Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses.

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Abstract
Postmortem proteolysis in skeletal muscle and factors affecting this process were examined in pork, lamb and beef longissimus muscles (LM) to determine the cause of differences in meat tenderness among these species. Fat thickness differed among species in the following order: pork > beef > lamb. The following patterns were observed for rate of temperature and pH decline: lamb > pork > beef and pork > beef > lamb, respectively. At 1 d postmortem, pork was the most tender, followed by beef and lamb, respectively. Between 1 and 14 d of postmortem storage, lamb LM was the most improved in tenderness, followed by beef and pork, respectively. Species did not differ (P > .05) in LM collagen solubility. Pork LM from fed pigs had the highest (P< .05) level of cathepsins B + L and cystatin(s) activities, whereas no differences (P > .05) were observed among the species for cathepsin B activity. The lowest (P< .01) Ca2+-dependent protease (CDP)-II and CDP inhibitor activities were observed in pork LM. Beef LM had the highest GDP inhibitor activity (P < .05) but was intermediate in CDP-II activity. No differences were observed among species for GDP-I activity. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of myofibrils isolated at 0, 1 and 14 d postmortem indicated that by d 1, desmin hydrolysis was most extensive in pork muscle, followed by lamb and beef.(ABSTRACT TRUNCATED AT 250 WORDS)

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