Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation

Jason Krause, Shonisani C. Tshidino, Tomohisa Ogawa, Yasuharu Watanabe, Vaughan Oosthuizen, Benesh Somai, Koji Muramoto, Ryno J. Naudé

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Cathepsin D was purified from ostrich (Struthio camelus) skeletal muscle using pepstatin-A chromatography. The enzyme was comprised of two subunits (29.1 and 14kDa). The N-terminal amino acid sequence of both subunits were determined and showed high amino acid sequence identity to other cathepsin D homologs. Ostrich cathepsin D was optimally active at pH 4 and at a temperature of 45°C, and was strongly inhibited by pepstatin-A (Ki=3.07×10-9M) and dithiothreitol. Cathepsin D activities from five ostriches were monitored over a 30-day period. Cathepsin D remained substantially active throughout the 30-day storage period with an average remaining activity of 112±8.57% at day 30 (mean value from 5 ostriches).

Original languageEnglish
Pages (from-to)196-201
Number of pages6
JournalMeat Science
Volume87
Issue number3
DOIs
Publication statusPublished - 2011 Mar

Keywords

  • Cathepsin D
  • Ostrich muscle
  • Pepstatin-A
  • Postmortem proteolysis

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