Changes in the calpain-calpastatin and cathepsin (B, B+L, H and D) during postmortem storage of goat muscles

Nagaraj Nagathihalli, K. R. Anilakumar, K. Santhanam

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The objective of this study was to elucidate a relationship between some endogenous proteinases and their inhibitors in four different goat muscles during postmortem storage. Samples were taken from the longissimus dorsi (LD), biceps femoris (BF), semimembranosus (SM) and semitendinosus (ST) muscles stored up to 20 days postmortem at 5C. Activities of calpain-I, calpain-II, calpastatin, cathepsins (B, B+L, H and D) and cystatin(s) were determined. Decreases in calpain-I and calpastatin activities were significantly more than that of calpain-II activity. The cathepsin B, B+L, H and cystatin level were found to fall by 9-35% after 20 days, whereas the cathepsin D showed 11-17% decline in all the muscles. Thus changes in muscle proteinases and their inhibitors during postmortem storage differ and the results may shed light on their role in myofibrillar proteolysis and goat meat tenderization.

Original languageEnglish (US)
Pages (from-to)75-89
Number of pages15
JournalJournal of Food Biochemistry
Volume26
Issue number1
StatePublished - 2002
Externally publishedYes

Fingerprint

calpastatin
cathepsin B
Cathepsin B
calpain
Calpain
Goats
Muscle
goats
Cystatins
cystatins
Muscles
muscles
Peptide Hydrolases
proteinases
Proteolysis
cathepsin D
goat meat
semitendinosus muscle
tenderizing
Cathepsin D

ASJC Scopus subject areas

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

Cite this

Changes in the calpain-calpastatin and cathepsin (B, B+L, H and D) during postmortem storage of goat muscles. / Nagathihalli, Nagaraj; Anilakumar, K. R.; Santhanam, K.

In: Journal of Food Biochemistry, Vol. 26, No. 1, 2002, p. 75-89.

Research output: Contribution to journalArticle

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AB - The objective of this study was to elucidate a relationship between some endogenous proteinases and their inhibitors in four different goat muscles during postmortem storage. Samples were taken from the longissimus dorsi (LD), biceps femoris (BF), semimembranosus (SM) and semitendinosus (ST) muscles stored up to 20 days postmortem at 5C. Activities of calpain-I, calpain-II, calpastatin, cathepsins (B, B+L, H and D) and cystatin(s) were determined. Decreases in calpain-I and calpastatin activities were significantly more than that of calpain-II activity. The cathepsin B, B+L, H and cystatin level were found to fall by 9-35% after 20 days, whereas the cathepsin D showed 11-17% decline in all the muscles. Thus changes in muscle proteinases and their inhibitors during postmortem storage differ and the results may shed light on their role in myofibrillar proteolysis and goat meat tenderization.

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