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Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus

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Abstract

A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time. The purified protein, with an isoelectric point of pH 4.5, had a molecular mass of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile-Asp-Glu-Ala. The optimum pH and temperature for the reaction were 7.5 and 35°C, respectively. The properties of the superoxide dismutase were compared with those of the enzyme from thermophilic Bacillus stearothermophilus.

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Authors and Affiliations

  1. Tochigi Research Laboratories of Kao Corporation, 2606 Akabane; Ichikai, Haga, Tochigi 321-34, Japan; Tel. +81 285 687400, Fax +81-285-687403; e-mail: 300475@kastanet.kao.co.jp , , , , , , JP

    Yoshihiro Hakamada, Kenzo Koike, Tohru Kobayashi & Susumu Ito

Authors
  1. Yoshihiro Hakamada
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  2. Kenzo Koike
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  3. Tohru Kobayashi
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  4. Susumu Ito
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Received: September 3, 1996 / Accepted: October 4, 1996

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Hakamada, Y., Koike, K., Kobayashi, T. et al. Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus . Extremophiles 1, 74–78 (1997). https://doi.org/10.1007/s007920050017

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  • DOI: https://doi.org/10.1007/s007920050017

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