Abstract <p>The minor zinc-dependent metalloendopeptidase secreted by the rhizosphere strain <i>Bacillus pumilus</i> 3-19 is classified at a unique intermediate position between two families of the metzincin clan: adamalysin and astacins. To investigate the functional role of this metalloendopeptidase in more detail, it is necessary to obtain a pure preparation of the protein in a sufficient amount. Since the native level of the enzyme secretion by <i>B. pumilus</i> 3-19 is extremely low, recombinant MprBp-producing strains were constructed based on proteaseless strains of <i>Bacillus subtilis</i> and methylotrophic yeast <i>Pichia</i> <i>pastoris</i>, and their efficiency as metalloendopeptidase producers was evaluated. The highest yield of the target protein was observed for the strain <i>B.&#xa0;subtilis</i> BG2036+<i>mprBp.</i></p>

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Efficiency of Recombinant Strains as Producers of Metalloendopeptidase from Bacillus pumilis 3-19

  • N. L. Rudakova,
  • D. I. Khasanov,
  • M. R. Sharipova

摘要

Abstract

The minor zinc-dependent metalloendopeptidase secreted by the rhizosphere strain Bacillus pumilus 3-19 is classified at a unique intermediate position between two families of the metzincin clan: adamalysin and astacins. To investigate the functional role of this metalloendopeptidase in more detail, it is necessary to obtain a pure preparation of the protein in a sufficient amount. Since the native level of the enzyme secretion by B. pumilus 3-19 is extremely low, recombinant MprBp-producing strains were constructed based on proteaseless strains of Bacillus subtilis and methylotrophic yeast Pichia pastoris, and their efficiency as metalloendopeptidase producers was evaluated. The highest yield of the target protein was observed for the strain B. subtilis BG2036+mprBp.