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@ARTICLE{Falkenberg:908891,
      author       = {Falkenberg, Fabian and Rahba, Jade and Fischer, David and
                      Bott, Michael and Bongaerts, Johannes and Siegert, Petra},
      title        = {{B}iochemical characterization of a novel oxidatively
                      stable, halotolerant, and high‐alkaline subtilisin from
                      {A}lkalihalobacillus okhensis {K}h10‐101 {T}},
      journal      = {FEBS Open Bio},
      volume       = {12},
      number       = {10},
      issn         = {2211-5463},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {FZJ-2022-02898},
      pages        = {1729-1746},
      year         = {2022},
      note         = {Biotechnologie 1},
      abstract     = {Halophilic and halotolerant microorganisms represent a
                      promising source of salt-tolerant enzymes suitable for
                      various biotechnological applications where high salt
                      concentrations would otherwise limit enzymatic activity.
                      Considering the current growing enzyme market and the need
                      for more efficient and new biocatalysts, the present study
                      aimed at the characterization of a high-alkaline subtilisin
                      from Alkalihalobacillus okhensis Kh10-101T. The protease
                      gene was cloned and expressed in Bacillus subtilis DB104.
                      The recombinant protease SPAO with 269 amino acids belongs
                      to the subfamily of high-alkaline subtilisins. The
                      biochemical characteristics of purified SPAO were analyzed
                      in comparison with subtilisin Carlsberg, Savinase, and BPN'.
                      SPAO, a monomer with a molecular mass of 27.1 kDa, was
                      active over a wide range of pH 6.0–12.0 and temperature
                      20–80 °C, optimally at pH 9.0–9.5 and 55 °C. The
                      protease is highly oxidatively stable to hydrogen peroxide
                      and retained $58\%$ of residual activity when incubated at
                      10 °C with $5\%$ (v/v) H2O2 for 1 h while stimulated at
                      $1\%$ (v/v) H2O2. Furthermore, SPAO was very stable and
                      active at NaCl concentrations up to 5.0 m. This study
                      demonstrates the potential of SPAO for biotechnological
                      applications in the future.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35727859},
      UT           = {WOS:000820971100001},
      doi          = {10.1002/2211-5463.13457},
      url          = {https://juser.fz-juelich.de/record/908891},
}