An On-Demand Metalloprotease from Psychro-Tolerant Exiguobacterium undae Su-1, the Activity and Stability of Which Are Controlled by the Ca²⁺ Concentration An On-Demand Metalloprotease from Psychro-Tolerant Exiguobacterium undae Su-1, the Activity and Stability of Which Are Controlled by the Ca^<2+> Concentration

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We reported an on-demand type of metalloprotease from <i>Exiguobacterium undae</i> Su-1. Although this species of bacterium is known to inhabit the permafrost, there are no reports on either strong proteases or peptidases. We found that Su-1 protease is superior to commercially available proteases in proteolytic activity in a lower to normal range of temperature (10–50 °C) as well as in rapid inactivation heat-dependently on the Ca<sup>2+</sup> concentration. These characteristics meet well with the demands from food processing and manufacturing. Biochemical investigations of the purified enzyme and protein structural analysis after gene cloning confirmed that Su-1 protease conserved high identity in its primary sequence with thermophilic proteases of the M4 family. On the other hand, its flexibility was enhanced when one Ca<sup>2+</sup> binding site was lost and by replacement for proline and isoleucine residues.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(5), 986-992, 2012-05-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030753012
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    023681973
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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