drip, total (TPS), myofibrillar (MPS) and sarcoplasmic (SPS) protein solubilities, and Hunter L (∗), a (∗) and b (∗) values were determined at 24 hr and on thawed samples. Electrical stimulation did not significantly affect any of the parameters measured. The ultimate pH of samples entering rigor at 10 and 25 °C was lower (p < 0.001) than that of samples held at the other temperatures. Rather surprisingly, there was no significant difference in sarcomere length due to rigor temperature. Samples entering rigor at 35 °C had lower TPS, MPS and SPS values than samples held at 0 to 25 °C (p < 0.001). The MPS increased with rigor temperature up to 25 °C (p < 0.001). Drip and total moisture losses, and Hunter L (∗), a (∗) and b (∗) values also increased with rigor temperature (p < 0.001) whereas SPS decreased and NMR meat water spin-lattice relaxation time (T1) shortened with increasing rigor temperature (p < 0.001). Hue angle and cook loss decreased with rigor temperature in 24 hr samples but increased with rigor temperature in frozen samples. After frozen storage, SPS, T1, cook loss and Hunter L (∗), a (∗), b (∗) values decreased, but TPS, MPS, drip losses and hue angle increased. There were significant (p < 0.05) correlations between SPS, hue angle, drip losses and T1.