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

N. S. Nagaraj; K. R. Anilakumar; K. Santhanam

doi:10.1111/j.1745-4514.2002.tb00051.x

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

N. S. Nagaraj, K. R. Anilakumar, K. Santhanam

Research output: Contribution to journal › Article

13 Scopus citations

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 language	English (US)
Pages (from-to)	75-89
Number of pages	15
Journal	Journal of Food Biochemistry
Volume	26
Issue number	1
DOIs	https://doi.org/10.1111/j.1745-4514.2002.tb00051.x
State	Published - Jan 1 2002
Externally published	Yes

ASJC Scopus subject areas

Food Science
Biophysics
Pharmacology
Cell Biology

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Nagaraj, N. S., Anilakumar, K. R., & Santhanam, K. (2002). Changes in the calpain-calpastatin and cathepsin (B, B+L, H and D) during postmortem storage of goat muscles. Journal of Food Biochemistry, 26(1), 75-89. https://doi.org/10.1111/j.1745-4514.2002.tb00051.x

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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.",

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N2 - 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.

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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