1 Ocak 2019 Dergi makalesi Açık Erişim

Arabaci, Nihan; Arikan, Burhan

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/75147</identifier>
  <creators>
    <creator>
      <creatorName>Arabaci, Nihan</creatorName>
      <givenName>Nihan</givenName>
      <familyName>Arabaci</familyName>
      <affiliation>Cukurova Univ, Dept Biol, TR-01330 Adana, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Arikan, Burhan</creatorName>
      <givenName>Burhan</givenName>
      <familyName>Arikan</familyName>
      <affiliation>Cukurova Univ, Dept Biol, TR-01330 Adana, Turkey</affiliation>
    </creator>
  </creators>
  <titles>
    <title>An Amylopullulanase (Apunp1) From Geobacillus Thermoleovorans Np1: Biochemical Characterization And Its Potential Industrial Applications</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2019</publicationYear>
  <dates>
    <date dateType="Issued">2019-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/75147</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1080/10826068.2018.1550655</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>
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  <descriptions>
    <description descriptionType="Abstract">An amylopullulanase was produced by Geobacillus thermoleovorans NP1. The optimum enzyme production occurred at 45 degrees C and pH 7.0 (12 hr). NP1 amylopullulanase (ApuNP1) exhibited the maximal activity at 50 degrees C and pH 6.0 and was stable between 30-50 degrees C, and pH 3.0-12.0 for 24 hr. The enzyme showed two bands with molecular weights of 112 and 107 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The amylopullulanase retained 100% of its activity in the presence of 10 mM of Ca2+, Ba2+, Zn2+, Mg2+, Cu2+, EDTA, and PMSF. While the enzyme showed resistance to 5% of TritonX-100, Tween 20, and Tween 80, the activity was inhibited by 5% -mercaptoethanol and H2O2. While the hydrolysis products of pullulan were maltose, maltotriose, and maltodextrin, the starch was hydrolyzed to maltose, maltotriose, and maltodextrin units. This shows that NP1 pullulanase is a type II pullulanase (amylopullulanase). After the liquefaction assay, 12% glucose content was measured with a refractometer in the presence of 20% starch. According to the wash performance tests, the mixture of ApuNP1 and 1% detergent removed almost all of the stains. This novel thermo-acidic amylopullulanase has a potency to be used in detergent, starch, food, baking, textile, and cosmetic industries.</description>
  </descriptions>
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