Effect of Cathepsin D on Bovine Myofibrils under Different Conditions of pH and Temperature

MICHAEL G. ZEECE, KEISUKE KATOH, RICHARD M. ROBSON, FREDERICK C. PARRISH

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)769-773
Number of pages5
JournalJournal of food science
Volume51
Issue number3
DOIs
Publication statusPublished - May 1986

    Fingerprint

ASJC Scopus subject areas

  • Food Science

Cite this

ZEECE, MICHAEL. G., KATOH, KEISUKE., ROBSON, RICHARD. M., & PARRISH, FREDERICK. C. (1986). Effect of Cathepsin D on Bovine Myofibrils under Different Conditions of pH and Temperature. Journal of food science, 51(3), 769-773. https://doi.org/10.1111/j.1365-2621.1986.tb13930.x