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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  <dc:creator>Oeztuerk, Selcuk</dc:creator>
  <dc:creator>Oezeren-Morgan, Mueserref</dc:creator>
  <dc:creator>Dilgimen, Aydan Salman</dc:creator>
  <dc:creator>Denizci, Aziz Akin</dc:creator>
  <dc:creator>Arikan, Burhan</dc:creator>
  <dc:creator>Kazan, Dilek</dc:creator>
  <dc:date>2009-01-01</dc:date>
  <dc: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.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/89969</dc:identifier>
  <dc:identifier>oai:zenodo.org:89969</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>ANNALS OF MICROBIOLOGY 59(1) 83-90</dc:source>
  <dc:title>Alkaline serine protease from halatoerant Bacillus licheniformis BA17</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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