Lactate dehydrogenase enzyme activity in raw, cured, and heated porcine muscle Academic Article uri icon

abstract

  • Semimembranosus, semitendinosus, biceps femoris, rectus femoris, and adductor muscles were dissected from nine fresh hams. Each muscle was analyzed for lactate dehydrogenase (LDH) activity after receiving one of the following treatments: fresh, aged, frozen, frozen-thawed, heated, cured, and cured-heated. Aging resulted in an increase in LDH activity, while freezing and freezing-thawing resulted in a marked decrease in activity. Heating fresh tissue to 65-68 °C resulted in large activity losses. Heating to 68 °C and above significantly inactivated the enzyme. Curing and heating to 63.8 °C eliminated almost all LDH activity. Pyruvate kinase, malate dehydrogenase, adenylate kinase, isocitrate dehydrogenase, creatine kinase, aspartate aminotransferase, fructose- 1,6-bisphosphate aldolase, citrate synthase, and glutamate-oxaloacetate transminase activities were monitored in cured ham muscle heated to 64.5 and 68.8 °C. No appreciable enzyme activity was detected in any cured/heated samples. © 1991, American Chemical Society. All rights reserved.

author list (cited authors)

  • Collins, S. S., Keeton, J. T., & Smith, S. B.

citation count

  • 18

publication date

  • July 1991