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Role of Ca ++ ‐Dependent Proteases and Lysosomal Enyzmes in Postmortem Changes in Bovine Skeletal Muscle
Author(s) -
KOOHMARAIE M.,
BABIKER A.S.,
MERKEL R.A.,
DUTSON T.R.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb09251.x
Subject(s) - egta , myofibril , chemistry , calcium , cathepsin , tris , autolysis (biology) , cathepsin b , ethylene glycol , protease , longissimus , biochemistry , enzyme , anatomy , biology , organic chemistry
Bovine longissimus muscles excised at slaughter were compared to cross‐sectional slices of contralateral longissimus muscles obtained 12 hr postmortem for calcium‐dependent protease (CDP), cathepsins B, H and L activity, and myofibrillar fragmentation index (MFI). Slices were suspended in either Tris‐acetate buffer, buffer + ethylene diaminotetraacetic acid (EDTA), buffer + ethylene glycol‐bis (β, aminoethyl ether) N, N, N', N'‐tetraacetic acid (EGTA) or buffer + CaCl 2 for either 1, 3, or 7 days while the postmortem associated changes were followed. EDTA, EGTA and Ca ++ had no effect on cathepsin B, H or L activities. EDTA and EGTA treated slices had 149% whereas Ca ++ 48% of control CDP activity. Postmortem changes were completed after 24 hr of Ca ++ treatment but did not occur in EDTA‐ and EGTA‐treated slices. Thus, the changes observed during postmortem storage appeared to be associated with CDP activity rather than catheptic enzymes.