1 Ocak 2009 Dergi makalesi Açık Erişim

Oeztuerk, Selcuk; Oezeren-Morgan, Mueserref; Dilgimen, Aydan Salman; Denizci, Aziz Akin; Arikan, Burhan; Kazan, Dilek

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        "affiliation": "Marmara Univ, Fac Arts & Sci, Dept Biol, TR-81040 Istanbul, Turkey", 
        "name": "Oeztuerk, Selcuk"
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        "affiliation": "Marmara Univ, Fac Arts & Sci, Dept Biol, TR-81040 Istanbul, Turkey", 
        "name": "Oezeren-Morgan, Mueserref"
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      {
        "affiliation": "Marmara Univ, Fac Engn, Dept Bioengn, TR-34722 Istanbul, Turkey", 
        "name": "Dilgimen, Aydan Salman"
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        "affiliation": "MRC, GEBI, Sci Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Kocaeli, Turkey", 
        "name": "Denizci, Aziz Akin"
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      {
        "affiliation": "Cukurova Univ, Fac Art & Sci, Dept Biol, Adana, Turkey", 
        "name": "Arikan, Burhan"
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    "description": "An alkaline protease from halotolerant Bacillus licheniformis BA17, isolated from Van Lake in Turkey, was purified 5.4 fold with 58% yield. The molecular weight was 19.7 kDa and the optimum temperature and pH were 60 degrees C and 10, respectively. The half-life of the pure enzyme was 38 h, 93 min, 14 min and 6 min at 40, 50, 60 and 70 degrees C, respectively. BA17 protease is very active at 30 degrees C between pH 8.0 and 10. Enzyme activity increased in the presence of Cu+2, Mg+2, Mn+2 and K+1 ions, Enzyme retained activity with 5% SDS (w/v) and 1% Triton X-100 (v/v). Inhibition with PMSF and EDTA suggested that the enzyme is a serine protease and is a metal-activated enzyme. Based on the N-terminal sequence of the first 13 amino acids, B. licheniformis BA17 alkaline protease did not show identity to any of those from other Bacillus species.", 
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      "issue": "1", 
      "pages": "83-90", 
      "title": "ANNALS OF MICROBIOLOGY", 
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    "title": "Alkaline serine protease from halatoerant Bacillus licheniformis BA17"
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