E. D. Aberle

Bovine muscle shortening and protein degradation after electrical stimulation, excision and chilling☆

Electrical stimulation-dependent improvement in beef tenderness resulted from mechanisms other than avoidance of cold shortening in excised muscle chilled at a normal rate (10°C at 10h post-stimulation). At normal chilling rate, electrical stimulation enhanced degradation of the myofibrillar proteins, alpha actinin and troponin-T, and increased the amount of a 30 000 dalton protein, as assessed by gel electrophoresis, whereas sarcomere lengths were not different from unstimulated muscle. Under slightly accelerated chilling conditions (10°C at 5 h post stimulation), electrical stimulation prevented cold shortening but the meat was more tender than, and had the same sarcomere length as, unstimulated muscle chilled to 10°C in 10 h. Electrical stimulation did not improve the tenderness of beef chilled at a rapid rate (10°C at 2 h post stimulation), nor did it prevent cold shortening when muscles were chilled rapidly.

Antioxidative activity of α-tocopherol in cooked and uncooked ground pork.

The effect of α-tocopherol (0, 100, 200 ppm) on lipid oxidation either in cooked or uncooked ground pork was studied during aerobic storage at 4°C and -20°C. Lipid oxidation was measured using the 2-thiobarbituric acid (TBA) method and rancidity development was scored by a trained sensory panel. Alpha-tocopherol slowed the rate of oxidation in cooked ground pork stored at either 4°C or -20°C and uncooked samples refrigerated for extended periods of time (12 days). In cooked product stored at 4°C where oxidation development was intense and off-flavors were strong, panelists did not detect flavor differences due to treatments. But in cooked product stored at -20°C sensory results were consistent with TBA analysis. Pre-rigor grinding, known to induce a high pH and inhibit lipid oxidation in uncooked fresh pork, had no protective effect on lipid oxidation as measured by TBA values in cooked ground pork, regardless of storage condition. TBA numbers increased during storage of cooked product at 4°C with an increase in internal cooking temperature between 50°C and 80°C. Internal cooking temperatures of 70°C or higher induced a rapid rate of oxidation when stored at 4°C.

Effects of early post-mortem ageing on intramuscular collagen stability, yield and composition☆

Post-mortem changes in the composition and physical stability of bovine intramuscular collagen were evaluated during a 24 h ageing period. The yield of intramuscular connective tissue (IMCT) isolated from the infraspinatus muscle samples and the carbohydrate content of that material did not change significantly (P > 0·05) during the ageing period. The collagen content and total protein content of the isolated IMCT increased (P < 0·05) through 8 h post-mortem. Moisture content of the isolated material decreased numerically but not significantly (P > 0·05). Collagen thermal shrinkage temperature (T(s)) decreased (P < 0·01) and collagen solubility increased (P < 0·05) during the ageing period with most of the changes occurring in the first 8 h.

Myofibrillar protein degradation after eccentric exercise

Male rats were run downhill for 90 minutes (nonexhaustive). Following the exercise, muscle protein degradation was increased, as determined by urinary 3-methylhistidine. However, minimal changes were observed in the relative percentage of the minor myofibrillar proteins and in the protease calcium activated factor in the long head of the triceps brachii muscle (eccentrically exercised) following the exercise bout.

Shortening and tenderness of pre-rigor heated beef: Part 2 — Effect of heating rate on muscles of electrically stimulated carcasses

This study was conducted to compare the effects of rapid and slow heating rates on muscles from electrically stimulated beef carcasses. Myofibrillar and cooking shortening and related changes were measured with physiograph recordings on pre-rigor M. triceps brachii strips suspended in paraffin oil during heating. Warner-Bratzler shear values were determined on pre-rigor and post-rigor M. triceps brachii samples heated at approximately the same rates at which muscle strips were heated (2°C/2 min and 2°C/12 min), on pre-rigor M. triceps brachii samples heated at 2°C/6 min, 2°C/9 min and 2°C/12 min and on pre-rigor and post-rigor M. triceps brachii and M. longissimus muscle heated similarly at 2°C/12 min. Rapid heating (2°C/2 min) of pre-rigor muscle produced more severe myofibrillar shortening that was complete at higher muscle temperature than slow heating (2°C/12 min). Slow heating, in contrast to rapid heating, resulted in a cooked product of lower shear value in both the pre-rigor and post-rigor states. The slower the heating rate of the pre-rigor M. triceps brachii, the more tender was the product. Heating at a rate of 2°C/12 min produced acceptable tenderness in both the pre-rigor M. longissimus and M. triceps brachii muscles but even greater tenderness when both muscles were heated in the post-rigor state. The tenderizing action of severe muscle shortening could not be induced in electrically stimulated muscle.