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University of Minnesota4, St. Paul 55101
Abstract
Three experiments utilizing 46 pigs were conducted to study the possible relationship of blood enzymes, as influenced by stress, to postmortem porcine muscle glycolysis. Animals were stressed 40 min. antemortem by transportation, physical handling and restraint for 15 minutes. Postmortem decline in pH and protein solubility and color-structure were determined on longissimus muscle. Pigs from Experiment 1 (19 Poland China) exhibited more rapid pH decline than those from Experiments 2 (11 Hamp x York) and 3 (16 heterogeneous). Significant correlation coefficients were noted between enzyme activity and muscle properties in all experiments. Correlations were much higher, however, in Experiments 2 and 3 as both blood enzyme activities and muscle properties were more variable. In Experiment 2, the activities of lactate dehydrogenase (LDH), aldolase (ALD) and creatine kinase (CPK) were correlated with muscle pH at death (r = .83, P<.01; r = .78, P<.01; r = .63, P<.05) and 1 hr. (r = .72, P< .01; r = .86, P<.01, r = .57, P<.05) postmortem. LDH, ALD and CPK were correlated with decrease in sarcoplasmic and myofibrillar protein solubility (between 0 and 24 hr postmortem) as follows: 0.59, P<.05; 0.56, P<.05; 0.39, P<0.5 and 0.80, P<.01; 0.76, P<.01; 0.64, P<.05. In Experiment 3, LDH and CPK were correlated with 45 min. pH (r=.96 and r=.95, P<.01) and significantly related to muscle protein solubility parameters (P<.01 and P<.05). The response to thermal stress (43 C for 10 min.) in terms of blood enzyme activity was highly repeatable in pigs from Experiment 3.
1 Presented at the 64th Annual Meeting of the AMERICAN SOCIETY OF ANIMAL SCIENCE, Virginia Polytechnic Institute and State University, Blacksburg.
2 Scientific Journal Series Paper No. 8285, Minnesota Agricultural Experiment Station.
3 This research was supported in part by research grants from the American Meat Institute Foundation and Wilson-Sinclair.
4 Department of Food Science and Nutrition.
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