1 Ocak 2010 Dergi makalesi Açık Erişim

Uzun, K.; Cevik, E.; Senel, M.; Sozeri, H.; Baykal, A.; Abasiyanik, M. F.; Toprak, M. S.

Dublin Core

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<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Uzun, K.</dc:creator>
  <dc:creator>Cevik, E.</dc:creator>
  <dc:creator>Senel, M.</dc:creator>
  <dc:creator>Sozeri, H.</dc:creator>
  <dc:creator>Baykal, A.</dc:creator>
  <dc:creator>Abasiyanik, M. F.</dc:creator>
  <dc:creator>Toprak, M. S.</dc:creator>
  <dc:date>2010-01-01</dc:date>
  <dc:description>In this study, polyamidoamine (PAMAM) dendrimer was synthesized on the surface of superparamagnetite nanoparticles to enhance invertase immobilization. The amount of immobilized enzyme on the surface-hyperbranched magnetite nanoparticle was up to 2.5 times (i.e., 250%) as much as that of magnetite nanoparticle modified with only amino silane. Maximum reaction rate (V (max)) and Michaelis-Menten constant (K (m)) were determined for the free and immobilized enzymes. Various characteristics of immobilized invertase such as; the temperature activity, thermal stability, operational stability, and storage stability were evaluated and results revealed that stability of the enzyme is improved upon immobilization.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/92915</dc:identifier>
  <dc:identifier>oai:zenodo.org:92915</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>JOURNAL OF NANOPARTICLE RESEARCH 12(8) 3057-3067</dc:source>
  <dc:title>Covalent immobilization of invertase on PAMAM-dendrimer modified superparamagnetic iron oxide nanoparticles</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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