1 Ocak 2009 Dergi makalesi Açık Erişim

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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  "@id": 94311, 
  "@type": "ScholarlyArticle", 
  "creator": [
    {
      "@type": "Person", 
      "name": "Kazan, Dilek"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Marmara Univ, Fac Art & Sci, Dept Biol, Istanbul, Turkey", 
      "name": "Bal, Hulya"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
      "name": "Denizci, Aziz Akin"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
      "name": "Ozturk, Nurcin Celik"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
      "name": "Ozturk, Hasan Umit"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Marmara Univ, Fac Engn, Dept Bioengn, Istanbul, Turkey", 
      "name": "Dilgimen, Aydan Salman"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Genet Engn & Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci & Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey", 
      "name": "Ozturk, Dilek Coskuner"
    }, 
    {
      "@type": "Person", 
      "name": "Erarslan, Altan"
    }
  ], 
  "datePublished": "2009-01-01", 
  "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.", 
  "headline": "Studies on Alkaline Serine Protease Produced by Bacillus clausii GMBE 22", 
  "identifier": 94311, 
  "image": "https://aperta.ulakbim.gov.tr/static/img/logo/aperta_logo_with_icon.svg", 
  "license": "http://www.opendefinition.org/licenses/cc-by", 
  "name": "Studies on Alkaline Serine Protease Produced by Bacillus clausii GMBE 22", 
  "url": "https://aperta.ulakbim.gov.tr/record/94311"
}