Effect of frozen temperature and storage time on calpains, cathepsins (B, B + L, H and D) and their endogenous inhibitors in goat muscles

N. S. Nagaraj, K. Santhanam

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The effects of frozen storage on the biochemical properties of myofibrils, muscle proteinases (cathepsins and calpains) and their endogenous inhibitors were investigated. Longissimus dorsi, biceps femoris, semimembranosus and semitendinosus muscles from goat were frozen (-15C) and studied up to 120 days. The results showed that the percentage change in sarcomere length was 8.4-13.1. The calpain activity was determined after separation on a diethylaminoethyl- Sephacel column (Sigma, St. Louis, MO). Significantly greater percentage of calpain II activity was recovered when compared to calpain I. There was a 15-25% loss in calpastatin inhibitory activity, and the cystatin level fell by 11-16% after 80 days. Cathepsin B, B + L, H and D were very stable when compared to calpains. The calcium concentration may also be the factor for calpain activation. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis result showed the appearance of 55 kDa components. It was concluded that calpains, not cathepsins, play an important role in the proteolysis of myofibrillar proteins at the freezing temperature.

Original languageEnglish (US)
Pages (from-to)155-173
Number of pages19
JournalJournal of Food Biochemistry
Volume30
Issue number2
DOIs
StatePublished - Apr 1 2006
Externally publishedYes

ASJC Scopus subject areas

  • Food Science
  • Biophysics
  • Pharmacology
  • Cell Biology

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