TY - JOUR
T1 - Effect of Cathepsin D on Bovine Myofibrils under Different Conditions of pH and Temperature
AU - ZEECE, MICHAEL G.
AU - KATOH, KEISUKE
AU - ROBSON, RICHARD M.
AU - PARRISH, FREDERICK C.
PY - 1986/5
Y1 - 1986/5
N2 - Purified cathepsin D was incubated with bovine skeletal muscle myofibrils under in virro conditions resembling those found in postmortem muscle. SDS‐PAGE analysis of myofibrils treated at pH 5.5 and 37°C and the sedimented, showed degradation of myosin heavy chains and titin. A small amount of actin, tropomyosin, troponins T and I, and myosin light chains also were degraded. The cathepsin D treated myofibrils were not fragmented to any greater extend than untreated myofibrils. Raising the pH and/or lowering the temperature greatly reduced the effectiveness of cathepsin D suggesting that the enzyme does not play a principal role in the tenderization process occurring in muscle postmortem.
AB - Purified cathepsin D was incubated with bovine skeletal muscle myofibrils under in virro conditions resembling those found in postmortem muscle. SDS‐PAGE analysis of myofibrils treated at pH 5.5 and 37°C and the sedimented, showed degradation of myosin heavy chains and titin. A small amount of actin, tropomyosin, troponins T and I, and myosin light chains also were degraded. The cathepsin D treated myofibrils were not fragmented to any greater extend than untreated myofibrils. Raising the pH and/or lowering the temperature greatly reduced the effectiveness of cathepsin D suggesting that the enzyme does not play a principal role in the tenderization process occurring in muscle postmortem.
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U2 - 10.1111/j.1365-2621.1986.tb13930.x
DO - 10.1111/j.1365-2621.1986.tb13930.x
M3 - Article
AN - SCOPUS:0001437089
SN - 0022-1147
VL - 51
SP - 769
EP - 773
JO - Journal of food science
JF - Journal of food science
IS - 3
ER -