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

  • HARADA Junko
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University
  • TAKAKU Shusaku
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University
  • WATANABE Kunihiko
    Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University

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

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We reported an on-demand type of metalloprotease from Exiguobacterium undae 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 Ca2+ 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 Ca2+ binding site was lost and by replacement for proline and isoleucine residues.

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