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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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/94311</identifier>
  <creators>
    <creator>
      <creatorName>Kazan, Dilek</creatorName>
      <givenName>Dilek</givenName>
      <familyName>Kazan</familyName>
    </creator>
    <creator>
      <creatorName>Bal, Hulya</creatorName>
      <givenName>Hulya</givenName>
      <familyName>Bal</familyName>
      <affiliation>Marmara Univ, Fac Art &amp; Sci, Dept Biol, Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Denizci, Aziz Akin</creatorName>
      <givenName>Aziz Akin</givenName>
      <familyName>Denizci</familyName>
      <affiliation>Genet Engn &amp; Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci &amp; Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Ozturk, Nurcin Celik</creatorName>
      <givenName>Nurcin Celik</givenName>
      <familyName>Ozturk</familyName>
      <affiliation>Genet Engn &amp; Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci &amp; Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Ozturk, Hasan Umit</creatorName>
      <givenName>Hasan Umit</givenName>
      <familyName>Ozturk</familyName>
      <affiliation>Genet Engn &amp; Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci &amp; Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Dilgimen, Aydan Salman</creatorName>
      <givenName>Aydan Salman</givenName>
      <familyName>Dilgimen</familyName>
      <affiliation>Marmara Univ, Fac Engn, Dept Bioengn, Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Ozturk, Dilek Coskuner</creatorName>
      <givenName>Dilek Coskuner</givenName>
      <familyName>Ozturk</familyName>
      <affiliation>Genet Engn &amp; Biotechnol Inst GEBI, Marmara Res Ctr MRC, Sci &amp; Technol Res Council Turkey TUBITAK, TR-41470 Gebze, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Erarslan, Altan</creatorName>
      <givenName>Altan</givenName>
      <familyName>Erarslan</familyName>
    </creator>
  </creators>
  <titles>
    <title>Studies On Alkaline Serine Protease Produced By Bacillus Clausii Gmbe 22</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2009</publicationYear>
  <dates>
    <date dateType="Issued">2009-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/94311</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1080/10826060902953269</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">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.</description>
  </descriptions>
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