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 |
| State | Published - 2002 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Changes in the calpain-calpastatin and cathepsin (B, B+L, H and D) during postmortem storage of goat muscles
AU - Nagathihalli, Nagaraj
AU - Anilakumar, K. R.
AU - Santhanam, K.
PY - 2002
Y1 - 2002
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.
UR - http://www.scopus.com/inward/record.url?scp=0036002459&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036002459&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0036002459
VL - 26
SP - 75
EP - 89
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
SN - 0145-8884
IS - 1
ER -