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

    研究成果: Article査読

    7 被引用数 (Scopus)

    抄録

    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).

    本文言語English
    ページ(範囲)196-201
    ページ数6
    ジャーナルMeat Science
    87
    3
    DOI
    出版ステータスPublished - 2011 3月

    ASJC Scopus subject areas

    • 食品科学

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