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Studies on Alkaline Serine Protease Produced by Bacillus clausii GMBE 22

Kazan, Dilek; Bal, Hulya; Denizci, Aziz Akin; Ozturk, Nurcin Celik; Ozturk, Hasan Umit; Dilgimen, Aydan Salman; Ozturk, Dilek Coskuner; Erarslan, Altan


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      {
        "name": "Kazan, Dilek"
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      {
        "affiliation": "Marmara Univ, Fac Art & Sci, Dept Biol, Istanbul, Turkey", 
        "name": "Bal, Hulya"
      }, 
      {
        "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
        "name": "Denizci, Aziz Akin"
      }, 
      {
        "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
        "name": "Ozturk, Nurcin Celik"
      }, 
      {
        "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
        "name": "Ozturk, Hasan Umit"
      }, 
      {
        "affiliation": "Marmara Univ, Fac Engn, Dept Bioengn, Istanbul, Turkey", 
        "name": "Dilgimen, Aydan Salman"
      }, 
      {
        "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
        "name": "Ozturk, Dilek Coskuner"
      }, 
      {
        "name": "Erarslan, Altan"
      }
    ], 
    "description": "An alkali tolerant Bacillus strain having extracellular serine alkaline protease activity was newly isolated from compost and identified as Bacillus clausii GMBE 22. An alkaline protease (AP22) was 4.66-fold purified in 51.5% yield from Bacillus clausii GMBE 22 by ethanol precipitation and DEAE-cellulose anion exchange chromatography. The purified enzyme was identified as serine protease by LC-ESI-MS analysis. Its complete inhibition by phenylmethanesulfonylfluoride (PMSF) also justified that it is a serine alkaline protease. The molecular weight of the enzyme is 25.4kDa. Optimal temperature and pH values are 60C and 12.0, respectively. The enzyme showed highest specificity to N-Suc-Ala-Ala-Pro-Phe-pNA. The Km and kcat values for hydrolysis of this substrate are 0.347mM and 1141min-1 respectively. The enzyme was affected by surface active agents to varying extents. The enzyme is stable for 2h at 30C and pH 10.5. AP22 is also stable for 5 days over the pH range 9.0-11.0 at room temperature. AP22 has good pH stability compared with the alkaline proteases belonging to other strains of Bacillus clausii reported in the literature.", 
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      "issue": "3", 
      "pages": "289-307", 
      "title": "PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY", 
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    "title": "Studies on Alkaline Serine Protease Produced by Bacillus clausii GMBE 22"
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