Effects of muscle proteases, endogenous protease inhibitors and myofibril fragmentation on postmortem aging of goat meat

Nagaraj Nagathihalli, K. Santhanam

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The present study was conducted to evaluate the extent of postmortem proteolysis in longissimus dorsi, biceps femoris, semimembranosus and semitendinosus goat muscles on postmortem aging at an ambient (27C) temperature. The activities of calpains and calpastatin were determined after separation on a (diethylamino)ethyl-Sephacel column (Sigma, St. Louis, MO) and cathepsin (B, B + L and H) by carboxymethyl-Sepharose column (Sigma). The results showed that the decrease in calpain I and calpastatin activities was significantly higher than that of calpain II. Cathepsin B, B + L, H and cystatin were found to fall by 30-80% after 12 h, whereas cathepsin D decreased significantly in all the muscles. The disappearance of titin 1 and nebulin, and the appearance of a 30-kDa component were confirmed by Western blot analysis. The appearance of the 30-kDa component reported here explains the time-induced structural changes of myofibrils. The Z-line degradation had occurred by 6 h postmortem. Cathepsins are not stable compared to calpains during postmortem aging, and both enzymes may play a significant role in the proteolysis of myofibrillar proteins at ambient temperature.

Original languageEnglish (US)
Pages (from-to)269-291
Number of pages23
JournalJournal of Food Biochemistry
Volume30
Issue number3
DOIs
StatePublished - Jun 2006
Externally publishedYes

Fingerprint

meat aging
goat meat
calpain
Calpain
Myofibrils
Meats
myofibrils
proteinase inhibitors
Protease Inhibitors
Goats
Meat
Muscle
Peptide Hydrolases
proteinases
Aging of materials
Proteolysis
calpastatin
cathepsin B
Muscles
muscles

ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

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abstract = "The present study was conducted to evaluate the extent of postmortem proteolysis in longissimus dorsi, biceps femoris, semimembranosus and semitendinosus goat muscles on postmortem aging at an ambient (27C) temperature. The activities of calpains and calpastatin were determined after separation on a (diethylamino)ethyl-Sephacel column (Sigma, St. Louis, MO) and cathepsin (B, B + L and H) by carboxymethyl-Sepharose column (Sigma). The results showed that the decrease in calpain I and calpastatin activities was significantly higher than that of calpain II. Cathepsin B, B + L, H and cystatin were found to fall by 30-80{\%} after 12 h, whereas cathepsin D decreased significantly in all the muscles. The disappearance of titin 1 and nebulin, and the appearance of a 30-kDa component were confirmed by Western blot analysis. The appearance of the 30-kDa component reported here explains the time-induced structural changes of myofibrils. The Z-line degradation had occurred by 6 h postmortem. Cathepsins are not stable compared to calpains during postmortem aging, and both enzymes may play a significant role in the proteolysis of myofibrillar proteins at ambient temperature.",
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AB - The present study was conducted to evaluate the extent of postmortem proteolysis in longissimus dorsi, biceps femoris, semimembranosus and semitendinosus goat muscles on postmortem aging at an ambient (27C) temperature. The activities of calpains and calpastatin were determined after separation on a (diethylamino)ethyl-Sephacel column (Sigma, St. Louis, MO) and cathepsin (B, B + L and H) by carboxymethyl-Sepharose column (Sigma). The results showed that the decrease in calpain I and calpastatin activities was significantly higher than that of calpain II. Cathepsin B, B + L, H and cystatin were found to fall by 30-80% after 12 h, whereas cathepsin D decreased significantly in all the muscles. The disappearance of titin 1 and nebulin, and the appearance of a 30-kDa component were confirmed by Western blot analysis. The appearance of the 30-kDa component reported here explains the time-induced structural changes of myofibrils. The Z-line degradation had occurred by 6 h postmortem. Cathepsins are not stable compared to calpains during postmortem aging, and both enzymes may play a significant role in the proteolysis of myofibrillar proteins at ambient temperature.

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