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Alkaline serine protease from halatoerant Bacillus licheniformis BA17

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


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{
  "URL": "https://aperta.ulakbim.gov.tr/record/89969", 
  "abstract": "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.", 
  "author": [
    {
      "family": "Oeztuerk", 
      "given": " Selcuk"
    }, 
    {
      "family": "Oezeren-Morgan", 
      "given": " Mueserref"
    }, 
    {
      "family": "Dilgimen", 
      "given": " Aydan Salman"
    }, 
    {
      "family": "Denizci", 
      "given": " Aziz Akin"
    }, 
    {
      "family": "Arikan", 
      "given": " Burhan"
    }, 
    {
      "family": "Kazan", 
      "given": " Dilek"
    }
  ], 
  "container_title": "ANNALS OF MICROBIOLOGY", 
  "id": "89969", 
  "issue": "1", 
  "issued": {
    "date-parts": [
      [
        2009, 
        1, 
        1
      ]
    ]
  }, 
  "page": "83-90", 
  "title": "Alkaline serine protease from halatoerant Bacillus licheniformis BA17", 
  "type": "article-journal", 
  "volume": "59"
}
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